ID HD_HUMAN Reviewed; 3142 AA.
AC P42858; Q9UQB7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 27-MAR-2024, entry version 227.
DE RecName: Full=Huntingtin;
DE AltName: Full=Huntington disease protein;
DE Short=HD protein;
DE Contains:
DE RecName: Full=Huntingtin, myristoylated N-terminal fragment;
GN Name=HTT; Synonyms=HD, IT15;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN HD.
RC TISSUE=Retina;
RX PubMed=8458085; DOI=10.1016/0092-8674(93)90585-e;
RA Macdonald M., Ambrose C.M., Duyao M.P., Myers R.H., Lin C.S., Srinidhi J.,
RA Barnes G., Taylor S.A., James M., Groot N., McFarlane H., Jenkins B.,
RA Anderson M.A., Wexler N.S., Gusella J.F., Bates G.P., Baxendale S.,
RA Hummerich H., Kirby S., North M., Youngman S., Mott R., Zehetner G.,
RA Sedlacek Z., Poustka A., Frischauf A.-M., Lehrach H., Buckler A.J.,
RA Church D., Doucette-Stamm L., O'Donovan M.C., Riba-Ramirez L., Shah M.,
RA Stanton V.P., Strobel S.A., Draths K.M., Wales J.L., Dervan P.,
RA Housman D.E., Altherr M., Shiang R., Thompson L., Fielder T., Wasmuth J.J.,
RA Tagle D., Valdes J., Elmer L., Allard M., Castilla L., Swaroop M.,
RA Blanchard K., Collins F.S., Snell R., Holloway T., Gillespie K., Datson N.,
RA Shaw S., Harper P.S.;
RT "A novel gene containing a trinucleotide repeat that is expanded and
RT unstable on Huntington's disease chromosomes.";
RL Cell 72:971-983(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=11013077; DOI=10.1006/geno.2000.6317;
RA Matsuyama N., Hadano S., Onoe K., Osuga H., Shouguchi-Miyata J., Gondo Y.,
RA Ikeda J.-E.;
RT "Identification and characterization of the miniature pig Huntington's
RT disease gene homolog: evidence for conservation and polymorphism in the CAG
RT triplet repeat.";
RL Genomics 69:72-85(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-203.
RX PubMed=8197474; DOI=10.1007/bf02257483;
RA Ambrose C.M., Duyao M.P., Barnes G., Bates G.P., Lin C.S., Srinidhi J.,
RA Baxendale S., Hummerich H., Lehrach H., Altherr M., Wasmuth J., Buckler A.,
RA Church D., Housman D., Berks M., Micklem G., Durbin R., Dodge A., Read A.,
RA Gusella J.F., Macdonald M.E.;
RT "Structure and expression of the Huntington's disease gene: evidence
RT against simple inactivation due to an expanded CAG repeat.";
RL Somat. Cell Mol. Genet. 20:27-38(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88.
RX PubMed=7759106; DOI=10.1016/0888-7543(95)80014-d;
RA Lin B., Nasir J., Kalchman M.A., McDonald H., Zeisler J., Goldberg Y.P.,
RA Hayden M.R.;
RT "Structural analysis of the 5' region of mouse and human Huntington disease
RT genes reveals conservation of putative promoter region and di- and
RT trinucleotide polymorphisms.";
RL Genomics 25:707-715(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2561-3142, AND VARIANT ILE-2786.
RC TISSUE=Brain, Caudate nucleus, Frontal cortex, Muscle, and Retina;
RX PubMed=7903579; DOI=10.1093/hmg/2.10.1541;
RA Lin B., Rommens J.M., Graham R.K., Kalchman M., Macdonald H., Nasir J.,
RA Delaney A., Goldberg Y.P., Hayden M.R.;
RT "Differential 3' polyadenylation of the Huntington disease gene results in
RT two mRNA species with variable tissue expression.";
RL Hum. Mol. Genet. 2:1541-1545(1993).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=7647777; DOI=10.1038/ng0595-104;
RA Trottier Y., Devys D., Imbert G., Saudou F., An I., Lutz Y., Weber C.,
RA Agid Y., Hirsch E.C., Mandel J.-L.;
RT "Cellular localization of the Huntington's disease protein and
RT discrimination of the normal and mutated form.";
RL Nat. Genet. 10:104-110(1995).
RN [8]
RP PROTEOLYTIC CLEAVAGE BY CASPASE-3.
RX PubMed=8696339; DOI=10.1038/ng0896-442;
RA Goldberg Y.P., Nicholson D.W., Rasper D.M., Kalchman M.A., Koide H.B.,
RA Graham R.K., Bromm M., Kazemi-Esfarjani P., Thornberry N.A.,
RA Vaillancourt J.P., Hayden M.R.;
RT "Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is
RT modulated by the polyglutamine tract.";
RL Nat. Genet. 13:442-449(1996).
RN [9]
RP PROTEOLYTIC CLEAVAGE BY CASPASE-3 AT ASP-511, AND MUTAGENESIS OF ASP-511
RP AND ASP-528.
RX PubMed=9535906; DOI=10.1074/jbc.273.15.9158;
RA Wellington C.L., Ellerby L.M., Hackam A.S., Margolis R.L., Trifiro M.A.,
RA Singaraja R., McCutcheon K., Salvesen G.S., Propp S.S., Bromm M.,
RA Rowland K.J., Zhang T., Rasper D., Roy S., Thornberry N., Pinsky L.,
RA Kakizuka A., Ross C.A., Nicholson D.W., Bredesen D.E., Hayden M.R.;
RT "Caspase cleavage of gene products associated with triplet expansion
RT disorders generates truncated fragments containing the polyglutamine
RT tract.";
RL J. Biol. Chem. 273:9158-9167(1998).
RN [10]
RP INTERACTION WITH PRPF40A AND SETD2.
RX PubMed=9700202; DOI=10.1093/hmg/7.9.1463;
RA Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F.,
RA MacDonald M.E.;
RT "Huntingtin interacts with a family of WW domain proteins.";
RL Hum. Mol. Genet. 7:1463-1474(1998).
RN [11]
RP INTERACTION WITH PQBP1.
RC TISSUE=Brain;
RX PubMed=10332029; DOI=10.1093/hmg/8.6.977;
RA Waragai M., Lammers C.-H., Takeuchi S., Imafuku I., Udagawa Y.,
RA Kanazawa I., Kawabata M., Mouradian M.M., Okazawa H.;
RT "PQBP-1, a novel polyglutamine tract binding protein, inhibits
RT transcription activation by Brn-2 and affects cell survival.";
RL Hum. Mol. Genet. 8:977-987(1999).
RN [12]
RP PROTEOLYTIC CLEAVAGE BY CASPASE-6 AT ASP-584, AND MUTAGENESIS OF ASP-584.
RX PubMed=10770929; DOI=10.1074/jbc.m001475200;
RA Wellington C.L., Singaraja R., Ellerby L., Savill J., Roy S., Leavitt B.,
RA Cattaneo E., Hackam A., Sharp A., Thornberry N., Nicholson D.W.,
RA Bredesen D.E., Hayden M.R.;
RT "Inhibiting caspase cleavage of huntingtin reduces toxicity and aggregate
RT formation in neuronal and nonneuronal cells.";
RL J. Biol. Chem. 275:19831-19838(2000).
RN [13]
RP INTERACTION WITH SETD2.
RX PubMed=10958656; DOI=10.1093/hmg/9.14.2175;
RA Passani L.A., Bedford M.T., Faber P.W., McGinnis K.M., Sharp A.H.,
RA Gusella J.F., Vonsattel J.-P., MacDonald M.E.;
RT "Huntingtin's WW domain partners in Huntington's disease post-mortem brain
RT fulfill genetic criteria for direct involvement in Huntington's disease
RT pathogenesis.";
RL Hum. Mol. Genet. 9:2175-2182(2000).
RN [14]
RP INTERACTION WITH SETD2.
RX PubMed=11461154; DOI=10.1006/mcne.2001.1004;
RA Rega S., Stiewe T., Chang D.-I., Pollmeier B., Esche H., Bardenheuer W.,
RA Marquitan G., Puetzer B.M.;
RT "Identification of the full-length huntingtin-interacting protein
RT p231HBP/HYPB as a DNA-binding factor.";
RL Mol. Cell. Neurosci. 18:68-79(2001).
RN [15]
RP NUCLEAR EXPORT SIGNAL.
RX PubMed=12783847; DOI=10.1093/hmg/ddg156;
RA Xia J., Lee D.H., Taylor J., Vandelft M., Truant R.;
RT "Huntingtin contains a highly conserved nuclear export signal.";
RL Hum. Mol. Genet. 12:1393-1403(2003).
RN [16]
RP INTERACTION WITH TPR, AND SUBCELLULAR LOCATION.
RX PubMed=15654337; DOI=10.1038/ng1503;
RA Cornett J., Cao F., Wang C.E., Ross C.A., Bates G.P., Li S.H., Li X.J.;
RT "Polyglutamine expansion of huntingtin impairs its nuclear export.";
RL Nat. Genet. 37:198-204(2005).
RN [17]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16391387; DOI=10.1385/nmm:7:4:297;
RA Sayer J.A., Manczak M., Akileswaran L., Reddy P.H., Coghlan V.M.;
RT "Interaction of the nuclear matrix protein NAKAP with HypA and huntingtin:
RT implications for nuclear toxicity in Huntington's disease pathogenesis.";
RL NeuroMolecular Med. 7:297-310(2005).
RN [18]
RP SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH
RP F8A1/F8A2/F8A3 AND RAB5A, AND INTERACTION WITH F8A1/F8A2/F8A3.
RX PubMed=16476778; DOI=10.1083/jcb.200509091;
RA Pal A., Severin F., Lommer B., Shevchenko A., Zerial M.;
RT "Huntingtin-HAP40 complex is a novel Rab5 effector that regulates early
RT endosome motility and is up-regulated in Huntington's disease.";
RL J. Cell Biol. 172:605-618(2006).
RN [19]
RP INTERACTION WITH SYVN, AND UBIQUITINATION.
RX PubMed=17141218; DOI=10.1016/j.yexcr.2006.10.031;
RA Yang H., Zhong X., Ballar P., Luo S., Shen Y., Rubinsztein D.C.,
RA Monteiro M.J., Fang S.;
RT "Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity
RT of polyglutamine-expanded huntingtin.";
RL Exp. Cell Res. 313:538-550(2007).
RN [20]
RP PHOSPHORYLATION AT SER-1179 AND SER-1199.
RX PubMed=17611284; DOI=10.1523/jneurosci.1831-07.2007;
RA Anne S.L., Saudou F., Humbert S.;
RT "Phosphorylation of huntingtin by cyclin-dependent kinase 5 is induced by
RT DNA damage and regulates wild-type and mutant huntingtin toxicity in
RT neurons.";
RL J. Neurosci. 27:7318-7328(2007).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1870, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [23]
RP INTERACTION WITH PFN1.
RX PubMed=18573880; DOI=10.1128/mcb.00079-08;
RA Shao J., Welch W.J., Diprospero N.A., Diamond M.I.;
RT "Phosphorylation of profilin by ROCK1 regulates polyglutamine
RT aggregation.";
RL Mol. Cell. Biol. 28:5196-5208(2008).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-1870 AND SER-1874,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432 AND SER-1874, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1870 AND SER-1874, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [29]
RP ACETYLATION AT LYS-9; LYS-176; LYS-234; LYS-343 AND LYS-442.
RX PubMed=21685499; DOI=10.1074/mcp.m111.009829;
RA Cong X., Held J.M., Degiacomo F., Bonner A., Chen J.M., Schilling B.,
RA Czerwieniec G.A., Gibson B.W., Ellerby L.M.;
RT "Mass spectrometric identification of novel lysine acetylation sites in
RT huntingtin.";
RL Mol. Cell. Proteomics 0:0-0(2011).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640; SER-643; SER-1199 AND
RP SER-1874, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [33]
RP INTERACTION WITH ZDHHC17 AND ZDHHC13, AND MUTAGENESIS OF ILE-495; GLN-498
RP AND PRO-499.
RX PubMed=26198635; DOI=10.1074/jbc.m115.657668;
RA Lemonidis K., Sanchez-Perez M.C., Chamberlain L.H.;
RT "Identification of a novel sequence motif recognized by the ankyrin repeat
RT domain of zDHHC17/13 S-acyltransferases.";
RL J. Biol. Chem. 290:21939-21950(2015).
RN [34]
RP INTERACTION WITH ZDHHC17.
RX PubMed=28882895; DOI=10.1074/jbc.m117.799650;
RA Lemonidis K., MacLeod R., Baillie G.S., Chamberlain L.H.;
RT "Peptide array based screening reveals a large number of proteins
RT interacting with the ankyrin repeat domain of the zDHHC17 S-
RT acyltransferase.";
RL J. Biol. Chem. 292:17190-17202(2017).
RN [35]
RP INTERACTION WITH ZDHHC17, AND MUTAGENESIS OF 498-GLN-PRO-499.
RX PubMed=28757145; DOI=10.1016/j.str.2017.06.018;
RA Verardi R., Kim J.S., Ghirlando R., Banerjee A.;
RT "Structural basis for substrate recognition by the ankyrin repeat domain of
RT human DHHC17 palmitoyltransferase.";
RL Structure 0:0-0(2017).
RN [36]
RP FUNCTION, SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-551, AND MUTAGENESIS
RP OF GLY-551.
RX PubMed=24459296; DOI=10.1093/hmg/ddu027;
RA Martin D.D., Heit R.J., Yap M.C., Davidson M.W., Hayden M.R.,
RA Berthiaume L.G.;
RT "Identification of a post-translationally myristoylated autophagy-inducing
RT domain released by caspase cleavage of huntingtin.";
RL Hum. Mol. Genet. 23:3166-3179(2014).
RN [37]
RP PROTEOLYTIC CLEAVAGE AT ASP-550, MYRISTOYLATION AT GLY-551, MUTAGENESIS OF
RP ASP-550 AND GLY-551, AND CHARACTERIZATION OF VARIANT GLU-551.
RX PubMed=29802276; DOI=10.1038/s41598-018-25903-w;
RA Martin D.D.O., Kay C., Collins J.A., Nguyen Y.T., Slama R.A., Hayden M.R.;
RT "A human huntingtin SNP alters post-translational modification and
RT pathogenic proteolysis of the protein causing Huntington disease.";
RL Sci. Rep. 8:8096-8096(2018).
RN [38] {ECO:0007744|PDB:3IO4, ECO:0007744|PDB:3IO6, ECO:0007744|PDB:3IOR, ECO:0007744|PDB:3IOT, ECO:0007744|PDB:3IOU, ECO:0007744|PDB:3IOV, ECO:0007744|PDB:3IOW}
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-64, AND DOMAIN.
RX PubMed=19748341; DOI=10.1016/j.str.2009.08.002;
RA Kim M.W., Chelliah Y., Kim S.W., Otwinowski Z., Bezprozvanny I.;
RT "Secondary structure of Huntingtin amino-terminal region.";
RL Structure 17:1205-1212(2009).
RN [39] {ECO:0007744|PDB:3LRH}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 5-18.
RX PubMed=21968397; DOI=10.1016/j.jmb.2011.09.034;
RA Schiefner A., Chatwell L., Korner J., Neumaier I., Colby D.W., Volkmer R.,
RA Wittrup K.D., Skerra A.;
RT "A disulfide-free single-domain V(L) intrabody with blocking activity
RT towards huntingtin reveals a novel mode of epitope recognition.";
RL J. Mol. Biol. 414:337-355(2011).
RN [40] {ECO:0007744|PDB:2LD0, ECO:0007744|PDB:2LD2}
RP STRUCTURE BY NMR OF 1-17.
RX PubMed=23931318; DOI=10.1016/j.bpj.2013.06.030;
RA Michalek M., Salnikov E.S., Bechinger B.;
RT "Structure and topology of the huntingtin 1-17 membrane anchor by a
RT combined solution and solid-state NMR approach.";
RL Biophys. J. 105:699-710(2013).
RN [41] {ECO:0007744|PDB:4FE8, ECO:0007744|PDB:4FEB, ECO:0007744|PDB:4FEC, ECO:0007744|PDB:4FED}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-64.
RX PubMed=23370273; DOI=10.4161/pri.23807;
RA Kim M.;
RT "Beta conformation of polyglutamine track revealed by a crystal structure
RT of Huntingtin N-terminal region with insertion of three histidine
RT residues.";
RL Prion 7:221-228(2013).
RN [42] {ECO:0007744|PDB:4RAV}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-17.
RX PubMed=25861763; DOI=10.1016/j.jmb.2015.03.021;
RA De Genst E., Chirgadze D.Y., Klein F.A., Butler D.C., Matak-Vinkovic D.,
RA Trottier Y., Huston J.S., Messer A., Dobson C.M.;
RT "Structure of a single-chain Fv bound to the 17 N-terminal residues of
RT huntingtin provides insights into pathogenic amyloid formation and
RT suppression.";
RL J. Mol. Biol. 427:2166-2178(2015).
RN [43] {ECO:0007744|PDB:6EZ8}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS) IN COMPLEX WITH
RP F8A1/F8A2/F8A3, AND INTERACTION WITH F8A1/F8A2/F8A3.
RX PubMed=29466333; DOI=10.1038/nature25502;
RA Guo Q., Huang B., Cheng J., Seefelder M., Engler T., Pfeifer G., Oeckl P.,
RA Otto M., Moser F., Maurer M., Pautsch A., Baumeister W.,
RA Fernandez-Busnadiego R., Kochanek S.;
RT "The cryo-electron microscopy structure of huntingtin.";
RL Nature 555:117-120(2018).
RN [44]
RP INVOLVEMENT IN LOMARS, AND VARIANT LOMARS LEU-2717.
RX PubMed=27329733; DOI=10.1038/ejhg.2016.74;
RA Rodan L.H., Cohen J., Fatemi A., Gillis T., Lucente D., Gusella J.,
RA Picker J.D.;
RT "A novel neurodevelopmental disorder associated with compound heterozygous
RT variants in the huntingtin gene.";
RL Eur. J. Hum. Genet. 24:1826-1827(2016).
RN [45]
RP VARIANT LOMARS LEU-703, AND VARIANT MET-1260.
RX PubMed=26740508; DOI=10.1136/jmedgenet-2015-103568;
RA Lopes F., Barbosa M., Ameur A., Soares G., de Sa J., Dias A.I.,
RA Oliveira G., Cabral P., Temudo T., Calado E., Cruz I.F., Vieira J.P.,
RA Oliveira R., Esteves S., Sauer S., Jonasson I., Syvaenen A.C.,
RA Gyllensten U., Pinto D., Maciel P.;
RT "Identification of novel genetic causes of Rett syndrome-like phenotypes.";
RL J. Med. Genet. 53:190-199(2016).
CC -!- FUNCTION: [Huntingtin]: May play a role in microtubule-mediated
CC transport or vesicle function.
CC -!- FUNCTION: [Huntingtin, myristoylated N-terminal fragment]: Promotes the
CC formation of autophagic vesicles. {ECO:0000269|PubMed:24459296}.
CC -!- SUBUNIT: Interacts with PFN1 (PubMed:18573880). Interacts through its
CC N-terminus with PRPF40A (PubMed:9700202). Interacts with PQBP1
CC (PubMed:10332029). Interacts with SETD2 (PubMed:9700202,
CC PubMed:10958656, PubMed:11461154). Interacts with SH3GLB1 (By
CC similarity). Interacts with SYVN (PubMed:17141218). Interacts with TPR;
CC the interaction is inhibited by forms of Huntingtin with expanded
CC polyglutamine stretch (PubMed:15654337). Interacts with ZDHHC13 (via
CC ANK repeats) (PubMed:26198635). Interacts with ZDHHC17 (via ANK
CC repeats) (PubMed:26198635, PubMed:28882895, PubMed:28757145). Interacts
CC with F8A1/F8A2/F8A3 (PubMed:29466333, PubMed:16476778). Found in a
CC complex with F8A1/F8A2/F8A3, HTT and RAB5A; mediates the recruitment of
CC HTT by RAB5A (PubMed:16476778). {ECO:0000250|UniProtKB:P42859,
CC ECO:0000269|PubMed:10332029, ECO:0000269|PubMed:10958656,
CC ECO:0000269|PubMed:11461154, ECO:0000269|PubMed:15654337,
CC ECO:0000269|PubMed:16476778, ECO:0000269|PubMed:17141218,
CC ECO:0000269|PubMed:18573880, ECO:0000269|PubMed:26198635,
CC ECO:0000269|PubMed:28757145, ECO:0000269|PubMed:28882895,
CC ECO:0000269|PubMed:29466333, ECO:0000269|PubMed:9700202}.
CC -!- INTERACTION:
CC P42858; Q9H7C9: AAMDC; NbExp=3; IntAct=EBI-466029, EBI-10308705;
CC P42858; Q6PCB6: ABHD17C; NbExp=21; IntAct=EBI-466029, EBI-22011868;
CC P42858; Q9ULW3: ABT1; NbExp=9; IntAct=EBI-466029, EBI-2602396;
CC P42858; P60709: ACTB; NbExp=3; IntAct=EBI-466029, EBI-353944;
CC P42858; P63261: ACTG1; NbExp=16; IntAct=EBI-466029, EBI-351292;
CC P42858; P42025: ACTR1B; NbExp=3; IntAct=EBI-466029, EBI-367493;
CC P42858; Q15848: ADIPOQ; NbExp=9; IntAct=EBI-466029, EBI-10827839;
CC P42858; Q9Y4W6: AFG3L2; NbExp=3; IntAct=EBI-466029, EBI-358755;
CC P42858; Q53H12: AGK; NbExp=3; IntAct=EBI-466029, EBI-2269837;
CC P42858; Q53H12-2: AGK; NbExp=12; IntAct=EBI-466029, EBI-25944242;
CC P42858; Q5TGY3: AHDC1; NbExp=12; IntAct=EBI-466029, EBI-948813;
CC P42858; Q9UIJ7: AK3; NbExp=9; IntAct=EBI-466029, EBI-3916527;
CC P42858; P14550: AKR1A1; NbExp=6; IntAct=EBI-466029, EBI-372388;
CC P42858; P31749: AKT1; NbExp=3; IntAct=EBI-466029, EBI-296087;
CC P42858; Q3SY69: ALDH1L2; NbExp=3; IntAct=EBI-466029, EBI-6916128;
CC P42858; P04075-2: ALDOA; NbExp=6; IntAct=EBI-466029, EBI-10194102;
CC P42858; Q9H553: ALG2; NbExp=3; IntAct=EBI-466029, EBI-25806804;
CC P42858; Q8IWZ3-3: ANKHD1; NbExp=3; IntAct=EBI-466029, EBI-25833200;
CC P42858; Q6ZTN6-2: ANKRD13D; NbExp=9; IntAct=EBI-466029, EBI-25840993;
CC P42858; Q5TZF3-1: ANKRD45; NbExp=3; IntAct=EBI-466029, EBI-22011535;
CC P42858; Q16853: AOC3; NbExp=3; IntAct=EBI-466029, EBI-3921628;
CC P42858; P63010-2: AP2B1; NbExp=18; IntAct=EBI-466029, EBI-11529439;
CC P42858; O00203: AP3B1; NbExp=6; IntAct=EBI-466029, EBI-1044383;
CC P42858; Q9Y2T2: AP3M1; NbExp=3; IntAct=EBI-466029, EBI-2371151;
CC P42858; P05067: APP; NbExp=6; IntAct=EBI-466029, EBI-77613;
CC P42858; P48444: ARCN1; NbExp=3; IntAct=EBI-466029, EBI-1044491;
CC P42858; Q9NP61: ARFGAP3; NbExp=22; IntAct=EBI-466029, EBI-2875816;
CC P42858; P53365: ARFIP2; NbExp=3; IntAct=EBI-466029, EBI-638194;
CC P42858; Q8N264: ARHGAP24; NbExp=3; IntAct=EBI-466029, EBI-988764;
CC P42858; Q52LW3-2: ARHGAP29; NbExp=3; IntAct=EBI-466029, EBI-22012297;
CC P42858; Q0P5N6: ARL16; NbExp=18; IntAct=EBI-466029, EBI-10186132;
CC P42858; Q6P1M9: ARMCX5; NbExp=6; IntAct=EBI-466029, EBI-10252512;
CC P42858; Q86TN1: ARNT2; NbExp=9; IntAct=EBI-466029, EBI-25844820;
CC P42858; Q9Y575-3: ASB3; NbExp=6; IntAct=EBI-466029, EBI-14199987;
CC P42858; Q6XD76: ASCL4; NbExp=6; IntAct=EBI-466029, EBI-10254793;
CC P42858; Q96FT7-4: ASIC4; NbExp=3; IntAct=EBI-466029, EBI-9089489;
CC P42858; Q12797-6: ASPH; NbExp=6; IntAct=EBI-466029, EBI-12092171;
CC P42858; Q12797-7: ASPH; NbExp=3; IntAct=EBI-466029, EBI-25953099;
CC P42858; Q96DT6: ATG4C; NbExp=15; IntAct=EBI-466029, EBI-3225845;
CC P42858; Q8WXF7: ATL1; NbExp=18; IntAct=EBI-466029, EBI-2410266;
CC P42858; P25705: ATP5F1A; NbExp=3; IntAct=EBI-466029, EBI-351437;
CC P42858; P24539: ATP5PB; NbExp=3; IntAct=EBI-466029, EBI-1044810;
CC P42858; P48047: ATP5PO; NbExp=6; IntAct=EBI-466029, EBI-355815;
CC P42858; Q15904: ATP6AP1; NbExp=3; IntAct=EBI-466029, EBI-714667;
CC P42858; P61421: ATP6V0D1; NbExp=6; IntAct=EBI-466029, EBI-954063;
CC P42858; P21281: ATP6V1B2; NbExp=3; IntAct=EBI-466029, EBI-4290814;
CC P42858; Q9UI12: ATP6V1H; NbExp=3; IntAct=EBI-466029, EBI-724719;
CC P42858; Q9UQB8-3: BAIAP2; NbExp=18; IntAct=EBI-466029, EBI-9091996;
CC P42858; Q9UQB8-6: BAIAP2; NbExp=18; IntAct=EBI-466029, EBI-9092016;
CC P42858; Q16520: BATF; NbExp=12; IntAct=EBI-466029, EBI-749503;
CC P42858; Q9NRL2: BAZ1A; NbExp=4; IntAct=EBI-466029, EBI-927511;
CC P42858; Q9BUW7: BBLN; NbExp=6; IntAct=EBI-466029, EBI-752084;
CC P42858; Q8WY36-3: BBX; NbExp=6; IntAct=EBI-466029, EBI-22013474;
CC P42858; P51572: BCAP31; NbExp=4; IntAct=EBI-466029, EBI-77683;
CC P42858; Q14457: BECN1; NbExp=14; IntAct=EBI-466029, EBI-949378;
CC P42858; Q00994: BEX3; NbExp=6; IntAct=EBI-466029, EBI-741753;
CC P42858; O15392: BIRC5; NbExp=15; IntAct=EBI-466029, EBI-518823;
CC P42858; Q9GZL8: BPESC1; NbExp=15; IntAct=EBI-466029, EBI-25861458;
CC P42858; P38398-6: BRCA1; NbExp=3; IntAct=EBI-466029, EBI-25833510;
CC P42858; Q8WUW1: BRK1; NbExp=6; IntAct=EBI-466029, EBI-2837444;
CC P42858; Q13901: C1D; NbExp=6; IntAct=EBI-466029, EBI-3844053;
CC P42858; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-466029, EBI-946029;
CC P42858; Q9BXJ4: C1QTNF3; NbExp=3; IntAct=EBI-466029, EBI-10697546;
CC P42858; Q9NUB4: C20orf141; NbExp=6; IntAct=EBI-466029, EBI-9088162;
CC P42858; Q6P5X5-2: C22orf39; NbExp=3; IntAct=EBI-466029, EBI-10692329;
CC P42858; Q9BRJ6: C7orf50; NbExp=6; IntAct=EBI-466029, EBI-751612;
CC P42858; Q8IVU9: CABCOCO1; NbExp=3; IntAct=EBI-466029, EBI-21771960;
CC P42858; P62158: CALM3; NbExp=10; IntAct=EBI-466029, EBI-397435;
CC P42858; Q14012: CAMK1; NbExp=3; IntAct=EBI-466029, EBI-6380130;
CC P42858; Q8N5S9-2: CAMKK1; NbExp=9; IntAct=EBI-466029, EBI-25850646;
CC P42858; Q9HC96: CAPN10; NbExp=12; IntAct=EBI-466029, EBI-3915761;
CC P42858; P29466-3: CASP1; NbExp=3; IntAct=EBI-466029, EBI-12248206;
CC P42858; P42574: CASP3; NbExp=9; IntAct=EBI-466029, EBI-524064;
CC P42858; P55212: CASP6; NbExp=15; IntAct=EBI-466029, EBI-718729;
CC P42858; P55210: CASP7; NbExp=12; IntAct=EBI-466029, EBI-523958;
CC P42858; P22681: CBL; NbExp=18; IntAct=EBI-466029, EBI-518228;
CC P42858; P35520: CBS; NbExp=12; IntAct=EBI-466029, EBI-740135;
CC P42858; P83916: CBX1; NbExp=15; IntAct=EBI-466029, EBI-78129;
CC P42858; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-466029, EBI-744556;
CC P42858; Q96M83-3: CCDC7; NbExp=18; IntAct=EBI-466029, EBI-18211613;
CC P42858; Q9Y3X0: CCDC9; NbExp=3; IntAct=EBI-466029, EBI-2557532;
CC P42858; Q13939: CCIN; NbExp=3; IntAct=EBI-466029, EBI-25879469;
CC P42858; Q9NPC3: CCNB1IP1; NbExp=6; IntAct=EBI-466029, EBI-745269;
CC P42858; P24863: CCNC; NbExp=9; IntAct=EBI-466029, EBI-395261;
CC P42858; O96020: CCNE2; NbExp=6; IntAct=EBI-466029, EBI-375033;
CC P42858; P51959: CCNG1; NbExp=3; IntAct=EBI-466029, EBI-3905829;
CC P42858; P78371: CCT2; NbExp=6; IntAct=EBI-466029, EBI-357407;
CC P42858; P48643: CCT5; NbExp=3; IntAct=EBI-466029, EBI-355710;
CC P42858; P40227: CCT6A; NbExp=10; IntAct=EBI-466029, EBI-356687;
CC P42858; P50990: CCT8; NbExp=4; IntAct=EBI-466029, EBI-356507;
CC P42858; P13987: CD59; NbExp=10; IntAct=EBI-466029, EBI-297972;
CC P42858; Q9H3Q1: CDC42EP4; NbExp=3; IntAct=EBI-466029, EBI-744665;
CC P42858; Q99459: CDC5L; NbExp=3; IntAct=EBI-466029, EBI-374880;
CC P42858; O00311: CDC7; NbExp=3; IntAct=EBI-466029, EBI-374980;
CC P42858; Q9BWT1: CDCA7; NbExp=3; IntAct=EBI-466029, EBI-7054803;
CC P42858; P55290: CDH13; NbExp=6; IntAct=EBI-466029, EBI-7205595;
CC P42858; O95674: CDS2; NbExp=9; IntAct=EBI-466029, EBI-3913685;
CC P42858; Q8N2Z9: CENPS; NbExp=3; IntAct=EBI-466029, EBI-5529649;
CC P42858; Q7Z7K6: CENPV; NbExp=15; IntAct=EBI-466029, EBI-1210604;
CC P42858; Q9P2H0: CEP126; NbExp=2; IntAct=EBI-466029, EBI-473176;
CC P42858; Q53EZ4: CEP55; NbExp=9; IntAct=EBI-466029, EBI-747776;
CC P42858; Q96MT8-3: CEP63; NbExp=12; IntAct=EBI-466029, EBI-11522539;
CC P42858; Q8NHQ1-3: CEP70; NbExp=6; IntAct=EBI-466029, EBI-11526150;
CC P42858; P41208: CETN2; NbExp=13; IntAct=EBI-466029, EBI-1789926;
CC P42858; Q9Y6H1: CHCHD2; NbExp=10; IntAct=EBI-466029, EBI-2321769;
CC P42858; Q9NX63: CHCHD3; NbExp=6; IntAct=EBI-466029, EBI-743375;
CC P42858; Q12873: CHD3; NbExp=3; IntAct=EBI-466029, EBI-523590;
CC P42858; Q9HD42: CHMP1A; NbExp=12; IntAct=EBI-466029, EBI-1057156;
CC P42858; O43633: CHMP2A; NbExp=3; IntAct=EBI-466029, EBI-2692789;
CC P42858; Q9H444: CHMP4B; NbExp=7; IntAct=EBI-466029, EBI-749627;
CC P42858; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-466029, EBI-7062247;
CC P42858; P06732: CKM; NbExp=3; IntAct=EBI-466029, EBI-4287089;
CC P42858; Q9Y240: CLEC11A; NbExp=12; IntAct=EBI-466029, EBI-3957044;
CC P42858; Q92478: CLEC2B; NbExp=9; IntAct=EBI-466029, EBI-13350535;
CC P42858; Q16740: CLPP; NbExp=6; IntAct=EBI-466029, EBI-1056029;
CC P42858; Q8NCR9: CLRN3; NbExp=9; IntAct=EBI-466029, EBI-9091272;
CC P42858; Q9H9A5: CNOT10; NbExp=4; IntAct=EBI-466029, EBI-1054261;
CC P42858; Q9H9A5-3: CNOT10; NbExp=3; IntAct=EBI-466029, EBI-25957177;
CC P42858; Q9UIV1: CNOT7; NbExp=13; IntAct=EBI-466029, EBI-2105113;
CC P42858; P09543: CNP; NbExp=10; IntAct=EBI-466029, EBI-1059219;
CC P42858; Q96MW5: COG8; NbExp=12; IntAct=EBI-466029, EBI-720875;
CC P42858; P53618: COPB1; NbExp=6; IntAct=EBI-466029, EBI-359063;
CC P42858; Q9UNS2: COPS3; NbExp=22; IntAct=EBI-466029, EBI-350590;
CC P42858; Q86WV2: COX4I1; NbExp=3; IntAct=EBI-466029, EBI-10260134;
CC P42858; P10606: COX5B; NbExp=7; IntAct=EBI-466029, EBI-1053725;
CC P42858; P12074: COX6A1; NbExp=4; IntAct=EBI-466029, EBI-2115950;
CC P42858; P09669: COX6C; NbExp=4; IntAct=EBI-466029, EBI-715040;
CC P42858; Q9UKF6: CPSF3; NbExp=3; IntAct=EBI-466029, EBI-1044699;
CC P42858; A2RRE8: CPT1B; NbExp=6; IntAct=EBI-466029, EBI-25865477;
CC P42858; Q9BSW2: CRACR2A; NbExp=9; IntAct=EBI-466029, EBI-739773;
CC P42858; P16220: CREB1; NbExp=3; IntAct=EBI-466029, EBI-711855;
CC P42858; Q92793: CREBBP; NbExp=2; IntAct=EBI-466029, EBI-81215;
CC P42858; Q6UXH1-2: CRELD2; NbExp=6; IntAct=EBI-466029, EBI-21670927;
CC P42858; P46108: CRK; NbExp=3; IntAct=EBI-466029, EBI-886;
CC P42858; Q14194: CRMP1; NbExp=14; IntAct=EBI-466029, EBI-473101;
CC P42858; P02489: CRYAA; NbExp=3; IntAct=EBI-466029, EBI-6875961;
CC P42858; P53672: CRYBA2; NbExp=3; IntAct=EBI-466029, EBI-750444;
CC P42858; P04141: CSF2; NbExp=15; IntAct=EBI-466029, EBI-1809826;
CC P42858; P48730-2: CSNK1D; NbExp=15; IntAct=EBI-466029, EBI-9087876;
CC P42858; P50461: CSRP3; NbExp=3; IntAct=EBI-466029, EBI-5658719;
CC P42858; Q9H6J7-2: CSTPP1; NbExp=6; IntAct=EBI-466029, EBI-13328871;
CC P42858; P56545-3: CTBP2; NbExp=3; IntAct=EBI-466029, EBI-10171902;
CC P42858; P35222: CTNNB1; NbExp=14; IntAct=EBI-466029, EBI-491549;
CC P42858; Q13618: CUL3; NbExp=3; IntAct=EBI-466029, EBI-456129;
CC P42858; Q93034: CUL5; NbExp=10; IntAct=EBI-466029, EBI-1057139;
CC P42858; Q8TB03: CXorf38; NbExp=15; IntAct=EBI-466029, EBI-12024320;
CC P42858; P08574: CYC1; NbExp=7; IntAct=EBI-466029, EBI-1224514;
CC P42858; P20815: CYP3A5; NbExp=3; IntAct=EBI-466029, EBI-3908011;
CC P42858; Q5D0E6-2: DALRD3; NbExp=9; IntAct=EBI-466029, EBI-9090939;
CC P42858; Q9UN19: DAPP1; NbExp=9; IntAct=EBI-466029, EBI-3918199;
CC P42858; Q9UER7: DAXX; NbExp=15; IntAct=EBI-466029, EBI-77321;
CC P42858; Q15038: DAZAP2; NbExp=3; IntAct=EBI-466029, EBI-724310;
CC P42858; Q9UJU6: DBNL; NbExp=3; IntAct=EBI-466029, EBI-751783;
CC P42858; P61962: DCAF7; NbExp=10; IntAct=EBI-466029, EBI-359808;
CC P42858; Q9H816: DCLRE1B; NbExp=9; IntAct=EBI-466029, EBI-3508943;
CC P42858; Q13561: DCTN2; NbExp=12; IntAct=EBI-466029, EBI-715074;
CC P42858; Q9UJW0: DCTN4; NbExp=3; IntAct=EBI-466029, EBI-2134033;
CC P42858; Q9UHI6: DDX20; NbExp=6; IntAct=EBI-466029, EBI-347658;
CC P42858; Q9NR30: DDX21; NbExp=3; IntAct=EBI-466029, EBI-357942;
CC P42858; O00148: DDX39A; NbExp=3; IntAct=EBI-466029, EBI-348253;
CC P42858; Q9UJV9: DDX41; NbExp=6; IntAct=EBI-466029, EBI-1046350;
CC P42858; Q14154: DELE1; NbExp=18; IntAct=EBI-466029, EBI-2805660;
CC P42858; P78524: DENND2B; NbExp=3; IntAct=EBI-466029, EBI-962633;
CC P42858; P17661: DES; NbExp=9; IntAct=EBI-466029, EBI-1055572;
CC P42858; Q05D60: DEUP1; NbExp=15; IntAct=EBI-466029, EBI-748597;
CC P42858; Q5T7M9-2: DIPK1A; NbExp=3; IntAct=EBI-466029, EBI-25960650;
CC P42858; P09622: DLD; NbExp=3; IntAct=EBI-466029, EBI-353366;
CC P42858; P36957: DLST; NbExp=3; IntAct=EBI-466029, EBI-351007;
CC P42858; O60479: DLX3; NbExp=3; IntAct=EBI-466029, EBI-3908248;
CC P42858; P31689: DNAJA1; NbExp=17; IntAct=EBI-466029, EBI-347834;
CC P42858; Q96EY1: DNAJA3; NbExp=5; IntAct=EBI-466029, EBI-356767;
CC P42858; Q9UDY4: DNAJB4; NbExp=3; IntAct=EBI-466029, EBI-356960;
CC P42858; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-466029, EBI-12593112;
CC P42858; Q9NVH1: DNAJC11; NbExp=3; IntAct=EBI-466029, EBI-1055336;
CC P42858; Q5F1R6: DNAJC21; NbExp=6; IntAct=EBI-466029, EBI-2654581;
CC P42858; Q9NNZ3: DNAJC4; NbExp=12; IntAct=EBI-466029, EBI-4397791;
CC P42858; O14645: DNALI1; NbExp=15; IntAct=EBI-466029, EBI-395638;
CC P42858; Q05193: DNM1; NbExp=3; IntAct=EBI-466029, EBI-713135;
CC P42858; P50570-2: DNM2; NbExp=6; IntAct=EBI-466029, EBI-10968534;
CC P42858; Q9H147: DNTTIP1; NbExp=15; IntAct=EBI-466029, EBI-2795449;
CC P42858; Q9H3H5: DPAGT1; NbExp=3; IntAct=EBI-466029, EBI-3922860;
CC P42858; Q16555: DPYSL2; NbExp=3; IntAct=EBI-466029, EBI-1104711;
CC P42858; Q9BPU6: DPYSL5; NbExp=9; IntAct=EBI-466029, EBI-724653;
CC P42858; Q14204: DYNC1H1; NbExp=8; IntAct=EBI-466029, EBI-356015;
CC P42858; P63167: DYNLL1; NbExp=10; IntAct=EBI-466029, EBI-349105;
CC P42858; A0AVK6: E2F8; NbExp=12; IntAct=EBI-466029, EBI-7779316;
CC P42858; Q13011: ECH1; NbExp=2; IntAct=EBI-466029, EBI-711968;
CC P42858; O60869: EDF1; NbExp=6; IntAct=EBI-466029, EBI-781301;
CC P42858; Q3B7T1: EDRF1; NbExp=18; IntAct=EBI-466029, EBI-2870947;
CC P42858; Q05639: EEF1A2; NbExp=3; IntAct=EBI-466029, EBI-354943;
CC P42858; P24534: EEF1B2; NbExp=7; IntAct=EBI-466029, EBI-354334;
CC P42858; P29692: EEF1D; NbExp=6; IntAct=EBI-466029, EBI-358607;
CC P42858; P13639: EEF2; NbExp=3; IntAct=EBI-466029, EBI-352560;
CC P42858; Q12805: EFEMP1; NbExp=3; IntAct=EBI-466029, EBI-536772;
CC P42858; O14602: EIF1AY; NbExp=6; IntAct=EBI-466029, EBI-286439;
CC P42858; P20042: EIF2S2; NbExp=12; IntAct=EBI-466029, EBI-711977;
CC P42858; P41091: EIF2S3; NbExp=3; IntAct=EBI-466029, EBI-1054228;
CC P42858; O75821: EIF3G; NbExp=4; IntAct=EBI-466029, EBI-366632;
CC P42858; Q13347: EIF3I; NbExp=13; IntAct=EBI-466029, EBI-354047;
CC P42858; Q14240-2: EIF4A2; NbExp=3; IntAct=EBI-466029, EBI-10232522;
CC P42858; O60573: EIF4E2; NbExp=4; IntAct=EBI-466029, EBI-398610;
CC P42858; P55010: EIF5; NbExp=3; IntAct=EBI-466029, EBI-286450;
CC P42858; O95163: ELP1; NbExp=4; IntAct=EBI-466029, EBI-347559;
CC P42858; Q9Y6C2-2: EMILIN1; NbExp=3; IntAct=EBI-466029, EBI-11748557;
CC P42858; Q8TC29: ENKUR; NbExp=6; IntAct=EBI-466029, EBI-9246952;
CC P42858; P06733: ENO1; NbExp=13; IntAct=EBI-466029, EBI-353877;
CC P42858; Q9Y5L3: ENTPD2; NbExp=3; IntAct=EBI-466029, EBI-3913907;
CC P42858; O75356: ENTPD5; NbExp=3; IntAct=EBI-466029, EBI-7416931;
CC P42858; A0A0C4DH22: EPB41L1; NbExp=6; IntAct=EBI-466029, EBI-25865535;
CC P42858; Q8TE68-3: EPS8L1; NbExp=3; IntAct=EBI-466029, EBI-21574901;
CC P42858; Q2NKX8: ERCC6L; NbExp=20; IntAct=EBI-466029, EBI-1042535;
CC P42858; A1L162: ERICH2; NbExp=3; IntAct=EBI-466029, EBI-2682520;
CC P42858; Q96DN0: ERP27; NbExp=3; IntAct=EBI-466029, EBI-953772;
CC P42858; Q6NXG1-3: ESRP1; NbExp=6; IntAct=EBI-466029, EBI-21567429;
CC P42858; Q9UI08-2: EVL; NbExp=20; IntAct=EBI-466029, EBI-6448852;
CC P42858; Q01844-4: EWSR1; NbExp=3; IntAct=EBI-466029, EBI-25896785;
CC P42858; O00471: EXOC5; NbExp=3; IntAct=EBI-466029, EBI-949824;
CC P42858; Q99504: EYA3; NbExp=6; IntAct=EBI-466029, EBI-9089567;
CC P42858; P15311: EZR; NbExp=4; IntAct=EBI-466029, EBI-1056902;
CC P42858; P23610: F8A3; NbExp=3; IntAct=EBI-466029, EBI-5663973;
CC P42858; Q6SJ93: FAM111B; NbExp=12; IntAct=EBI-466029, EBI-6309082;
CC P42858; Q96GL9: FAM163A; NbExp=12; IntAct=EBI-466029, EBI-11793142;
CC P42858; Q96KS9: FAM167A; NbExp=6; IntAct=EBI-466029, EBI-10290462;
CC P42858; Q5HYJ3-3: FAM76B; NbExp=6; IntAct=EBI-466029, EBI-11956087;
CC P42858; Q5JUQ0: FAM78A; NbExp=3; IntAct=EBI-466029, EBI-21900888;
CC P42858; Q8IZU1: FAM9A; NbExp=18; IntAct=EBI-466029, EBI-8468186;
CC P42858; Q9NPI8: FANCF; NbExp=3; IntAct=EBI-466029, EBI-81589;
CC P42858; Q8TC84: FANK1; NbExp=3; IntAct=EBI-466029, EBI-21975404;
CC P42858; Q9NSD9: FARSB; NbExp=3; IntAct=EBI-466029, EBI-353803;
CC P42858; P49327: FASN; NbExp=13; IntAct=EBI-466029, EBI-356658;
CC P42858; Q53R41: FASTKD1; NbExp=9; IntAct=EBI-466029, EBI-3957005;
CC P42858; Q8NFZ0: FBH1; NbExp=6; IntAct=EBI-466029, EBI-724767;
CC P42858; P09467: FBP1; NbExp=3; IntAct=EBI-466029, EBI-712740;
CC P42858; Q99689: FEZ1; NbExp=6; IntAct=EBI-466029, EBI-396435;
CC P42858; Q9UHY8: FEZ2; NbExp=18; IntAct=EBI-466029, EBI-396453;
CC P42858; Q13643: FHL3; NbExp=9; IntAct=EBI-466029, EBI-741101;
CC P42858; Q9BVA6: FICD; NbExp=3; IntAct=EBI-466029, EBI-3907198;
CC P42858; P26885: FKBP2; NbExp=6; IntAct=EBI-466029, EBI-719873;
CC P42858; O75955: FLOT1; NbExp=4; IntAct=EBI-466029, EBI-603643;
CC P42858; Q8N3X1: FNBP4; NbExp=6; IntAct=EBI-466029, EBI-310600;
CC P42858; Q3SYB3: FOXD4L6; NbExp=6; IntAct=EBI-466029, EBI-6425864;
CC P42858; Q6PIV2: FOXR1; NbExp=12; IntAct=EBI-466029, EBI-10253815;
CC P42858; O95073-2: FSBP; NbExp=3; IntAct=EBI-466029, EBI-10696047;
CC P42858; P02792: FTL; NbExp=20; IntAct=EBI-466029, EBI-713279;
CC P42858; P06241-3: FYN; NbExp=12; IntAct=EBI-466029, EBI-10691738;
CC P42858; Q9ULV1: FZD4; NbExp=9; IntAct=EBI-466029, EBI-2466380;
CC P42858; Q7L622: G2E3; NbExp=6; IntAct=EBI-466029, EBI-751757;
CC P42858; Q13283: G3BP1; NbExp=16; IntAct=EBI-466029, EBI-1047359;
CC P42858; Q9UQC2: GAB2; NbExp=3; IntAct=EBI-466029, EBI-975200;
CC P42858; Q8N4A0: GALNT4; NbExp=12; IntAct=EBI-466029, EBI-21555925;
CC P42858; P04406: GAPDH; NbExp=7; IntAct=EBI-466029, EBI-354056;
CC P42858; P28676: GCA; NbExp=3; IntAct=EBI-466029, EBI-947242;
CC P42858; P14136: GFAP; NbExp=10; IntAct=EBI-466029, EBI-744302;
CC P42858; Q9NXC2: GFOD1; NbExp=9; IntAct=EBI-466029, EBI-8799578;
CC P42858; Q9UG22: GIMAP2; NbExp=6; IntAct=EBI-466029, EBI-15891037;
CC P42858; Q9Y2X7: GIT1; NbExp=10; IntAct=EBI-466029, EBI-466061;
CC P42858; P48060: GLIPR1; NbExp=3; IntAct=EBI-466029, EBI-2833130;
CC P42858; P09471: GNAO1; NbExp=7; IntAct=EBI-466029, EBI-715087;
CC P42858; P62873: GNB1; NbExp=10; IntAct=EBI-466029, EBI-357130;
CC P42858; P62879: GNB2; NbExp=10; IntAct=EBI-466029, EBI-356942;
CC P42858; Q08379: GOLGA2; NbExp=3; IntAct=EBI-466029, EBI-618309;
CC P42858; Q9H4A5: GOLPH3L; NbExp=20; IntAct=EBI-466029, EBI-4403434;
CC P42858; Q8IYG2: GPC3; NbExp=3; IntAct=EBI-466029, EBI-25896879;
CC P42858; Q8IV16: GPIHBP1; NbExp=3; IntAct=EBI-466029, EBI-9080234;
CC P42858; P51674: GPM6A; NbExp=4; IntAct=EBI-466029, EBI-7187133;
CC P42858; Q86YB0: GPM6A; NbExp=3; IntAct=EBI-466029, EBI-25966592;
CC P42858; Q7Z602: GPR141; NbExp=3; IntAct=EBI-466029, EBI-21649723;
CC P42858; Q96D09: GPRASP2; NbExp=5; IntAct=EBI-466029, EBI-473189;
CC P42858; Q96SL4: GPX7; NbExp=3; IntAct=EBI-466029, EBI-749411;
CC P42858; Q13588: GRAP; NbExp=12; IntAct=EBI-466029, EBI-2847510;
CC P42858; Q8IY40: GRIK2; NbExp=9; IntAct=EBI-466029, EBI-25832107;
CC P42858; P49840: GSK3A; NbExp=6; IntAct=EBI-466029, EBI-1044067;
CC P42858; Q9Y5Q9: GTF3C3; NbExp=12; IntAct=EBI-466029, EBI-1054873;
CC P42858; Q9BZE4: GTPBP4; NbExp=3; IntAct=EBI-466029, EBI-1056249;
CC P42858; O75409: H2AP; NbExp=16; IntAct=EBI-466029, EBI-6447217;
CC P42858; Q93079: H2BC9; NbExp=18; IntAct=EBI-466029, EBI-352469;
CC P42858; Q6NXT2: H3-5; NbExp=15; IntAct=EBI-466029, EBI-2868501;
CC P42858; P68431: H3C12; NbExp=20; IntAct=EBI-466029, EBI-79722;
CC P42858; Q71DI3: H3C15; NbExp=18; IntAct=EBI-466029, EBI-750650;
CC P42858; P62805: H4C9; NbExp=3; IntAct=EBI-466029, EBI-302023;
CC P42858; P40939: HADHA; NbExp=3; IntAct=EBI-466029, EBI-356720;
CC P42858; P54257-2: HAP1; NbExp=8; IntAct=EBI-466029, EBI-9392340;
CC P42858; Q99871: HAUS7; NbExp=18; IntAct=EBI-466029, EBI-395719;
CC P42858; O00165: HAX1; NbExp=14; IntAct=EBI-466029, EBI-357001;
CC P42858; Q8N779: hCG_1998195; NbExp=15; IntAct=EBI-466029, EBI-10267476;
CC P42858; Q969S8: HDAC10; NbExp=21; IntAct=EBI-466029, EBI-301762;
CC P42858; Q9UBN7: HDAC6; NbExp=9; IntAct=EBI-466029, EBI-301697;
CC P42858; Q9HCC6: HES4; NbExp=12; IntAct=EBI-466029, EBI-2680288;
CC P42858; Q9UBP5: HEY2; NbExp=2; IntAct=EBI-466029, EBI-750630;
CC P42858; O00291: HIP1; NbExp=7; IntAct=EBI-466029, EBI-473886;
CC P42858; Q9BW71: HIRIP3; NbExp=6; IntAct=EBI-466029, EBI-723624;
CC P42858; P52790: HK3; NbExp=3; IntAct=EBI-466029, EBI-2965780;
CC P42858; P08397: HMBS; NbExp=3; IntAct=EBI-466029, EBI-9090148;
CC P42858; Q9NP66: HMG20A; NbExp=2; IntAct=EBI-466029, EBI-740641;
CC P42858; Q9P0W2: HMG20B; NbExp=3; IntAct=EBI-466029, EBI-713401;
CC P42858; P09429: HMGB1; NbExp=13; IntAct=EBI-466029, EBI-389432;
CC P42858; P07910: HNRNPC; NbExp=7; IntAct=EBI-466029, EBI-357966;
CC P42858; P07910-2: HNRNPC; NbExp=9; IntAct=EBI-466029, EBI-5280084;
CC P42858; P61978: HNRNPK; NbExp=12; IntAct=EBI-466029, EBI-304185;
CC P42858; P20719: HOXA5; NbExp=9; IntAct=EBI-466029, EBI-8470697;
CC P42858; O43248: HOXC11; NbExp=7; IntAct=EBI-466029, EBI-2652631;
CC P42858; P09017: HOXC4; NbExp=16; IntAct=EBI-466029, EBI-3923226;
CC P42858; P00492: HPRT1; NbExp=15; IntAct=EBI-466029, EBI-748210;
CC P42858; P0DMV8: HSPA1A; NbExp=9; IntAct=EBI-466029, EBI-11052499;
CC P42858; P54652: HSPA2; NbExp=3; IntAct=EBI-466029, EBI-356991;
CC P42858; P11142: HSPA8; NbExp=14; IntAct=EBI-466029, EBI-351896;
CC P42858; P42858: HTT; NbExp=11; IntAct=EBI-466029, EBI-466029;
CC P42858; Q12891: HYAL2; NbExp=9; IntAct=EBI-466029, EBI-2806068;
CC P42858; Q9NX55: HYPK; NbExp=4; IntAct=EBI-466029, EBI-1048743;
CC P42858; Q02363: ID2; NbExp=6; IntAct=EBI-466029, EBI-713450;
CC P42858; Q8IY31-2: IFT20; NbExp=6; IntAct=EBI-466029, EBI-11742277;
CC P42858; Q8IY31-3: IFT20; NbExp=18; IntAct=EBI-466029, EBI-9091197;
CC P42858; Q9NWB7: IFT57; NbExp=3; IntAct=EBI-466029, EBI-725672;
CC P42858; P22692: IGFBP4; NbExp=6; IntAct=EBI-466029, EBI-2831948;
CC P42858; Q14005-2: IL16; NbExp=15; IntAct=EBI-466029, EBI-17178971;
CC P42858; Q16891: IMMT; NbExp=7; IntAct=EBI-466029, EBI-473801;
CC P42858; P29218-3: IMPA1; NbExp=6; IntAct=EBI-466029, EBI-12330251;
CC P42858; Q9UNL4: ING4; NbExp=3; IntAct=EBI-466029, EBI-2866661;
CC P42858; Q8WYH8-2: ING5; NbExp=18; IntAct=EBI-466029, EBI-21602071;
CC P42858; Q8NBZ0: INO80E; NbExp=3; IntAct=EBI-466029, EBI-769401;
CC P42858; Q8TEX9: IPO4; NbExp=7; IntAct=EBI-466029, EBI-395967;
CC P42858; O00410-3: IPO5; NbExp=3; IntAct=EBI-466029, EBI-9641587;
CC P42858; Q6DN90-2: IQSEC1; NbExp=18; IntAct=EBI-466029, EBI-21911304;
CC P42858; Q96N16: JAKMIP1; NbExp=10; IntAct=EBI-466029, EBI-2680803;
CC P42858; Q92993: KAT5; NbExp=15; IntAct=EBI-466029, EBI-399080;
CC P42858; Q13303: KCNAB2; NbExp=3; IntAct=EBI-466029, EBI-948729;
CC P42858; Q9Y691: KCNMB2; NbExp=3; IntAct=EBI-466029, EBI-7932244;
CC P42858; Q96SI1-2: KCTD15; NbExp=6; IntAct=EBI-466029, EBI-12382297;
CC P42858; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-466029, EBI-743960;
CC P42858; A0A384DVV8: KIAA0040; NbExp=3; IntAct=EBI-466029, EBI-20764875;
CC P42858; Q6ZU52: KIAA0408; NbExp=6; IntAct=EBI-466029, EBI-739493;
CC P42858; Q5T5P2-6: KIAA1217; NbExp=3; IntAct=EBI-466029, EBI-10188326;
CC P42858; O14901: KLF11; NbExp=7; IntAct=EBI-466029, EBI-948266;
CC P42858; Q9Y4X4: KLF12; NbExp=3; IntAct=EBI-466029, EBI-750750;
CC P42858; P57682: KLF3; NbExp=6; IntAct=EBI-466029, EBI-8472267;
CC P42858; Q53G59: KLHL12; NbExp=3; IntAct=EBI-466029, EBI-740929;
CC P42858; Q9Y2M5: KLHL20; NbExp=9; IntAct=EBI-466029, EBI-714379;
CC P42858; O60259: KLK8; NbExp=3; IntAct=EBI-466029, EBI-3915857;
CC P42858; O15229-2: KMO; NbExp=3; IntAct=EBI-466029, EBI-21870540;
CC P42858; Q9Y448: KNSTRN; NbExp=3; IntAct=EBI-466029, EBI-373334;
CC P42858; O00505: KPNA3; NbExp=11; IntAct=EBI-466029, EBI-358297;
CC P42858; P05783: KRT18; NbExp=6; IntAct=EBI-466029, EBI-297888;
CC P42858; P08727: KRT19; NbExp=6; IntAct=EBI-466029, EBI-742756;
CC P42858; P35900: KRT20; NbExp=9; IntAct=EBI-466029, EBI-742094;
CC P42858; Q14525: KRT33B; NbExp=12; IntAct=EBI-466029, EBI-1049638;
CC P42858; P60409: KRTAP10-7; NbExp=9; IntAct=EBI-466029, EBI-10172290;
CC P42858; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-466029, EBI-1052037;
CC P42858; Q8IUC2: KRTAP8-1; NbExp=6; IntAct=EBI-466029, EBI-10261141;
CC P42858; Q9BYQ4: KRTAP9-2; NbExp=9; IntAct=EBI-466029, EBI-1044640;
CC P42858; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-466029, EBI-11985629;
CC P42858; O43813: LANCL1; NbExp=10; IntAct=EBI-466029, EBI-3046631;
CC P42858; Q92615: LARP4B; NbExp=3; IntAct=EBI-466029, EBI-1052558;
CC P42858; O95447: LCA5L; NbExp=18; IntAct=EBI-466029, EBI-8473670;
CC P42858; Q5T7P3: LCE1B; NbExp=15; IntAct=EBI-466029, EBI-10245913;
CC P42858; Q86U70-2: LDB1; NbExp=3; IntAct=EBI-466029, EBI-11979761;
CC P42858; Q9BYZ2: LDHAL6B; NbExp=18; IntAct=EBI-466029, EBI-1108377;
CC P42858; P07195: LDHB; NbExp=9; IntAct=EBI-466029, EBI-358748;
CC P42858; O95751: LDOC1; NbExp=5; IntAct=EBI-466029, EBI-740738;
CC P42858; Q8TCE9: LGALS14; NbExp=3; IntAct=EBI-466029, EBI-10274069;
CC P42858; Q9H2C1: LHX5; NbExp=15; IntAct=EBI-466029, EBI-25835523;
CC P42858; Q9UPM6: LHX6; NbExp=12; IntAct=EBI-466029, EBI-10258746;
CC P42858; Q68G74: LHX8; NbExp=12; IntAct=EBI-466029, EBI-8474075;
CC P42858; Q9H9Z2: LIN28A; NbExp=18; IntAct=EBI-466029, EBI-2462365;
CC P42858; Q8N0U6: LINC00518; NbExp=6; IntAct=EBI-466029, EBI-10264791;
CC P42858; Q9H0V9: LMAN2L; NbExp=3; IntAct=EBI-466029, EBI-9091707;
CC P42858; Q8TBB1: LNX1; NbExp=6; IntAct=EBI-466029, EBI-739832;
CC P42858; Q8N448: LNX2; NbExp=3; IntAct=EBI-466029, EBI-2340947;
CC P42858; A2RU56: LOC401296; NbExp=9; IntAct=EBI-466029, EBI-9088215;
CC P42858; Q1L5Z9: LONRF2; NbExp=3; IntAct=EBI-466029, EBI-2510853;
CC P42858; Q14693: LPIN1; NbExp=12; IntAct=EBI-466029, EBI-5278370;
CC P42858; Q96CN5: LRRC45; NbExp=3; IntAct=EBI-466029, EBI-2805176;
CC P42858; Q32MZ4: LRRFIP1; NbExp=3; IntAct=EBI-466029, EBI-1369100;
CC P42858; O95777: LSM8; NbExp=15; IntAct=EBI-466029, EBI-347779;
CC P42858; Q9Y383: LUC7L2; NbExp=9; IntAct=EBI-466029, EBI-352851;
CC P42858; Q8N1E2: LYG1; NbExp=3; IntAct=EBI-466029, EBI-13309213;
CC P42858; Q9H063: MAF1; NbExp=3; IntAct=EBI-466029, EBI-720354;
CC P42858; P43357: MAGEA3; NbExp=6; IntAct=EBI-466029, EBI-5651459;
CC P42858; Q96M61: MAGEB18; NbExp=16; IntAct=EBI-466029, EBI-741835;
CC P42858; Q8N7X4: MAGEB6; NbExp=2; IntAct=EBI-466029, EBI-6447163;
CC P42858; Q96EH3: MALSU1; NbExp=6; IntAct=EBI-466029, EBI-2339737;
CC P42858; Q99683: MAP3K5; NbExp=6; IntAct=EBI-466029, EBI-476263;
CC P42858; Q00266: MAT1A; NbExp=3; IntAct=EBI-466029, EBI-967087;
CC P42858; P43243: MATR3; NbExp=4; IntAct=EBI-466029, EBI-352602;
CC P42858; P56270-2: MAZ; NbExp=3; IntAct=EBI-466029, EBI-12068586;
CC P42858; Q9UIS9: MBD1; NbExp=2; IntAct=EBI-466029, EBI-867196;
CC P42858; O95243-2: MBD4; NbExp=19; IntAct=EBI-466029, EBI-6448717;
CC P42858; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-466029, EBI-348259;
CC P42858; Q9HAF1: MEAF6; NbExp=6; IntAct=EBI-466029, EBI-399266;
CC P42858; P51608: MECP2; NbExp=18; IntAct=EBI-466029, EBI-1189067;
CC P42858; Q96RN5: MED15; NbExp=3; IntAct=EBI-466029, EBI-394506;
CC P42858; Q96RN5-2: MED15; NbExp=6; IntAct=EBI-466029, EBI-11030807;
CC P42858; Q15528-2: MED22; NbExp=12; IntAct=EBI-466029, EBI-12954271;
CC P42858; Q9H204: MED28; NbExp=9; IntAct=EBI-466029, EBI-514199;
CC P42858; Q96HR3: MED30; NbExp=3; IntAct=EBI-466029, EBI-394659;
CC P42858; Q9Y3C7: MED31; NbExp=9; IntAct=EBI-466029, EBI-394707;
CC P42858; P50221: MEOX1; NbExp=19; IntAct=EBI-466029, EBI-2864512;
CC P42858; Q8N6F8: METTL27; NbExp=9; IntAct=EBI-466029, EBI-8487781;
CC P42858; Q8TDB4: MGARP; NbExp=21; IntAct=EBI-466029, EBI-4397720;
CC P42858; O94851: MICAL2; NbExp=3; IntAct=EBI-466029, EBI-2804835;
CC P42858; A4FUJ8: MKL1; NbExp=15; IntAct=EBI-466029, EBI-21250407;
CC P42858; Q9BUB5: MKNK1; NbExp=18; IntAct=EBI-466029, EBI-73837;
CC P42858; Q9H000: MKRN2; NbExp=12; IntAct=EBI-466029, EBI-2341005;
CC P42858; P22033: MMUT; NbExp=12; IntAct=EBI-466029, EBI-2690467;
CC P42858; P51948: MNAT1; NbExp=9; IntAct=EBI-466029, EBI-716139;
CC P42858; P41218: MNDA; NbExp=18; IntAct=EBI-466029, EBI-2829677;
CC P42858; Q16653-13: MOG; NbExp=12; IntAct=EBI-466029, EBI-24226707;
CC P42858; Q15014: MORF4L2; NbExp=12; IntAct=EBI-466029, EBI-399257;
CC P42858; Q8N594: MPND; NbExp=3; IntAct=EBI-466029, EBI-2512452;
CC P42858; P49959: MRE11; NbExp=5; IntAct=EBI-466029, EBI-396513;
CC P42858; Q9Y605: MRFAP1; NbExp=19; IntAct=EBI-466029, EBI-995714;
CC P42858; Q96HT8: MRFAP1L1; NbExp=21; IntAct=EBI-466029, EBI-748896;
CC P42858; Q9BYD1: MRPL13; NbExp=3; IntAct=EBI-466029, EBI-1054936;
CC P42858; O43196-4: MSH5; NbExp=3; IntAct=EBI-466029, EBI-25860238;
CC P42858; Q9Y3D2: MSRB2; NbExp=12; IntAct=EBI-466029, EBI-9092052;
CC P42858; P35548: MSX2; NbExp=12; IntAct=EBI-466029, EBI-6447480;
CC P42858; P02795: MT2A; NbExp=6; IntAct=EBI-466029, EBI-996616;
CC P42858; O43312: MTSS1; NbExp=3; IntAct=EBI-466029, EBI-473954;
CC P42858; Q9ULD2-3: MTUS1; NbExp=3; IntAct=EBI-466029, EBI-18051665;
CC P42858; Q9ULD2-4: MTUS1; NbExp=9; IntAct=EBI-466029, EBI-25866497;
CC P42858; O15069: NACAD; NbExp=15; IntAct=EBI-466029, EBI-7108375;
CC P42858; Q9ULW6: NAP1L2; NbExp=3; IntAct=EBI-466029, EBI-3911716;
CC P42858; P54920: NAPA; NbExp=3; IntAct=EBI-466029, EBI-749652;
CC P42858; Q14596: NBR1; NbExp=3; IntAct=EBI-466029, EBI-742698;
CC P42858; P14598: NCF1; NbExp=6; IntAct=EBI-466029, EBI-395044;
CC P42858; Q969V3: NCLN; NbExp=9; IntAct=EBI-466029, EBI-1056979;
CC P42858; O75376: NCOR1; NbExp=3; IntAct=EBI-466029, EBI-347233;
CC P42858; Q99608: NDN; NbExp=6; IntAct=EBI-466029, EBI-718177;
CC P42858; Q9P0J0: NDUFA13; NbExp=4; IntAct=EBI-466029, EBI-372742;
CC P42858; Q16795: NDUFA9; NbExp=7; IntAct=EBI-466029, EBI-1045087;
CC P42858; O96000: NDUFB10; NbExp=13; IntAct=EBI-466029, EBI-1246371;
CC P42858; O96000-2: NDUFB10; NbExp=3; IntAct=EBI-466029, EBI-25930682;
CC P42858; Q9Y6M9: NDUFB9; NbExp=10; IntAct=EBI-466029, EBI-713654;
CC P42858; P28331-5: NDUFS1; NbExp=6; IntAct=EBI-466029, EBI-25876328;
CC P42858; O43920: NDUFS5; NbExp=7; IntAct=EBI-466029, EBI-1246091;
CC P42858; O76041: NEBL; NbExp=18; IntAct=EBI-466029, EBI-2880203;
CC P42858; I6L9F6: NEFL; NbExp=9; IntAct=EBI-466029, EBI-10178578;
CC P42858; Q86SG6: NEK8; NbExp=3; IntAct=EBI-466029, EBI-1752987;
CC P42858; Q13562: NEUROD1; NbExp=6; IntAct=EBI-466029, EBI-3908303;
CC P42858; P19838-2: NFKB1; NbExp=3; IntAct=EBI-466029, EBI-1452242;
CC P42858; Q8N5V2: NGEF; NbExp=3; IntAct=EBI-466029, EBI-718372;
CC P42858; Q9NX24: NHP2; NbExp=3; IntAct=EBI-466029, EBI-1050064;
CC P42858; Q9UBE8: NLK; NbExp=3; IntAct=EBI-466029, EBI-366978;
CC P42858; Q96AM0: NLRP1; NbExp=3; IntAct=EBI-466029, EBI-25860999;
CC P42858; O00746: NME4; NbExp=20; IntAct=EBI-466029, EBI-744871;
CC P42858; P56597: NME5; NbExp=6; IntAct=EBI-466029, EBI-740667;
CC P42858; Q9C002: NMES1; NbExp=3; IntAct=EBI-466029, EBI-3905285;
CC P42858; Q9Y239: NOD1; NbExp=9; IntAct=EBI-466029, EBI-1051262;
CC P42858; O15130-2: NPFF; NbExp=18; IntAct=EBI-466029, EBI-25840002;
CC P42858; Q9Y639-1: NPTN; NbExp=6; IntAct=EBI-466029, EBI-12839590;
CC P42858; Q13133-2: NR1H3; NbExp=3; IntAct=EBI-466029, EBI-12699353;
CC P42858; Q86WQ0: NR2C2AP; NbExp=3; IntAct=EBI-466029, EBI-10260040;
CC P42858; Q6X4W1-6: NSMF; NbExp=6; IntAct=EBI-466029, EBI-25842707;
CC P42858; P36639-4: NUDT1; NbExp=6; IntAct=EBI-466029, EBI-25834643;
CC P42858; Q9NZJ9: NUDT4; NbExp=6; IntAct=EBI-466029, EBI-4280066;
CC P42858; Q7Z417: NUFIP2; NbExp=6; IntAct=EBI-466029, EBI-1210753;
CC P42858; Q9BVL2: NUP58; NbExp=7; IntAct=EBI-466029, EBI-2811583;
CC P42858; Q9NPJ8-3: NXT2; NbExp=15; IntAct=EBI-466029, EBI-10698339;
CC P42858; Q96GC1: ODF2L; NbExp=3; IntAct=EBI-466029, EBI-12176953;
CC P42858; Q02218: OGDH; NbExp=3; IntAct=EBI-466029, EBI-747213;
CC P42858; Q86WS3: OOSP2; NbExp=9; IntAct=EBI-466029, EBI-25888682;
CC P42858; Q6B0I4: OPCML; NbExp=3; IntAct=EBI-466029, EBI-25954356;
CC P42858; Q96CV9: OPTN; NbExp=13; IntAct=EBI-466029, EBI-748974;
CC P42858; Q96CV9-2: OPTN; NbExp=18; IntAct=EBI-466029, EBI-9091423;
CC P42858; Q92882: OSTF1; NbExp=5; IntAct=EBI-466029, EBI-1051152;
CC P42858; Q3ZCN5: OTOGL; NbExp=3; IntAct=EBI-466029, EBI-25954043;
CC P42858; Q8IVL6-2: P3H3; NbExp=6; IntAct=EBI-466029, EBI-12149899;
CC P42858; P13674: P4HA1; NbExp=5; IntAct=EBI-466029, EBI-1237386;
CC P42858; Q6VY07: PACS1; NbExp=18; IntAct=EBI-466029, EBI-2555014;
CC P42858; Q9BY11: PACSIN1; NbExp=3; IntAct=EBI-466029, EBI-721769;
CC P42858; Q13177: PAK2; NbExp=2; IntAct=EBI-466029, EBI-1045887;
CC P42858; Q9P286: PAK5; NbExp=3; IntAct=EBI-466029, EBI-741896;
CC P42858; Q9NP74: PALMD; NbExp=6; IntAct=EBI-466029, EBI-2811699;
CC P42858; Q8N3R9: PALS1; NbExp=3; IntAct=EBI-466029, EBI-2513978;
CC P42858; Q86WK9: PAQR7; NbExp=3; IntAct=EBI-466029, EBI-10694587;
CC P42858; Q99497: PARK7; NbExp=6; IntAct=EBI-466029, EBI-1164361;
CC P42858; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-466029, EBI-11022007;
CC P42858; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-466029, EBI-10302990;
CC P42858; Q9Y5G3-2: PCDHGB1; NbExp=3; IntAct=EBI-466029, EBI-21584477;
CC P42858; Q6UW60-2: PCSK4; NbExp=3; IntAct=EBI-466029, EBI-25960845;
CC P42858; P54750-4: PDE1A; NbExp=3; IntAct=EBI-466029, EBI-25952361;
CC P42858; Q15119: PDK2; NbExp=10; IntAct=EBI-466029, EBI-726271;
CC P42858; Q96HC4: PDLIM5; NbExp=9; IntAct=EBI-466029, EBI-751267;
CC P42858; O15530-4: PDPK1; NbExp=6; IntAct=EBI-466029, EBI-9087775;
CC P42858; Q13113: PDZK1IP1; NbExp=21; IntAct=EBI-466029, EBI-716063;
CC P42858; Q96FA3: PELI1; NbExp=3; IntAct=EBI-466029, EBI-448369;
CC P42858; Q9BRX2: PELO; NbExp=12; IntAct=EBI-466029, EBI-1043580;
CC P42858; O00541: PES1; NbExp=3; IntAct=EBI-466029, EBI-1053271;
CC P42858; Q99471: PFDN5; NbExp=3; IntAct=EBI-466029, EBI-357275;
CC P42858; P35080: PFN2; NbExp=7; IntAct=EBI-466029, EBI-473138;
CC P42858; O75925: PIAS1; NbExp=19; IntAct=EBI-466029, EBI-629434;
CC P42858; Q8N2W9: PIAS4; NbExp=6; IntAct=EBI-466029, EBI-473160;
CC P42858; Q8WXW3: PIBF1; NbExp=3; IntAct=EBI-466029, EBI-2558770;
CC P42858; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-466029, EBI-79165;
CC P42858; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-466029, EBI-10232538;
CC P42858; P42336: PIK3CA; NbExp=3; IntAct=EBI-466029, EBI-2116585;
CC P42858; P27986: PIK3R1; NbExp=7; IntAct=EBI-466029, EBI-79464;
CC P42858; P27986-2: PIK3R1; NbExp=18; IntAct=EBI-466029, EBI-9090282;
CC P42858; O00459: PIK3R2; NbExp=6; IntAct=EBI-466029, EBI-346930;
CC P42858; Q92569: PIK3R3; NbExp=18; IntAct=EBI-466029, EBI-79893;
CC P42858; Q9BXM7: PINK1; NbExp=9; IntAct=EBI-466029, EBI-2846068;
CC P42858; Q96J94: PIWIL1; NbExp=3; IntAct=EBI-466029, EBI-527417;
CC P42858; P14618: PKM; NbExp=9; IntAct=EBI-466029, EBI-353408;
CC P42858; Q9BS22: PLA2G1B; NbExp=3; IntAct=EBI-466029, EBI-25961917;
CC P42858; Q9UP65: PLA2G4C; NbExp=12; IntAct=EBI-466029, EBI-25848809;
CC P42858; Q15149: PLEC; NbExp=4; IntAct=EBI-466029, EBI-297903;
CC P42858; Q6ZR37: PLEKHG7; NbExp=12; IntAct=EBI-466029, EBI-12891828;
CC P42858; Q9HCM2-3: PLXNA4; NbExp=3; IntAct=EBI-466029, EBI-25962330;
CC P42858; Q6P1K2-3: PMF1; NbExp=3; IntAct=EBI-466029, EBI-12906008;
CC P42858; Q8NBT0: POC1A; NbExp=15; IntAct=EBI-466029, EBI-2557132;
CC P42858; Q9H2U2-3: PPA2; NbExp=3; IntAct=EBI-466029, EBI-25972548;
CC P42858; Q9H2U2-6: PPA2; NbExp=3; IntAct=EBI-466029, EBI-25972564;
CC P42858; Q07869: PPARA; NbExp=3; IntAct=EBI-466029, EBI-78615;
CC P42858; Q03181-2: PPARD; NbExp=3; IntAct=EBI-466029, EBI-10223258;
CC P42858; P37231: PPARG; NbExp=16; IntAct=EBI-466029, EBI-781384;
CC P42858; Q59EV6: PPGB; NbExp=10; IntAct=EBI-466029, EBI-14210385;
CC P42858; O43447: PPIH; NbExp=10; IntAct=EBI-466029, EBI-1055615;
CC P42858; O60437: PPL; NbExp=8; IntAct=EBI-466029, EBI-368321;
CC P42858; P62136: PPP1CA; NbExp=10; IntAct=EBI-466029, EBI-357253;
CC P42858; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-466029, EBI-10293968;
CC P42858; Q6ZMI0-5: PPP1R21; NbExp=9; IntAct=EBI-466029, EBI-25835994;
CC P42858; Q16537: PPP2R5E; NbExp=15; IntAct=EBI-466029, EBI-968374;
CC P42858; O75170-4: PPP6R2; NbExp=3; IntAct=EBI-466029, EBI-11079164;
CC P42858; O60828: PQBP1; NbExp=3; IntAct=EBI-466029, EBI-713867;
CC P42858; P49642: PRIM1; NbExp=3; IntAct=EBI-466029, EBI-726050;
CC P42858; P17612: PRKACA; NbExp=3; IntAct=EBI-466029, EBI-476586;
CC P42858; P55345: PRMT2; NbExp=3; IntAct=EBI-466029, EBI-78458;
CC P42858; P04156: PRNP; NbExp=13; IntAct=EBI-466029, EBI-977302;
CC P42858; Q53TL4: PRO0132; NbExp=3; IntAct=EBI-466029, EBI-25960611;
CC P42858; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-466029, EBI-1567797;
CC P42858; O75400: PRPF40A; NbExp=15; IntAct=EBI-466029, EBI-473291;
CC P42858; O75400-2: PRPF40A; NbExp=9; IntAct=EBI-466029, EBI-5280197;
CC P42858; Q96M27: PRRC1; NbExp=7; IntAct=EBI-466029, EBI-2560879;
CC P42858; Q8WUY3: PRUNE2; NbExp=3; IntAct=EBI-466029, EBI-743880;
CC P42858; P25786: PSMA1; NbExp=3; IntAct=EBI-466029, EBI-359352;
CC P42858; P25789: PSMA4; NbExp=4; IntAct=EBI-466029, EBI-359310;
CC P42858; P60900: PSMA6; NbExp=4; IntAct=EBI-466029, EBI-357793;
CC P42858; O14818: PSMA7; NbExp=13; IntAct=EBI-466029, EBI-603272;
CC P42858; P20618: PSMB1; NbExp=7; IntAct=EBI-466029, EBI-372273;
CC P42858; P49721: PSMB2; NbExp=7; IntAct=EBI-466029, EBI-359335;
CC P42858; P49720: PSMB3; NbExp=3; IntAct=EBI-466029, EBI-603340;
CC P42858; P28072: PSMB6; NbExp=3; IntAct=EBI-466029, EBI-359288;
CC P42858; P28062-2: PSMB8; NbExp=3; IntAct=EBI-466029, EBI-372312;
CC P42858; P17980: PSMC3; NbExp=6; IntAct=EBI-466029, EBI-359720;
CC P42858; O00487: PSMD14; NbExp=7; IntAct=EBI-466029, EBI-722193;
CC P42858; O43242: PSMD3; NbExp=3; IntAct=EBI-466029, EBI-357622;
CC P42858; P55036: PSMD4; NbExp=5; IntAct=EBI-466029, EBI-359318;
CC P42858; P51665: PSMD7; NbExp=10; IntAct=EBI-466029, EBI-357659;
CC P42858; Q13635-3: PTCH1; NbExp=3; IntAct=EBI-466029, EBI-14199621;
CC P42858; P41222: PTGDS; NbExp=3; IntAct=EBI-466029, EBI-948821;
CC P42858; Q13882: PTK6; NbExp=4; IntAct=EBI-466029, EBI-1383632;
CC P42858; Q9UHX1-2: PUF60; NbExp=6; IntAct=EBI-466029, EBI-11529177;
CC P42858; Q9UHX1-6: PUF60; NbExp=9; IntAct=EBI-466029, EBI-11085298;
CC P42858; P47897: QARS1; NbExp=6; IntAct=EBI-466029, EBI-347462;
CC P42858; Q15286: RAB35; NbExp=3; IntAct=EBI-466029, EBI-722275;
CC P42858; P61020: RAB5B; NbExp=3; IntAct=EBI-466029, EBI-399401;
CC P42858; P54725: RAD23A; NbExp=3; IntAct=EBI-466029, EBI-746453;
CC P42858; P78406: RAE1; NbExp=4; IntAct=EBI-466029, EBI-724495;
CC P42858; P62826: RAN; NbExp=6; IntAct=EBI-466029, EBI-286642;
CC P42858; P46060: RANGAP1; NbExp=10; IntAct=EBI-466029, EBI-396091;
CC P42858; Q8WZA2: RAPGEF4; NbExp=3; IntAct=EBI-466029, EBI-948476;
CC P42858; Q13702-2: RAPSN; NbExp=18; IntAct=EBI-466029, EBI-22012855;
CC P42858; P20936: RASA1; NbExp=3; IntAct=EBI-466029, EBI-1026476;
CC P42858; Q6T310: RASL11A; NbExp=3; IntAct=EBI-466029, EBI-4401868;
CC P42858; Q9NS23-4: RASSF1; NbExp=3; IntAct=EBI-466029, EBI-438710;
CC P42858; P50749: RASSF2; NbExp=3; IntAct=EBI-466029, EBI-960081;
CC P42858; Q8WWW0-2: RASSF5; NbExp=3; IntAct=EBI-466029, EBI-960502;
CC P42858; O43251-3: RBFOX2; NbExp=3; IntAct=EBI-466029, EBI-11531589;
CC P42858; P57052: RBM11; NbExp=9; IntAct=EBI-466029, EBI-741332;
CC P42858; P52756: RBM5; NbExp=6; IntAct=EBI-466029, EBI-714003;
CC P42858; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-466029, EBI-740343;
CC P42858; Q9UKA8: RCAN3; NbExp=18; IntAct=EBI-466029, EBI-9091952;
CC P42858; Q15293: RCN1; NbExp=3; IntAct=EBI-466029, EBI-948278;
CC P42858; Q9GZR2: REXO4; NbExp=3; IntAct=EBI-466029, EBI-2856313;
CC P42858; Q8IXN7: RIMKLA; NbExp=3; IntAct=EBI-466029, EBI-21890191;
CC P42858; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-466029, EBI-726876;
CC P42858; Q5TAB7: RIPPLY2; NbExp=6; IntAct=EBI-466029, EBI-10246897;
CC P42858; Q6ZNA4-2: RNF111; NbExp=18; IntAct=EBI-466029, EBI-21535400;
CC P42858; Q9ULX5: RNF112; NbExp=21; IntAct=EBI-466029, EBI-25829984;
CC P42858; Q96D59: RNF183; NbExp=3; IntAct=EBI-466029, EBI-743938;
CC P42858; Q5VTR2: RNF20; NbExp=24; IntAct=EBI-466029, EBI-2372238;
CC P42858; Q9H0F5-2: RNF38; NbExp=21; IntAct=EBI-466029, EBI-25866807;
CC P42858; O75150: RNF40; NbExp=12; IntAct=EBI-466029, EBI-744408;
CC P42858; P26373: RPL13; NbExp=10; IntAct=EBI-466029, EBI-356849;
CC P42858; Q6NZ55: RPL13; NbExp=3; IntAct=EBI-466029, EBI-10252046;
CC P42858; P61313: RPL15; NbExp=3; IntAct=EBI-466029, EBI-443462;
CC P42858; Q07020: RPL18; NbExp=12; IntAct=EBI-466029, EBI-352694;
CC P42858; P84098: RPL19; NbExp=6; IntAct=EBI-466029, EBI-916524;
CC P42858; P35268: RPL22; NbExp=3; IntAct=EBI-466029, EBI-354533;
CC P42858; Q9UNX3: RPL26L1; NbExp=3; IntAct=EBI-466029, EBI-2949703;
CC P42858; P61353: RPL27; NbExp=6; IntAct=EBI-466029, EBI-352760;
CC P42858; P62899: RPL31; NbExp=3; IntAct=EBI-466029, EBI-1053664;
CC P42858; P36578: RPL4; NbExp=14; IntAct=EBI-466029, EBI-348313;
CC P42858; P25398: RPS12; NbExp=3; IntAct=EBI-466029, EBI-354542;
CC P42858; P62244: RPS15A; NbExp=3; IntAct=EBI-466029, EBI-347895;
CC P42858; P39019: RPS19; NbExp=3; IntAct=EBI-466029, EBI-354451;
CC P42858; P62979: RPS27A; NbExp=6; IntAct=EBI-466029, EBI-357375;
CC P42858; P23396: RPS3; NbExp=3; IntAct=EBI-466029, EBI-351193;
CC P42858; P46782: RPS5; NbExp=3; IntAct=EBI-466029, EBI-350569;
CC P42858; Q16799-3: RTN1; NbExp=9; IntAct=EBI-466029, EBI-10180131;
CC P42858; Q6ZNE9: RUFY4; NbExp=3; IntAct=EBI-466029, EBI-10181525;
CC P42858; Q66K80: RUSC1-AS1; NbExp=6; IntAct=EBI-466029, EBI-10248967;
CC P42858; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-466029, EBI-8636004;
CC P42858; P48443: RXRG; NbExp=18; IntAct=EBI-466029, EBI-712405;
CC P42858; Q8N488: RYBP; NbExp=9; IntAct=EBI-466029, EBI-752324;
CC P42858; P25815: S100P; NbExp=9; IntAct=EBI-466029, EBI-743700;
CC P42858; Q8N6K7-2: SAMD3; NbExp=3; IntAct=EBI-466029, EBI-11528848;
CC P42858; G3V2R1: SAMD4A; NbExp=3; IntAct=EBI-466029, EBI-21264240;
CC P42858; O75446: SAP30; NbExp=3; IntAct=EBI-466029, EBI-632609;
CC P42858; Q6UVJ0: SASS6; NbExp=15; IntAct=EBI-466029, EBI-1570153;
CC P42858; Q9BY12-3: SCAPER; NbExp=6; IntAct=EBI-466029, EBI-25837959;
CC P42858; Q8WVM8: SCFD1; NbExp=3; IntAct=EBI-466029, EBI-722569;
CC P42858; Q96NL6-3: SCLT1; NbExp=3; IntAct=EBI-466029, EBI-25961722;
CC P42858; Q12765-2: SCRN1; NbExp=3; IntAct=EBI-466029, EBI-12027936;
CC P42858; O00560: SDCBP; NbExp=12; IntAct=EBI-466029, EBI-727004;
CC P42858; P55735-3: SEC13; NbExp=15; IntAct=EBI-466029, EBI-12235008;
CC P42858; Q15437: SEC23B; NbExp=3; IntAct=EBI-466029, EBI-742673;
CC P42858; Q96T21: SECISBP2; NbExp=3; IntAct=EBI-466029, EBI-954116;
CC P42858; O43236: SEPTIN4; NbExp=3; IntAct=EBI-466029, EBI-1047513;
CC P42858; Q14141: SEPTIN6; NbExp=18; IntAct=EBI-466029, EBI-745901;
CC P42858; Q16181-2: SEPTIN7; NbExp=9; IntAct=EBI-466029, EBI-10176094;
CC P42858; Q9UHV2: SERTAD1; NbExp=3; IntAct=EBI-466029, EBI-748601;
CC P42858; Q9BYW2: SETD2; NbExp=4; IntAct=EBI-466029, EBI-945869;
CC P42858; Q15047-2: SETDB1; NbExp=15; IntAct=EBI-466029, EBI-9090795;
CC P42858; Q12874: SF3A3; NbExp=3; IntAct=EBI-466029, EBI-1051880;
CC P42858; Q15393: SF3B3; NbExp=3; IntAct=EBI-466029, EBI-346977;
CC P42858; Q9BWM7: SFXN3; NbExp=9; IntAct=EBI-466029, EBI-1171999;
CC P42858; Q2NKQ1-4: SGSM1; NbExp=12; IntAct=EBI-466029, EBI-10182463;
CC P42858; Q99961: SH3GL1; NbExp=3; IntAct=EBI-466029, EBI-697911;
CC P42858; Q99963: SH3GL3; NbExp=9; IntAct=EBI-466029, EBI-473910;
CC P42858; Q9NR46: SH3GLB2; NbExp=3; IntAct=EBI-466029, EBI-749607;
CC P42858; Q8IYI0: SHLD1; NbExp=3; IntAct=EBI-466029, EBI-2560428;
CC P42858; Q9Y2K2-7: SIK3; NbExp=3; IntAct=EBI-466029, EBI-17172855;
CC P42858; Q96ST3: SIN3A; NbExp=4; IntAct=EBI-466029, EBI-347218;
CC P42858; Q9GZS3: SKIC8; NbExp=22; IntAct=EBI-466029, EBI-358545;
CC P42858; P43004: SLC1A2; NbExp=12; IntAct=EBI-466029, EBI-3440986;
CC P42858; Q02978: SLC25A11; NbExp=6; IntAct=EBI-466029, EBI-359174;
CC P42858; Q00325-2: SLC25A3; NbExp=3; IntAct=EBI-466029, EBI-5456178;
CC P42858; Q8NCS7: SLC44A5; NbExp=3; IntAct=EBI-466029, EBI-21504521;
CC P42858; Q12824: SMARCB1; NbExp=9; IntAct=EBI-466029, EBI-358419;
CC P42858; Q8TAQ2-2: SMARCC2; NbExp=3; IntAct=EBI-466029, EBI-11990400;
CC P42858; Q96GM5: SMARCD1; NbExp=12; IntAct=EBI-466029, EBI-358489;
CC P42858; Q16637-3: SMN2; NbExp=9; IntAct=EBI-466029, EBI-395447;
CC P42858; Q9HCE7-2: SMURF1; NbExp=6; IntAct=EBI-466029, EBI-9845742;
CC P42858; P60880-2: SNAP25; NbExp=9; IntAct=EBI-466029, EBI-12177361;
CC P42858; O95721: SNAP29; NbExp=3; IntAct=EBI-466029, EBI-490676;
CC P42858; P37840: SNCA; NbExp=4; IntAct=EBI-466029, EBI-985879;
CC P42858; P62316: SNRPD2; NbExp=3; IntAct=EBI-466029, EBI-297993;
CC P42858; P62306: SNRPF; NbExp=3; IntAct=EBI-466029, EBI-356900;
CC P42858; Q13573: SNW1; NbExp=12; IntAct=EBI-466029, EBI-632715;
CC P42858; Q9UMY4: SNX12; NbExp=3; IntAct=EBI-466029, EBI-1752602;
CC P42858; O60749: SNX2; NbExp=6; IntAct=EBI-466029, EBI-1046690;
CC P42858; Q8WV41: SNX33; NbExp=6; IntAct=EBI-466029, EBI-2481535;
CC P42858; Q8WXH5: SOCS4; NbExp=3; IntAct=EBI-466029, EBI-3942425;
CC P42858; Q9BX66: SORBS1; NbExp=4; IntAct=EBI-466029, EBI-433642;
CC P42858; O95416: SOX14; NbExp=12; IntAct=EBI-466029, EBI-9087806;
CC P42858; Q9BT81: SOX7; NbExp=15; IntAct=EBI-466029, EBI-7239117;
CC P42858; Q02447: SP3; NbExp=4; IntAct=EBI-466029, EBI-348158;
CC P42858; Q3SY56: SP6; NbExp=3; IntAct=EBI-466029, EBI-11175533;
CC P42858; Q99932-2: SPAG8; NbExp=18; IntAct=EBI-466029, EBI-11959123;
CC P42858; Q9NY87: SPANXC; NbExp=3; IntAct=EBI-466029, EBI-10316585;
CC P42858; Q7Z6I5: SPATA12; NbExp=3; IntAct=EBI-466029, EBI-10696971;
CC P42858; Q8NHS9: SPATA22; NbExp=9; IntAct=EBI-466029, EBI-7067260;
CC P42858; Q8IUW3: SPATA2L; NbExp=6; IntAct=EBI-466029, EBI-2510414;
CC P42858; P61009: SPCS3; NbExp=6; IntAct=EBI-466029, EBI-6166040;
CC P42858; Q01892: SPIB; NbExp=18; IntAct=EBI-466029, EBI-2800992;
CC P42858; Q1W4C9: SPINK13; NbExp=3; IntAct=EBI-466029, EBI-25953827;
CC P42858; Q8N865: SPMIP4; NbExp=3; IntAct=EBI-466029, EBI-10174456;
CC P42858; Q7Z698: SPRED2; NbExp=6; IntAct=EBI-466029, EBI-7082156;
CC P42858; Q13501: SQSTM1; NbExp=8; IntAct=EBI-466029, EBI-307104;
CC P42858; P36956: SREBF1; NbExp=3; IntAct=EBI-466029, EBI-948313;
CC P42858; Q7Z6B7: SRGAP1; NbExp=4; IntAct=EBI-466029, EBI-2481729;
CC P42858; O75044: SRGAP2; NbExp=3; IntAct=EBI-466029, EBI-1051034;
CC P42858; O43295: SRGAP3; NbExp=4; IntAct=EBI-466029, EBI-368166;
CC P42858; Q8IXS7: SRGAP3; NbExp=3; IntAct=EBI-466029, EBI-18616594;
CC P42858; Q9BXP5: SRRT; NbExp=3; IntAct=EBI-466029, EBI-712721;
CC P42858; Q9BXP5-3: SRRT; NbExp=6; IntAct=EBI-466029, EBI-25866384;
CC P42858; Q9BXP5-4: SRRT; NbExp=3; IntAct=EBI-466029, EBI-16701991;
CC P42858; P05455: SSB; NbExp=3; IntAct=EBI-466029, EBI-358037;
CC P42858; Q9NP77: SSU72; NbExp=3; IntAct=EBI-466029, EBI-2515416;
CC P42858; P50502: ST13; NbExp=13; IntAct=EBI-466029, EBI-357285;
CC P42858; O75886: STAM2; NbExp=6; IntAct=EBI-466029, EBI-373258;
CC P42858; P49675: STAR; NbExp=3; IntAct=EBI-466029, EBI-722932;
CC P42858; Q9H668: STN1; NbExp=3; IntAct=EBI-466029, EBI-746930;
CC P42858; Q9Y3F4: STRAP; NbExp=4; IntAct=EBI-466029, EBI-727414;
CC P42858; A1L378: STRC; NbExp=6; IntAct=EBI-466029, EBI-22013242;
CC P42858; Q9UNE7: STUB1; NbExp=12; IntAct=EBI-466029, EBI-357085;
CC P42858; O14662-5: STX16; NbExp=15; IntAct=EBI-466029, EBI-9089968;
CC P42858; P61764: STXBP1; NbExp=7; IntAct=EBI-466029, EBI-960169;
CC P42858; Q9BR01-2: SULT4A1; NbExp=15; IntAct=EBI-466029, EBI-25831443;
CC P42858; Q8NBJ7: SUMF2; NbExp=6; IntAct=EBI-466029, EBI-723091;
CC P42858; P63165: SUMO1; NbExp=3; IntAct=EBI-466029, EBI-80140;
CC P42858; P55854: SUMO3; NbExp=9; IntAct=EBI-466029, EBI-474067;
CC P42858; A1L190: SYCE3; NbExp=15; IntAct=EBI-466029, EBI-10283466;
CC P42858; Q92797: SYMPK; NbExp=3; IntAct=EBI-466029, EBI-1051992;
CC P42858; Q92797-2: SYMPK; NbExp=9; IntAct=EBI-466029, EBI-21560407;
CC P42858; P08247: SYP; NbExp=13; IntAct=EBI-466029, EBI-9071725;
CC P42858; Q9BQS2-2: SYT15; NbExp=3; IntAct=EBI-466029, EBI-13373352;
CC P42858; Q8N9I0: SYT2; NbExp=10; IntAct=EBI-466029, EBI-8032987;
CC P42858; Q9BQG1: SYT3; NbExp=12; IntAct=EBI-466029, EBI-17284568;
CC P42858; Q5T7P8-2: SYT6; NbExp=3; IntAct=EBI-466029, EBI-10246152;
CC P42858; O75410: TACC1; NbExp=4; IntAct=EBI-466029, EBI-624237;
CC P42858; O75410-7: TACC1; NbExp=12; IntAct=EBI-466029, EBI-12007872;
CC P42858; Q86TJ2-3: TADA2B; NbExp=3; IntAct=EBI-466029, EBI-18173581;
CC P42858; P37802: TAGLN2; NbExp=3; IntAct=EBI-466029, EBI-1056740;
CC P42858; P37837: TALDO1; NbExp=3; IntAct=EBI-466029, EBI-1056712;
CC P42858; Q6NW12: TANK; NbExp=9; IntAct=EBI-466029, EBI-25948253;
CC P42858; Q92844: TANK; NbExp=3; IntAct=EBI-466029, EBI-356349;
CC P42858; Q92844-3: TANK; NbExp=3; IntAct=EBI-466029, EBI-25967460;
CC P42858; Q9H2K8: TAOK3; NbExp=3; IntAct=EBI-466029, EBI-1384100;
CC P42858; Q5VWN6: TASOR2; NbExp=12; IntAct=EBI-466029, EBI-745958;
CC P42858; Q92609: TBC1D5; NbExp=3; IntAct=EBI-466029, EBI-742381;
CC P42858; Q32MN6: TBP; NbExp=9; IntAct=EBI-466029, EBI-10239991;
CC P42858; Q16650: TBR1; NbExp=12; IntAct=EBI-466029, EBI-1047158;
CC P42858; Q9Y458: TBX22; NbExp=12; IntAct=EBI-466029, EBI-6427217;
CC P42858; O14776: TCERG1; NbExp=9; IntAct=EBI-466029, EBI-473271;
CC P42858; P17987: TCP1; NbExp=3; IntAct=EBI-466029, EBI-356553;
CC P42858; Q8TDR4: TCP10L; NbExp=3; IntAct=EBI-466029, EBI-3923210;
CC P42858; P28347-2: TEAD1; NbExp=18; IntAct=EBI-466029, EBI-12151837;
CC P42858; Q86WV5: TEN1; NbExp=9; IntAct=EBI-466029, EBI-2562799;
CC P42858; Q96A09: TENT5B; NbExp=6; IntAct=EBI-466029, EBI-752030;
CC P42858; Q15554-4: TERF2; NbExp=15; IntAct=EBI-466029, EBI-25840535;
CC P42858; Q96M34: TEX55; NbExp=3; IntAct=EBI-466029, EBI-25961624;
CC P42858; Q03403: TFF2; NbExp=18; IntAct=EBI-466029, EBI-4314702;
CC P42858; Q92734: TFG; NbExp=3; IntAct=EBI-466029, EBI-357061;
CC P42858; O95455: TGDS; NbExp=3; IntAct=EBI-466029, EBI-1761487;
CC P42858; P37173: TGFBR2; NbExp=3; IntAct=EBI-466029, EBI-296151;
CC P42858; P21980-2: TGM2; NbExp=6; IntAct=EBI-466029, EBI-25842075;
CC P42858; Q96MW7: TIGD1; NbExp=9; IntAct=EBI-466029, EBI-9091586;
CC P42858; O60220: TIMM8A; NbExp=15; IntAct=EBI-466029, EBI-1049822;
CC P42858; Q08117: TLE5; NbExp=3; IntAct=EBI-466029, EBI-717810;
CC P42858; Q9BZW5-2: TM6SF1; NbExp=3; IntAct=EBI-466029, EBI-25852210;
CC P42858; Q96EY4: TMA16; NbExp=3; IntAct=EBI-466029, EBI-1045338;
CC P42858; Q9NUM4: TMEM106B; NbExp=3; IntAct=EBI-466029, EBI-10490807;
CC P42858; Q12893: TMEM115; NbExp=3; IntAct=EBI-466029, EBI-8633987;
CC P42858; Q6UW68: TMEM205; NbExp=3; IntAct=EBI-466029, EBI-6269551;
CC P42858; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-466029, EBI-11528917;
CC P42858; Q9NV96-2: TMEM30A; NbExp=3; IntAct=EBI-466029, EBI-12921610;
CC P42858; Q9BTV4: TMEM43; NbExp=3; IntAct=EBI-466029, EBI-721293;
CC P42858; Q9BQJ4: TMEM47; NbExp=3; IntAct=EBI-466029, EBI-13370320;
CC P42858; Q8IUR5-4: TMTC1; NbExp=6; IntAct=EBI-466029, EBI-9089156;
CC P42858; Q71RG4-4: TMUB2; NbExp=6; IntAct=EBI-466029, EBI-25831574;
CC P42858; Q13829: TNFAIP1; NbExp=3; IntAct=EBI-466029, EBI-2505861;
CC P42858; O00300: TNFRSF11B; NbExp=3; IntAct=EBI-466029, EBI-15481185;
CC P42858; O95150: TNFSF15; NbExp=3; IntAct=EBI-466029, EBI-16355546;
CC P42858; Q96KP6: TNIP3; NbExp=9; IntAct=EBI-466029, EBI-2509913;
CC P42858; P22105-1: TNXB; NbExp=3; IntAct=EBI-466029, EBI-20753895;
CC P42858; Q9NS69: TOMM22; NbExp=6; IntAct=EBI-466029, EBI-1047508;
CC P42858; P04637: TP53; NbExp=19; IntAct=EBI-466029, EBI-366083;
CC P42858; P60174: TPI1; NbExp=6; IntAct=EBI-466029, EBI-717475;
CC P42858; Q12933: TRAF2; NbExp=3; IntAct=EBI-466029, EBI-355744;
CC P42858; O14545: TRAFD1; NbExp=5; IntAct=EBI-466029, EBI-1396921;
CC P42858; P19474: TRIM21; NbExp=21; IntAct=EBI-466029, EBI-81290;
CC P42858; Q9UPQ4-2: TRIM35; NbExp=9; IntAct=EBI-466029, EBI-17716262;
CC P42858; P0CI25: TRIM49; NbExp=9; IntAct=EBI-466029, EBI-6427421;
CC P42858; Q15642-2: TRIP10; NbExp=18; IntAct=EBI-466029, EBI-6550597;
CC P42858; Q15654: TRIP6; NbExp=3; IntAct=EBI-466029, EBI-742327;
CC P42858; Q99614: TTC1; NbExp=9; IntAct=EBI-466029, EBI-742074;
CC P42858; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-466029, EBI-948354;
CC P42858; Q5W5X9-3: TTC23; NbExp=18; IntAct=EBI-466029, EBI-9090990;
CC P42858; Q71U36: TUBA1A; NbExp=3; IntAct=EBI-466029, EBI-302552;
CC P42858; P07437: TUBB; NbExp=9; IntAct=EBI-466029, EBI-350864;
CC P42858; Q9BUF5: TUBB6; NbExp=3; IntAct=EBI-466029, EBI-356735;
CC P42858; Q9UGJ1-2: TUBGCP4; NbExp=6; IntAct=EBI-466029, EBI-10964469;
CC P42858; Q15672: TWIST1; NbExp=3; IntAct=EBI-466029, EBI-1797287;
CC P42858; Q8WVJ9: TWIST2; NbExp=15; IntAct=EBI-466029, EBI-1797313;
CC P42858; Q99757: TXN2; NbExp=3; IntAct=EBI-466029, EBI-2932492;
CC P42858; Q6PKC3: TXNDC11; NbExp=7; IntAct=EBI-466029, EBI-749812;
CC P42858; Q01081: U2AF1; NbExp=3; IntAct=EBI-466029, EBI-632461;
CC P42858; P22314: UBA1; NbExp=3; IntAct=EBI-466029, EBI-709688;
CC P42858; Q9BSL1: UBAC1; NbExp=26; IntAct=EBI-466029, EBI-749370;
CC P42858; P0CG48: UBC; NbExp=3; IntAct=EBI-466029, EBI-3390054;
CC P42858; Q9Y2X8: UBE2D4; NbExp=3; IntAct=EBI-466029, EBI-745527;
CC P42858; P62256: UBE2H; NbExp=3; IntAct=EBI-466029, EBI-2129909;
CC P42858; P63279: UBE2I; NbExp=3; IntAct=EBI-466029, EBI-80168;
CC P42858; P61086: UBE2K; NbExp=24; IntAct=EBI-466029, EBI-473850;
CC P42858; Q9UHD9: UBQLN2; NbExp=12; IntAct=EBI-466029, EBI-947187;
CC P42858; Q92890: UFD1; NbExp=7; IntAct=EBI-466029, EBI-1994090;
CC P42858; O75385: ULK1; NbExp=8; IntAct=EBI-466029, EBI-908831;
CC P42858; Q495M9: USH1G; NbExp=3; IntAct=EBI-466029, EBI-8601749;
CC P42858; Q9UMW8: USP18; NbExp=3; IntAct=EBI-466029, EBI-356206;
CC P42858; O75604-3: USP2; NbExp=6; IntAct=EBI-466029, EBI-10696113;
CC P42858; Q9UPU5: USP24; NbExp=21; IntAct=EBI-466029, EBI-1642365;
CC P42858; Q8NFA0-2: USP32; NbExp=18; IntAct=EBI-466029, EBI-12220239;
CC P42858; Q93008: USP9X; NbExp=8; IntAct=EBI-466029, EBI-302524;
CC P42858; Q9BVJ6: UTP14A; NbExp=4; IntAct=EBI-466029, EBI-473284;
CC P42858; Q9NYH9: UTP6; NbExp=3; IntAct=EBI-466029, EBI-749211;
CC P42858; Q08AM6: VAC14; NbExp=3; IntAct=EBI-466029, EBI-2107455;
CC P42858; Q9HCJ6: VAT1L; NbExp=3; IntAct=EBI-466029, EBI-10234766;
CC P42858; P55072: VCP; NbExp=10; IntAct=EBI-466029, EBI-355164;
CC P42858; P45880: VDAC2; NbExp=22; IntAct=EBI-466029, EBI-354022;
CC P42858; P40337-2: VHL; NbExp=12; IntAct=EBI-466029, EBI-12157263;
CC P42858; P09327-2: VIL1; NbExp=3; IntAct=EBI-466029, EBI-25958818;
CC P42858; P08670: VIM; NbExp=4; IntAct=EBI-466029, EBI-353844;
CC P42858; Q9UK41: VPS28; NbExp=16; IntAct=EBI-466029, EBI-727424;
CC P42858; Q8NEZ2: VPS37A; NbExp=6; IntAct=EBI-466029, EBI-2850578;
CC P42858; O75351: VPS4B; NbExp=3; IntAct=EBI-466029, EBI-2514459;
CC P42858; Q9BTA9: WAC; NbExp=5; IntAct=EBI-466029, EBI-749118;
CC P42858; Q9BTA9-5: WAC; NbExp=3; IntAct=EBI-466029, EBI-25956668;
CC P42858; O75554: WBP4; NbExp=3; IntAct=EBI-466029, EBI-7251981;
CC P42858; Q8IZQ1: WDFY3; NbExp=10; IntAct=EBI-466029, EBI-1569256;
CC P42858; A4D1P6: WDR91; NbExp=16; IntAct=EBI-466029, EBI-718046;
CC P42858; Q15007-2: WTAP; NbExp=3; IntAct=EBI-466029, EBI-25840023;
CC P42858; O00308: WWP2; NbExp=9; IntAct=EBI-466029, EBI-743923;
CC P42858; Q9HCS7: XAB2; NbExp=3; IntAct=EBI-466029, EBI-295232;
CC P42858; Q8WTP9: XAGE3; NbExp=3; IntAct=EBI-466029, EBI-6448284;
CC P42858; P12956: XRCC6; NbExp=21; IntAct=EBI-466029, EBI-353208;
CC P42858; O95070: YIF1A; NbExp=12; IntAct=EBI-466029, EBI-2799703;
CC P42858; P31946: YWHAB; NbExp=11; IntAct=EBI-466029, EBI-359815;
CC P42858; Q9H869-2: YY1AP1; NbExp=3; IntAct=EBI-466029, EBI-12150045;
CC P42858; Q9H171: ZBP1; NbExp=6; IntAct=EBI-466029, EBI-6264672;
CC P42858; Q05516: ZBTB16; NbExp=4; IntAct=EBI-466029, EBI-711925;
CC P42858; O43167-2: ZBTB24; NbExp=9; IntAct=EBI-466029, EBI-25842419;
CC P42858; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-466029, EBI-14104088;
CC P42858; Q6PEW1: ZCCHC12; NbExp=3; IntAct=EBI-466029, EBI-748373;
CC P42858; Q8IUH5: ZDHHC17; NbExp=30; IntAct=EBI-466029, EBI-524753;
CC P42858; Q8WVZ1-3: ZDHHC19; NbExp=3; IntAct=EBI-466029, EBI-25961277;
CC P42858; G3V1X1: ZFC3H1; NbExp=5; IntAct=EBI-466029, EBI-6448783;
CC P42858; Q6ZN57: ZFP2; NbExp=12; IntAct=EBI-466029, EBI-7236323;
CC P42858; Q96K21: ZFYVE19; NbExp=21; IntAct=EBI-466029, EBI-6448240;
CC P42858; Q9UKY1: ZHX1; NbExp=6; IntAct=EBI-466029, EBI-347767;
CC P42858; Q96EF9: ZHX1-C8orf76; NbExp=18; IntAct=EBI-466029, EBI-25830993;
CC P42858; Q9BRR0: ZKSCAN3; NbExp=3; IntAct=EBI-466029, EBI-1965777;
CC P42858; Q15776: ZKSCAN8; NbExp=9; IntAct=EBI-466029, EBI-2602314;
CC P42858; Q96NC0: ZMAT2; NbExp=20; IntAct=EBI-466029, EBI-2682299;
CC P42858; O95789-4: ZMYM6; NbExp=3; IntAct=EBI-466029, EBI-12949277;
CC P42858; P52744: ZNF138; NbExp=9; IntAct=EBI-466029, EBI-10746567;
CC P42858; Q9UJW8-4: ZNF180; NbExp=9; IntAct=EBI-466029, EBI-12055755;
CC P42858; P17023: ZNF19; NbExp=3; IntAct=EBI-466029, EBI-12884200;
CC P42858; Q9BSG1: ZNF2; NbExp=3; IntAct=EBI-466029, EBI-8489229;
CC P42858; Q9Y2X9: ZNF281; NbExp=3; IntAct=EBI-466029, EBI-396200;
CC P42858; Q9HBT8: ZNF286A; NbExp=9; IntAct=EBI-466029, EBI-10754950;
CC P42858; Q9NR11-2: ZNF302; NbExp=3; IntAct=EBI-466029, EBI-12988373;
CC P42858; Q8N895: ZNF366; NbExp=15; IntAct=EBI-466029, EBI-2813661;
CC P42858; Q9C0F3: ZNF436; NbExp=15; IntAct=EBI-466029, EBI-8489702;
CC P42858; Q8N0Y2-2: ZNF444; NbExp=9; IntAct=EBI-466029, EBI-12010736;
CC P42858; Q6ZNH5: ZNF497; NbExp=9; IntAct=EBI-466029, EBI-10486136;
CC P42858; O60304: ZNF500; NbExp=6; IntAct=EBI-466029, EBI-18234077;
CC P42858; Q8N988-2: ZNF557; NbExp=12; IntAct=EBI-466029, EBI-10699005;
CC P42858; Q68EA5: ZNF57; NbExp=15; IntAct=EBI-466029, EBI-8490788;
CC P42858; Q7Z3I7: ZNF572; NbExp=9; IntAct=EBI-466029, EBI-10172590;
CC P42858; Q96N77-2: ZNF641; NbExp=18; IntAct=EBI-466029, EBI-12939666;
CC P42858; Q8N720: ZNF655; NbExp=14; IntAct=EBI-466029, EBI-625509;
CC P42858; Q5TEC3: ZNF697; NbExp=3; IntAct=EBI-466029, EBI-25845217;
CC P42858; Q3KNS6-3: ZNF829; NbExp=6; IntAct=EBI-466029, EBI-18036029;
CC P42858; Q5JTY5: ZNG1C; NbExp=6; IntAct=EBI-466029, EBI-723434;
CC P42858; O15535: ZSCAN9; NbExp=9; IntAct=EBI-466029, EBI-751531;
CC P42858; Q2QGD7: ZXDC; NbExp=3; IntAct=EBI-466029, EBI-1538838;
CC P42858; A8K3Q9; NbExp=3; IntAct=EBI-466029, EBI-10174314;
CC P42858; A8K878; NbExp=21; IntAct=EBI-466029, EBI-25831303;
CC P42858; B7Z3E8; NbExp=6; IntAct=EBI-466029, EBI-25831617;
CC P42858; Q0VG73; NbExp=6; IntAct=EBI-466029, EBI-25953074;
CC P42858; Q7L8T7; NbExp=6; IntAct=EBI-466029, EBI-25831943;
CC P42858; Q86V28; NbExp=6; IntAct=EBI-466029, EBI-10259496;
CC P42858; Q96IQ6; NbExp=6; IntAct=EBI-466029, EBI-10295632;
CC P42858; O88485: Dync1i1; Xeno; NbExp=2; IntAct=EBI-466029, EBI-492834;
CC P42858; P54256: Hap1; Xeno; NbExp=3; IntAct=EBI-466029, EBI-994539;
CC P42858; P51660: Hsd17b4; Xeno; NbExp=15; IntAct=EBI-466029, EBI-8328056;
CC P42858; P29994: Itpr1; Xeno; NbExp=2; IntAct=EBI-466029, EBI-8614640;
CC P42858; Q99KR7: Ppif; Xeno; NbExp=3; IntAct=EBI-466029, EBI-6455001;
CC -!- SUBCELLULAR LOCATION: [Huntingtin]: Cytoplasm
CC {ECO:0000269|PubMed:15654337, ECO:0000269|PubMed:16476778,
CC ECO:0000269|PubMed:7647777}. Nucleus {ECO:0000269|PubMed:15654337,
CC ECO:0000269|PubMed:16391387}. Early endosome
CC {ECO:0000269|PubMed:16476778}. Note=The mutant Huntingtin protein
CC colocalizes with AKAP8L in the nuclear matrix of Huntington disease
CC neurons. Shuttles between cytoplasm and nucleus in a Ran GTPase-
CC independent manner (PubMed:15654337). Recruits onto early endosomes in
CC a Rab5- and HAP40-dependent fashion (PubMed:16476778).
CC {ECO:0000269|PubMed:15654337, ECO:0000269|PubMed:16476778}.
CC -!- SUBCELLULAR LOCATION: [Huntingtin, myristoylated N-terminal fragment]:
CC Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:24459296}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain cortex (at protein level).
CC Widely expressed with the highest level of expression in the brain
CC (nerve fibers, varicosities, and nerve endings). In the brain, the
CC regions where it can be mainly found are the cerebellar cortex, the
CC neocortex, the striatum, and the hippocampal formation.
CC {ECO:0000269|PubMed:16391387}.
CC -!- DOMAIN: The N-terminal Gln-rich and Pro-rich domain has great
CC conformational flexibility and is likely to exist in a fluctuating
CC equilibrium of alpha-helical, random coil, and extended conformations.
CC {ECO:0000269|PubMed:19748341}.
CC -!- PTM: [Huntingtin]: Cleaved by caspases downstream of the polyglutamine
CC stretch (PubMed:8696339, PubMed:9535906, PubMed:10770929,
CC PubMed:29802276). The resulting N-terminal fragments are cytotoxic and
CC provokes apoptosis (PubMed:10770929). {ECO:0000269|PubMed:10770929,
CC ECO:0000269|PubMed:29802276, ECO:0000269|PubMed:8696339,
CC ECO:0000269|PubMed:9535906}.
CC -!- PTM: [Huntingtin]: Forms with expanded polyglutamine expansion are
CC specifically ubiquitinated by SYVN1, which promotes their proteasomal
CC degradation. {ECO:0000269|PubMed:17141218}.
CC -!- PTM: [Huntingtin]: Phosphorylation at Ser-1179 and Ser-1199 by CDK5 in
CC response to DNA damage in nuclei of neurons protects neurons against
CC polyglutamine expansion as well as DNA damage mediated toxicity.
CC {ECO:0000269|PubMed:17611284}.
CC -!- PTM: [Huntingtin, myristoylated N-terminal fragment]: Myristoylated at
CC Gly-551, following proteolytic cleavage at Asp-550.
CC {ECO:0000269|PubMed:24459296, ECO:0000269|PubMed:29802276}.
CC -!- POLYMORPHISM: The poly-Gln region of HTT is highly polymorphic (10 to
CC 35 repeats) in the normal population and is expanded to about 36-120
CC repeats in Huntington disease patients. The repeat length usually
CC increases in successive generations, but contracts also on occasion.
CC The adjacent poly-Pro region is also polymorphic and varies between 7-
CC 12 residues. Polyglutamine expansion leads to elevated susceptibility
CC to apopain cleavage and likely result in accelerated neuronal apoptosis
CC (PubMed:8696339). {ECO:0000269|PubMed:8696339}.
CC -!- DISEASE: Huntington disease (HD) [MIM:143100]: A neurodegenerative
CC disorder characterized by involuntary movements (chorea), general motor
CC impairment, psychiatric disorders and dementia. Onset of the disease
CC occurs usually in the third or fourth decade of life. Onset and
CC clinical course depend on the degree of poly-Gln repeat expansion,
CC longer expansions resulting in earlier onset and more severe clinical
CC manifestations. Neuropathology of Huntington disease displays a
CC distinctive pattern with loss of neurons, especially in the caudate and
CC putamen. {ECO:0000269|PubMed:8458085}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Lopes-Maciel-Rodan syndrome (LOMARS) [MIM:617435]: An
CC autosomal recessive neurodevelopmental disorder characterized by
CC developmental regression in infancy, delayed psychomotor development,
CC severe intellectual disability, and cerebral and cerebellar atrophy.
CC Additional features include swallowing problems, dystonia,
CC bradykinesia, and continuous manual stereotypies without chorea. Some
CC patients manifest seizures. {ECO:0000269|PubMed:26740508,
CC ECO:0000269|PubMed:27329733}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the huntingtin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Huntingtin entry;
CC URL="https://en.wikipedia.org/wiki/Huntingtin";
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DR EMBL; L12392; AAB38240.1; -; mRNA.
DR EMBL; AB016794; BAA36753.1; -; mRNA.
DR EMBL; Z49154; CAA89024.1; -; Genomic_DNA.
DR EMBL; Z49155; CAA89025.1; -; Genomic_DNA.
DR EMBL; Z49208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z49769; CAA89839.1; -; Genomic_DNA.
DR EMBL; Z68756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z69649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L27350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L27351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L27352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L27353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L27354; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L34020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L20431; AAA52702.1; -; mRNA.
DR CCDS; CCDS43206.1; -.
DR PIR; A46068; A46068.
DR RefSeq; NP_002102.4; NM_002111.8.
DR PDB; 2LD0; NMR; -; A=1-17.
DR PDB; 2LD2; NMR; -; A=1-17.
DR PDB; 3IO4; X-ray; 3.63 A; A/B/C=1-64.
DR PDB; 3IO6; X-ray; 3.70 A; A/B/C=1-64.
DR PDB; 3IOR; X-ray; 3.60 A; A/B/C=1-64.
DR PDB; 3IOT; X-ray; 3.50 A; A/B/C=1-64.
DR PDB; 3IOU; X-ray; 3.70 A; A/B/C=1-64.
DR PDB; 3IOV; X-ray; 3.70 A; A/B/C=1-64.
DR PDB; 3IOW; X-ray; 3.50 A; A/B/C=1-64.
DR PDB; 3LRH; X-ray; 2.60 A; B/D/F/H/J/L/N/P=5-18.
DR PDB; 4FE8; X-ray; 3.00 A; A/B/C=1-64.
DR PDB; 4FEB; X-ray; 2.80 A; A/B/C=1-64.
DR PDB; 4FEC; X-ray; 3.00 A; A/B/C=1-64.
DR PDB; 4FED; X-ray; 2.81 A; A/B/C=1-64.
DR PDB; 4RAV; X-ray; 2.50 A; E/F=1-17.
DR PDB; 6EZ8; EM; 4.00 A; A=1-3142.
DR PDB; 6N8C; NMR; -; A/B/C/D=2-24.
DR PDB; 6RMH; EM; 9.60 A; A=1-3142.
DR PDB; 6X9O; EM; 2.60 A; A=1-3142.
DR PDB; 6YEJ; EM; 18.20 A; A=18-3142.
DR PDB; 7DXJ; EM; 3.60 A; A=1-3142.
DR PDB; 7DXK; EM; 4.10 A; A=18-3142.
DR PDB; 8SAH; EM; 3.20 A; A=2093-3136.
DR PDBsum; 2LD0; -.
DR PDBsum; 2LD2; -.
DR PDBsum; 3IO4; -.
DR PDBsum; 3IO6; -.
DR PDBsum; 3IOR; -.
DR PDBsum; 3IOT; -.
DR PDBsum; 3IOU; -.
DR PDBsum; 3IOV; -.
DR PDBsum; 3IOW; -.
DR PDBsum; 3LRH; -.
DR PDBsum; 4FE8; -.
DR PDBsum; 4FEB; -.
DR PDBsum; 4FEC; -.
DR PDBsum; 4FED; -.
DR PDBsum; 4RAV; -.
DR PDBsum; 6EZ8; -.
DR PDBsum; 6N8C; -.
DR PDBsum; 6RMH; -.
DR PDBsum; 6X9O; -.
DR PDBsum; 6YEJ; -.
DR PDBsum; 7DXJ; -.
DR PDBsum; 7DXK; -.
DR PDBsum; 8SAH; -.
DR BMRB; P42858; -.
DR EMDB; EMD-10793; -.
DR EMDB; EMD-28766; -.
DR EMDB; EMD-28767; -.
DR EMDB; EMD-2947; -.
DR EMDB; EMD-4937; -.
DR SASBDB; P42858; -.
DR SMR; P42858; -.
DR BioGRID; 109314; 452.
DR CORUM; P42858; -.
DR DIP; DIP-32492N; -.
DR ELM; P42858; -.
DR IntAct; P42858; 1111.
DR MINT; P42858; -.
DR STRING; 9606.ENSP00000347184; -.
DR BindingDB; P42858; -.
DR ChEMBL; CHEMBL5514; -.
DR DrugBank; DB09130; Copper.
DR MoonDB; P42858; Predicted.
DR TCDB; 8.A.222.1.1; the huntingtin (htt) family.
DR GlyCosmos; P42858; 3 sites, 1 glycan.
DR GlyGen; P42858; 7 sites, 1 O-linked glycan (7 sites).
DR iPTMnet; P42858; -.
DR MetOSite; P42858; -.
DR PhosphoSitePlus; P42858; -.
DR SwissPalm; P42858; -.
DR BioMuta; HTT; -.
DR DMDM; 296434520; -.
DR EPD; P42858; -.
DR jPOST; P42858; -.
DR MassIVE; P42858; -.
DR MaxQB; P42858; -.
DR PaxDb; 9606-ENSP00000347184; -.
DR PeptideAtlas; P42858; -.
DR ProteomicsDB; 55561; -.
DR Pumba; P42858; -.
DR ABCD; P42858; 5 sequenced antibodies.
DR Antibodypedia; 3449; 886 antibodies from 41 providers.
DR DNASU; 3064; -.
DR Ensembl; ENST00000355072.11; ENSP00000347184.5; ENSG00000197386.14.
DR GeneID; 3064; -.
DR KEGG; hsa:3064; -.
DR MANE-Select; ENST00000355072.11; ENSP00000347184.5; NM_001388492.1; NP_001375421.1.
DR UCSC; uc062uto.1; human.
DR AGR; HGNC:4851; -.
DR CTD; 3064; -.
DR DisGeNET; 3064; -.
DR GeneCards; HTT; -.
DR GeneReviews; HTT; -.
DR HGNC; HGNC:4851; HTT.
DR HPA; ENSG00000197386; Low tissue specificity.
DR MalaCards; HTT; -.
DR MIM; 143100; phenotype.
DR MIM; 613004; gene.
DR MIM; 617435; phenotype.
DR neXtProt; NX_P42858; -.
DR OpenTargets; ENSG00000197386; -.
DR Orphanet; 399; Huntington disease.
DR Orphanet; 248111; Juvenile Huntington disease.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA164741646; -.
DR VEuPathDB; HostDB:ENSG00000197386; -.
DR eggNOG; ENOG502QR1D; Eukaryota.
DR GeneTree; ENSGT00390000015863; -.
DR HOGENOM; CLU_000428_0_0_1; -.
DR InParanoid; P42858; -.
DR OMA; PNKMEEP; -.
DR OrthoDB; 6903at2759; -.
DR PhylomeDB; P42858; -.
DR TreeFam; TF323608; -.
DR PathwayCommons; P42858; -.
DR Reactome; R-HSA-9022692; Regulation of MECP2 expression and activity.
DR SignaLink; P42858; -.
DR SIGNOR; P42858; -.
DR BioGRID-ORCS; 3064; 35 hits in 1164 CRISPR screens.
DR ChiTaRS; HTT; human.
DR EvolutionaryTrace; P42858; -.
DR GeneWiki; Huntingtin; -.
DR GenomeRNAi; 3064; -.
DR Pharos; P42858; Tchem.
DR PRO; PR:P42858; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P42858; Protein.
DR Bgee; ENSG00000197386; Expressed in sural nerve and 134 other cell types or tissues.
DR ExpressionAtlas; P42858; baseline and differential.
DR Genevisible; P42858; HS.
DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005814; C:centriole; IDA:SYSCILIA_CCNET.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016234; C:inclusion body; IMP:CAFA.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IMP:CAFA.
DR GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO.
DR GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
DR GO; GO:0034452; F:dynactin binding; IPI:UniProtKB.
DR GO; GO:0045505; F:dynein intermediate chain binding; IDA:UniProtKB.
DR GO; GO:0031072; F:heat shock protein binding; IPI:CAFA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019900; F:kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
DR GO; GO:0005522; F:profilin binding; IPI:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0099111; P:microtubule-based transport; IBA:GO_Central.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:1905337; P:positive regulation of aggrephagy; IMP:ParkinsonsUK-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:CAFA.
DR GO; GO:0045724; P:positive regulation of cilium assembly; IMP:SYSCILIA_CCNET.
DR GO; GO:0031587; P:positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IDA:UniProtKB.
DR GO; GO:1904504; P:positive regulation of lipophagy; IMP:ParkinsonsUK-UCL.
DR GO; GO:1901526; P:positive regulation of mitophagy; IMP:ParkinsonsUK-UCL.
DR GO; GO:0031648; P:protein destabilization; IMP:CAFA.
DR GO; GO:1905289; P:regulation of CAMKK-AMPK signaling cascade; IMP:ARUK-UCL.
DR GO; GO:2000479; P:regulation of cAMP-dependent protein kinase activity; IMP:ARUK-UCL.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IMP:dictyBase.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:UniProtKB.
DR GO; GO:0047496; P:vesicle transport along microtubule; IMP:UniProtKB.
DR GO; GO:0042297; P:vocal learning; IMP:AgBase.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR048412; Htt_bridge.
DR InterPro; IPR048413; Htt_C-HEAT_rpt.
DR InterPro; IPR048411; Htt_N_HEAT_rpt-1.
DR InterPro; IPR000091; Huntingtin.
DR InterPro; IPR028426; Huntingtin_fam.
DR InterPro; IPR024613; Huntingtin_N_HEAT_rpt-2.
DR PANTHER; PTHR10170:SF10; HUNTINGTIN; 1.
DR PANTHER; PTHR10170; HUNTINGTON DISEASE PROTEIN; 1.
DR Pfam; PF20925; Htt_bridge; 1.
DR Pfam; PF20927; Htt_C-HEAT; 1.
DR Pfam; PF12372; Htt_N-HEAT; 1.
DR Pfam; PF20926; Htt_N-HEAT_1; 1.
DR PRINTS; PR00375; HUNTINGTIN.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Apoptosis; Cytoplasm; Cytoplasmic vesicle;
KW Disease variant; Endosome; Intellectual disability; Lipoprotein; Myristate;
KW Neurodegeneration; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Triplet repeat expansion; Ubl conjugation.
FT CHAIN 1..3142
FT /note="Huntingtin"
FT /id="PRO_0000083942"
FT CHAIN 551..584
FT /note="Huntingtin, myristoylated N-terminal fragment"
FT /id="PRO_0000447477"
FT REPEAT 204..241
FT /note="HEAT 1"
FT REPEAT 246..283
FT /note="HEAT 2"
FT REPEAT 316..360
FT /note="HEAT 3"
FT REPEAT 802..839
FT /note="HEAT 4"
FT REPEAT 902..940
FT /note="HEAT 5"
FT REGION 3..13
FT /note="Sufficient for interaction with TPR"
FT /evidence="ECO:0000269|PubMed:15654337"
FT REGION 14..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..502
FT /note="Interaction with ZDHHC17"
FT /evidence="ECO:0000269|PubMed:28757145"
FT REGION 517..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2330..2351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2633..2662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2395..2404
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 14..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..82
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2335..2349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 511..512
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000269|PubMed:9535906"
FT SITE 528..529
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000255"
FT SITE 550..551
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000269|PubMed:29802276"
FT SITE 584..585
FT /note="Cleavage; by caspase-6"
FT /evidence="ECO:0000269|PubMed:10770929"
FT SITE 587..588
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000255"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:21685499"
FT MOD_RES 176
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:21685499"
FT MOD_RES 234
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:21685499"
FT MOD_RES 343
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:21685499"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42859"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42859"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 442
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:21685499"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1179
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000269|PubMed:17611284"
FT MOD_RES 1199
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000269|PubMed:17611284,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1870
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231"
FT MOD_RES 1874
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT LIPID 551
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:24459296,
FT ECO:0000269|PubMed:29802276"
FT VARIANT 18
FT /note="Q -> QQQ"
FT /id="VAR_005268"
FT VARIANT 551
FT /note="G -> E (inhibits proteolytic cleavage at D-550;
FT abolishes post-translational myristoylation; results in
FT increased cleavage at D-511; dbSNP:rs118005095)"
FT /evidence="ECO:0000269|PubMed:29802276"
FT /id="VAR_081737"
FT VARIANT 703
FT /note="P -> L (in LOMARS; dbSNP:rs768047421)"
FT /evidence="ECO:0000269|PubMed:26740508"
FT /id="VAR_079026"
FT VARIANT 893
FT /note="G -> R (in dbSNP:rs363075)"
FT /id="VAR_060170"
FT VARIANT 1064
FT /note="V -> I (in dbSNP:rs35892913)"
FT /id="VAR_060171"
FT VARIANT 1091
FT /note="I -> M (in dbSNP:rs1143646)"
FT /id="VAR_060172"
FT VARIANT 1173
FT /note="T -> A (in dbSNP:rs3025843)"
FT /id="VAR_060173"
FT VARIANT 1260
FT /note="T -> M (found in a patient with Rett syndrome-like
FT phenotype; uncertain significance; dbSNP:rs34315806)"
FT /evidence="ECO:0000269|PubMed:26740508"
FT /id="VAR_060174"
FT VARIANT 1382
FT /note="E -> A (in dbSNP:rs3025837)"
FT /id="VAR_054017"
FT VARIANT 1385
FT /note="N -> H (in dbSNP:rs3025837)"
FT /id="VAR_060175"
FT VARIANT 1720
FT /note="T -> N (in dbSNP:rs363125)"
FT /id="VAR_060176"
FT VARIANT 2113
FT /note="D -> Y (in dbSNP:rs1143648)"
FT /id="VAR_060177"
FT VARIANT 2309
FT /note="Y -> H (in dbSNP:rs362331)"
FT /id="VAR_060178"
FT VARIANT 2717
FT /note="F -> L (in LOMARS; dbSNP:rs1085307052)"
FT /evidence="ECO:0000269|PubMed:27329733"
FT /id="VAR_079027"
FT VARIANT 2786
FT /note="V -> I (in dbSNP:rs362272)"
FT /evidence="ECO:0000269|PubMed:7903579"
FT /id="VAR_060179"
FT MUTAGEN 495
FT /note="I->A: Inhibits interaction with ZDHHC13 and
FT ZDHHC17."
FT /evidence="ECO:0000269|PubMed:26198635"
FT MUTAGEN 498..499
FT /note="QP->AA: Abolishes interaction with ZDHHC17."
FT /evidence="ECO:0000269|PubMed:28757145"
FT MUTAGEN 498
FT /note="Q->A: Inhibits interaction with ZDHHC13 and
FT ZDHHC17."
FT /evidence="ECO:0000269|PubMed:26198635"
FT MUTAGEN 499
FT /note="P->A: Inhibits interaction with ZDHHC13 and
FT ZDHHC17."
FT /evidence="ECO:0000269|PubMed:26198635"
FT MUTAGEN 511
FT /note="D->A: Loss of proteolytic cleavage."
FT /evidence="ECO:0000269|PubMed:9535906"
FT MUTAGEN 528
FT /note="D->A: No effect on proteolytic cleavage."
FT /evidence="ECO:0000269|PubMed:9535906"
FT MUTAGEN 550
FT /note="D->E: Loss of proteolytic cleavage. Loss of
FT myristoylation."
FT /evidence="ECO:0000269|PubMed:29802276"
FT MUTAGEN 551
FT /note="G->A: Loss of myristoylation."
FT /evidence="ECO:0000269|PubMed:24459296,
FT ECO:0000269|PubMed:29802276"
FT MUTAGEN 551
FT /note="G->S: Loss of myristoylation."
FT /evidence="ECO:0000269|PubMed:29802276"
FT MUTAGEN 584
FT /note="D->A: Loss of proteolytic cleavage."
FT /evidence="ECO:0000269|PubMed:10770929"
FT CONFLICT 823
FT /note="C -> S (in Ref. 2; BAA36753)"
FT /evidence="ECO:0000305"
FT HELIX 4..10
FT /evidence="ECO:0007829|PDB:4RAV"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:4RAV"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:3IOT"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:3IOT"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 119..132
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 142..157
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 159..175
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 180..191
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 202..217
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 222..239
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 245..256
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 264..279
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 284..297
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 309..321
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 351..364
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 370..385
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 389..396
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 400..403
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 676..678
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 680..692
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 696..699
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 704..706
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 709..725
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 727..731
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 732..734
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 741..743
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 750..758
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 762..764
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 765..782
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 787..797
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 804..806
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 808..815
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 820..838
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 843..853
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 854..858
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 862..873
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 877..886
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 890..893
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 894..896
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 903..910
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 911..913
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 914..917
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 921..934
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 935..937
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 949..961
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 996..1014
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1019..1035
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 1038..1040
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 1042..1045
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1065..1074
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 1076..1078
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1079..1081
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1083..1098
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1101..1103
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1135..1156
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1234..1250
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1262..1277
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1278..1280
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1283..1286
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 1287..1289
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1290..1300
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 1301..1303
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1305..1319
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 1324..1326
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 1356..1359
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1360..1372
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1422..1425
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1426..1438
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1442..1457
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1462..1465
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 1467..1469
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1470..1484
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 1491..1493
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1494..1506
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 1508..1515
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1517..1529
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 1530..1532
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 1534..1537
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1538..1550
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1563..1577
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 1578..1580
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1582..1598
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1602..1620
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1628..1640
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1643..1646
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1650..1656
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 1663..1665
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1666..1686
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1689..1698
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1703..1706
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1708..1715
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1736..1756
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 1760..1763
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1766..1788
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 1789..1791
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1793..1803
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 1808..1812
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1815..1823
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 1824..1828
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1830..1842
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 1848..1850
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1851..1854
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1889..1908
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1914..1929
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 1930..1932
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1934..1944
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1947..1958
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 1959..1965
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1967..1978
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1982..1984
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 1987..1994
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2002..2021
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2024..2030
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2033..2045
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2048..2051
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2053..2066
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2097..2108
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2116..2123
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2128..2130
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 2131..2136
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2142..2144
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2145..2156
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 2157..2159
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2163..2181
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 2192..2194
FT /evidence="ECO:0007829|PDB:8SAH"
FT STRAND 2196..2198
FT /evidence="ECO:0007829|PDB:8SAH"
FT HELIX 2201..2208
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2215..2217
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2218..2229
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2232..2234
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2237..2239
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2245..2266
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 2267..2269
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2272..2285
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2289..2295
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2301..2319
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2354..2368
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 2369..2374
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2379..2381
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 2386..2388
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2389..2400
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2403..2409
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2413..2417
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 2426..2429
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2437..2439
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2443..2456
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2461..2475
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2498..2512
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 2516..2518
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 2522..2524
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 2537..2542
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2543..2562
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2594..2596
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 2598..2600
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2619..2625
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 2663..2666
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2668..2680
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2694..2707
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 2708..2710
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2714..2730
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 2736..2738
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2739..2752
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 2757..2760
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2763..2771
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2776..2790
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2795..2798
FT /evidence="ECO:0007829|PDB:8SAH"
FT HELIX 2802..2816
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 2821..2824
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2826..2842
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 2844..2846
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 2851..2853
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2854..2863
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 2867..2869
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2872..2887
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 2893..2895
FT /evidence="ECO:0007829|PDB:8SAH"
FT HELIX 2897..2900
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 2904..2906
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2912..2928
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2952..2967
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2970..2987
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2990..2992
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 2994..3001
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 3009..3023
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 3024..3027
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 3031..3037
FT /evidence="ECO:0007829|PDB:6X9O"
FT STRAND 3040..3042
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 3049..3062
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 3067..3069
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 3070..3072
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 3073..3077
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 3085..3100
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 3101..3103
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 3106..3116
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 3117..3119
FT /evidence="ECO:0007829|PDB:6X9O"
FT TURN 3122..3126
FT /evidence="ECO:0007829|PDB:6X9O"
FT HELIX 3127..3135
FT /evidence="ECO:0007829|PDB:6X9O"
SQ SEQUENCE 3142 AA; 347603 MW; A267509E84D52F0D CRC64;
MATLEKLMKA FESLKSFQQQ QQQQQQQQQQ QQQQQQQQPP PPPPPPPPPQ LPQPPPQAQP
LLPQPQPPPP PPPPPPGPAV AEEPLHRPKK ELSATKKDRV NHCLTICENI VAQSVRNSPE
FQKLLGIAME LFLLCSDDAE SDVRMVADEC LNKVIKALMD SNLPRLQLEL YKEIKKNGAP
RSLRAALWRF AELAHLVRPQ KCRPYLVNLL PCLTRTSKRP EESVQETLAA AVPKIMASFG
NFANDNEIKV LLKAFIANLK SSSPTIRRTA AGSAVSICQH SRRTQYFYSW LLNVLLGLLV
PVEDEHSTLL ILGVLLTLRY LVPLLQQQVK DTSLKGSFGV TRKEMEVSPS AEQLVQVYEL
TLHHTQHQDH NVVTGALELL QQLFRTPPPE LLQTLTAVGG IGQLTAAKEE SGGRSRSGSI
VELIAGGGSS CSPVLSRKQK GKVLLGEEEA LEDDSESRSD VSSSALTASV KDEISGELAA
SSGVSTPGSA GHDIITEQPR SQHTLQADSV DLASCDLTSS ATDGDEEDIL SHSSSQVSAV
PSDPAMDLND GTQASSPISD SSQTTTEGPD SAVTPSDSSE IVLDGTDNQY LGLQIGQPQD
EDEEATGILP DEASEAFRNS SMALQQAHLL KNMSHCRQPS DSSVDKFVLR DEATEPGDQE
NKPCRIKGDI GQSTDDDSAP LVHCVRLLSA SFLLTGGKNV LVPDRDVRVS VKALALSCVG
AAVALHPESF FSKLYKVPLD TTEYPEEQYV SDILNYIDHG DPQVRGATAI LCGTLICSIL
SRSRFHVGDW MGTIRTLTGN TFSLADCIPL LRKTLKDESS VTCKLACTAV RNCVMSLCSS
SYSELGLQLI IDVLTLRNSS YWLVRTELLE TLAEIDFRLV SFLEAKAENL HRGAHHYTGL
LKLQERVLNN VVIHLLGDED PRVRHVAAAS LIRLVPKLFY KCDQGQADPV VAVARDQSSV
YLKLLMHETQ PPSHFSVSTI TRIYRGYNLL PSITDVTMEN NLSRVIAAVS HELITSTTRA
LTFGCCEALC LLSTAFPVCI WSLGWHCGVP PLSASDESRK SCTVGMATMI LTLLSSAWFP
LDLSAHQDAL ILAGNLLAAS APKSLRSSWA SEEEANPAAT KQEEVWPALG DRALVPMVEQ
LFSHLLKVIN ICAHVLDDVA PGPAIKAALP SLTNPPSLSP IRRKGKEKEP GEQASVPLSP
KKGSEASAAS RQSDTSGPVT TSKSSSLGSF YHLPSYLKLH DVLKATHANY KVTLDLQNST
EKFGGFLRSA LDVLSQILEL ATLQDIGKCV EEILGYLKSC FSREPMMATV CVQQLLKTLF
GTNLASQFDG LSSNPSKSQG RAQRLGSSSV RPGLYHYCFM APYTHFTQAL ADASLRNMVQ
AEQENDTSGW FDVLQKVSTQ LKTNLTSVTK NRADKNAIHN HIRLFEPLVI KALKQYTTTT
CVQLQKQVLD LLAQLVQLRV NYCLLDSDQV FIGFVLKQFE YIEVGQFRES EAIIPNIFFF
LVLLSYERYH SKQIIGIPKI IQLCDGIMAS GRKAVTHAIP ALQPIVHDLF VLRGTNKADA
GKELETQKEV VVSMLLRLIQ YHQVLEMFIL VLQQCHKENE DKWKRLSRQI ADIILPMLAK
QQMHIDSHEA LGVLNTLFEI LAPSSLRPVD MLLRSMFVTP NTMASVSTVQ LWISGILAIL
RVLISQSTED IVLSRIQELS FSPYLISCTV INRLRDGDST STLEEHSEGK QIKNLPEETF
SRFLLQLVGI LLEDIVTKQL KVEMSEQQHT FYCQELGTLL MCLIHIFKSG MFRRITAAAT
RLFRSDGCGG SFYTLDSLNL RARSMITTHP ALVLLWCQIL LLVNHTDYRW WAEVQQTPKR
HSLSSTKLLS PQMSGEEEDS DLAAKLGMCN REIVRRGALI LFCDYVCQNL HDSEHLTWLI
VNHIQDLISL SHEPPVQDFI SAVHRNSAAS GLFIQAIQSR CENLSTPTML KKTLQCLEGI
HLSQSGAVLT LYVDRLLCTP FRVLARMVDI LACRRVEMLL AANLQSSMAQ LPMEELNRIQ
EYLQSSGLAQ RHQRLYSLLD RFRLSTMQDS LSPSPPVSSH PLDGDGHVSL ETVSPDKDWY
VHLVKSQCWT RSDSALLEGA ELVNRIPAED MNAFMMNSEF NLSLLAPCLS LGMSEISGGQ
KSALFEAARE VTLARVSGTV QQLPAVHHVF QPELPAEPAA YWSKLNDLFG DAALYQSLPT
LARALAQYLV VVSKLPSHLH LPPEKEKDIV KFVVATLEAL SWHLIHEQIP LSLDLQAGLD
CCCLALQLPG LWSVVSSTEF VTHACSLIYC VHFILEAVAV QPGEQLLSPE RRTNTPKAIS
EEEEEVDPNT QNPKYITAAC EMVAEMVESL QSVLALGHKR NSGVPAFLTP LLRNIIISLA
RLPLVNSYTR VPPLVWKLGW SPKPGGDFGT AFPEIPVEFL QEKEVFKEFI YRINTLGWTS
RTQFEETWAT LLGVLVTQPL VMEQEESPPE EDTERTQINV LAVQAITSLV LSAMTVPVAG
NPAVSCLEQQ PRNKPLKALD TRFGRKLSII RGIVEQEIQA MVSKRENIAT HHLYQAWDPV
PSLSPATTGA LISHEKLLLQ INPERELGSM SYKLGQVSIH SVWLGNSITP LREEEWDEEE
EEEADAPAPS SPPTSPVNSR KHRAGVDIHS CSQFLLELYS RWILPSSSAR RTPAILISEV
VRSLLVVSDL FTERNQFELM YVTLTELRRV HPSEDEILAQ YLVPATCKAA AVLGMDKAVA
EPVSRLLEST LRSSHLPSRV GALHGVLYVL ECDLLDDTAK QLIPVISDYL LSNLKGIAHC
VNIHSQQHVL VMCATAFYLI ENYPLDVGPE FSASIIQMCG VMLSGSEEST PSIIYHCALR
GLERLLLSEQ LSRLDAESLV KLSVDRVNVH SPHRAMAALG LMLTCMYTGK EKVSPGRTSD
PNPAAPDSES VIVAMERVSV LFDRIRKGFP CEARVVARIL PQFLDDFFPP QDIMNKVIGE
FLSNQQPYPQ FMATVVYKVF QTLHSTGQSS MVRDWVMLSL SNFTQRAPVA MATWSLSCFF
VSASTSPWVA AILPHVISRM GKLEQVDVNL FCLVATDFYR HQIEEELDRR AFQSVLEVVA
APGSPYHRLL TCLRNVHKVT TC
//
