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Database: UniProt
Entry: Q9ULU4
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Original site: Q9ULU4 
ID   PKCB1_HUMAN             Reviewed;        1186 AA.
AC   Q9ULU4; B3KVL2; B7Z2A8; B7Z3E0; B7Z680; B7ZM62; E1P5U5; F5H0X3;
AC   H7C0U2; J3KPU3; Q13517; Q2HXV1; Q2HXV2; Q2HXV3; Q2HXV4; Q2HXV7;
AC   Q2HXV8; Q2HXV9; Q2HXW0; Q2HXW1; Q2HXW2; Q4JJ94; Q4JJ95; Q5TH09;
AC   Q5TH11; Q6MZM1; Q8WXC5; Q9H1F3; Q9H1F4; Q9H1F5; Q9H1L8; Q9H1L9;
AC   Q9H2G5; Q9NYN3; Q9UIX6;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2002, sequence version 2.
DT   08-MAY-2019, entry version 185.
DE   RecName: Full=Protein kinase C-binding protein 1;
DE   AltName: Full=Cutaneous T-cell lymphoma-associated antigen se14-3;
DE            Short=CTCL-associated antigen se14-3;
DE   AltName: Full=Rack7;
DE   AltName: Full=Zinc finger MYND domain-containing protein 8;
GN   Name=ZMYND8; Synonyms=KIAA1125, PRKCBP1, RACK7;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH PRKCB1.
RC   TISSUE=Hippocampus;
RX   PubMed=11003709; DOI=10.1007/s003350010174;
RA   Fossey S.C., Kuroda S., Price J.A., Pendleton J.K., Freedman B.I.,
RA   Bowden D.W.;
RT   "Identification and characterization of PRKCBP1, a candidate RACK-like
RT   protein.";
RL   Mamm. Genome 11:919-925(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
RC   TISSUE=Testis;
RX   PubMed=11149944; DOI=10.1073/pnas.98.2.629;
RA   Eichmueller S., Usener D., Dummer R., Stein A., Thiel D.,
RA   Schadendorf D.;
RT   "Serological detection of cutaneous T-cell lymphoma-associated
RT   antigens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:629-634(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 7 AND 8), AND VARIANT ALA-752.
RC   TISSUE=Mammary tumor;
RA   Mikhailik A., Keller J., Yang J., Hearing P., Bar-Sagi D.;
RT   "Characterization of a novel BS69-related transcriptional repressor,
RT   BSR.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5; 7; 10; 12; 13; 14; 15; 16 AND
RP   18).
RA   Grkovic S., Velasco G., Ansieau S.;
RT   "Characterization of RACK7, a novel heterochromatin and mitotic
RT   chromosome associated protein.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA   Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT   "Characterization of cDNA clones selected by the GeneMark analysis
RT   from size-fractionated cDNA libraries from human brain.";
RL   DNA Res. 6:329-336(1999).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 11; 19; 20 AND 23).
RC   TISSUE=Amygdala, Brain, Hippocampus, and Trachea;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
RC   TISSUE=Salivary gland;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA   Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA   Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA   Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA   Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA   Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA   Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA   Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA   Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA   Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA   Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA   Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA   Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 17).
RC   TISSUE=Brain, Eye, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; SER-462; SER-465;
RP   SER-486; SER-490; SER-495; THR-541; SER-547 AND SER-756, AND
RP   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   [14]
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.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; SER-486; SER-490
RP   AND SER-495, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [16]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-413, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-404; SER-406; SER-486;
RP   SER-495 AND SER-668, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [18]
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.,
RA   Buerckstuemmer T., 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   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425; SER-432; SER-444;
RP   SER-490; SER-547; SER-682; THR-746; SER-754 AND SER-756, AND
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.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-406; SER-417;
RP   SER-425; SER-444; SER-460; SER-465; SER-495; SER-514; SER-523;
RP   SER-547; THR-563; SER-652; SER-655; SER-668; SER-737; SER-756;
RP   SER-1119 AND SER-1141, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   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   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; SER-490; SER-547;
RP   SER-668; SER-707 AND SER-709, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [22]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-611 AND LYS-645, SUMOYLATION
RP   [LARGE SCALE ANALYSIS] AT LYS-12 (ISOFORMS 10; 12; 13; 14; 15; 16; 17;
RP   18; 22; 5; 7 AND 8), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [23]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-611, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA   Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL   Cell Rep. 10:1778-1791(2015).
RN   [24]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-611 AND LYS-645, SUMOYLATION
RP   [LARGE SCALE ANALYSIS] AT LYS-12 (ISOFORMS 10; 12; 13; 14; 15; 16; 17;
RP   18; 22; 5; 7 AND 8), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.O114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to
RT   replication stress reveals novel small ubiquitin-like modified target
RT   proteins and acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [25]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-56; LYS-70; LYS-390;
RP   LYS-413; LYS-453; LYS-505; LYS-530; LYS-549; LYS-611; LYS-645; LYS-657
RP   AND LYS-1115, SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-12 (ISOFORMS
RP   10; 12; 13; 14; 15; 16; 17; 18; 22; 5; 7 AND 8), AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-
RT   modification with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 93-426, FUNCTION, INTERACTION
RP   WITH KDM5D; KDM1A AND HISTONE H3, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF ASP-76; ASP-79; ASP-84; ASP-88; PHE-89; GLU-104 AND
RP   227-TYR-ASN-228.
RX   PubMed=27477906; DOI=10.1016/j.molcel.2016.06.035;
RA   Li N., Li Y., Lv J., Zheng X., Wen H., Shen H., Zhu G., Chen T.Y.,
RA   Dhar S.S., Kan P.Y., Wang Z., Shiekhattar R., Shi X., Lan F., Chen K.,
RA   Li W., Li H., Lee M.G.;
RT   "ZMYND8 reads the dual histone mark H3K4me1-H3K14ac to antagonize the
RT   expression of metastasis-linked genes.";
RL   Mol. Cell 63:470-484(2016).
RN   [27] {ECO:0000244|PDB:5Y1Z}
RP   X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 83-406 IN COMPLEX WITH ZINC
RP   AND DBN1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF VAL-240; HIS-311
RP   AND ASP-312.
RX   PubMed=28966017; DOI=10.1016/j.str.2017.08.014;
RA   Yao N., Li J., Liu H., Wan J., Liu W., Zhang M.;
RT   "The Structure of the ZMYND8/Drebrin Complex Suggests a Cytoplasmic
RT   Sequestering Mechanism of ZMYND8 by Drebrin.";
RL   Structure 25:1657-1666(2017).
CC   -!- FUNCTION: May act as a transcriptional corepressor for KDM5D.
CC       Required for KDM5D-mediated down-regulation of diverse metastasis-
CC       associated genes; the function seems to involve the recognition of
CC       the dual histone signature H3K4me1-H3K14ac. Suppresses prostate
CC       cancer cell invasion. {ECO:0000269|PubMed:27477906}.
CC   -!- SUBUNIT: Interacts in vitro with PRKCB1 (PubMed:11003709).
CC       Interacts with KDM5D and KDM1A (PubMed:27477906). Interacts with
CC       histone H3 (via N-terminus) that is both methylated at 'Lys-4'
CC       (H3K4me1) and acetylated at 'Lys-14' (H3K14ac), and with histone
CC       H3 (via N-terminus) unmodified at 'Lys-4' (H3K4me0) and acetylated
CC       at 'Lys-14' (H3K14ac) (PubMed:27477906). Interacts (via PHD-type
CC       Zinc finger, Bromo and PWWP domains) with DBN1 (via ADF-H domain);
CC       the interaction leads to sequestering of ZMYND8 in the cytoplasm
CC       (PubMed:28966017). {ECO:0000269|PubMed:11003709,
CC       ECO:0000269|PubMed:27477906, ECO:0000269|PubMed:28966017}.
CC   -!- INTERACTION:
CC       P41182:BCL6; NbExp=3; IntAct=EBI-765834, EBI-765407;
CC       Q16643:DBN1; NbExp=4; IntAct=EBI-765834, EBI-351394;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27477906,
CC       ECO:0000269|PubMed:28966017}. Cytoplasm
CC       {ECO:0000269|PubMed:28966017}. Note=Sequestered in the cytoplasm
CC       through the interaction with DBN1. {ECO:0000269|PubMed:28966017}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=23;
CC       Name=1;
CC         IsoId=Q9ULU4-1; Sequence=Displayed;
CC         Note=No experimental confirmation available.;
CC       Name=2;
CC         IsoId=Q9ULU4-2; Sequence=VSP_000566, VSP_000568;
CC         Note=Ref.1 (AAF71262) sequence is in conflict in position:
CC         297:T->S. {ECO:0000305};
CC       Name=3;
CC         IsoId=Q9ULU4-3; Sequence=VSP_000564, VSP_000568;
CC       Name=4;
CC         IsoId=Q9ULU4-4; Sequence=VSP_000565, VSP_000568;
CC       Name=5;
CC         IsoId=Q9ULU4-5; Sequence=VSP_000563, VSP_000567;
CC         Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
CC         with G-Cter in SUMO2) at position 12.
CC         {ECO:0000244|PubMed:25218447, ECO:0000244|PubMed:25755297,
CC         ECO:0000244|PubMed:28112733};
CC       Name=6;
CC         IsoId=Q9ULU4-6; Sequence=VSP_000564, VSP_000568, VSP_000570;
CC         Note=No experimental confirmation available.;
CC       Name=7;
CC         IsoId=Q9ULU4-7; Sequence=VSP_000563, VSP_000570;
CC         Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
CC         with G-Cter in SUMO2) at position 12.
CC         {ECO:0000244|PubMed:25218447, ECO:0000244|PubMed:25755297,
CC         ECO:0000244|PubMed:28112733};
CC       Name=8;
CC         IsoId=Q9ULU4-8; Sequence=VSP_000563, VSP_017096, VSP_000570;
CC         Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
CC         with G-Cter in SUMO2) at position 12.
CC         {ECO:0000244|PubMed:25218447, ECO:0000244|PubMed:25755297,
CC         ECO:0000244|PubMed:28112733};
CC       Name=9;
CC         IsoId=Q9ULU4-9; Sequence=VSP_000568, VSP_000570;
CC         Note=No experimental confirmation available.;
CC       Name=10;
CC         IsoId=Q9ULU4-10; Sequence=VSP_000563;
CC         Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
CC         with G-Cter in SUMO2) at position 12.
CC         {ECO:0000244|PubMed:25218447, ECO:0000244|PubMed:25755297,
CC         ECO:0000244|PubMed:28112733};
CC       Name=11;
CC         IsoId=Q9ULU4-11; Sequence=VSP_000570;
CC       Name=12;
CC         IsoId=Q9ULU4-12; Sequence=VSP_000563, VSP_000568;
CC         Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
CC         with G-Cter in SUMO2) at position 12.
CC         {ECO:0000244|PubMed:25218447, ECO:0000244|PubMed:25755297,
CC         ECO:0000244|PubMed:28112733};
CC       Name=13;
CC         IsoId=Q9ULU4-13; Sequence=VSP_000563, VSP_000568, VSP_000570;
CC         Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
CC         with G-Cter in SUMO2) at position 12.
CC         {ECO:0000244|PubMed:25218447, ECO:0000244|PubMed:25755297,
CC         ECO:0000244|PubMed:28112733};
CC       Name=14;
CC         IsoId=Q9ULU4-14; Sequence=VSP_000563, VSP_000567, VSP_000568;
CC         Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
CC         with G-Cter in SUMO2) at position 12.
CC         {ECO:0000244|PubMed:25218447, ECO:0000244|PubMed:25755297,
CC         ECO:0000244|PubMed:28112733};
CC       Name=15;
CC         IsoId=Q9ULU4-15; Sequence=VSP_000563, VSP_000567, VSP_053400,
CC                                   VSP_000568;
CC         Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
CC         with G-Cter in SUMO2) at position 12.
CC         {ECO:0000244|PubMed:25218447, ECO:0000244|PubMed:25755297,
CC         ECO:0000244|PubMed:28112733};
CC       Name=16;
CC         IsoId=Q9ULU4-16; Sequence=VSP_000563, VSP_000567, VSP_000568,
CC                                   VSP_000570;
CC         Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
CC         with G-Cter in SUMO2) at position 12.
CC         {ECO:0000244|PubMed:25218447, ECO:0000244|PubMed:25755297,
CC         ECO:0000244|PubMed:28112733};
CC       Name=17;
CC         IsoId=Q9ULU4-17; Sequence=VSP_000563, VSP_000567, VSP_017096;
CC         Note=No experimental confirmation available. Contains a glycyl
CC         lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) at
CC         position 12. {ECO:0000244|PubMed:25218447,
CC         ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:28112733};
CC       Name=18;
CC         IsoId=Q9ULU4-18; Sequence=VSP_000563, VSP_000567, VSP_053400;
CC         Note=No experimental confirmation available. Contains a glycyl
CC         lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) at
CC         position 12. {ECO:0000244|PubMed:25218447,
CC         ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:28112733};
CC       Name=19;
CC         IsoId=Q9ULU4-19; Sequence=VSP_054810, VSP_000570;
CC         Note=No experimental confirmation available.;
CC       Name=20;
CC         IsoId=Q9ULU4-20; Sequence=VSP_054811, VSP_000567;
CC         Note=No experimental confirmation available.;
CC       Name=21;
CC         IsoId=Q9ULU4-21; Sequence=VSP_000567, VSP_000568;
CC         Note=No experimental confirmation available.;
CC       Name=22;
CC         IsoId=Q9ULU4-22; Sequence=VSP_000563, VSP_000568, VSP_054814,
CC                                   VSP_000570;
CC         Note=Gene prediction based on EST data. Contains a glycyl lysine
CC         isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) at
CC         position 12. {ECO:0000244|PubMed:25218447,
CC         ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:28112733};
CC       Name=23;
CC         IsoId=Q9ULU4-23; Sequence=VSP_000567, VSP_054812, VSP_000568,
CC                                   VSP_000570;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined with highest
CC       expression in brain, lung, pancreas, and placenta. Expressed in
CC       cutaneous T-cell lymphomas (CTCL).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC72244.1; Type=Frameshift; Positions=816; Evidence={ECO:0000305};
CC       Sequence=BAA86439.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; AF233453; AAF71262.1; -; mRNA.
DR   EMBL; U48251; AAC72244.1; ALT_FRAME; mRNA.
DR   EMBL; AF454056; AAL50790.1; -; mRNA.
DR   EMBL; AF273045; AAG34905.1; -; mRNA.
DR   EMBL; DQ082998; AAY85630.1; -; mRNA.
DR   EMBL; DQ082999; AAY85631.1; -; mRNA.
DR   EMBL; DQ368669; ABC86680.1; -; mRNA.
DR   EMBL; DQ368670; ABC86681.1; -; mRNA.
DR   EMBL; DQ368671; ABC86682.1; -; mRNA.
DR   EMBL; DQ368672; ABC86683.1; -; mRNA.
DR   EMBL; DQ368673; ABC86684.1; -; mRNA.
DR   EMBL; DQ368674; ABC86685.1; -; mRNA.
DR   EMBL; DQ368677; ABC86688.1; -; mRNA.
DR   EMBL; DQ368678; ABC86689.1; -; mRNA.
DR   EMBL; DQ368679; ABC86690.1; -; mRNA.
DR   EMBL; DQ368680; ABC86691.1; -; mRNA.
DR   EMBL; AB032951; BAA86439.1; ALT_INIT; mRNA.
DR   EMBL; AK122966; BAG53824.1; -; mRNA.
DR   EMBL; AK294511; BAH11794.1; -; mRNA.
DR   EMBL; AK295747; BAH12176.1; -; mRNA.
DR   EMBL; AK299899; BAH13166.1; -; mRNA.
DR   EMBL; BX641005; CAE46008.1; -; mRNA.
DR   EMBL; AL031666; CAI21842.1; -; Genomic_DNA.
DR   EMBL; AL049540; CAI21842.1; JOINED; Genomic_DNA.
DR   EMBL; AL022342; CAI21842.1; JOINED; Genomic_DNA.
DR   EMBL; AL049540; CAI23169.1; -; Genomic_DNA.
DR   EMBL; AL031666; CAI23169.1; JOINED; Genomic_DNA.
DR   EMBL; AL022342; CAI23169.1; JOINED; Genomic_DNA.
DR   EMBL; AL049540; CAI23168.1; -; Genomic_DNA.
DR   EMBL; AL031666; CAI23168.1; JOINED; Genomic_DNA.
DR   EMBL; AL390212; CAI23168.1; JOINED; Genomic_DNA.
DR   EMBL; CH471077; EAW75703.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW75706.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW75709.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW75711.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW75712.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW75715.1; -; Genomic_DNA.
DR   EMBL; BC030721; AAH30721.2; -; mRNA.
DR   EMBL; BC136608; AAI36609.1; -; mRNA.
DR   EMBL; BC144289; AAI44290.1; -; mRNA.
DR   CCDS; CCDS13404.1; -. [Q9ULU4-12]
DR   CCDS; CCDS13405.1; -. [Q9ULU4-13]
DR   CCDS; CCDS46613.1; -. [Q9ULU4-14]
DR   CCDS; CCDS63300.1; -. [Q9ULU4-11]
DR   CCDS; CCDS63301.1; -. [Q9ULU4-9]
DR   CCDS; CCDS63303.1; -. [Q9ULU4-18]
DR   CCDS; CCDS63304.1; -. [Q9ULU4-17]
DR   CCDS; CCDS63306.1; -. [Q9ULU4-7]
DR   CCDS; CCDS74738.1; -. [Q9ULU4-20]
DR   CCDS; CCDS86961.1; -. [Q9ULU4-1]
DR   CCDS; CCDS86962.1; -. [Q9ULU4-19]
DR   RefSeq; NP_001268700.1; NM_001281771.2. [Q9ULU4-17]
DR   RefSeq; NP_001268701.1; NM_001281772.2. [Q9ULU4-20]
DR   RefSeq; NP_001268702.1; NM_001281773.2. [Q9ULU4-11]
DR   RefSeq; NP_001268703.1; NM_001281774.2. [Q9ULU4-9]
DR   RefSeq; NP_001268704.1; NM_001281775.2. [Q9ULU4-7]
DR   RefSeq; NP_001268705.1; NM_001281776.2. [Q9ULU4-8]
DR   RefSeq; NP_001268706.1; NM_001281777.2. [Q9ULU4-16]
DR   RefSeq; NP_001268707.1; NM_001281778.2. [Q9ULU4-5]
DR   RefSeq; NP_001268710.1; NM_001281781.2. [Q9ULU4-15]
DR   RefSeq; NP_001268711.1; NM_001281782.2.
DR   RefSeq; NP_001268712.1; NM_001281783.2. [Q9ULU4-10]
DR   RefSeq; NP_001268713.1; NM_001281784.2. [Q9ULU4-18]
DR   RefSeq; NP_036540.3; NM_012408.5. [Q9ULU4-12]
DR   RefSeq; NP_898868.1; NM_183047.3. [Q9ULU4-13]
DR   RefSeq; NP_898869.1; NM_183048.3. [Q9ULU4-14]
DR   RefSeq; XP_005260413.1; XM_005260356.4.
DR   RefSeq; XP_005260417.1; XM_005260360.4. [Q9ULU4-11]
DR   RefSeq; XP_005260423.1; XM_005260366.2. [Q9ULU4-1]
DR   RefSeq; XP_006723825.1; XM_006723762.3. [Q9ULU4-11]
DR   RefSeq; XP_011527053.1; XM_011528751.1. [Q9ULU4-11]
DR   RefSeq; XP_016883250.1; XM_017027761.1. [Q9ULU4-11]
DR   RefSeq; XP_016883256.1; XM_017027767.1. [Q9ULU4-1]
DR   RefSeq; XP_016883257.1; XM_017027768.1.
DR   PDB; 4COS; X-ray; 1.67 A; A=83-406.
DR   PDB; 5B73; X-ray; 1.80 A; A=73-406.
DR   PDB; 5MQ4; X-ray; 2.70 A; A/B/C/D/E/F=949-1073.
DR   PDB; 5Y1Z; X-ray; 2.68 A; C/D=83-406.
DR   PDBsum; 4COS; -.
DR   PDBsum; 5B73; -.
DR   PDBsum; 5MQ4; -.
DR   PDBsum; 5Y1Z; -.
DR   SMR; Q9ULU4; -.
DR   BioGrid; 117146; 65.
DR   IntAct; Q9ULU4; 47.
DR   MINT; Q9ULU4; -.
DR   STRING; 9606.ENSP00000420095; -.
DR   BindingDB; Q9ULU4; -.
DR   ChEMBL; CHEMBL3627580; -.
DR   iPTMnet; Q9ULU4; -.
DR   PhosphoSitePlus; Q9ULU4; -.
DR   BioMuta; ZMYND8; -.
DR   DMDM; 25453223; -.
DR   EPD; Q9ULU4; -.
DR   jPOST; Q9ULU4; -.
DR   PeptideAtlas; Q9ULU4; -.
DR   PRIDE; Q9ULU4; -.
DR   ProteomicsDB; 85109; -.
DR   ProteomicsDB; 85110; -. [Q9ULU4-10]
DR   ProteomicsDB; 85111; -. [Q9ULU4-11]
DR   ProteomicsDB; 85112; -. [Q9ULU4-12]
DR   ProteomicsDB; 85113; -. [Q9ULU4-13]
DR   ProteomicsDB; 85114; -. [Q9ULU4-14]
DR   ProteomicsDB; 85115; -. [Q9ULU4-2]
DR   ProteomicsDB; 85116; -. [Q9ULU4-3]
DR   ProteomicsDB; 85117; -. [Q9ULU4-4]
DR   ProteomicsDB; 85118; -. [Q9ULU4-5]
DR   ProteomicsDB; 85119; -. [Q9ULU4-6]
DR   ProteomicsDB; 85120; -. [Q9ULU4-7]
DR   ProteomicsDB; 85121; -. [Q9ULU4-8]
DR   ProteomicsDB; 85122; -. [Q9ULU4-9]
DR   Ensembl; ENST00000262975; ENSP00000262975; ENSG00000101040. [Q9ULU4-9]
DR   Ensembl; ENST00000311275; ENSP00000312237; ENSG00000101040. [Q9ULU4-1]
DR   Ensembl; ENST00000352431; ENSP00000335537; ENSG00000101040. [Q9ULU4-12]
DR   Ensembl; ENST00000355972; ENSP00000348246; ENSG00000101040. [Q9ULU4-11]
DR   Ensembl; ENST00000360911; ENSP00000354166; ENSG00000101040. [Q9ULU4-14]
DR   Ensembl; ENST00000372023; ENSP00000361093; ENSG00000101040. [Q9ULU4-23]
DR   Ensembl; ENST00000396281; ENSP00000379577; ENSG00000101040. [Q9ULU4-20]
DR   Ensembl; ENST00000446994; ENSP00000396725; ENSG00000101040. [Q9ULU4-11]
DR   Ensembl; ENST00000458360; ENSP00000392964; ENSG00000101040. [Q9ULU4-17]
DR   Ensembl; ENST00000461685; ENSP00000418210; ENSG00000101040. [Q9ULU4-13]
DR   Ensembl; ENST00000471951; ENSP00000420095; ENSG00000101040. [Q9ULU4-7]
DR   Ensembl; ENST00000536340; ENSP00000439800; ENSG00000101040. [Q9ULU4-19]
DR   Ensembl; ENST00000540497; ENSP00000443086; ENSG00000101040. [Q9ULU4-18]
DR   GeneID; 23613; -.
DR   KEGG; hsa:23613; -.
DR   UCSC; uc002xss.3; human. [Q9ULU4-1]
DR   CTD; 23613; -.
DR   DisGeNET; 23613; -.
DR   GeneCards; ZMYND8; -.
DR   H-InvDB; HIX0015888; -.
DR   HGNC; HGNC:9397; ZMYND8.
DR   HPA; HPA020949; -.
DR   neXtProt; NX_Q9ULU4; -.
DR   OpenTargets; ENSG00000101040; -.
DR   PharmGKB; PA162409890; -.
DR   GeneTree; ENSGT00940000154897; -.
DR   HOGENOM; HOG000230951; -.
DR   InParanoid; Q9ULU4; -.
DR   OMA; AAKIDKQ; -.
DR   OrthoDB; 369818at2759; -.
DR   PhylomeDB; Q9ULU4; -.
DR   TreeFam; TF317221; -.
DR   ChiTaRS; ZMYND8; human.
DR   GeneWiki; ZMYND8; -.
DR   GenomeRNAi; 23613; -.
DR   PRO; PR:Q9ULU4; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   Bgee; ENSG00000101040; Expressed in 247 organ(s), highest expression level in caput epididymis.
DR   ExpressionAtlas; Q9ULU4; baseline and differential.
DR   Genevisible; Q9ULU4; HS.
DR   GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
DR   GO; GO:0043198; C:dendritic shaft; IEA:Ensembl.
DR   GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
DR   GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; IDA:UniProtKB.
DR   GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR   GO; GO:0070491; F:repressing transcription factor binding; ISS:BHF-UCL.
DR   GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0098815; P:modulation of excitatory postsynaptic potential; IEA:Ensembl.
DR   GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
DR   GO; GO:0060999; P:positive regulation of dendritic spine development; IEA:Ensembl.
DR   GO; GO:1902952; P:positive regulation of dendritic spine maintenance; IEA:Ensembl.
DR   GO; GO:0051491; P:positive regulation of filopodium assembly; IEA:Ensembl.
DR   GO; GO:1902897; P:regulation of postsynaptic density protein 95 clustering; IEA:Ensembl.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd05508; Bromo_RACK7; 1.
DR   CDD; cd05841; BS69_related; 1.
DR   Gene3D; 1.20.920.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR000313; PWWP_dom.
DR   InterPro; IPR037967; RACK7_Bromo_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR021931; ZMYND8.
DR   InterPro; IPR035505; ZMYND8/11_PWWP.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR002893; Znf_MYND.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF12064; DUF3544; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00293; PWWP; 1.
DR   SUPFAM; SSF47370; SSF47370; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS50812; PWWP; 1.
DR   PROSITE; PS01360; ZF_MYND_1; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Bromodomain;
KW   Complete proteome; Cytoplasm; Isopeptide bond; Metal-binding; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1   1186       Protein kinase C-binding protein 1.
FT                                /FTId=PRO_0000211209.
FT   DOMAIN      165    235       Bromo. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00035}.
FT   DOMAIN      277    327       PWWP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00162}.
FT   ZN_FING      88    133       PHD-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1028   1062       MYND-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00134}.
FT   REGION       75    406       Interaction with histone H3K14ac.
FT                                {ECO:0000269|PubMed:27477906}.
FT   REGION       75    268       Interaction with histone H3K4me0.
FT                                {ECO:0000269|PubMed:27477906}.
FT   REGION     1147   1186       Interaction with PRKCB1.
FT   COMPBIAS     43     47       Poly-Lys.
FT   COMPBIAS    838    854       Poly-Gln.
FT   COMPBIAS   1089   1092       Poly-Ser.
FT   METAL        91     91       Zinc 1. {ECO:0000244|PDB:5Y1Z,
FT                                ECO:0000269|PubMed:28966017}.
FT   METAL        94     94       Zinc 1. {ECO:0000244|PDB:5Y1Z,
FT                                ECO:0000269|PubMed:28966017}.
FT   METAL       103    103       Zinc 2. {ECO:0000244|PDB:5Y1Z,
FT                                ECO:0000269|PubMed:28966017}.
FT   METAL       106    106       Zinc 2. {ECO:0000244|PDB:5Y1Z,
FT                                ECO:0000269|PubMed:28966017}.
FT   METAL       111    111       Zinc 1; via pros nitrogen.
FT                                {ECO:0000244|PDB:5Y1Z,
FT                                ECO:0000269|PubMed:28966017}.
FT   METAL       114    114       Zinc 1. {ECO:0000244|PDB:5Y1Z,
FT                                ECO:0000269|PubMed:28966017}.
FT   METAL       127    127       Zinc 2. {ECO:0000244|PDB:5Y1Z,
FT                                ECO:0000269|PubMed:28966017}.
FT   METAL       130    130       Zinc 2. {ECO:0000244|PDB:5Y1Z,
FT                                ECO:0000269|PubMed:28966017}.
FT   METAL       255    255       Zinc 3. {ECO:0000244|PDB:5Y1Z,
FT                                ECO:0000269|PubMed:28966017}.
FT   METAL       258    258       Zinc 3. {ECO:0000244|PDB:5Y1Z,
FT                                ECO:0000269|PubMed:28966017}.
FT   METAL       274    274       Zinc 3. {ECO:0000244|PDB:5Y1Z,
FT                                ECO:0000269|PubMed:28966017}.
FT   MOD_RES      24     24       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     404    404       Phosphothreonine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES     406    406       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     413    413       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     417    417       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     425    425       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     432    432       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     444    444       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     460    460       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     462    462       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     465    465       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     486    486       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231}.
FT   MOD_RES     490    490       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     495    495       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     514    514       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     523    523       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     541    541       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     547    547       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     563    563       Phosphothreonine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     652    652       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     655    655       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     668    668       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     682    682       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     707    707       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     709    709       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     737    737       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     746    746       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     754    754       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     756    756       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1119   1119       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1141   1141       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   CROSSLNK     56     56       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK     70     70       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    390    390       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    413    413       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate. {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    453    453       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    505    505       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    530    530       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    549    549       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    611    611       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:25755297,
FT                                ECO:0000244|PubMed:25772364,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    645    645       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:25755297,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    657    657       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK   1115   1115       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   VAR_SEQ       1    526       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:11003709}.
FT                                /FTId=VSP_000566.
FT   VAR_SEQ       1    376       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:11149944}.
FT                                /FTId=VSP_000565.
FT   VAR_SEQ       1    145       Missing (in isoform 3 and isoform 6).
FT                                {ECO:0000303|PubMed:11149944,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_000564.
FT   VAR_SEQ       1      1       M -> MVFLEEFEARSCLAEEEIKTEQEVVEGM (in
FT                                isoform 19).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_054810.
FT   VAR_SEQ       1      1       M -> MFSSLQKSFNLAEEEIKTEQEVVEGM (in
FT                                isoform 20).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_054811.
FT   VAR_SEQ       1      1       M -> MHPQSLAEEEIKTEQEVVEGM (in isoform 5,
FT                                isoform 7, isoform 8, isoform 10, isoform
FT                                12, isoform 13, isoform 14, isoform 15,
FT                                isoform 16, isoform 17, isoform 18 and
FT                                isoform 22).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.3, ECO:0000303|Ref.4}.
FT                                /FTId=VSP_000563.
FT   VAR_SEQ      58     82       Missing (in isoform 5, isoform 14,
FT                                isoform 15, isoform 16, isoform 17,
FT                                isoform 18, isoform 20, isoform 21 and
FT                                isoform 23).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.4}.
FT                                /FTId=VSP_000567.
FT   VAR_SEQ     132    169       Missing (in isoform 23).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_054812.
FT   VAR_SEQ     474    520       Missing (in isoform 15 and isoform 18).
FT                                {ECO:0000303|Ref.4}.
FT                                /FTId=VSP_053400.
FT   VAR_SEQ     742    868       Missing (in isoform 8 and isoform 17).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.3}.
FT                                /FTId=VSP_017096.
FT   VAR_SEQ     823    869       SKFQTSSQKWHMQKMQRQQQQQQQQNQQQQPQSSQGTRYQT
FT                                RQAVKA -> T (in isoform 2, isoform 3,
FT                                isoform 4, isoform 6, isoform 9, isoform
FT                                12, isoform 13, isoform 14, isoform 15,
FT                                isoform 16, isoform 21, isoform 22 and
FT                                isoform 23).
FT                                {ECO:0000303|PubMed:11003709,
FT                                ECO:0000303|PubMed:11149944,
FT                                ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:17974005,
FT                                ECO:0000303|Ref.4}.
FT                                /FTId=VSP_000568.
FT   VAR_SEQ     933    959       Missing (in isoform 22). {ECO:0000305}.
FT                                /FTId=VSP_054814.
FT   VAR_SEQ    1142   1142       D -> VSKRCDKQPAYAPTTTDHQPHPNYPAQKY (in
FT                                isoform 6, isoform 7, isoform 8, isoform
FT                                9, isoform 11, isoform 13, isoform 16,
FT                                isoform 19, isoform 22 and isoform 23).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:17974005,
FT                                ECO:0000303|Ref.3, ECO:0000303|Ref.4}.
FT                                /FTId=VSP_000570.
FT   VARIANT     752    752       V -> A (in dbSNP:rs2275801).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_055559.
FT   MUTAGEN      76     76       D->A: Decreases interaction with histone
FT                                H3K4me0. {ECO:0000269|PubMed:27477906}.
FT   MUTAGEN      79     79       D->A: Decreases interaction with histone
FT                                H3K4me0. {ECO:0000269|PubMed:27477906}.
FT   MUTAGEN      84     84       D->A: Decreases interaction with histone
FT                                H3K4me0. {ECO:0000269|PubMed:27477906}.
FT   MUTAGEN      88     88       D->A: Decreases interaction with histone
FT                                H3K4me0. {ECO:0000269|PubMed:27477906}.
FT   MUTAGEN      89     89       F->D: Increases interaction with histone
FT                                H3K4me0. {ECO:0000269|PubMed:27477906}.
FT   MUTAGEN     104    104       E->A: Decreases interaction with histone
FT                                H3K4me0. {ECO:0000269|PubMed:27477906}.
FT   MUTAGEN     227    228       YN->AA: Decreases interaction with
FT                                histone H3K4me0.
FT                                {ECO:0000269|PubMed:27477906}.
FT   MUTAGEN     240    240       V->Q: Decreases binding to DBN1.
FT                                {ECO:0000269|PubMed:28966017}.
FT   MUTAGEN     311    311       H->A: Loss of binding to DBN1. Loss of
FT                                cytoplasmic localization.
FT                                {ECO:0000269|PubMed:28966017}.
FT   MUTAGEN     312    312       D->R: Loss of binding to DBN1.
FT                                {ECO:0000269|PubMed:28966017}.
FT   CONFLICT    119    119       S -> P (in Ref. 6; BAH11794).
FT                                {ECO:0000305}.
FT   CONFLICT    202    202       A -> T (in Ref. 6; BAH12176).
FT                                {ECO:0000305}.
FT   CONFLICT    325    325       S -> F (in Ref. 6; BAH12176).
FT                                {ECO:0000305}.
FT   CONFLICT    391    391       I -> V (in Ref. 2; AAL50790).
FT                                {ECO:0000305}.
FT   CONFLICT    399    399       L -> P (in Ref. 6; BAH11794).
FT                                {ECO:0000305}.
FT   CONFLICT    470    470       D -> G (in Ref. 6; BAH11794).
FT                                {ECO:0000305}.
FT   CONFLICT    874    874       E -> G (in Ref. 6; BAG53824).
FT                                {ECO:0000305}.
FT   CONFLICT    894    894       P -> A (in Ref. 2; AAG34905/AAL50790).
FT                                {ECO:0000305}.
FT   CONFLICT    967    967       I -> T (in Ref. 7; CAE46008).
FT                                {ECO:0000305}.
FT   STRAND       89     91       {ECO:0000244|PDB:4COS}.
FT   TURN         92     94       {ECO:0000244|PDB:4COS}.
FT   STRAND      104    107       {ECO:0000244|PDB:4COS}.
FT   HELIX       112    115       {ECO:0000244|PDB:4COS}.
FT   HELIX       128    137       {ECO:0000244|PDB:4COS}.
FT   HELIX       139    141       {ECO:0000244|PDB:4COS}.
FT   HELIX       144    147       {ECO:0000244|PDB:4COS}.
FT   HELIX       151    165       {ECO:0000244|PDB:4COS}.
FT   HELIX       171    173       {ECO:0000244|PDB:4COS}.
FT   TURN        179    181       {ECO:0000244|PDB:4COS}.
FT   HELIX       185    188       {ECO:0000244|PDB:4COS}.
FT   HELIX       195    203       {ECO:0000244|PDB:4COS}.
FT   HELIX       210    228       {ECO:0000244|PDB:4COS}.
FT   HELIX       233    254       {ECO:0000244|PDB:4COS}.
FT   HELIX       256    264       {ECO:0000244|PDB:4COS}.
FT   HELIX       269    271       {ECO:0000244|PDB:4COS}.
FT   STRAND      280    283       {ECO:0000244|PDB:4COS}.
FT   STRAND      291    299       {ECO:0000244|PDB:4COS}.
FT   STRAND      302    307       {ECO:0000244|PDB:4COS}.
FT   TURN        308    310       {ECO:0000244|PDB:4COS}.
FT   STRAND      313    317       {ECO:0000244|PDB:4COS}.
FT   HELIX       318    320       {ECO:0000244|PDB:4COS}.
FT   STRAND      321    323       {ECO:0000244|PDB:4COS}.
FT   STRAND      325    327       {ECO:0000244|PDB:5Y1Z}.
FT   HELIX       336    357       {ECO:0000244|PDB:4COS}.
FT   HELIX       375    377       {ECO:0000244|PDB:4COS}.
FT   HELIX       384    386       {ECO:0000244|PDB:4COS}.
FT   HELIX       953    972       {ECO:0000244|PDB:5MQ4}.
FT   HELIX       975   1023       {ECO:0000244|PDB:5MQ4}.
FT   TURN       1029   1031       {ECO:0000244|PDB:5MQ4}.
FT   STRAND     1037   1040       {ECO:0000244|PDB:5MQ4}.
FT   STRAND     1043   1047       {ECO:0000244|PDB:5MQ4}.
FT   HELIX      1048   1058       {ECO:0000244|PDB:5MQ4}.
FT   HELIX      1059   1061       {ECO:0000244|PDB:5MQ4}.
SQ   SEQUENCE   1186 AA;  131692 MW;  BAE8CDEF240E647A CRC64;
     MDISTRSKDP GSAERTAQKR KFPSPPHSSN GHSPQDTSTS PIKKKKKPGL LNSNNKEQSE
     LRHGPFYYMK QPLTTDPVDV VPQDGRNDFY CWVCHREGQV LCCELCPRVY HAKCLRLTSE
     PEGDWFCPEC EKITVAECIE TQSKAMTMLT IEQLSYLLKF AIQKMKQPGT DAFQKPVPLE
     QHPDYAEYIF HPMDLCTLEK NAKKKMYGCT EAFLADAKWI LHNCIIYNGG NHKLTQIAKV
     VIKICEHEMN EIEVCPECYL AACQKRDNWF CEPCSNPHPL VWAKLKGFPF WPAKALRDKD
     GQVDARFFGQ HDRAWVPINN CYLMSKEIPF SVKKTKSIFN SAMQEMEVYV ENIRRKFGVF
     NYSPFRTPYT PNSQYQMLLD PTNPSAGTAK IDKQEKVKLN FDMTASPKIL MSKPVLSGGT
     GRRISLSDMP RSPMSTNSSV HTGSDVEQDA EKKATSSHFS ASEESMDFLD KSTASPASTK
     TGQAGSLSGS PKPFSPQLSA PITTKTDKTS TTGSILNLNL DRSKAEMDLK ELSESVQQQS
     TPVPLISPKR QIRSRFQLNL DKTIESCKAQ LGINEISEDV YTAVEHSDSE DSEKSDSSDS
     EYISDDEQKS KNEPEDTEDK EGCQMDKEPS AVKKKPKPTN PVEIKEELKS TSPASEKADP
     GAVKDKASPE PEKDFSEKAK PSPHPIKDKL KGKDETDSPT VHLGLDSDSE SELVIDLGED
     HSGREGRKNK KEPKEPSPKQ DVVGKTPPST TVGSHSPPET PVLTRSSAQT SAAGATATTS
     TSSTVTVTAP APAATGSPVK KQRPLLPKET APAVQRVVWN SSSKFQTSSQ KWHMQKMQRQ
     QQQQQQQNQQ QQPQSSQGTR YQTRQAVKAV QQKEITQSPS TSTITLVTST QSSPLVTSSG
     SMSTLVSSVN ADLPIATASA DVAADIAKYT SKMMDAIKGT MTEIYNDLSK NTTGSTIAEI
     RRLRIEIEKL QWLHQQELSE MKHNLELTMA EMRQSLEQER DRLIAEVKKQ LELEKQQAVD
     ETKKKQWCAN CKKEAIFYCC WNTSYCDYPC QQAHWPEHMK SCTQSATAPQ QEADAEVNTE
     TLNKSSQGSS SSTQSAPSET ASASKEKETS AEKSKESGST LDLSGSRETP SSILLGSNQG
     SDHSRSNKSS WSSSDEKRGS TRSDHNTSTS TKSLLPKESR LDTFWD
//
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