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Database: UniProt
Entry: Q96NY9
LinkDB: Q96NY9
Original site: Q96NY9 
ID   MUS81_HUMAN             Reviewed;         551 AA.
AC   Q96NY9; Q9H7D9;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 3.
DT   02-JUN-2021, entry version 171.
DE   RecName: Full=Crossover junction endonuclease MUS81;
DE            EC=3.1.22.-;
GN   Name=MUS81;
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], VARIANTS HIS-37 AND PRO-180, FUNCTION,
RP   COFACTOR, INTERACTION WITH CHEK2, SUBCELLULAR LOCATION, INDUCTION, AND
RP   MUTAGENESIS OF 306-GLY-ASP-307; 333-GLU-ARG-334 AND 338-ASP-ASP-339.
RC   TISSUE=Cerebellum;
RX   PubMed=11741546; DOI=10.1016/s1097-2765(01)00375-6;
RA   Chen X.-B., Melchionna R., Denis C.-M., Gaillard P.-H.L., Blasina A.,
RA   Van de Weyer I., Boddy M.N., Russell P., Vialard J., McGowan C.H.;
RT   "Human Mus81-associated endonuclease cleaves Holliday junctions in vitro.";
RL   Mol. Cell 8:1117-1127(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-37 AND PRO-180.
RC   TISSUE=Brain;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-551, AND VARIANTS HIS-37 AND
RP   PRO-180.
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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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   [4]
RP   FUNCTION.
RX   PubMed=12374758; DOI=10.1093/emboj/cdf554;
RA   Constantinou A., Chen X.-B., McGowan C.H., West S.C.;
RT   "Holliday junction resolution in human cells: two junction endonucleases
RT   with distinct substrate specificities.";
RL   EMBO J. 21:5577-5585(2002).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH EME1.
RX   PubMed=12686547; DOI=10.1074/jbc.m302484200;
RA   Oegruenc M., Sancar A.;
RT   "Identification and characterization of human MUS81-MMS4 structure-specific
RT   endonuclease.";
RL   J. Biol. Chem. 278:21715-21720(2003).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH EME1.
RX   PubMed=12721304; DOI=10.1074/jbc.m302882200;
RA   Ciccia A., Constantinou A., West S.C.;
RT   "Identification and characterization of the human mus81-eme1
RT   endonuclease.";
RL   J. Biol. Chem. 278:25172-25178(2003).
RN   [7]
RP   SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=14638871; DOI=10.1091/mbc.e03-05-0276;
RA   Gao H., Chen X.-B., McGowan C.H.;
RT   "Mus81 endonuclease localizes to nucleoli and to regions of DNA damage in
RT   human S-phase cells.";
RL   Mol. Biol. Cell 14:4826-4834(2003).
RN   [8]
RP   FUNCTION, SELF-ASSOCIATION, INTERACTION WITH EME1, SUBCELLULAR LOCATION,
RP   AND MUTAGENESIS OF 338-ASP-ASP-339.
RX   PubMed=14617801; DOI=10.1091/mbc.e03-08-0580;
RA   Blais V., Gao H., Elwell C.A., Boddy M.N., Gaillard P.-H.L., Russell P.,
RA   McGowan C.H.;
RT   "RNA interference inhibition of Mus81 reduces mitotic recombination in
RT   human cells.";
RL   Mol. Biol. Cell 15:552-562(2004).
RN   [9]
RP   FUNCTION, INTERACTION WITH BLM, AND SUBCELLULAR LOCATION.
RX   PubMed=15805243; DOI=10.1158/0008-5472.can-04-2421;
RA   Zhang R., Sengupta S., Yang Q., Linke S.P., Yanaihara N., Bradsher J.,
RA   Blais V., McGowan C.H., Harris C.C.;
RT   "BLM helicase facilitates Mus81 endonuclease activity in human cells.";
RL   Cancer Res. 65:2526-2531(2005).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH EME1 AND EME2.
RX   PubMed=17289582; DOI=10.1016/j.molcel.2007.01.003;
RA   Ciccia A., Ling C., Coulthard R., Yan Z., Xue Y., Meetei A.R.,
RA   Laghmani el H., Joenje H., McDonald N., de Winter J.P., Wang W., West S.C.;
RT   "Identification of FAAP24, a Fanconi anemia core complex protein that
RT   interacts with FANCM.";
RL   Mol. Cell 25:331-343(2007).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [12]
RP   INTERACTION WITH DCLRE1B.
RX   PubMed=18469862; DOI=10.1038/onc.2008.139;
RA   Bae J.B., Mukhopadhyay S.S., Liu L., Zhang N., Tan J., Akhter S., Liu X.,
RA   Shen X., Li L., Legerski R.J.;
RT   "Snm1B/Apollo mediates replication fork collapse and S Phase checkpoint
RT   activation in response to DNA interstrand cross-links.";
RL   Oncogene 27:5045-5056(2008).
RN   [13]
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   FUNCTION, AND INTERACTION WITH SLX4.
RX   PubMed=19595721; DOI=10.1016/j.molcel.2009.06.020;
RA   Munoz I.M., Hain K., Declais A.-C., Gardiner M., Toh G.W.,
RA   Sanchez-Pulido L., Heuckmann J.M., Toth R., Macartney T., Eppink B.,
RA   Kanaar R., Ponting C.P., Lilley D.M.J., Rouse J.;
RT   "Coordination of structure-specific nucleases by human SLX4/BTBD12 is
RT   required for DNA repair.";
RL   Mol. Cell 35:116-127(2009).
RN   [15]
RP   FUNCTION, AND INTERACTION WITH SLX4.
RX   PubMed=19596235; DOI=10.1016/j.cell.2009.06.030;
RA   Svendsen J.M., Smogorzewska A., Sowa M.E., O'Connell B.C., Gygi S.P.,
RA   Elledge S.J., Harper J.W.;
RT   "Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is
RT   required for DNA repair.";
RL   Cell 138:63-77(2009).
RN   [16]
RP   INTERACTION WITH SLX4.
RX   PubMed=19596236; DOI=10.1016/j.cell.2009.06.029;
RA   Fekairi S., Scaglione S., Chahwan C., Taylor E.R., Tissier A., Coulon S.,
RA   Dong M.-Q., Ruse C., Yates J.R. III, Russell P., Fuchs R.P., McGowan C.H.,
RA   Gaillard P.-H.L.;
RT   "Human SLX4 is a Holliday junction resolvase subunit that binds multiple
RT   DNA repair/recombination endonucleases.";
RL   Cell 138:78-89(2009).
RN   [17]
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   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-101, AND
RP   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).
CC   -!- FUNCTION: Interacts with EME1 and EME2 to form a DNA structure-specific
CC       endonuclease with substrate preference for branched DNA structures with
CC       a 5'-end at the branch nick. Typical substrates include 3'-flap
CC       structures, replication forks and nicked Holliday junctions. May be
CC       required in mitosis for the processing of stalled or collapsed
CC       replication forks. {ECO:0000269|PubMed:11741546,
CC       ECO:0000269|PubMed:12374758, ECO:0000269|PubMed:12686547,
CC       ECO:0000269|PubMed:12721304, ECO:0000269|PubMed:14617801,
CC       ECO:0000269|PubMed:15805243, ECO:0000269|PubMed:17289582,
CC       ECO:0000269|PubMed:19595721, ECO:0000269|PubMed:19596235}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:11741546};
CC   -!- SUBUNIT: May self-associate. Interacts with EME1, EME2 and CHEK2.
CC       Interacts with BLM, and this interaction may stimulate the endonuclease
CC       activity of MUS81. Interacts with SLX4/BTBD12; this interaction is
CC       direct and links the MUS81-EME1 complex to SLX4, which may coordinate
CC       the action of the structure-specific endonuclease during DNA repair.
CC       Interacts with DCLRE1B/Apollo. {ECO:0000269|PubMed:11741546,
CC       ECO:0000269|PubMed:12686547, ECO:0000269|PubMed:12721304,
CC       ECO:0000269|PubMed:14617801, ECO:0000269|PubMed:15805243,
CC       ECO:0000269|PubMed:17289582, ECO:0000269|PubMed:18469862,
CC       ECO:0000269|PubMed:19595721, ECO:0000269|PubMed:19596235,
CC       ECO:0000269|PubMed:19596236}.
CC   -!- INTERACTION:
CC       Q96NY9; Q96AY2: EME1; NbExp=9; IntAct=EBI-2370806, EBI-2370825;
CC       Q96NY9; A4GXA9: EME2; NbExp=3; IntAct=EBI-2370806, EBI-7838486;
CC       Q96NY9; P39748: FEN1; NbExp=5; IntAct=EBI-2370806, EBI-707816;
CC       Q96NY9; Q8IY92: SLX4; NbExp=13; IntAct=EBI-2370806, EBI-2370740;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11741546,
CC       ECO:0000269|PubMed:14617801, ECO:0000269|PubMed:14638871,
CC       ECO:0000269|PubMed:15805243}. Note=Recruited to foci of DNA damage in
CC       S-phase cells.
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- DEVELOPMENTAL STAGE: Expressed in S phase and G2 phase.
CC       {ECO:0000269|PubMed:14638871}.
CC   -!- INDUCTION: Up-regulated in cells treated with agents that damage DNA or
CC       block replication. This up-regulation seems to be independent of
CC       transcription. {ECO:0000269|PubMed:11741546}.
CC   -!- SIMILARITY: Belongs to the XPF family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB14953.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF425646; AAL28065.1; -; mRNA.
DR   EMBL; BC009999; AAH09999.2; -; mRNA.
DR   EMBL; AK024665; BAB14953.1; ALT_INIT; mRNA.
DR   CCDS; CCDS8115.1; -.
DR   RefSeq; NP_079404.3; NM_025128.4.
DR   RefSeq; XP_011543572.1; XM_011545270.1.
DR   PDB; 2MC3; NMR; -; A=127-230.
DR   PDB; 2ZIX; X-ray; 3.50 A; A=246-551.
DR   PDB; 4P0P; X-ray; 2.80 A; A=246-551.
DR   PDB; 4P0Q; X-ray; 2.85 A; A=246-551.
DR   PDB; 4P0R; X-ray; 6.50 A; A/C=246-551.
DR   PDB; 4P0S; X-ray; 6.00 A; A/C/E/G=246-551.
DR   PDB; 6VWB; NMR; -; A=2-90.
DR   PDBsum; 2MC3; -.
DR   PDBsum; 2ZIX; -.
DR   PDBsum; 4P0P; -.
DR   PDBsum; 4P0Q; -.
DR   PDBsum; 4P0R; -.
DR   PDBsum; 4P0S; -.
DR   PDBsum; 6VWB; -.
DR   BMRB; Q96NY9; -.
DR   SMR; Q96NY9; -.
DR   BioGRID; 123170; 89.
DR   ComplexPortal; CPX-511; Deoxyribonuclease complex MUS81-EME1.
DR   ComplexPortal; CPX-586; Deoxyribonuclease complex MUS81-EME2.
DR   CORUM; Q96NY9; -.
DR   DIP; DIP-48630N; -.
DR   IntAct; Q96NY9; 16.
DR   MINT; Q96NY9; -.
DR   STRING; 9606.ENSP00000307853; -.
DR   iPTMnet; Q96NY9; -.
DR   PhosphoSitePlus; Q96NY9; -.
DR   BioMuta; MUS81; -.
DR   DMDM; 166898077; -.
DR   EPD; Q96NY9; -.
DR   jPOST; Q96NY9; -.
DR   MassIVE; Q96NY9; -.
DR   MaxQB; Q96NY9; -.
DR   PaxDb; Q96NY9; -.
DR   PeptideAtlas; Q96NY9; -.
DR   PRIDE; Q96NY9; -.
DR   ProteomicsDB; 77579; -.
DR   Antibodypedia; 16020; 186 antibodies.
DR   DNASU; 80198; -.
DR   Ensembl; ENST00000308110; ENSP00000307853; ENSG00000172732.
DR   GeneID; 80198; -.
DR   KEGG; hsa:80198; -.
DR   UCSC; uc001ofv.5; human.
DR   CTD; 80198; -.
DR   DisGeNET; 80198; -.
DR   GeneCards; MUS81; -.
DR   HGNC; HGNC:29814; MUS81.
DR   HPA; ENSG00000172732; Low tissue specificity.
DR   MIM; 606591; gene.
DR   neXtProt; NX_Q96NY9; -.
DR   OpenTargets; ENSG00000172732; -.
DR   PharmGKB; PA134881809; -.
DR   VEuPathDB; HostDB:ENSG00000172732.11; -.
DR   eggNOG; KOG2379; Eukaryota.
DR   GeneTree; ENSGT00390000005498; -.
DR   HOGENOM; CLU_014329_3_0_1; -.
DR   InParanoid; Q96NY9; -.
DR   OMA; MLDWIVE; -.
DR   OrthoDB; 738810at2759; -.
DR   PhylomeDB; Q96NY9; -.
DR   TreeFam; TF315113; -.
DR   BRENDA; 3.1.22.4; 2681.
DR   PathwayCommons; Q96NY9; -.
DR   Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR   Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
DR   BioGRID-ORCS; 80198; 63 hits in 1001 CRISPR screens.
DR   ChiTaRS; MUS81; human.
DR   EvolutionaryTrace; Q96NY9; -.
DR   GeneWiki; MUS81; -.
DR   GenomeRNAi; 80198; -.
DR   Pharos; Q96NY9; Tbio.
DR   PRO; PR:Q96NY9; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q96NY9; protein.
DR   Bgee; ENSG00000172732; Expressed in body of uterus and 235 other tissues.
DR   ExpressionAtlas; Q96NY9; baseline and differential.
DR   Genevisible; Q96NY9; HS.
DR   GO; GO:0048476; C:Holliday junction resolvase complex; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0048257; F:3'-flap endonuclease activity; IMP:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IMP:MGI.
DR   GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR   GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR   GO; GO:0036297; P:interstrand cross-link repair; TAS:Reactome.
DR   GO; GO:0031573; P:intra-S DNA damage checkpoint; IBA:GO_Central.
DR   GO; GO:0033687; P:osteoblast proliferation; IMP:CACAO.
DR   GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR   GO; GO:0072429; P:response to intra-S DNA damage checkpoint signaling; IMP:MGI.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.150.110; -; 1.
DR   IDEAL; IID00098; -.
DR   InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR   InterPro; IPR006166; ERCC4_domain.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF02732; ERCC4; 1.
DR   SMART; SM00891; ERCC4; 1.
DR   SUPFAM; SSF47802; SSF47802; 1.
DR   SUPFAM; SSF52980; SSF52980; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA damage; DNA recombination; DNA repair; Endonuclease;
KW   Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..551
FT                   /note="Crossover junction endonuclease MUS81"
FT                   /id="PRO_0000198858"
FT   DOMAIN          270..372
FT                   /note="ERCC4"
FT   REGION          84..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          125..244
FT                   /note="Interaction with BLM"
FT                   /evidence="ECO:0000269|PubMed:15805243"
FT   MOD_RES         95
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         37
FT                   /note="R -> H (in dbSNP:rs13817)"
FT                   /evidence="ECO:0000269|PubMed:11741546,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT                   /id="VAR_025340"
FT   VARIANT         115
FT                   /note="S -> F (in dbSNP:rs34381357)"
FT                   /id="VAR_061988"
FT   VARIANT         180
FT                   /note="R -> P (in dbSNP:rs545500)"
FT                   /evidence="ECO:0000269|PubMed:11741546,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT                   /id="VAR_038521"
FT   VARIANT         189
FT                   /note="L -> F (in dbSNP:rs2298447)"
FT                   /id="VAR_021990"
FT   VARIANT         350
FT                   /note="R -> W (in dbSNP:rs34891773)"
FT                   /id="VAR_038522"
FT   VARIANT         481
FT                   /note="Q -> H (in dbSNP:rs765593)"
FT                   /id="VAR_025341"
FT   MUTAGEN         306..307
FT                   /note="GD->AE: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11741546"
FT   MUTAGEN         333..334
FT                   /note="ER->AG: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11741546"
FT   MUTAGEN         338..339
FT                   /note="DD->AA: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11741546,
FT                   ECO:0000269|PubMed:14617801"
FT   HELIX           137..149
FT                   /evidence="ECO:0007829|PDB:2MC3"
FT   HELIX           152..154
FT                   /evidence="ECO:0007829|PDB:2MC3"
FT   HELIX           160..170
FT                   /evidence="ECO:0007829|PDB:2MC3"
FT   HELIX           184..190
FT                   /evidence="ECO:0007829|PDB:2MC3"
FT   STRAND          193..195
FT                   /evidence="ECO:0007829|PDB:2MC3"
FT   STRAND          198..200
FT                   /evidence="ECO:0007829|PDB:2MC3"
FT   STRAND          203..205
FT                   /evidence="ECO:0007829|PDB:2MC3"
FT   HELIX           207..219
FT                   /evidence="ECO:0007829|PDB:2MC3"
FT   TURN            220..222
FT                   /evidence="ECO:0007829|PDB:2MC3"
FT   STRAND          224..226
FT                   /evidence="ECO:0007829|PDB:2MC3"
FT   STRAND          266..274
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   STRAND          275..277
FT                   /evidence="ECO:0007829|PDB:2ZIX"
FT   HELIX           287..293
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   STRAND          298..301
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   STRAND          307..316
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   STRAND          325..336
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   HELIX           337..345
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   HELIX           348..357
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   TURN            358..360
FT                   /evidence="ECO:0007829|PDB:2ZIX"
FT   STRAND          363..369
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   STRAND          371..373
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   HELIX           381..393
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   STRAND          398..401
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   HELIX           405..422
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   TURN            423..425
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   STRAND          428..430
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   STRAND          452..455
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   HELIX           456..462
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   TURN            465..467
FT                   /evidence="ECO:0007829|PDB:2ZIX"
FT   HELIX           471..479
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   HELIX           487..496
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   HELIX           500..509
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   HELIX           513..517
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   TURN            518..522
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   TURN            526..529
FT                   /evidence="ECO:0007829|PDB:4P0P"
FT   HELIX           535..545
FT                   /evidence="ECO:0007829|PDB:4P0P"
SQ   SEQUENCE   551 AA;  61173 MW;  D0F331CC2269D847 CRC64;
     MAAPVRLGRK RPLPACPNPL FVRWLTEWRD EATRSRRRTR FVFQKALRSL RRYPLPLRSG
     KEAKILQHFG DGLCRMLDER LQRHRTSGGD HAPDSPSGEN SPAPQGRLAE VQDSSMPVPA
     QPKAGGSGSY WPARHSGARV ILLVLYREHL NPNGHHFLTK EELLQRCAQK SPRVAPGSAR
     PWPALRSLLH RNLVLRTHQP ARYSLTPEGL ELAQKLAESE GLSLLNVGIG PKEPPGEETA
     VPGAASAELA SEAGVQQQPL ELRPGEYRVL LCVDIGETRG GGHRPELLRE LQRLHVTHTV
     RKLHVGDFVW VAQETNPRDP ANPGELVLDH IVERKRLDDL CSSIIDGRFR EQKFRLKRCG
     LERRVYLVEE HGSVHNLSLP ESTLLQAVTN TQVIDGFFVK RTADIKESAA YLALLTRGLQ
     RLYQGHTLRS RPWGTPGNPE SGAMTSPNPL CSLLTFSDFN AGAIKNKAQS VREVFARQLM
     QVRGVSGEKA AALVDRYSTP ASLLAAYDAC ATPKEQETLL STIKCGRLQR NLGPALSRTL
     SQLYCSYGPL T
//
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