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STAG2_HUMAN
ID   STAG2_HUMAN             Reviewed;        1231 AA.
AC   Q8N3U4; B1AMT5; D3DTF5; O00540; Q5JTI6; Q68DE9; Q9H1N8;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 3.
DT   03-AUG-2022, entry version 184.
DE   RecName: Full=Cohesin subunit SA-2;
DE   AltName: Full=SCC3 homolog 2;
DE   AltName: Full=Stromal antigen 2;
GN   Name=STAG2; Synonyms=SA2;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Retina, and Spinal cord;
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., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye;
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 48-1231 (ISOFORM 1).
RC   TISSUE=Thymus;
RX   PubMed=9305759; DOI=10.1016/s0378-1119(97)00121-2;
RA   Carramolino L., Lee B.C., Zaballos A., Peled A., Barthelemy I.,
RA   Shav-Tal Y., Prieto I., Carmi P., Gothelf Y., Gonzalez de Buitrago G.,
RA   Aracil M., Marquez G., Barbero J.L., Zipori D.;
RT   "SA-1, a nuclear protein encoded by one member of a novel gene family:
RT   molecular cloning and detection in hemopoietic organs.";
RL   Gene 195:151-159(1997).
RN   [6]
RP   ERRATUM OF PUBMED:9305759.
RA   Carramolino L., Lee B.C., Zaballos A., Peled A., Barthelemy I.,
RA   Shav-Tal Y., Prieto I., Carmi P., Gothelf Y., Gonzalez de Buitrago G.,
RA   Aracil M., Marquez G., Barbero J.L., Zipori D.;
RL   Gene 206:283-286(1998).
RN   [7]
RP   IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1A AND SMC3.
RX   PubMed=11076961; DOI=10.1083/jcb.151.4.749;
RA   Sumara I., Vorlaufer E., Gieffers C., Peters B.H., Peters J.-M.;
RT   "Characterization of vertebrate cohesin complexes and their regulation in
RT   prophase.";
RL   J. Cell Biol. 151:749-762(2000).
RN   [8]
RP   FUNCTION IN EARLY STEPS OF MEIOSIS.
RX   PubMed=12034751; DOI=10.1093/embo-reports/kvf108;
RA   Prieto I., Pezzi N., Buesa J.M., Kremer L., Barthelemy I., Carreiro C.,
RA   Roncal F., Martinez A., Gomez L., Fernandez R., Martinez-A C.,
RA   Barbero J.L.;
RT   "STAG2 and Rad21 mammalian mitotic cohesins are implicated in meiosis.";
RL   EMBO Rep. 3:543-550(2002).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1061, AND IDENTIFICATION BY
RP   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., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1058 AND SER-1061, 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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1058; SER-1061 AND THR-1112,
RP   AND 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   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-607, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   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   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-1061; SER-1177 AND SER-1178, AND IDENTIFICATION BY MASS
RP   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   [14]
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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1061, AND IDENTIFICATION BY
RP   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   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1058 AND SER-1061, 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).
RN   [17]
RP   IDENTIFICATION BY 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   [18]
RP   FUNCTION, INVOLVEMENT IN MKMS, VARIANTS MKMS 69-ARG--PHE-1231 DEL AND
RP   GLN-604, AND CHARACTERIZATION OF VARIANT MKMS 69-ARG--PHE-1231 DEL.
RX   PubMed=28296084; DOI=10.1002/ajmg.a.38207;
RG   UCLA Clinical Genomics Center;
RA   Mullegama S.V., Klein S.D., Mulatinho M.V., Senaratne T.N., Singh K.,
RA   Nguyen D.C., Gallant N.M., Strom S.P., Ghahremani S., Rao N.P.,
RA   Martinez-Agosto J.A.;
RT   "De novo loss-of-function variants in STAG2 are associated with
RT   developmental delay, microcephaly, and congenital anomalies.";
RL   Am. J. Med. Genet. A 173:1319-1327(2017).
RN   [19]
RP   FUNCTION, IDENTIFICATION IN COHESIN COMPLEX, INVOLVEMENT IN MKMS, VARIANT
RP   MKMS ASN-327, AND CHARACTERIZATION OF VARIANT MKMS ASN-327.
RX   PubMed=29263825; DOI=10.1038/s41525-017-0009-4;
RA   Soardi F.C., Machado-Silva A., Linhares N.D., Zheng G., Qu Q., Pena H.B.,
RA   Martins T.M.M., Vieira H.G.S., Pereira N.B., Melo-Minardi R.C., Gomes C.C.,
RA   Gomez R.S., Gomes D.A., Pires D.E.V., Ascher D.B., Yu H., Pena S.D.J.;
RT   "Familial STAG2 germline mutation defines a new human cohesinopathy.";
RL   NPJ Genom. Med. 2:7-7(2017).
RN   [20]
RP   INVOLVEMENT IN HPE13, AND VARIANTS HPE13 69-ARG--PHE-1231 DEL;
RP   146-ARG--PHE-1231 DEL; 259-ARG--PHE-1231 DEL AND 1012-ARG--PHE-1231 DEL.
RX   PubMed=31334757; DOI=10.1093/brain/awz210;
RA   Kruszka P., Berger S.I., Casa V., Dekker M.R., Gaesser J., Weiss K.,
RA   Martinez A.F., Murdock D.R., Louie R.J., Prijoles E.J., Lichty A.W.,
RA   Brouwer O.F., Zonneveld-Huijssoon E., Stephan M.J., Hogue J., Hu P.,
RA   Tanima-Nagai M., Everson J.L., Prasad C., Cereda A., Iascone M.,
RA   Schreiber A., Zurcher V., Corsten-Janssen N., Escobar L., Clegg N.J.,
RA   Delgado M.R., Hajirnis O., Balasubramanian M., Kayserili H., Deardorff M.,
RA   Poot R.A., Wendt K.S., Lipinski R.J., Muenke M.;
RT   "Cohesin complex-associated holoprosencephaly.";
RL   Brain 142:2631-2643(2019).
RN   [21]
RP   VARIANTS MKMS 140-GLN--PHE-1231 DEL; CYS-159; 535-CYS--PHE-1231 DEL AND
RP   GLN-604.
RX   PubMed=30158690; DOI=10.1038/s41436-018-0085-6;
RG   DDD Study;
RA   Yuan B., Neira J., Pehlivan D., Santiago-Sim T., Song X., Rosenfeld J.,
RA   Posey J.E., Patel V., Jin W., Adam M.P., Baple E.L., Dean J., Fong C.T.,
RA   Hickey S.E., Hudgins L., Leon E., Madan-Khetarpal S., Rawlins L.,
RA   Rustad C.F., Stray-Pedersen A., Tveten K., Wenger O., Diaz J., Jenkins L.,
RA   Martin L., McGuire M., Pietryga M., Ramsdell L., Slattery L., Abid F.,
RA   Bertuch A.A., Grange D., Immken L., Schaaf C.P., Van Esch H., Bi W.,
RA   Cheung S.W., Breman A.M., Smith J.L., Shaw C., Crosby A.H., Eng C.,
RA   Yang Y., Lupski J.R., Xiao R., Liu P.;
RT   "Clinical exome sequencing reveals locus heterogeneity and phenotypic
RT   variability of cohesinopathies.";
RL   Genet. Med. 21:663-675(2019).
RN   [22]
RP   RETRACTED PAPER.
RX   PubMed=30765867; DOI=10.1038/s10038-019-0571-y;
RA   Aoi H., Lei M., Mizuguchi T., Nishioka N., Goto T., Miyama S., Suzuki T.,
RA   Iwama K., Uchiyama Y., Mitsuhashi S., Itakura A., Takeda S., Matsumoto N.;
RT   "Nonsense variants in STAG2 result in distinct sex-dependent phenotypes.";
RL   J. Hum. Genet. 64:487-492(2019).
RN   [23]
RP   RETRACTION NOTICE OF PUBMED:30765867.
RX   PubMed=32536687; DOI=10.1038/s10038-020-0782-2;
RA   Aoi H., Lei M., Mizuguchi T., Nishioka N., Goto T., Miyama S., Suzuki T.,
RA   Iwama K., Uchiyama Y., Mitsuhashi S., Itakura A., Takeda S., Matsumoto N.;
RL   J. Hum. Genet. 65:811-811(2020).
RN   [24]
RP   VARIANT MKMS ASN-1009.
RX   PubMed=30447054; DOI=10.1002/mgg3.501;
RG   UCLA Clinical Genomics Center;
RA   Mullegama S.V., Klein S.D., Signer R.H., Vilain E., Martinez-Agosto J.A.;
RT   "Mutations in STAG2 cause an X-linked cohesinopathy associated with
RT   undergrowth, developmental delay, and dysmorphia: Expanding the phenotype
RT   in males.";
RL   Mol. Genet. Genomic Med. 7:E00501-E00501(2019).
CC   -!- FUNCTION: Component of cohesin complex, a complex required for the
CC       cohesion of sister chromatids after DNA replication. The cohesin
CC       complex apparently forms a large proteinaceous ring within which sister
CC       chromatids can be trapped. At anaphase, the complex is cleaved and
CC       dissociates from chromatin, allowing sister chromatids to segregate.
CC       The cohesin complex may also play a role in spindle pole assembly
CC       during mitosis. {ECO:0000269|PubMed:12034751}.
CC   -!- SUBUNIT: Interacts directly with RAD21 in cohesin complex. Cohesin
CC       complexes are composed of a heterodimer between a SMC1 protein (SMC1A
CC       or SMC1B) and SMC3, which are attached via their hinge domain, and
CC       RAD21 which link them at their heads, and one STAG protein (STAG1,
CC       STAG2 or STAG3). In cohesin complexes, STAG2 is mutually exclusive with
CC       STAG1 and STAG3. {ECO:0000269|PubMed:11076961}.
CC   -!- INTERACTION:
CC       Q8N3U4; Q29RF7: PDS5A; NbExp=6; IntAct=EBI-1057252, EBI-1175454;
CC       Q8N3U4; Q9NTI5: PDS5B; NbExp=4; IntAct=EBI-1057252, EBI-1175604;
CC       Q8N3U4; O60216: RAD21; NbExp=19; IntAct=EBI-1057252, EBI-80739;
CC       Q8N3U4; Q5FBB7: SGO1; NbExp=7; IntAct=EBI-1057252, EBI-989069;
CC       Q8N3U4; Q14683: SMC1A; NbExp=12; IntAct=EBI-1057252, EBI-80690;
CC       Q8N3U4; Q9UQE7: SMC3; NbExp=17; IntAct=EBI-1057252, EBI-80718;
CC       Q8N3U4; Q9NP77: SSU72; NbExp=4; IntAct=EBI-1057252, EBI-2515416;
CC       Q8N3U4; Q8WVM7: STAG1; NbExp=5; IntAct=EBI-1057252, EBI-1175097;
CC       Q8N3U4; Q7Z5K2: WAPL; NbExp=13; IntAct=EBI-1057252, EBI-1022242;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere.
CC       Note=Associates with chromatin. Before prophase it is scattered along
CC       chromosome arms. During prophase, most of cohesin complexes dissociate
CC       from chromatin probably because of phosphorylation by PLK1, except at
CC       centromeres, where cohesin complexes remain. At anaphase, the RAD21
CC       subunit of cohesin is cleaved, leading to the dissociation of the
CC       complex from chromosomes, allowing chromosome separation. In germ
CC       cells, cohesin complex dissociates from chromatin at prophase I, and
CC       may be replaced by a meiosis-specific cohesin complex.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8N3U4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8N3U4-2; Sequence=VSP_041119;
CC   -!- PTM: Phosphorylated by PLK1. The large dissociation of cohesin from
CC       chromosome arms during prophase is partly due to its phosphorylation
CC       (By similarity). {ECO:0000250}.
CC   -!- DISEASE: Mullegama-Klein-Martinez syndrome (MKMS) [MIM:301022]: An X-
CC       linked neurodevelopmental disorder with variable features including
CC       intellectual deficiency, microcephaly, microtia, hearing loss,
CC       developmental delay, dysmorphic features, language delay, congenital
CC       heart defect, and clinodactyly of the 5th finger.
CC       {ECO:0000269|PubMed:28296084, ECO:0000269|PubMed:29263825,
CC       ECO:0000269|PubMed:30158690, ECO:0000269|PubMed:30447054}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Holoprosencephaly 13, X-linked (HPE13) [MIM:301043]: An X-
CC       linked form of holoprosencephaly, a structural anomaly of the brain in
CC       which the developing forebrain fails to correctly separate into right
CC       and left hemispheres. Holoprosencephaly is genetically heterogeneous
CC       and associated with several distinct facies and phenotypic variability.
CC       HPE13 features range from full alobar holoprosencephaly with cyclopia
CC       to semilobar holoprosencephaly or septooptic dysplasia. Dysmorphic
CC       features include microcephaly, hypotelorism, low-set ears,
CC       micrognathia, and cleft lip/palate. Patients with a more severe
CC       phenotype may die in the newborn period, whereas those with a less
CC       severe phenotype show global developmental delay.
CC       {ECO:0000269|PubMed:31334757}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the SCC3 family. {ECO:0000305}.
CC   -!- CAUTION: Variants MKMS 743-TRP--PHE-1231 DEL and HPE13 1033-ARG--PHE-
CC       1231 DEL were previously described; however, the corresponding paper
CC       has been retracted as Case 1's sex was incorrectly reported
CC       invalidating the conclusions. {ECO:0000269|PubMed:30765867,
CC       ECO:0000305|PubMed:32536687}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA99732.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL831939; CAD38591.1; -; mRNA.
DR   EMBL; CR749433; CAH18271.1; -; mRNA.
DR   EMBL; AL355476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471107; EAX11853.1; -; Genomic_DNA.
DR   EMBL; CH471107; EAX11854.1; -; Genomic_DNA.
DR   EMBL; CH471107; EAX11855.1; -; Genomic_DNA.
DR   EMBL; CH471107; EAX11856.1; -; Genomic_DNA.
DR   EMBL; CH471107; EAX11857.1; -; Genomic_DNA.
DR   EMBL; BC001765; AAH01765.2; -; mRNA.
DR   EMBL; Z75331; CAA99732.1; ALT_INIT; mRNA.
DR   CCDS; CCDS14607.1; -. [Q8N3U4-1]
DR   CCDS; CCDS43990.1; -. [Q8N3U4-2]
DR   RefSeq; NP_001036214.1; NM_001042749.2. [Q8N3U4-2]
DR   RefSeq; NP_001036215.1; NM_001042750.1. [Q8N3U4-2]
DR   RefSeq; NP_001036216.1; NM_001042751.1. [Q8N3U4-1]
DR   RefSeq; NP_001269347.1; NM_001282418.1. [Q8N3U4-1]
DR   RefSeq; NP_006594.3; NM_006603.4. [Q8N3U4-1]
DR   RefSeq; XP_005262414.1; XM_005262357.2. [Q8N3U4-2]
DR   RefSeq; XP_005262415.1; XM_005262358.2. [Q8N3U4-2]
DR   RefSeq; XP_005262416.1; XM_005262359.3. [Q8N3U4-2]
DR   RefSeq; XP_005262417.1; XM_005262360.2. [Q8N3U4-2]
DR   RefSeq; XP_005262418.1; XM_005262361.2. [Q8N3U4-1]
DR   RefSeq; XP_006724790.1; XM_006724727.1. [Q8N3U4-2]
DR   RefSeq; XP_011529555.1; XM_011531253.2. [Q8N3U4-2]
DR   RefSeq; XP_016884721.1; XM_017029232.1. [Q8N3U4-1]
DR   RefSeq; XP_016884722.1; XM_017029233.1. [Q8N3U4-1]
DR   RefSeq; XP_016884723.1; XM_017029234.1.
DR   PDB; 4PJU; X-ray; 3.05 A; A=80-1060.
DR   PDB; 4PJW; X-ray; 2.85 A; A=80-1060.
DR   PDB; 4PK7; X-ray; 2.95 A; A=80-1060.
DR   PDB; 6QNX; X-ray; 2.70 A; A=1-1231.
DR   PDBsum; 4PJU; -.
DR   PDBsum; 4PJW; -.
DR   PDBsum; 4PK7; -.
DR   PDBsum; 6QNX; -.
DR   AlphaFoldDB; Q8N3U4; -.
DR   SMR; Q8N3U4; -.
DR   BioGRID; 115958; 200.
DR   ComplexPortal; CPX-5991; Nuclear meiotic cohesin complex, STAG2 variant.
DR   CORUM; Q8N3U4; -.
DR   DIP; DIP-35418N; -.
DR   IntAct; Q8N3U4; 53.
DR   MINT; Q8N3U4; -.
DR   STRING; 9606.ENSP00000218089; -.
DR   GlyGen; Q8N3U4; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8N3U4; -.
DR   MetOSite; Q8N3U4; -.
DR   PhosphoSitePlus; Q8N3U4; -.
DR   SwissPalm; Q8N3U4; -.
DR   BioMuta; STAG2; -.
DR   DMDM; 73621291; -.
DR   EPD; Q8N3U4; -.
DR   jPOST; Q8N3U4; -.
DR   MassIVE; Q8N3U4; -.
DR   MaxQB; Q8N3U4; -.
DR   PaxDb; Q8N3U4; -.
DR   PeptideAtlas; Q8N3U4; -.
DR   PRIDE; Q8N3U4; -.
DR   ProteomicsDB; 71836; -. [Q8N3U4-1]
DR   ProteomicsDB; 71837; -. [Q8N3U4-2]
DR   Antibodypedia; 500; 323 antibodies from 37 providers.
DR   DNASU; 10735; -.
DR   Ensembl; ENST00000218089.13; ENSP00000218089.9; ENSG00000101972.20. [Q8N3U4-2]
DR   Ensembl; ENST00000371144.7; ENSP00000360186.3; ENSG00000101972.20. [Q8N3U4-1]
DR   Ensembl; ENST00000371145.8; ENSP00000360187.4; ENSG00000101972.20. [Q8N3U4-2]
DR   Ensembl; ENST00000371157.7; ENSP00000360199.3; ENSG00000101972.20. [Q8N3U4-1]
DR   Ensembl; ENST00000371160.5; ENSP00000360202.1; ENSG00000101972.20. [Q8N3U4-1]
DR   Ensembl; ENST00000687852.1; ENSP00000509048.1; ENSG00000101972.20. [Q8N3U4-2]
DR   GeneID; 10735; -.
DR   KEGG; hsa:10735; -.
DR   MANE-Select; ENST00000371145.8; ENSP00000360187.4; NM_001042750.2; NP_001036215.1. [Q8N3U4-2]
DR   UCSC; uc004eua.5; human. [Q8N3U4-1]
DR   CTD; 10735; -.
DR   DisGeNET; 10735; -.
DR   GeneCards; STAG2; -.
DR   HGNC; HGNC:11355; STAG2.
DR   HPA; ENSG00000101972; Low tissue specificity.
DR   MalaCards; STAG2; -.
DR   MIM; 300826; gene.
DR   MIM; 301022; phenotype.
DR   MIM; 301043; phenotype.
DR   neXtProt; NX_Q8N3U4; -.
DR   OpenTargets; ENSG00000101972; -.
DR   Orphanet; 93925; Alobar holoprosencephaly.
DR   Orphanet; 220386; Semilobar holoprosencephaly.
DR   Orphanet; 521258; Xq25 microduplication syndrome.
DR   PharmGKB; PA36177; -.
DR   VEuPathDB; HostDB:ENSG00000101972; -.
DR   eggNOG; KOG2011; Eukaryota.
DR   GeneTree; ENSGT00950000182972; -.
DR   HOGENOM; CLU_005067_1_0_1; -.
DR   InParanoid; Q8N3U4; -.
DR   OMA; EAMPEKY; -.
DR   PhylomeDB; Q8N3U4; -.
DR   TreeFam; TF314604; -.
DR   PathwayCommons; Q8N3U4; -.
DR   Reactome; R-HSA-1221632; Meiotic synapsis.
DR   Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-HSA-2468052; Establishment of Sister Chromatid Cohesion.
DR   Reactome; R-HSA-2470946; Cohesin Loading onto Chromatin.
DR   Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR   Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR   SignaLink; Q8N3U4; -.
DR   SIGNOR; Q8N3U4; -.
DR   BioGRID-ORCS; 10735; 118 hits in 711 CRISPR screens.
DR   ChiTaRS; STAG2; human.
DR   GeneWiki; STAG2; -.
DR   GenomeRNAi; 10735; -.
DR   Pharos; Q8N3U4; Tbio.
DR   PRO; PR:Q8N3U4; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q8N3U4; protein.
DR   Bgee; ENSG00000101972; Expressed in mucosa of paranasal sinus and 215 other tissues.
DR   ExpressionAtlas; Q8N3U4; baseline and differential.
DR   Genevisible; Q8N3U4; HS.
DR   GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR   GO; GO:0005694; C:chromosome; TAS:Reactome.
DR   GO; GO:0000775; C:chromosome, centromeric region; TAS:Reactome.
DR   GO; GO:0008278; C:cohesin complex; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
DR   GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR   GO; GO:0034991; C:nuclear meiotic cohesin complex; IPI:ComplexPortal.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0034089; P:establishment of meiotic sister chromatid cohesion; IC:ComplexPortal.
DR   GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
DR   GO; GO:0007062; P:sister chromatid cohesion; IMP:UniProtKB.
DR   IDEAL; IID00674; -.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR039662; Cohesin_Scc3/SA.
DR   InterPro; IPR020839; SCD.
DR   InterPro; IPR013721; STAG.
DR   PANTHER; PTHR11199; PTHR11199; 2.
DR   Pfam; PF08514; STAG; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS51425; SCD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW   Centromere; Chromosome; Chromosome partition; Disease variant;
KW   Holoprosencephaly; Meiosis; Mitosis; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..1231
FT                   /note="Cohesin subunit SA-2"
FT                   /id="PRO_0000120185"
FT   DOMAIN          293..378
FT                   /note="SCD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00750"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1064..1083
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         607
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         1058
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT   MOD_RES         1061
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1064
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O35638"
FT   MOD_RES         1065
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O35638"
FT   MOD_RES         1112
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         1177
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         1178
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   VAR_SEQ         1156
FT                   /note="N -> NTQVTWMLAQRQQEEARQQQERAAMSYVKLRTNLQHAI (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_041119"
FT   VARIANT         69..1231
FT                   /note="Missing (in HPE13 and MKMS; patient cells show
FT                   decreased protein abundance; increased sister chromatid
FT                   cohesion)"
FT                   /evidence="ECO:0000269|PubMed:28296084,
FT                   ECO:0000269|PubMed:31334757"
FT                   /id="VAR_083967"
FT   VARIANT         140..1231
FT                   /note="Missing (in MKMS)"
FT                   /evidence="ECO:0000269|PubMed:30158690"
FT                   /id="VAR_082294"
FT   VARIANT         146..1231
FT                   /note="Missing (in HPE13)"
FT                   /evidence="ECO:0000269|PubMed:31334757"
FT                   /id="VAR_083968"
FT   VARIANT         159
FT                   /note="Y -> C (in MKMS)"
FT                   /evidence="ECO:0000269|PubMed:30158690"
FT                   /id="VAR_082295"
FT   VARIANT         259..1231
FT                   /note="Missing (in HPE13)"
FT                   /evidence="ECO:0000269|PubMed:31334757"
FT                   /id="VAR_083969"
FT   VARIANT         327
FT                   /note="S -> N (in MKMS; loss of interaction with RAD21;
FT                   loss of interaction with cohesin complex)"
FT                   /evidence="ECO:0000269|PubMed:29263825"
FT                   /id="VAR_082296"
FT   VARIANT         535..1231
FT                   /note="Missing (in MKMS)"
FT                   /evidence="ECO:0000269|PubMed:30158690"
FT                   /id="VAR_082297"
FT   VARIANT         604
FT                   /note="R -> Q (in MKMS; unknown pathological significance)"
FT                   /evidence="ECO:0000269|PubMed:28296084,
FT                   ECO:0000269|PubMed:30158690"
FT                   /id="VAR_082298"
FT   VARIANT         699
FT                   /note="N -> K (in dbSNP:rs6655782)"
FT                   /id="VAR_060114"
FT   VARIANT         1009
FT                   /note="K -> N (in MKMS)"
FT                   /evidence="ECO:0000269|PubMed:30447054"
FT                   /id="VAR_082300"
FT   VARIANT         1012..1231
FT                   /note="Missing (in HPE13)"
FT                   /evidence="ECO:0000269|PubMed:31334757"
FT                   /id="VAR_083970"
FT   CONFLICT        46
FT                   /note="G -> D (in Ref. 1; CAD38591)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        302
FT                   /note="A -> R (in Ref. 5; CAA99732)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        327
FT                   /note="S -> G (in Ref. 1; CAD38591)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        607..608
FT                   /note="KH -> ND (in Ref. 5; CAA99732)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        706
FT                   /note="W -> R (in Ref. 5; CAA99732)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        710
FT                   /note="A -> V (in Ref. 1; CAD38591)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        835
FT                   /note="I -> T (in Ref. 1; CAD38591)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        971
FT                   /note="A -> T (in Ref. 1; CAH18271)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        992
FT                   /note="H -> Y (in Ref. 1; CAD38591)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1105
FT                   /note="S -> T (in Ref. 5; CAA99732)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1144
FT                   /note="M -> K (in Ref. 5; CAA99732)"
FT                   /evidence="ECO:0000305"
FT   HELIX           81..89
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           95..108
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           110..124
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           133..138
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           141..151
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           160..162
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           166..185
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   TURN            186..189
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           190..192
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   STRAND          193..195
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           196..207
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           213..252
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           261..291
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           293..296
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   STRAND          299..301
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           302..318
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           320..323
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           326..335
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           341..356
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           363..377
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           378..380
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   STRAND          381..383
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           384..400
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   STRAND          402..404
FT                   /evidence="ECO:0007829|PDB:4PJW"
FT   HELIX           407..415
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           416..418
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   STRAND          419..421
FT                   /evidence="ECO:0007829|PDB:4PJW"
FT   HELIX           422..436
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           458..470
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   STRAND          475..477
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           478..483
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   TURN            485..487
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           489..492
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           495..501
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           515..533
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   TURN            539..541
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           550..577
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   TURN            578..580
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           582..588
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           592..594
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           598..602
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           606..621
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           626..639
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           647..672
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   STRAND          674..676
FT                   /evidence="ECO:0007829|PDB:4PK7"
FT   HELIX           681..700
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           704..706
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           709..722
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           727..747
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   STRAND          751..753
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           757..775
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           781..797
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           800..802
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   TURN            804..806
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           808..810
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   TURN            811..813
FT                   /evidence="ECO:0007829|PDB:4PK7"
FT   HELIX           819..832
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           851..873
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           879..882
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           883..886
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   TURN            887..892
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           893..910
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           912..933
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           943..957
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           967..981
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   STRAND          982..984
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   STRAND          987..989
FT                   /evidence="ECO:0007829|PDB:4PJW"
FT   HELIX           995..998
FT                   /evidence="ECO:0007829|PDB:4PK7"
FT   HELIX           999..1003
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           1004..1009
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           1014..1025
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   HELIX           1028..1032
FT                   /evidence="ECO:0007829|PDB:6QNX"
FT   STRAND          1035..1037
FT                   /evidence="ECO:0007829|PDB:4PJU"
FT   HELIX           1039..1045
FT                   /evidence="ECO:0007829|PDB:6QNX"
SQ   SEQUENCE   1231 AA;  141326 MW;  692358EFFFF61BB9 CRC64;
     MIAAPEIPTD FNLLQESETH FSSDTDFEDI EGKNQKQGKG KTCKKGKKGP AEKGKGGNGG
     GKPPSGPNRM NGHHQQNGVE NMMLFEVVKM GKSAMQSVVD DWIESYKHDR DIALLDLINF
     FIQCSGCKGV VTAEMFRHMQ NSEIIRKMTE EFDEDSGDYP LTMAGPQWKK FKSSFCEFIG
     VLVRQCQYSI IYDEYMMDTV ISLLTGLSDS QVRAFRHTST LAAMKLMTAL VNVALNLSIN
     MDNTQRQYEA ERNKMIGKRA NERLELLLQK RKELQENQDE IENMMNAIFK GVFVHRYRDA
     IAEIRAICIE EIGIWMKMYS DAFLNDSYLK YVGWTMHDKQ GEVRLKCLTA LQGLYYNKEL
     NSKLELFTSR FKDRIVSMTL DKEYDVAVQA IKLLTLVLQS SEEVLTAEDC ENVYHLVYSA
     HRPVAVAAGE FLYKKLFSRR DPEEDGMMKR RGRQGPNANL VKTLVFFFLE SELHEHAAYL
     VDSMWDCATE LLKDWECMNS LLLEEPLSGE EALTDRQESA LIEIMLCTIR QAAECHPPVG
     RGTGKRVLTA KEKKTQLDDR TKITELFAVA LPQLLAKYSV DAEKVTNLLQ LPQYFDLEIY
     TTGRLEKHLD ALLRQIRNIV EKHTDTDVLE ACSKTYHALC NEEFTIFNRV DISRSQLIDE
     LADKFNRLLE DFLQEGEEPD EDDAYQVLST LKRITAFHNA HDLSKWDLFA CNYKLLKTGI
     ENGDMPEQIV IHALQCTHYV ILWQLAKITE SSSTKEDLLR LKKQMRVFCQ ICQHYLTNVN
     TTVKEQAFTI LCDILMIFSH QIMSGGRDML EPLVYTPDSS LQSELLSFIL DHVFIEQDDD
     NNSADGQQED EASKIEALHK RRNLLAAFCK LIVYTVVEMN TAADIFKQYM KYYNDYGDII
     KETMSKTRQI DKIQCAKTLI LSLQQLFNEM IQENGYNFDR SSSTFSGIKE LARRFALTFG
     LDQLKTREAI AMLHKDGIEF AFKEPNPQGE SHPPLNLAFL DILSEFSSKL LRQDKRTVYV
     YLEKFMTFQM SLRREDVWLP LMSYRNSLLA GGDDDTMSVI SGISSRGSTV RSKKSKPSTG
     KRKVVEGMQL SLTEESSSSD SMWLSREQTL HTPVMMQTPQ LTSTIMREPK RLRPEDSFMS
     VYPMQTEHHQ TPLDYNRRGT SLMEDDEEPI VEDVMMSSEG RIEDLNEGMD FDTMDIDLPP
     SKNRRERTEL KPDFFDPASI MDESVLGVSM F
 
 
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