STAG2_MOUSE
ID STAG2_MOUSE Reviewed; 1231 AA.
AC O35638; A2AFF5; Q6NZN7;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Cohesin subunit SA-2;
DE AltName: Full=SCC3 homolog 2;
DE AltName: Full=Stromal antigen 2;
GN Name=Stag2; Synonyms=Sa2, Sap2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RA Barbero J.L., Carreiro C.;
RT "Homologue to human nuclear protein SA2.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1058; SER-1061; SER-1064 AND
RP SER-1065, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000250}. Chromosome,
CC centromere {ECO:0000250}. Note=Associates with chromatin. Before
CC prophase it is scattered along chromosome arms. During prophase, most
CC of cohesin complexes dissociate from chromatin probably because of
CC phosphorylation by PLK1, except at centromeres, where cohesin complexes
CC remain. At anaphase, the RAD21 subunit of cohesin is cleaved, leading
CC to the dissociation of the complex from chromosomes, allowing
CC chromosome separation. In germ cells, cohesin complex dissociates from
CC chromatin at prophase I, and may be replaced by a meiosis-specific
CC cohesin complex (By similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the SCC3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC066041; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA05638.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ002636; CAA05638.1; ALT_FRAME; mRNA.
DR EMBL; AL672089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC066041; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS40952.1; -.
DR PIR; T30194; T30194.
DR RefSeq; NP_001071180.1; NM_001077712.2.
DR RefSeq; NP_067440.3; NM_021465.4.
DR RefSeq; XP_011249291.1; XM_011250989.2.
DR RefSeq; XP_017173935.1; XM_017318446.1.
DR AlphaFoldDB; O35638; -.
DR SMR; O35638; -.
DR BioGRID; 203518; 18.
DR DIP; DIP-56691N; -.
DR IntAct; O35638; 17.
DR MINT; O35638; -.
DR STRING; 10090.ENSMUSP00000063250; -.
DR iPTMnet; O35638; -.
DR PhosphoSitePlus; O35638; -.
DR EPD; O35638; -.
DR jPOST; O35638; -.
DR MaxQB; O35638; -.
DR PaxDb; O35638; -.
DR PeptideAtlas; O35638; -.
DR PRIDE; O35638; -.
DR ProteomicsDB; 258654; -.
DR Antibodypedia; 500; 323 antibodies from 37 providers.
DR DNASU; 20843; -.
DR Ensembl; ENSMUST00000069619; ENSMUSP00000063250; ENSMUSG00000025862.
DR Ensembl; ENSMUST00000115072; ENSMUSP00000110724; ENSMUSG00000025862.
DR GeneID; 20843; -.
DR KEGG; mmu:20843; -.
DR UCSC; uc009tax.2; mouse.
DR CTD; 10735; -.
DR MGI; MGI:1098583; Stag2.
DR VEuPathDB; HostDB:ENSMUSG00000025862; -.
DR eggNOG; KOG2011; Eukaryota.
DR GeneTree; ENSGT00950000182972; -.
DR HOGENOM; CLU_005067_1_0_1; -.
DR InParanoid; O35638; -.
DR OMA; ICDLLII; -.
DR TreeFam; TF314604; -.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2468052; Establishment of Sister Chromatid Cohesion.
DR Reactome; R-MMU-2470946; Cohesin Loading onto Chromatin.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR BioGRID-ORCS; 20843; 9 hits in 79 CRISPR screens.
DR ChiTaRS; Stag2; mouse.
DR PRO; PR:O35638; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; O35638; protein.
DR Bgee; ENSMUSG00000025862; Expressed in vestibular membrane of cochlear duct and 256 other tissues.
DR ExpressionAtlas; O35638; baseline and differential.
DR Genevisible; O35638; MM.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0008278; C:cohesin complex; ISS:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0097431; C:mitotic spindle pole; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR GO; GO:0034991; C:nuclear meiotic cohesin complex; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0090307; P:mitotic spindle assembly; ISO:MGI.
DR GO; GO:0007062; P:sister chromatid cohesion; ISS:UniProtKB.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
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 Acetylation; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Meiosis; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1231
FT /note="Cohesin subunit SA-2"
FT /id="PRO_0000120186"
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 1062..1087
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 COMPBIAS 61..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3U4"
FT MOD_RES 607
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3U4"
FT MOD_RES 1058
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1061
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1064
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1065
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1112
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3U4"
FT MOD_RES 1177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3U4"
FT MOD_RES 1178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3U4"
FT CONFLICT 8
FT /note="P -> Q (in Ref. 1; CAA05638)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="N -> I (in Ref. 1; CAA05638)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="D -> Y (in Ref. 1; CAA05638)"
FT /evidence="ECO:0000305"
FT CONFLICT 607..608
FT /note="KH -> ND (in Ref. 1; CAA05638)"
FT /evidence="ECO:0000305"
FT CONFLICT 881
FT /note="T -> S (in Ref. 1; CAA05638)"
FT /evidence="ECO:0000305"
FT CONFLICT 951
FT /note="L -> F (in Ref. 1; CAA05638)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1231 AA; 141281 MW; AD7ECB66E18C080B CRC64;
MIAAPEIPTD FNLLQESETH FSSDTDFEDI EGKNQKQGKG KTCKKGKKGP AEKGKSGNGG
GKPPSGSNRM 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 DPEEDGLMKR RGRQGPNANL VKTLVFFFLE SELHEHAAYL
VDSMWDCATE LLKDWECMNS LLLEEPLSGE EALTDRQESA LIEIMLCTIR QAAECHPPVG
RGTGKRVLTA KEKKTQLDDR TRITELFAVA LPQLLAKYSV DAEKVTNLLQ LPQYFDLEIY
TTGRLEKHLD ALLRQIRNIV EKHTDTDVLE ACSKTYHALC NEEFTIFNRV DISRSQLIDE
LADKFNRLLE DFLQEGEEPD EDDAYQVLST LKRITAFHNA HDLSKWDLFA CNYKLLKTGI
ENGDMPEQIV IHALQCAHYV ILWQLAKITE STSTKEDLLR LKKQMRVFCQ ICQHYLTNVN
TTVKEQAFTI LCDILMIFSH QIMSGGRDML EPLVYTPDSS LQSELLSFIL DHVFIEQDDD
SNSADGQQED EASKIEALHK RRNLLAAFCK LIVYTVVEMN TAADIFKQYM KYYNDYGDII
KETMSKTRQI DKIQCAKTLI LSLQQLFNEM IQENGYNFDR SSSTFSGIKE LARRFALTFG
LDQLKTREAI AMLHKDGIEF AFKEPNPQGE SHPPLNLAFL DILSEFSSKL LRQDKRTVYV
YLEKFMTFQM SLRREDVWLP LMSYRNSLLA GGDDDTMSVI SGMSSRGSTV RSKKSKPSTG
KRKVVEGMQL ALPEESSSSD SMWLSREQTL HTPVMMQTPQ LTSTIMREPK RLRPEDSFMS
VYPMQAEHHQ TPLDYNRRGT SLMEDDEEPI VEDVMMSSEG RIEDLNEGMD FDTMDIDLPP
SKNRRERTEL KPDFFDPASI MDESVLGVSM F
