STAG1_MOUSE
ID STAG1_MOUSE Reviewed; 1258 AA.
AC Q9D3E6; O08982; Q6P5D1;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Cohesin subunit SA-1;
DE AltName: Full=SCC3 homolog 1;
DE AltName: Full=Stromal antigen 1;
GN Name=Stag1; Synonyms=Sa1;
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=Bone marrow stroma;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1062 AND SER-1065, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, 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: Cohesin complexes are composed of a heterodimer between a SMC1
CC protein (SMC1A or SMC1B) and SMC3, which are attached via their hinge
CC domain, and RAD21 which link them at their heads, and one STAG protein
CC (STAG1, STAG2 or STAG3). In cohesin complexes, STAG1 is mutually
CC exclusive with STAG2 and STAG3. Interacts directly with RAD21 in
CC cohesin complex. Found in a cohesin complex with SMC1A, SMC3 and RAD21.
CC {ECO:0000250|UniProtKB:Q8WVM7, ECO:0000250|UniProtKB:Q9DGN1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00750}.
CC Chromosome {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 (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=BAB31022.1; Type=Miscellaneous discrepancy; Note=Probable exon deletions within the cDNA.; Evidence={ECO:0000305};
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DR EMBL; Z75332; CAA99733.1; -; mRNA.
DR EMBL; AK017978; BAB31022.1; ALT_SEQ; mRNA.
DR EMBL; BC062954; AAH62954.1; -; mRNA.
DR CCDS; CCDS23441.1; -.
DR PIR; T30252; T30252.
DR RefSeq; NP_033308.2; NM_009282.3.
DR RefSeq; XP_006510986.1; XM_006510923.2.
DR RefSeq; XP_006510987.1; XM_006510924.2.
DR AlphaFoldDB; Q9D3E6; -.
DR SMR; Q9D3E6; -.
DR BioGRID; 203517; 5.
DR IntAct; Q9D3E6; 4.
DR MINT; Q9D3E6; -.
DR STRING; 10090.ENSMUSP00000116205; -.
DR iPTMnet; Q9D3E6; -.
DR PhosphoSitePlus; Q9D3E6; -.
DR EPD; Q9D3E6; -.
DR MaxQB; Q9D3E6; -.
DR PaxDb; Q9D3E6; -.
DR PeptideAtlas; Q9D3E6; -.
DR PRIDE; Q9D3E6; -.
DR ProteomicsDB; 254578; -.
DR Antibodypedia; 17829; 271 antibodies from 28 providers.
DR DNASU; 20842; -.
DR Ensembl; ENSMUST00000129269; ENSMUSP00000116205; ENSMUSG00000037286.
DR GeneID; 20842; -.
DR KEGG; mmu:20842; -.
DR UCSC; uc009rfa.1; mouse.
DR CTD; 10274; -.
DR MGI; MGI:1098658; Stag1.
DR VEuPathDB; HostDB:ENSMUSG00000037286; -.
DR eggNOG; KOG2011; Eukaryota.
DR GeneTree; ENSGT00950000182972; -.
DR InParanoid; Q9D3E6; -.
DR OMA; XIVVQAL; -.
DR OrthoDB; 167826at2759; -.
DR PhylomeDB; Q9D3E6; -.
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; 20842; 9 hits in 76 CRISPR screens.
DR ChiTaRS; Stag1; mouse.
DR PRO; PR:Q9D3E6; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9D3E6; protein.
DR Bgee; ENSMUSG00000037286; Expressed in embryonic post-anal tail and 255 other tissues.
DR ExpressionAtlas; Q9D3E6; baseline and differential.
DR Genevisible; Q9D3E6; MM.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0008278; C:cohesin complex; ISO:MGI.
DR GO; GO:0097431; C:mitotic spindle pole; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; 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:0090307; P:mitotic spindle assembly; ISO:MGI.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039662; Cohesin_Scc3/SA.
DR InterPro; IPR020839; SCD.
DR InterPro; IPR013721; STAG.
DR PANTHER; PTHR11199; PTHR11199; 1.
DR Pfam; PF08514; STAG; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51425; SCD; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; Chromosome partition;
KW Isopeptide bond; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..1258
FT /note="Cohesin subunit SA-1"
FT /id="PRO_0000120183"
FT DOMAIN 296..381
FT /note="SCD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00750"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1077
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVM7"
FT MOD_RES 756
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVM7"
FT MOD_RES 1062
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 1093
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVM7"
FT CROSSLNK 1161
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WVM7"
FT CONFLICT 22..25
FT /note="AGSE -> HGRQ (in Ref. 1; CAA99733)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="A -> R (in Ref. 1; CAA99733)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1258 AA; 144440 MW; E32F33609D035F9C CRC64;
MITSELPVLQ DSTNETTAHS DAGSELEETE VKGKRKRGRP GRPPSTNKKP RKSPGEKSRI
EAGIRGAGRG RANGHPQQNG DGDPVTLFEV VKLGKSAMQS VVDDWIELYK QDRDIALLDL
INFFIQCSGC RGTVRIEMFR NMQNAEIIRK MTEEFDEDSG DYPLTMPGPQ WKKFRSNFCE
FIGVLIRQCQ YSIIYDEYMM DTVISLLTGL SDSQVRAFRH TSTLAAMKLM TALVNVALNL
SIHQDNTQRQ YEAERNKMIG KRANERLELL LQKRKELQEN QDEIENMMNS IFKGIFVHRY
RDAIAEIRAI CIEEIGVWMK MYSDAFLNDS YLKYVGWTLH DRQGEVRLKC LKALQSLYTN
RELFPKLELF TNRFKDRIVS MTLDKEYDVA VEAIRLVTLI LHGSEEALSN EDCENVYHLV
YSAHRPVAVA AGEFLHKKLF SRHDPQAEEA LAKRRGRNSP NGNLIRMLVL FFLESELHEH
AAYLVDSLWE SSQELLKDWE CMTELLLEEP VQGEEAMSDR QESALIELMV CTIRQAAEAH
PPVGRGTGKR VLTAKERKTQ IDDRNKLTEH FIITLPMLLS KYSADAEKVA NLLQIPQYFD
LEIYSTGRME KHLDALLKQI KFVVEKHVES DVLEACSKTY SILCSEEYTI QNRVDIARSQ
LIDEFVDRFN HSVEDLLQEG EEADDDDIYN VLSTLKRLTS FHNAHDLTKW DLFGNCYRLL
KTGIEHGAMP EQIVVQALQC SHYSILWQLV KITDGSPSKE DLLVLRKTVK SFLAVCQQCL
SNVNTPVKEQ AFMLLCDLLM IFSHQLMTGG REGLQPLVFN PDTGLQSELL SFVMDHVFID
QDEENQSMEG DEEDEANKIE ALHKRRNLLA AFSKLIIYDI VDMHAAADIF KHYMKYYNDY
GDIIKETLSK TRQIDKIQCA KTLILSLQQL FNELVQEQGP NLDRTSAHVS GIKELARRFA
LTFGLDQIKT REAVATLHKD GIEFAFKYQN QKGQEYPPPN LAFLEVLSEF SSKLLRQDKK
TVHSYLEKFL TEQMMERRED VWLPLISYRN SLVTGGEDDR MSVNSGSSSS KTSSVRSKKG
RPPLHRKRVE DESLDNTWLN RTDTMIQTPG PLPTPQLTST VLRENSRPMG EQIQEPESEH
GSEPDFLHNP QMQISWLGQP KLEDLNRKDR TGMNYMKVRA GVRHAVRGLM EEDAEPIFED
VMMSSRSQLE DMNEEFEDTM VIDLPPSRNR RERAELRPDF FDSAAIIEDD SGFGMPMF
