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Protein

Cohesin subunit SA-1

Gene

STAG1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition, Mitosis

Enzyme and pathway databases

ReactomeiR-HSA-1221632. Meiotic synapsis.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2468052. Establishment of Sister Chromatid Cohesion.
R-HSA-2470946. Cohesin Loading onto Chromatin.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Cohesin subunit SA-1
Alternative name(s):
SCC3 homolog 1
Stromal antigen 1
Gene namesi
Name:STAG1
Synonyms:SA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:11354. STAG1.

Subcellular locationi

  • Nucleus
  • Chromosome
  • Chromosomecentromere

  • Note: Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK1, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of cohesin is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation.

GO - Cellular componenti

  • chromatin Source: UniProtKB
  • chromosome Source: Reactome
  • chromosome, centromeric region Source: Reactome
  • cytosol Source: Reactome
  • nucleoplasm Source: HPA
  • nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36176.

Polymorphism and mutation databases

BioMutaiSTAG1.
DMDMi209572720.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12581258Cohesin subunit SA-1PRO_0000120182Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241PhosphoserineCombined sources
Modified residuei756 – 7561PhosphoserineCombined sources
Modified residuei1062 – 10621PhosphoserineCombined sources
Modified residuei1065 – 10651PhosphoserineBy similarity
Modified residuei1093 – 10931PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by PLK1. The large dissociation of cohesin from chromosome arms during prophase is partly due to its phosphorylation (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8WVM7.
MaxQBiQ8WVM7.
PaxDbiQ8WVM7.
PeptideAtlasiQ8WVM7.
PRIDEiQ8WVM7.

PTM databases

iPTMnetiQ8WVM7.
PhosphoSiteiQ8WVM7.

Expressioni

Gene expression databases

BgeeiQ8WVM7.
CleanExiHS_STAG1.
ExpressionAtlasiQ8WVM7. baseline and differential.
GenevisibleiQ8WVM7. HS.

Organism-specific databases

HPAiHPA035015.
HPA058653.

Interactioni

Subunit structurei

Interacts directly with RAD21 in cohesin complex. Cohesin complexes are composed of a heterodimer between a SMC1 protein (SMC1A or SMC1B) and SMC3, which are attached via their hinge domain, and RAD21 which link them at their heads, and one STAG protein (STAG1, STAG2 or STAG3). In cohesin complexes, STAG1 is mutually exclusive with STAG2 and STAG3.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PDS5AQ29RF73EBI-1175097,EBI-1175454
PDS5BQ9NTI53EBI-1175097,EBI-1175604
SMC3Q9UQE711EBI-1175097,EBI-80718
TERF1P542744EBI-1175097,EBI-710997

Protein-protein interaction databases

BioGridi115564. 33 interactions.
DIPiDIP-35421N.
IntActiQ8WVM7. 19 interactions.
STRINGi9606.ENSP00000372689.

Structurei

3D structure databases

ProteinModelPortaliQ8WVM7.
SMRiQ8WVM7. Positions 87-1052.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini296 – 38186SCDPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi684 – 6874Poly-Asp
Compositional biasi1065 – 10706Poly-Ser

Sequence similaritiesi

Belongs to the SCC3 family.Curated
Contains 1 SCD (stromalin conservative) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2011. Eukaryota.
COG5537. LUCA.
GeneTreeiENSGT00390000014094.
HOGENOMiHOG000231375.
HOVERGENiHBG057636.
InParanoidiQ8WVM7.
KOiK06671.
OMAiMQMSWLG.
OrthoDBiEOG7NGQ9M.
PhylomeDBiQ8WVM7.
TreeFamiTF314604.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR020839. SCD.
IPR013721. STAG.
[Graphical view]
PfamiPF08514. STAG. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
PROSITEiPS51425. SCD. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8WVM7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MITSELPVLQ DSTNETTAHS DAGSELEETE VKGKRKRGRP GRPPSTNKKP
60 70 80 90 100
RKSPGEKSRI EAGIRGAGRG RANGHPQQNG EGEPVTLFEV VKLGKSAMQS
110 120 130 140 150
VVDDWIESYK QDRDIALLDL INFFIQCSGC RGTVRIEMFR NMQNAEIIRK
160 170 180 190 200
MTEEFDEDSG DYPLTMPGPQ WKKFRSNFCE FIGVLIRQCQ YSIIYDEYMM
210 220 230 240 250
DTVISLLTGL SDSQVRAFRH TSTLAAMKLM TALVNVALNL SIHQDNTQRQ
260 270 280 290 300
YEAERNKMIG KRANERLELL LQKRKELQEN QDEIENMMNS IFKGIFVHRY
310 320 330 340 350
RDAIAEIRAI CIEEIGVWMK MYSDAFLNDS YLKYVGWTLH DRQGEVRLKC
360 370 380 390 400
LKALQSLYTN RELFPKLELF TNRFKDRIVS MTLDKEYDVA VEAIRLVTLI
410 420 430 440 450
LHGSEEALSN EDCENVYHLV YSAHRPVAVA AGEFLHKKLF SRHDPQAEEA
460 470 480 490 500
LAKRRGRNSP NGNLIRMLVL FFLESELHEH AAYLVDSLWE SSQELLKDWE
510 520 530 540 550
CMTELLLEEP VQGEEAMSDR QESALIELMV CTIRQAAEAH PPVGRGTGKR
560 570 580 590 600
VLTAKERKTQ IDDRNKLTEH FIITLPMLLS KYSADAEKVA NLLQIPQYFD
610 620 630 640 650
LEIYSTGRME KHLDALLKQI KFVVEKHVES DVLEACSKTY SILCSEEYTI
660 670 680 690 700
QNRVDIARSQ LIDEFVDRFN HSVEDLLQEG EEADDDDIYN VLSTLKRLTS
710 720 730 740 750
FHNAHDLTKW DLFGNCYRLL KTGIEHGAMP EQIVVQALQC SHYSILWQLV
760 770 780 790 800
KITDGSPSKE DLLVLRKTVK SFLAVCQQCL SNVNTPVKEQ AFMLLCDLLM
810 820 830 840 850
IFSHQLMTGG REGLQPLVFN PDTGLQSELL SFVMDHVFID QDEENQSMEG
860 870 880 890 900
DEEDEANKIE ALHKRRNLLA AFSKLIIYDI VDMHAAADIF KHYMKYYNDY
910 920 930 940 950
GDIIKETLSK TRQIDKIQCA KTLILSLQQL FNELVQEQGP NLDRTSAHVS
960 970 980 990 1000
GIKELARRFA LTFGLDQIKT REAVATLHKD GIEFAFKYQN QKGQEYPPPN
1010 1020 1030 1040 1050
LAFLEVLSEF SSKLLRQDKK TVHSYLEKFL TEQMMERRED VWLPLISYRN
1060 1070 1080 1090 1100
SLVTGGEDDR MSVNSGSSSS KTSSVRNKKG RPPLHKKRVE DESLDNTWLN
1110 1120 1130 1140 1150
RTDTMIQTPG PLPAPQLTST VLRENSRPMG DQIQEPESEH GSEPDFLHNP
1160 1170 1180 1190 1200
QMQISWLGQP KLEDLNRKDR TGMNYMKVRT GVRHAVRGLM EEDAEPIFED
1210 1220 1230 1240 1250
VMMSSRSQLE DMNEEFEDTM VIDLPPSRNR RERAELRPDF FDSAAIIEDD

SGFGMPMF
Length:1,258
Mass (Da):144,427
Last modified:October 14, 2008 - v3
Checksum:iFAF911998EC52179
GO
Isoform 2 (identifier: Q8WVM7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1150-1186: Missing.

Note: No experimental confirmation available.
Show »
Length:1,221
Mass (Da):140,090
Checksum:iF0FAFDD544430F8F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti645 – 6451S → N in CAA99731 (PubMed:9305759).Curated
Sequence conflicti702 – 7021H → Q in CAA99731 (PubMed:9305759).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1132 – 11321Q → H.
Corresponds to variant rs34149860 [ dbSNP | Ensembl ].
VAR_046968

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1150 – 118637Missing in isoform 2. 1 PublicationVSP_054496Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75330 mRNA. Translation: CAA99731.1.
AC069514 Genomic DNA. No translation available.
AC069524 Genomic DNA. No translation available.
AC107425 Genomic DNA. No translation available.
AC117382 Genomic DNA. No translation available.
AC128712 Genomic DNA. No translation available.
BC017735 mRNA. Translation: AAH17735.1.
BC064699 mRNA. Translation: AAH64699.1.
CCDSiCCDS3090.1. [Q8WVM7-1]
RefSeqiNP_005853.2. NM_005862.2. [Q8WVM7-1]
UniGeneiHs.412586.

Genome annotation databases

EnsembliENST00000236698; ENSP00000236698; ENSG00000118007. [Q8WVM7-2]
ENST00000383202; ENSP00000372689; ENSG00000118007. [Q8WVM7-1]
GeneIDi10274.
KEGGihsa:10274.
UCSCiuc003era.2. human. [Q8WVM7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75330 mRNA. Translation: CAA99731.1.
AC069514 Genomic DNA. No translation available.
AC069524 Genomic DNA. No translation available.
AC107425 Genomic DNA. No translation available.
AC117382 Genomic DNA. No translation available.
AC128712 Genomic DNA. No translation available.
BC017735 mRNA. Translation: AAH17735.1.
BC064699 mRNA. Translation: AAH64699.1.
CCDSiCCDS3090.1. [Q8WVM7-1]
RefSeqiNP_005853.2. NM_005862.2. [Q8WVM7-1]
UniGeneiHs.412586.

3D structure databases

ProteinModelPortaliQ8WVM7.
SMRiQ8WVM7. Positions 87-1052.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115564. 33 interactions.
DIPiDIP-35421N.
IntActiQ8WVM7. 19 interactions.
STRINGi9606.ENSP00000372689.

PTM databases

iPTMnetiQ8WVM7.
PhosphoSiteiQ8WVM7.

Polymorphism and mutation databases

BioMutaiSTAG1.
DMDMi209572720.

Proteomic databases

EPDiQ8WVM7.
MaxQBiQ8WVM7.
PaxDbiQ8WVM7.
PeptideAtlasiQ8WVM7.
PRIDEiQ8WVM7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000236698; ENSP00000236698; ENSG00000118007. [Q8WVM7-2]
ENST00000383202; ENSP00000372689; ENSG00000118007. [Q8WVM7-1]
GeneIDi10274.
KEGGihsa:10274.
UCSCiuc003era.2. human. [Q8WVM7-1]

Organism-specific databases

CTDi10274.
GeneCardsiSTAG1.
H-InvDBHIX0030898.
HGNCiHGNC:11354. STAG1.
HPAiHPA035015.
HPA058653.
MIMi604358. gene.
neXtProtiNX_Q8WVM7.
PharmGKBiPA36176.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2011. Eukaryota.
COG5537. LUCA.
GeneTreeiENSGT00390000014094.
HOGENOMiHOG000231375.
HOVERGENiHBG057636.
InParanoidiQ8WVM7.
KOiK06671.
OMAiMQMSWLG.
OrthoDBiEOG7NGQ9M.
PhylomeDBiQ8WVM7.
TreeFamiTF314604.

Enzyme and pathway databases

ReactomeiR-HSA-1221632. Meiotic synapsis.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2468052. Establishment of Sister Chromatid Cohesion.
R-HSA-2470946. Cohesin Loading onto Chromatin.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.

Miscellaneous databases

ChiTaRSiSTAG1. human.
GeneWikiiSTAG1.
GenomeRNAii10274.
PROiQ8WVM7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WVM7.
CleanExiHS_STAG1.
ExpressionAtlasiQ8WVM7. baseline and differential.
GenevisibleiQ8WVM7. HS.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR020839. SCD.
IPR013721. STAG.
[Graphical view]
PfamiPF08514. STAG. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
PROSITEiPS51425. SCD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "SA-1, a nuclear protein encoded by one member of a novel gene family: molecular cloning and detection in hemopoietic organs."
    Carramolino L., Lee B.C., Zaballos A., Peled A., Barthelemy I., Shav-Tal Y., Prieto I., Carmi P., Gothelf Y., Gonzalez de Buitrago G., Aracil M., Marquez G., Barbero J.L., Zipori D.
    Gene 195:151-159(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Thymus.
  2. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 787-1258 (ISOFORM 1).
    Tissue: Placenta.
  4. "Characterization of vertebrate cohesin complexes and their regulation in prophase."
    Sumara I., Vorlaufer E., Gieffers C., Peters B.H., Peters J.-M.
    J. Cell Biol. 151:749-762(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1A AND SMC3.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1062, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-756 AND SER-1093, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.

Entry informationi

Entry nameiSTAG1_HUMAN
AccessioniPrimary (citable) accession number: Q8WVM7
Secondary accession number(s): O00539, Q6P275
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 14, 2008
Last modified: July 6, 2016
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.