Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cohesin subunit SA-1

Gene

Stag1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

GO - Molecular functioni

  • chromatin binding Source: MGI
  • transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition, Mitosis

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2468052. Establishment of Sister Chromatid Cohesion.
R-MMU-2470946. Cohesin Loading onto Chromatin.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1098658. Stag1.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation
  • Chromosome By similarity

  • 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 (By similarity).By similarity

GO - Cellular componenti

  • chromatin Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12581258Cohesin subunit SA-1PRO_0000120183Add
BLAST

Amino acid modifications

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

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

EPDiQ9D3E6.
MaxQBiQ9D3E6.
PaxDbiQ9D3E6.
PeptideAtlasiQ9D3E6.
PRIDEiQ9D3E6.

PTM databases

iPTMnetiQ9D3E6.
PhosphoSiteiQ9D3E6.

Expressioni

Gene expression databases

BgeeiQ9D3E6.
CleanExiMM_STAG1.
ExpressionAtlasiQ9D3E6. baseline and differential.
GenevisibleiQ9D3E6. MM.

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi203517. 3 interactions.
IntActiQ9D3E6. 2 interactions.
MINTiMINT-4135756.
STRINGi10090.ENSMUSP00000116205.

Structurei

3D structure databases

ProteinModelPortaliQ9D3E6.
SMRiQ9D3E6. Positions 87-1052.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

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.
InParanoidiQ9D3E6.
KOiK06671.
OMAiMQMSWLG.
OrthoDBiEOG7NGQ9M.
PhylomeDBiQ9D3E6.
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]

Sequencei

Sequence statusi: Complete.

Q9D3E6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MITSELPVLQ DSTNETTAHS DAGSELEETE VKGKRKRGRP GRPPSTNKKP
60 70 80 90 100
RKSPGEKSRI EAGIRGAGRG RANGHPQQNG DGDPVTLFEV VKLGKSAMQS
110 120 130 140 150
VVDDWIELYK 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 KTSSVRSKKG RPPLHRKRVE DESLDNTWLN
1110 1120 1130 1140 1150
RTDTMIQTPG PLPTPQLTST VLRENSRPMG EQIQEPESEH GSEPDFLHNP
1160 1170 1180 1190 1200
QMQISWLGQP KLEDLNRKDR TGMNYMKVRA GVRHAVRGLM EEDAEPIFED
1210 1220 1230 1240 1250
VMMSSRSQLE DMNEEFEDTM VIDLPPSRNR RERAELRPDF FDSAAIIEDD

SGFGMPMF
Length:1,258
Mass (Da):144,440
Last modified:July 27, 2011 - v3
Checksum:iE32F33609D035F9C
GO

Sequence cautioni

The sequence BAB31022.1 differs from that shown.Probable exon deletions within the cDNA.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 254AGSE → HGRQ in CAA99733 (PubMed:9305759).Curated
Sequence conflicti97 – 971A → R in CAA99733 (PubMed:9305759).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75332 mRNA. Translation: CAA99733.1.
AK017978 mRNA. Translation: BAB31022.1. Sequence problems.
BC062954 mRNA. Translation: AAH62954.1.
CCDSiCCDS23441.1.
PIRiT30252.
RefSeqiNP_033308.2. NM_009282.3.
XP_006510986.1. XM_006510923.1.
XP_006510987.1. XM_006510924.1.
XP_011240993.1. XM_011242691.1.
UniGeneiMm.42135.

Genome annotation databases

EnsembliENSMUST00000129269; ENSMUSP00000116205; ENSMUSG00000037286.
GeneIDi20842.
KEGGimmu:20842.
UCSCiuc009rfa.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75332 mRNA. Translation: CAA99733.1.
AK017978 mRNA. Translation: BAB31022.1. Sequence problems.
BC062954 mRNA. Translation: AAH62954.1.
CCDSiCCDS23441.1.
PIRiT30252.
RefSeqiNP_033308.2. NM_009282.3.
XP_006510986.1. XM_006510923.1.
XP_006510987.1. XM_006510924.1.
XP_011240993.1. XM_011242691.1.
UniGeneiMm.42135.

3D structure databases

ProteinModelPortaliQ9D3E6.
SMRiQ9D3E6. Positions 87-1052.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203517. 3 interactions.
IntActiQ9D3E6. 2 interactions.
MINTiMINT-4135756.
STRINGi10090.ENSMUSP00000116205.

PTM databases

iPTMnetiQ9D3E6.
PhosphoSiteiQ9D3E6.

Proteomic databases

EPDiQ9D3E6.
MaxQBiQ9D3E6.
PaxDbiQ9D3E6.
PeptideAtlasiQ9D3E6.
PRIDEiQ9D3E6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000129269; ENSMUSP00000116205; ENSMUSG00000037286.
GeneIDi20842.
KEGGimmu:20842.
UCSCiuc009rfa.1. mouse.

Organism-specific databases

CTDi10274.
MGIiMGI:1098658. Stag1.

Phylogenomic databases

eggNOGiKOG2011. Eukaryota.
COG5537. LUCA.
GeneTreeiENSGT00390000014094.
HOGENOMiHOG000231375.
HOVERGENiHBG057636.
InParanoidiQ9D3E6.
KOiK06671.
OMAiMQMSWLG.
OrthoDBiEOG7NGQ9M.
PhylomeDBiQ9D3E6.
TreeFamiTF314604.

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2468052. Establishment of Sister Chromatid Cohesion.
R-MMU-2470946. Cohesin Loading onto Chromatin.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.

Miscellaneous databases

ChiTaRSiStag1. mouse.
PROiQ9D3E6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D3E6.
CleanExiMM_STAG1.
ExpressionAtlasiQ9D3E6. baseline and differential.
GenevisibleiQ9D3E6. MM.

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].
    Tissue: Bone marrow stroma.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Thymus.
  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].
    Strain: C57BL/6J.
    Tissue: Brain.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1062 AND SER-1065, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Lung, Spleen and Testis.

Entry informationi

Entry nameiSTAG1_MOUSE
AccessioniPrimary (citable) accession number: Q9D3E6
Secondary accession number(s): O08982, Q6P5D1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.