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-2

Gene

Stag2

Organism
Mus musculus (Mouse)
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 (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, Meiosis, 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-2
Alternative name(s):
SCC3 homolog 2
Stromal antigen 2
Gene namesi
Name:Stag2
Synonyms:Sa2, Sap2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1098583. Stag2.

Subcellular locationi

  • Nucleus
  • Chromosome By similarity
  • Chromosomecentromere 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. In germ cells, cohesin complex dissociates from chromatin at prophase I, and may be replaced by a meiosis-specific cohesin complex (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12311231Cohesin subunit SA-2PRO_0000120186Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei607 – 6071N6-acetyllysineBy similarity
Modified residuei1058 – 10581PhosphoserineCombined sources
Modified residuei1061 – 10611PhosphoserineCombined sources
Modified residuei1064 – 10641PhosphoserineCombined sources
Modified residuei1065 – 10651PhosphoserineCombined sources
Modified residuei1112 – 11121PhosphothreonineBy similarity
Modified residuei1177 – 11771PhosphoserineBy similarity
Modified residuei1178 – 11781PhosphoserineBy 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

Acetylation, Phosphoprotein

Proteomic databases

EPDiO35638.
MaxQBiO35638.
PaxDbiO35638.
PeptideAtlasiO35638.
PRIDEiO35638.

PTM databases

iPTMnetiO35638.
PhosphoSiteiO35638.

Expressioni

Gene expression databases

BgeeiENSMUSG00000025862.
CleanExiMM_STAG2.
ExpressionAtlasiO35638. baseline and differential.
GenevisibleiO35638. 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, STAG2 is mutually exclusive with STAG1 and STAG3 (By similarity).By similarity

Protein-protein interaction databases

BioGridi203518. 17 interactions.
DIPiDIP-56691N.
IntActiO35638. 17 interactions.
MINTiMINT-4135769.
STRINGi10090.ENSMUSP00000063250.

Structurei

3D structure databases

ProteinModelPortaliO35638.
SMRiO35638. Positions 83-1048.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini293 – 37886SCDPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1096 – 11016Poly-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.
InParanoidiO35638.
KOiK06671.
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.

O35638-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIAAPEIPTD FNLLQESETH FSSDTDFEDI EGKNQKQGKG KTCKKGKKGP
60 70 80 90 100
AEKGKSGNGG GKPPSGSNRM NGHHQQNGVE NMMLFEVVKM GKSAMQSVVD
110 120 130 140 150
DWIESYKHDR DIALLDLINF FIQCSGCKGV VTAEMFRHMQ NSEIIRKMTE
160 170 180 190 200
EFDEDSGDYP LTMAGPQWKK FKSSFCEFIG VLVRQCQYSI IYDEYMMDTV
210 220 230 240 250
ISLLTGLSDS QVRAFRHTST LAAMKLMTAL VNVALNLSIN MDNTQRQYEA
260 270 280 290 300
ERNKMIGKRA NERLELLLQK RKELQENQDE IENMMNAIFK GVFVHRYRDA
310 320 330 340 350
IAEIRAICIE EIGIWMKMYS DAFLNDSYLK YVGWTMHDKQ GEVRLKCLTA
360 370 380 390 400
LQGLYYNKEL NSKLELFTSR FKDRIVSMTL DKEYDVAVQA IKLLTLVLQS
410 420 430 440 450
SEEVLTAEDC ENVYHLVYSA HRPVAVAAGE FLYKKLFSRR DPEEDGLMKR
460 470 480 490 500
RGRQGPNANL VKTLVFFFLE SELHEHAAYL VDSMWDCATE LLKDWECMNS
510 520 530 540 550
LLLEEPLSGE EALTDRQESA LIEIMLCTIR QAAECHPPVG RGTGKRVLTA
560 570 580 590 600
KEKKTQLDDR TRITELFAVA LPQLLAKYSV DAEKVTNLLQ LPQYFDLEIY
610 620 630 640 650
TTGRLEKHLD ALLRQIRNIV EKHTDTDVLE ACSKTYHALC NEEFTIFNRV
660 670 680 690 700
DISRSQLIDE LADKFNRLLE DFLQEGEEPD EDDAYQVLST LKRITAFHNA
710 720 730 740 750
HDLSKWDLFA CNYKLLKTGI ENGDMPEQIV IHALQCAHYV ILWQLAKITE
760 770 780 790 800
STSTKEDLLR LKKQMRVFCQ ICQHYLTNVN TTVKEQAFTI LCDILMIFSH
810 820 830 840 850
QIMSGGRDML EPLVYTPDSS LQSELLSFIL DHVFIEQDDD SNSADGQQED
860 870 880 890 900
EASKIEALHK RRNLLAAFCK LIVYTVVEMN TAADIFKQYM KYYNDYGDII
910 920 930 940 950
KETMSKTRQI DKIQCAKTLI LSLQQLFNEM IQENGYNFDR SSSTFSGIKE
960 970 980 990 1000
LARRFALTFG LDQLKTREAI AMLHKDGIEF AFKEPNPQGE SHPPLNLAFL
1010 1020 1030 1040 1050
DILSEFSSKL LRQDKRTVYV YLEKFMTFQM SLRREDVWLP LMSYRNSLLA
1060 1070 1080 1090 1100
GGDDDTMSVI SGMSSRGSTV RSKKSKPSTG KRKVVEGMQL ALPEESSSSD
1110 1120 1130 1140 1150
SMWLSREQTL HTPVMMQTPQ LTSTIMREPK RLRPEDSFMS VYPMQAEHHQ
1160 1170 1180 1190 1200
TPLDYNRRGT SLMEDDEEPI VEDVMMSSEG RIEDLNEGMD FDTMDIDLPP
1210 1220 1230
SKNRRERTEL KPDFFDPASI MDESVLGVSM F
Length:1,231
Mass (Da):141,281
Last modified:July 27, 2011 - v3
Checksum:iAD7ECB66E18C080B
GO

Sequence cautioni

The sequence BC066041 differs from that shown. Reason: Frameshift at position 54. Curated
The sequence BC066041 differs from that shown. Reason: Frameshift at position 53. Curated
The sequence CAA05638 differs from that shown. Reason: Frameshift at position 22. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81P → Q in CAA05638 (Ref. 1) Curated
Sequence conflicti34 – 341N → I in CAA05638 (Ref. 1) Curated
Sequence conflicti299 – 2991D → Y in CAA05638 (Ref. 1) Curated
Sequence conflicti607 – 6082KH → ND in CAA05638 (Ref. 1) Curated
Sequence conflicti881 – 8811T → S in CAA05638 (Ref. 1) Curated
Sequence conflicti951 – 9511L → F in CAA05638 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ002636 mRNA. Translation: CAA05638.1. Frameshift.
AL672089 Genomic DNA. Translation: CAM20005.1.
BC066041 mRNA. No translation available.
CCDSiCCDS40952.1.
PIRiT30194.
RefSeqiNP_001071180.1. NM_001077712.2.
NP_067440.3. NM_021465.4.
XP_011249291.1. XM_011250989.1.
UniGeneiMm.290422.

Genome annotation databases

EnsembliENSMUST00000069619; ENSMUSP00000063250; ENSMUSG00000025862.
ENSMUST00000115072; ENSMUSP00000110724; ENSMUSG00000025862.
GeneIDi20843.
KEGGimmu:20843.
UCSCiuc009tax.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ002636 mRNA. Translation: CAA05638.1. Frameshift.
AL672089 Genomic DNA. Translation: CAM20005.1.
BC066041 mRNA. No translation available.
CCDSiCCDS40952.1.
PIRiT30194.
RefSeqiNP_001071180.1. NM_001077712.2.
NP_067440.3. NM_021465.4.
XP_011249291.1. XM_011250989.1.
UniGeneiMm.290422.

3D structure databases

ProteinModelPortaliO35638.
SMRiO35638. Positions 83-1048.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203518. 17 interactions.
DIPiDIP-56691N.
IntActiO35638. 17 interactions.
MINTiMINT-4135769.
STRINGi10090.ENSMUSP00000063250.

PTM databases

iPTMnetiO35638.
PhosphoSiteiO35638.

Proteomic databases

EPDiO35638.
MaxQBiO35638.
PaxDbiO35638.
PeptideAtlasiO35638.
PRIDEiO35638.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000069619; ENSMUSP00000063250; ENSMUSG00000025862.
ENSMUST00000115072; ENSMUSP00000110724; ENSMUSG00000025862.
GeneIDi20843.
KEGGimmu:20843.
UCSCiuc009tax.2. mouse.

Organism-specific databases

CTDi10735.
MGIiMGI:1098583. Stag2.

Phylogenomic databases

eggNOGiKOG2011. Eukaryota.
COG5537. LUCA.
GeneTreeiENSGT00390000014094.
HOGENOMiHOG000231375.
HOVERGENiHBG057636.
InParanoidiO35638.
KOiK06671.
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

PROiO35638.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000025862.
CleanExiMM_STAG2.
ExpressionAtlasiO35638. baseline and differential.
GenevisibleiO35638. 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...

Entry informationi

Entry nameiSTAG2_MOUSE
AccessioniPrimary (citable) accession number: O35638
Secondary accession number(s): A2AFF5, Q6NZN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: July 27, 2011
Last modified: September 7, 2016
This is version 118 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.