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Protein

Cohesin subunit SA-2

Gene

STAG2

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.1 Publication

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • cellular protein metabolic process Source: Reactome
  • meiotic cell cycle Source: UniProtKB-KW
  • mitotic cell cycle Source: Reactome
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of DNA endoreduplication Source: BHF-UCL
  • post-translational protein modification Source: Reactome
  • protein sumoylation Source: Reactome
  • sister chromatid cohesion Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition, Meiosis, 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-2
Alternative name(s):
SCC3 homolog 2
Stromal antigen 2
Gene namesi
Name:STAG2
Synonyms:SA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:11355. STAG2.

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. In germ cells, cohesin complex dissociates from chromatin at prophase I, and may be replaced by a meiosis-specific cohesin complex.

GO - Cellular componenti

  • actin cytoskeleton Source: HPA
  • chromatin Source: UniProtKB
  • chromosome Source: Reactome
  • chromosome, centromeric region Source: Reactome
  • cytosol Source: Reactome
  • intermediate filament cytoskeleton Source: HPA
  • membrane Source: UniProtKB
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36177.

Polymorphism and mutation databases

BioMutaiSTAG2.
DMDMi73621291.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12311231Cohesin subunit SA-2PRO_0000120185Add
BLAST

Amino acid modifications

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

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8N3U4.
MaxQBiQ8N3U4.
PaxDbiQ8N3U4.
PRIDEiQ8N3U4.

PTM databases

iPTMnetiQ8N3U4.
PhosphoSiteiQ8N3U4.

Expressioni

Gene expression databases

BgeeiQ8N3U4.
CleanExiHS_STAG2.
ExpressionAtlasiQ8N3U4. baseline and differential.
GenevisibleiQ8N3U4. HS.

Organism-specific databases

HPAiHPA002857.

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 STAG3.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PDS5AQ29RF73EBI-1057252,EBI-1175454
PDS5BQ9NTI53EBI-1057252,EBI-1175604
SMC3Q9UQE710EBI-1057252,EBI-80718
SSU72Q9NP774EBI-1057252,EBI-2515416

Protein-protein interaction databases

BioGridi115958. 45 interactions.
DIPiDIP-35418N.
IntActiQ8N3U4. 19 interactions.
MINTiMINT-6178117.
STRINGi9606.ENSP00000218089.

Structurei

Secondary structure

1
1231
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi84 – 907Combined sources
Helixi95 – 10814Combined sources
Helixi110 – 12314Combined sources
Turni124 – 1263Combined sources
Helixi133 – 1386Combined sources
Helixi141 – 15010Combined sources
Beta strandi155 – 1573Combined sources
Turni160 – 1623Combined sources
Helixi166 – 18419Combined sources
Turni185 – 1895Combined sources
Helixi190 – 1923Combined sources
Beta strandi193 – 1953Combined sources
Helixi196 – 20712Combined sources
Helixi213 – 25341Combined sources
Helixi261 – 29131Combined sources
Helixi293 – 2964Combined sources
Beta strandi299 – 3013Combined sources
Helixi302 – 31817Combined sources
Helixi320 – 3234Combined sources
Helixi326 – 33510Combined sources
Helixi341 – 35212Combined sources
Turni353 – 3553Combined sources
Helixi362 – 37716Combined sources
Helixi378 – 3803Combined sources
Beta strandi381 – 3833Combined sources
Helixi384 – 40017Combined sources
Beta strandi402 – 4043Combined sources
Helixi407 – 4159Combined sources
Helixi416 – 4183Combined sources
Beta strandi419 – 4213Combined sources
Helixi422 – 43615Combined sources
Helixi458 – 47013Combined sources
Beta strandi475 – 4773Combined sources
Helixi478 – 4847Combined sources
Turni485 – 4873Combined sources
Helixi489 – 4924Combined sources
Helixi495 – 5017Combined sources
Helixi515 – 53319Combined sources
Turni539 – 5413Combined sources
Helixi550 – 57829Combined sources
Helixi582 – 5887Combined sources
Helixi589 – 5946Combined sources
Helixi599 – 6024Combined sources
Helixi606 – 62217Combined sources
Helixi626 – 63914Combined sources
Helixi647 – 67327Combined sources
Beta strandi674 – 6763Combined sources
Helixi681 – 70020Combined sources
Helixi709 – 72214Combined sources
Helixi727 – 74620Combined sources
Helixi756 – 77419Combined sources
Helixi775 – 7773Combined sources
Helixi781 – 79717Combined sources
Helixi800 – 8023Combined sources
Turni803 – 8064Combined sources
Turni809 – 8135Combined sources
Helixi819 – 83214Combined sources
Helixi854 – 87320Combined sources
Helixi879 – 8824Combined sources
Helixi883 – 8864Combined sources
Turni887 – 8926Combined sources
Helixi893 – 90816Combined sources
Helixi912 – 93423Combined sources
Helixi943 – 95614Combined sources
Helixi968 – 98114Combined sources
Beta strandi982 – 9843Combined sources
Beta strandi987 – 9893Combined sources
Helixi995 – 9984Combined sources
Helixi999 – 10035Combined sources
Turni1004 – 10096Combined sources
Helixi1012 – 102211Combined sources
Turni1023 – 10253Combined sources
Helixi1028 – 10325Combined sources
Beta strandi1035 – 10373Combined sources
Helixi1039 – 10468Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PJUX-ray3.05A80-1060[»]
4PJWX-ray2.85A80-1060[»]
4PK7X-ray2.95A80-1060[»]
ProteinModelPortaliQ8N3U4.
SMRiQ8N3U4. 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.
HOVERGENiHBG057636.
InParanoidiQ8N3U4.
KOiK06671.
OMAiRWDLFGC.
PhylomeDBiQ8N3U4.
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: Q8N3U4-1) [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
MIAAPEIPTD FNLLQESETH FSSDTDFEDI EGKNQKQGKG KTCKKGKKGP
60 70 80 90 100
AEKGKGGNGG GKPPSGPNRM 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 DPEEDGMMKR
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 TKITELFAVA 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 IHALQCTHYV ILWQLAKITE
760 770 780 790 800
SSSTKEDLLR LKKQMRVFCQ ICQHYLTNVN TTVKEQAFTI LCDILMIFSH
810 820 830 840 850
QIMSGGRDML EPLVYTPDSS LQSELLSFIL DHVFIEQDDD NNSADGQQED
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 SGISSRGSTV RSKKSKPSTG KRKVVEGMQL SLTEESSSSD
1110 1120 1130 1140 1150
SMWLSREQTL HTPVMMQTPQ LTSTIMREPK RLRPEDSFMS VYPMQTEHHQ
1160 1170 1180 1190 1200
TPLDYNRRGT SLMEDDEEPI VEDVMMSSEG RIEDLNEGMD FDTMDIDLPP
1210 1220 1230
SKNRRERTEL KPDFFDPASI MDESVLGVSM F
Length:1,231
Mass (Da):141,326
Last modified:August 16, 2005 - v3
Checksum:i692358EFFFF61BB9
GO
Isoform 2 (identifier: Q8N3U4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1156-1156: N → NTQVTWMLAQRQQEEARQQQERAAMSYVKLRTNLQHAI

Show »
Length:1,268
Mass (Da):145,751
Checksum:i38F24736F06D9054
GO

Sequence cautioni

The sequence CAA99732.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461G → D in CAD38591 (PubMed:17974005).Curated
Sequence conflicti302 – 3021A → R in CAA99732 (PubMed:9305759).Curated
Sequence conflicti327 – 3271S → G in CAD38591 (PubMed:17974005).Curated
Sequence conflicti607 – 6082KH → ND in CAA99732 (PubMed:9305759).Curated
Sequence conflicti706 – 7061W → R in CAA99732 (PubMed:9305759).Curated
Sequence conflicti710 – 7101A → V in CAD38591 (PubMed:17974005).Curated
Sequence conflicti835 – 8351I → T in CAD38591 (PubMed:17974005).Curated
Sequence conflicti971 – 9711A → T in CAH18271 (PubMed:17974005).Curated
Sequence conflicti992 – 9921H → Y in CAD38591 (PubMed:17974005).Curated
Sequence conflicti1105 – 11051S → T in CAA99732 (PubMed:9305759).Curated
Sequence conflicti1144 – 11441M → K in CAA99732 (PubMed:9305759).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti699 – 6991N → K.
Corresponds to variant rs6655782 [ dbSNP | Ensembl ].
VAR_060114

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1156 – 11561N → NTQVTWMLAQRQQEEARQQQ ERAAMSYVKLRTNLQHAI in isoform 2. 1 PublicationVSP_041119

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL831939 mRNA. Translation: CAD38591.1.
CR749433 mRNA. Translation: CAH18271.1.
AL355476 Genomic DNA. Translation: CAI40990.1.
AL355476 Genomic DNA. Translation: CAI40991.1.
CH471107 Genomic DNA. Translation: EAX11853.1.
CH471107 Genomic DNA. Translation: EAX11854.1.
CH471107 Genomic DNA. Translation: EAX11855.1.
CH471107 Genomic DNA. Translation: EAX11856.1.
CH471107 Genomic DNA. Translation: EAX11857.1.
BC001765 mRNA. Translation: AAH01765.2.
Z75331 mRNA. Translation: CAA99732.1. Different initiation.
CCDSiCCDS14607.1. [Q8N3U4-1]
CCDS43990.1. [Q8N3U4-2]
RefSeqiNP_001036214.1. NM_001042749.2. [Q8N3U4-2]
NP_001036215.1. NM_001042750.1. [Q8N3U4-2]
NP_001036216.1. NM_001042751.1. [Q8N3U4-1]
NP_001269347.1. NM_001282418.1. [Q8N3U4-1]
NP_006594.3. NM_006603.4. [Q8N3U4-1]
XP_005262414.1. XM_005262357.1. [Q8N3U4-2]
XP_005262415.1. XM_005262358.1. [Q8N3U4-2]
XP_005262416.1. XM_005262359.2. [Q8N3U4-2]
XP_005262417.1. XM_005262360.1. [Q8N3U4-2]
XP_005262418.1. XM_005262361.1. [Q8N3U4-1]
XP_006724790.1. XM_006724727.1. [Q8N3U4-2]
XP_011529555.1. XM_011531253.1. [Q8N3U4-2]
XP_011529556.1. XM_011531254.1. [Q8N3U4-1]
UniGeneiHs.496710.
Hs.624663.

Genome annotation databases

EnsembliENST00000218089; ENSP00000218089; ENSG00000101972. [Q8N3U4-2]
ENST00000371144; ENSP00000360186; ENSG00000101972. [Q8N3U4-1]
ENST00000371145; ENSP00000360187; ENSG00000101972. [Q8N3U4-2]
ENST00000371157; ENSP00000360199; ENSG00000101972. [Q8N3U4-1]
ENST00000371160; ENSP00000360202; ENSG00000101972. [Q8N3U4-1]
GeneIDi10735.
KEGGihsa:10735.
UCSCiuc004eua.5. human. [Q8N3U4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL831939 mRNA. Translation: CAD38591.1.
CR749433 mRNA. Translation: CAH18271.1.
AL355476 Genomic DNA. Translation: CAI40990.1.
AL355476 Genomic DNA. Translation: CAI40991.1.
CH471107 Genomic DNA. Translation: EAX11853.1.
CH471107 Genomic DNA. Translation: EAX11854.1.
CH471107 Genomic DNA. Translation: EAX11855.1.
CH471107 Genomic DNA. Translation: EAX11856.1.
CH471107 Genomic DNA. Translation: EAX11857.1.
BC001765 mRNA. Translation: AAH01765.2.
Z75331 mRNA. Translation: CAA99732.1. Different initiation.
CCDSiCCDS14607.1. [Q8N3U4-1]
CCDS43990.1. [Q8N3U4-2]
RefSeqiNP_001036214.1. NM_001042749.2. [Q8N3U4-2]
NP_001036215.1. NM_001042750.1. [Q8N3U4-2]
NP_001036216.1. NM_001042751.1. [Q8N3U4-1]
NP_001269347.1. NM_001282418.1. [Q8N3U4-1]
NP_006594.3. NM_006603.4. [Q8N3U4-1]
XP_005262414.1. XM_005262357.1. [Q8N3U4-2]
XP_005262415.1. XM_005262358.1. [Q8N3U4-2]
XP_005262416.1. XM_005262359.2. [Q8N3U4-2]
XP_005262417.1. XM_005262360.1. [Q8N3U4-2]
XP_005262418.1. XM_005262361.1. [Q8N3U4-1]
XP_006724790.1. XM_006724727.1. [Q8N3U4-2]
XP_011529555.1. XM_011531253.1. [Q8N3U4-2]
XP_011529556.1. XM_011531254.1. [Q8N3U4-1]
UniGeneiHs.496710.
Hs.624663.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PJUX-ray3.05A80-1060[»]
4PJWX-ray2.85A80-1060[»]
4PK7X-ray2.95A80-1060[»]
ProteinModelPortaliQ8N3U4.
SMRiQ8N3U4. Positions 83-1048.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115958. 45 interactions.
DIPiDIP-35418N.
IntActiQ8N3U4. 19 interactions.
MINTiMINT-6178117.
STRINGi9606.ENSP00000218089.

PTM databases

iPTMnetiQ8N3U4.
PhosphoSiteiQ8N3U4.

Polymorphism and mutation databases

BioMutaiSTAG2.
DMDMi73621291.

Proteomic databases

EPDiQ8N3U4.
MaxQBiQ8N3U4.
PaxDbiQ8N3U4.
PRIDEiQ8N3U4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000218089; ENSP00000218089; ENSG00000101972. [Q8N3U4-2]
ENST00000371144; ENSP00000360186; ENSG00000101972. [Q8N3U4-1]
ENST00000371145; ENSP00000360187; ENSG00000101972. [Q8N3U4-2]
ENST00000371157; ENSP00000360199; ENSG00000101972. [Q8N3U4-1]
ENST00000371160; ENSP00000360202; ENSG00000101972. [Q8N3U4-1]
GeneIDi10735.
KEGGihsa:10735.
UCSCiuc004eua.5. human. [Q8N3U4-1]

Organism-specific databases

CTDi10735.
GeneCardsiSTAG2.
HGNCiHGNC:11355. STAG2.
HPAiHPA002857.
MIMi300826. gene.
neXtProtiNX_Q8N3U4.
PharmGKBiPA36177.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2011. Eukaryota.
COG5537. LUCA.
GeneTreeiENSGT00390000014094.
HOVERGENiHBG057636.
InParanoidiQ8N3U4.
KOiK06671.
OMAiRWDLFGC.
PhylomeDBiQ8N3U4.
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

ChiTaRSiSTAG2. human.
GeneWikiiSTAG2.
GenomeRNAii10735.
NextBioi40752.
PROiQ8N3U4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8N3U4.
CleanExiHS_STAG2.
ExpressionAtlasiQ8N3U4. baseline and differential.
GenevisibleiQ8N3U4. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Retina and Spinal cord.
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 1).
    Tissue: Eye.
  5. "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] OF 48-1231 (ISOFORM 1).
    Tissue: Thymus.
  6. "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.
  7. Cited for: FUNCTION IN EARLY STEPS OF MEIOSIS.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1061, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1058 AND SER-1061, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-1058; SER-1061 AND THR-1112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-607, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1061; SER-1177 AND SER-1178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1061, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSTAG2_HUMAN
AccessioniPrimary (citable) accession number: Q8N3U4
Secondary accession number(s): B1AMT5
, D3DTF5, O00540, Q5JTI6, Q68DE9, Q9H1N8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: August 16, 2005
Last modified: May 11, 2016
This is version 140 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.