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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
  • meiotic cell cycle Source: UniProtKB-KW
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of DNA endoreduplication Source: BHF-UCL
  • 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

BioCyciZFISH:ENSG00000101972-MONOMER.
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.
SIGNORiQ8N3U4.

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

DisGeNETi10735.
OpenTargetsiENSG00000101972.
PharmGKBiPA36177.

Polymorphism and mutation databases

BioMutaiSTAG2.
DMDMi73621291.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001201851 – 1231Cohesin subunit SA-2Add BLAST1231

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei607N6-acetyllysineCombined sources1
Modified residuei1058PhosphoserineCombined sources1
Modified residuei1061PhosphoserineCombined sources1
Modified residuei1064PhosphoserineBy similarity1
Modified residuei1065PhosphoserineBy similarity1
Modified residuei1112PhosphothreonineCombined sources1
Modified residuei1177PhosphoserineCombined sources1
Modified residuei1178PhosphoserineCombined sources1

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.
PeptideAtlasiQ8N3U4.
PRIDEiQ8N3U4.

PTM databases

iPTMnetiQ8N3U4.
PhosphoSitePlusiQ8N3U4.

Expressioni

Gene expression databases

BgeeiENSG00000101972.
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. 47 interactors.
DIPiDIP-35418N.
IntActiQ8N3U4. 19 interactors.
MINTiMINT-6178117.
STRINGi9606.ENSP00000218089.

Structurei

Secondary structure

11231
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi84 – 90Combined sources7
Helixi95 – 108Combined sources14
Helixi110 – 123Combined sources14
Turni124 – 126Combined sources3
Helixi133 – 138Combined sources6
Helixi141 – 150Combined sources10
Beta strandi155 – 157Combined sources3
Turni160 – 162Combined sources3
Helixi166 – 184Combined sources19
Turni185 – 189Combined sources5
Helixi190 – 192Combined sources3
Beta strandi193 – 195Combined sources3
Helixi196 – 207Combined sources12
Helixi213 – 253Combined sources41
Helixi261 – 291Combined sources31
Helixi293 – 296Combined sources4
Beta strandi299 – 301Combined sources3
Helixi302 – 318Combined sources17
Helixi320 – 323Combined sources4
Helixi326 – 335Combined sources10
Helixi341 – 352Combined sources12
Turni353 – 355Combined sources3
Helixi362 – 377Combined sources16
Helixi378 – 380Combined sources3
Beta strandi381 – 383Combined sources3
Helixi384 – 400Combined sources17
Beta strandi402 – 404Combined sources3
Helixi407 – 415Combined sources9
Helixi416 – 418Combined sources3
Beta strandi419 – 421Combined sources3
Helixi422 – 436Combined sources15
Helixi458 – 470Combined sources13
Beta strandi475 – 477Combined sources3
Helixi478 – 484Combined sources7
Turni485 – 487Combined sources3
Helixi489 – 492Combined sources4
Helixi495 – 501Combined sources7
Helixi515 – 533Combined sources19
Turni539 – 541Combined sources3
Helixi550 – 578Combined sources29
Helixi582 – 588Combined sources7
Helixi589 – 594Combined sources6
Helixi599 – 602Combined sources4
Helixi606 – 622Combined sources17
Helixi626 – 639Combined sources14
Helixi647 – 673Combined sources27
Beta strandi674 – 676Combined sources3
Helixi681 – 700Combined sources20
Helixi709 – 722Combined sources14
Helixi727 – 746Combined sources20
Helixi756 – 774Combined sources19
Helixi775 – 777Combined sources3
Helixi781 – 797Combined sources17
Helixi800 – 802Combined sources3
Turni803 – 806Combined sources4
Turni809 – 813Combined sources5
Helixi819 – 832Combined sources14
Helixi854 – 873Combined sources20
Helixi879 – 882Combined sources4
Helixi883 – 886Combined sources4
Turni887 – 892Combined sources6
Helixi893 – 908Combined sources16
Helixi912 – 934Combined sources23
Helixi943 – 956Combined sources14
Helixi968 – 981Combined sources14
Beta strandi982 – 984Combined sources3
Beta strandi987 – 989Combined sources3
Helixi995 – 998Combined sources4
Helixi999 – 1003Combined sources5
Turni1004 – 1009Combined sources6
Helixi1012 – 1022Combined sources11
Turni1023 – 1025Combined sources3
Helixi1028 – 1032Combined sources5
Beta strandi1035 – 1037Combined sources3
Helixi1039 – 1046Combined sources8

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini293 – 378SCDPROSITE-ProRule annotationAdd BLAST86

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1096 – 1101Poly-Ser6

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.
OrthoDBiEOG091G0195.
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 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti46G → D in CAD38591 (PubMed:17974005).Curated1
Sequence conflicti302A → R in CAA99732 (PubMed:9305759).Curated1
Sequence conflicti327S → G in CAD38591 (PubMed:17974005).Curated1
Sequence conflicti607 – 608KH → ND in CAA99732 (PubMed:9305759).Curated2
Sequence conflicti706W → R in CAA99732 (PubMed:9305759).Curated1
Sequence conflicti710A → V in CAD38591 (PubMed:17974005).Curated1
Sequence conflicti835I → T in CAD38591 (PubMed:17974005).Curated1
Sequence conflicti971A → T in CAH18271 (PubMed:17974005).Curated1
Sequence conflicti992H → Y in CAD38591 (PubMed:17974005).Curated1
Sequence conflicti1105S → T in CAA99732 (PubMed:9305759).Curated1
Sequence conflicti1144M → K in CAA99732 (PubMed:9305759).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_060114699N → K.Corresponds to variant rs6655782dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0411191156N → NTQVTWMLAQRQQEEARQQQ ERAAMSYVKLRTNLQHAI in isoform 2. 1 Publication1

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_005262357.2. [Q8N3U4-2]
XP_005262415.1. XM_005262358.2. [Q8N3U4-2]
XP_005262416.1. XM_005262359.3. [Q8N3U4-2]
XP_005262417.1. XM_005262360.2. [Q8N3U4-2]
XP_005262418.1. XM_005262361.2. [Q8N3U4-1]
XP_006724790.1. XM_006724727.1. [Q8N3U4-2]
XP_011529555.1. XM_011531253.2. [Q8N3U4-2]
XP_016884721.1. XM_017029232.1. [Q8N3U4-1]
XP_016884722.1. XM_017029233.1. [Q8N3U4-1]
XP_016884723.1. XM_017029234.1. [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_005262357.2. [Q8N3U4-2]
XP_005262415.1. XM_005262358.2. [Q8N3U4-2]
XP_005262416.1. XM_005262359.3. [Q8N3U4-2]
XP_005262417.1. XM_005262360.2. [Q8N3U4-2]
XP_005262418.1. XM_005262361.2. [Q8N3U4-1]
XP_006724790.1. XM_006724727.1. [Q8N3U4-2]
XP_011529555.1. XM_011531253.2. [Q8N3U4-2]
XP_016884721.1. XM_017029232.1. [Q8N3U4-1]
XP_016884722.1. XM_017029233.1. [Q8N3U4-1]
XP_016884723.1. XM_017029234.1. [Q8N3U4-1]
UniGeneiHs.496710.
Hs.624663.

3D structure databases

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

Protein-protein interaction databases

BioGridi115958. 47 interactors.
DIPiDIP-35418N.
IntActiQ8N3U4. 19 interactors.
MINTiMINT-6178117.
STRINGi9606.ENSP00000218089.

PTM databases

iPTMnetiQ8N3U4.
PhosphoSitePlusiQ8N3U4.

Polymorphism and mutation databases

BioMutaiSTAG2.
DMDMi73621291.

Proteomic databases

EPDiQ8N3U4.
MaxQBiQ8N3U4.
PaxDbiQ8N3U4.
PeptideAtlasiQ8N3U4.
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.
DisGeNETi10735.
GeneCardsiSTAG2.
HGNCiHGNC:11355. STAG2.
HPAiHPA002857.
MIMi300826. gene.
neXtProtiNX_Q8N3U4.
OpenTargetsiENSG00000101972.
PharmGKBiPA36177.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2011. Eukaryota.
COG5537. LUCA.
GeneTreeiENSGT00390000014094.
HOVERGENiHBG057636.
InParanoidiQ8N3U4.
KOiK06671.
OMAiRWDLFGC.
OrthoDBiEOG091G0195.
PhylomeDBiQ8N3U4.
TreeFamiTF314604.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000101972-MONOMER.
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.
SIGNORiQ8N3U4.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000101972.
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...

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: November 2, 2016
This is version 145 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.