STAG2
entrez
10735
canonical
uniprot
Q8N3U4
canonical
ensembl
ENSG00000101972
resolver
ensp
ENSP00000218089
resolver
ensp
ENSP00000360186
resolver
ensp
ENSP00000360187
resolver
ensp
ENSP00000360199
resolver
ensp
ENSP00000360202
resolver
ensp
ENSP00000397265
resolver
ensp
ENSP00000570023
resolver
ensp
ENSP00000570024
resolver
ensp
ENSP00000570026
resolver
ensp
ENSP00000570027
resolver
ensp
ENSP00000570028
resolver
ensp
ENSP00000570029
resolver
ensp
ENSP00000570030
resolver
ensp
ENSP00000570031
resolver
ensp
ENSP00000570032
resolver
ensp
ENSP00000570037
resolver
ensp
ENSP00000610213
resolver
ensp
ENSP00000610215
resolver
ensp
ENSP00000610216
resolver
genesymbol
STAG2
resolver
genesymbol_syn
SA2
resolver
hgnc
HGNC:11355
resolver
uniprot
B1AMT5
resolver
uniprot
D3DTF5
resolver
uniprot
O00540
resolver
uniprot
Q5JTI6
resolver
uniprot
Q68DE9
resolver
uniprot
Q9H1N8
resolver
uniprot_entry
STAG2_HUMAN
resolver
uniprot_sec
B1AMT5
resolver
uniprot_sec
D3DTF5
resolver
uniprot_sec
O00540
resolver
uniprot_sec
Q5JTI6
resolver
uniprot_sec
Q68DE9
resolver
uniprot_sec
Q9H1N8
resolver
amino_acid_sequence
MIAAPEIPTDFNLLQESETHFSSDTDFEDIEGKNQKQGKGKTCKKGKKGPAEKGKGGNGGGKPPSGPNRMNGHHQQNGVENMMLFEVVKMGKSAMQSVVDDWIESYKHDRDIALLDLINFFIQCSGCKGVVTAEMFRHMQNSEIIRKMTEEFDEDSGDYPLTMAGPQWKKFKSSFCEFIGVLVRQCQYSIIYDEYMMDTVISLLTGLSDSQVRAFRHTSTLAAMKLMTALVNVALNLSINMDNTQRQYEAERNKMIGKRANERLELLLQKRKELQENQDEIENMMNAIFKGVFVHRYRDAIAEIRAICIEEIGIWMKMYSDAFLNDSYLKYVGWTMHDKQGEVRLKCLTALQGLYYNKELNSKLELFTSRFKDRIVSMTLDKEYDVAVQAIKLLTLVLQSSEEVLTAEDCENVYHLVYSAHRPVAVAAGEFLYKKLFSRRDPEEDGMMKRRGRQGPNANLVKTLVFFFLESELHEHAAYLVDSMWDCATELLKDWECMNSLLLEEPLSGEEALTDRQESALIEIMLCTIRQAAECHPPVGRGTGKRVLTAKEKKTQLDDRTKITELFAVALPQLLAKYSVDAEKVTNLLQLPQYFDLEIYTTGRLEKHLDALLRQIRNIVEKHTDTDVLEACSKTYHALCNEEFTIFNRVDISRSQLIDELADKFNRLLEDFLQEGEEPDEDDAYQVLSTLKRITAFHNAHDLSKWDLFACNYKLLKTGIENGDMPEQIVIHALQCTHYVILWQLAKITESSSTKEDLLRLKKQMRVFCQICQHYLTNVNTTVKEQAFTILCDILMIFSHQIMSGGRDMLEPLVYTPDSSLQSELLSFILDHVFIEQDDDNNSADGQQEDEASKIEALHKRRNLLAAFCKLIVYTVVEMNTAADIFKQYMKYYNDYGDIIKETMSKTRQIDKIQCAKTLILSLQQLFNEMIQENGYNFDRSSSTFSGIKELARRFALTFGLDQLKTREAIAMLHKDGIEFAFKEPNPQGESHPPLNLAFLDILSEFSSKLLRQDKRTVYVYLEKFMTFQMSLRREDVWLPLMSYRNSLLAGGDDDTMSVISGISSRGSTVRSKKSKPSTGKRKVVEGMQLSLTEESSSSDSMWLSREQTLHTPVMMQTPQLTSTIMREPKRLRPEDSFMSVYPMQTEHHQTPLDYNRRGTSLMEDDEEPIVEDVMMSSEGRIEDLNEGMDFDTMDIDLPPSKNRRERTELKPDFFDPASIMDESVLGVSMF
uniprot
proteins
disease_involvement
DISEASE: Mullegama-Klein-Martinez syndrome (MKMS) [MIM:301022]: An X-linked neurodevelopmental disorder with variable features including intellectual deficiency, microcephaly, microtia, hearing loss, developmental delay, dysmorphic features, language delay, congenital heart defect, and clinodactyly of the 5th finger. {ECO:0000269|PubMed:28296084, ECO:0000269|PubMed:29263825, ECO:0000269|PubMed:30158690, ECO:0000269|PubMed:30447054}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Holoprosencephaly 13, X-linked (HPE13) [MIM:301043]: An X-linked form of holoprosencephaly, a structural anomaly of the brain in which the developing forebrain fails to correctly separate into right and left hemispheres. It is a genetically and clinically heterogeneous disorder with a wide spectrum of severity, ranging from alobar holoprosencephaly with severe facial abnormalities, such as cyclopia and proboscis, to mild forms that include lobar or microform holoprosencephaly, without cerebral malformations and with mild craniofacial defects. HPE13 features range from full alobar holoprosencephaly with cyclopia to semilobar holoprosencephaly or septooptic dysplasia. Dysmorphic features include microcephaly, hypotelorism, low-set ears, micrognathia, and cleft lip/palate. Patients with a more severe phenotype may die in the newborn period, whereas those with a less severe phenotype show global developmental delay. {ECO:0000269|PubMed:31334757}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: 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. {ECO:0000269|PubMed:12034751}.
uniprot
proteins
mass_dalton
141326
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by PLK1. The large dissociation of cohesin from chromosome arms during prophase is partly due to its phosphorylation (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
SCC3 family
uniprot
proteins
pubmed
11076961
uniprot
proteins
pubmed
12034751
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
28296084
uniprot
proteins
pubmed
29263825
uniprot
proteins
pubmed
30158690
uniprot
proteins
pubmed
30447054
uniprot
proteins
pubmed
30765867
uniprot
proteins
pubmed
31334757
uniprot
proteins
pubmed
32536687
uniprot
proteins
pubmed
9305759
uniprot
proteins
sequence_length
1231
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere. 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.
uniprot
proteins