SMC1A
entrez
8243
canonical
uniprot
Q14683
canonical
ensembl
ENSG00000072501
resolver
ensp
ENSP00000323421
resolver
ensp
ENSP00000364489
resolver
ensp
ENSP00000502524
resolver
enst
ENST00000322213
resolver
enst
ENST00000375340
resolver
enst
ENST00000675504
resolver
genesymbol
SMC1A
resolver
genesymbol
SMC1L1
resolver
genesymbol_syn
DXS423E
resolver
genesymbol_syn
KIAA0178
resolver
genesymbol_syn
SB1.8
resolver
genesymbol_syn
SMC1
resolver
genesymbol_syn
SMC1L1
resolver
hgnc
HGNC:11111
resolver
uniprot
A0A384MR33
resolver
uniprot
G8JLG1
resolver
uniprot
O14995
resolver
uniprot
Q16351
resolver
uniprot
Q2M228
resolver
uniprot
Q68EN4
resolver
uniprot_entry
A0A384MR33_HUMAN
resolver
uniprot_entry
G8JLG1_HUMAN
resolver
uniprot_entry
Q68EN4_HUMAN
resolver
uniprot_entry
SMC1A_HUMAN
resolver
uniprot_sec
O14995
resolver
uniprot_sec
Q16351
resolver
uniprot_sec
Q2M228
resolver
amino_acid_sequence
MGFLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPVGKPAANRAFVSMVYSEEGAEDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYACGNALVCDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEEGSSQGEDSVSGSQRISSIYAREALIEIDYGDLCEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESVATNIDEIYKALSRNSSAQAFLGPENPEEPYLDGINYNCVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTKAESLIGVYPEQGDCVISKVLTFDLTKYPDANPNPNEQ
uniprot
proteins
disease_involvement
DISEASE: Cornelia de Lange syndrome 2 (CDLS2) [MIM:300590]: A form of Cornelia de Lange syndrome, a clinically heterogeneous developmental disorder associated with malformations affecting multiple systems. Characterized by facial dysmorphisms, abnormal hands and feet, growth delay, cognitive retardation, hirsutism, gastroesophageal dysfunction and cardiac, ophthalmologic and genitourinary anomalies. {ECO:0000269|PubMed:16604071, ECO:0000269|PubMed:17221863, ECO:0000269|PubMed:17273969, ECO:0000269|PubMed:18996922, ECO:0000269|PubMed:19701948, ECO:0000269|PubMed:20358602, ECO:0000269|PubMed:20635401, ECO:0000269|PubMed:24124034}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Developmental and epileptic encephalopathy 85 with or without midline brain defects (DEE85) [MIM:301044]: An X-linked form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. DEE85 is characterized by onset of severe refractory seizures in the first year of life, global developmental delay with impaired intellectual development and poor or absent speech, and dysmorphic facial features. Many patients have midline brain defects on brain imaging. {ECO:0000269|PubMed:28166369, ECO:0000269|PubMed:31334757}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is 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. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint. {ECO:0000269|PubMed:11877377}.
uniprot
proteins
mass_dalton
143233
uniprot
proteins
mutagenesis
MUTAGEN 957; /note="S->A: Reduces phosphorylation and the S-phase checkpoint activation. Abolishes S-phase activation; when associated with A-966."; /evidence="ECO:0000269|PubMed:11877377"; MUTAGEN 966; /note="S->A: Reduces phosphorylation and the S-phase checkpoint activation. Increases sensitivity to DNA methylation. Abolishes S-phase activation; when associated with A-957."; /evidence="ECO:0000269|PubMed:11877377, ECO:0000269|PubMed:14657349
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by the DCX(DCAF15) complex, leading to its degradation. {ECO:0000269|PubMed:31452512}.; PTM: Phosphorylated by ATM upon ionizing radiation in a NBS1-dependent manner. Phosphorylated by ATR upon DNA methylation in a MSH2/MSH6-dependent manner. Phosphorylation of Ser-957 and Ser-966 activates it and is required for S-phase checkpoint activation. {ECO:0000269|PubMed:11877377, ECO:0000269|PubMed:14657349}.
uniprot
proteins
protein_family
SMC family
uniprot
proteins
protein_family
SMC1 subfamily
uniprot
proteins
pubmed
10409732
uniprot
proteins
pubmed
11076961
uniprot
proteins
pubmed
11877377
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
12199140
uniprot
proteins
pubmed
14657349
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
15837422
uniprot
proteins
pubmed
16604071
uniprot
proteins
pubmed
17221863
uniprot
proteins
pubmed
17273969
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18996922
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19701948
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20358602
uniprot
proteins
pubmed
20635401
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22628566
uniprot
proteins
pubmed
22977523
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24124034
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
28166369
uniprot
proteins
pubmed
31334757
uniprot
proteins
pubmed
31452512
uniprot
proteins
pubmed
32409525
uniprot
proteins
pubmed
7757074
uniprot
proteins
pubmed
8724849
uniprot
proteins
pubmed
9295362
uniprot
proteins
sequence_length
1233
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12199140}. Chromosome {ECO:0000269|PubMed:12199140}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12199140}. 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 PLK, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of the cohesin complex 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. The phosphorylated form on Ser-957 and Ser-966 associates with chromatin during G1/S/G2 phases but not during M phase, suggesting that phosphorylation does not regulate cohesin function. Integral component of the functional centromere-kinetochore complex at the kinetochore region during mitosis.
uniprot
proteins