ESCO1
entrez
114799
canonical
uniprot
Q5FWF5
canonical
ensembl
ENSG00000141446
resolver
ensp
ENSP00000269214
resolver
ensp
ENSP00000372763
resolver
ensp
ENSP00000562263
resolver
ensp
ENSP00000562264
resolver
ensp
ENSP00000593607
resolver
genesymbol
ESCO1
resolver
genesymbol_syn
EFO1
resolver
genesymbol_syn
KIAA1911
resolver
hgnc
HGNC:24645
resolver
uniprot
B0YJ11
resolver
uniprot
B0YJ12
resolver
uniprot
Q69YG4
resolver
uniprot
Q69YS3
resolver
uniprot
Q6IMD7
resolver
uniprot
Q8N3Z5
resolver
uniprot
Q8NBG2
resolver
uniprot
Q96PX7
resolver
uniprot_entry
ESCO1_HUMAN
resolver
uniprot_sec
B0YJ11
resolver
uniprot_sec
B0YJ12
resolver
uniprot_sec
Q69YG4
resolver
uniprot_sec
Q69YS3
resolver
uniprot_sec
Q6IMD7
resolver
uniprot_sec
Q8N3Z5
resolver
uniprot_sec
Q8NBG2
resolver
uniprot_sec
Q96PX7
resolver
amino_acid_sequence
MMSIQEKSKENSSKVTKKSDDKNSETEIQDSQKNLAKKSGPKETIKSQAKSSSESKINQPELETRMSTRSSKAASNDKATKSINKNTVTVRGYSQESTKKKLSQKKLVHENPKANEQLNRRSQRLQQLTEVSRRSLRSREIQGQVQAVKQSLPPTKKEQCSSTQSKSNKTSQKHVKRKVLEVKSDSKEDENLVINEVINSPKGKKRKVEHQTACACSSQCTQGSEKCPQKTTRRDETKPVPVTSEVKRSKMATSVVPKKNEMKKSVHTQVNTNTTLPKSPQPSVPEQSDNELEQAGKSKRGSILQLCEEIAGEIESDNVEVKKESSQMESVKEEKPTEIKLEETSVERQILHQKETNQDVQCNRFFPSRKTKPVKCILNGINSSAKKNSNWTKIKLSKFNSVQHNKLDSQVSPKLGLLRTSFSPPALEMHHPVTQSTFLGTKLHDRNITCQQEKMKEINSEEVKINDITVEINKTTERAPENCHLANEIKPSDPPLDNQMKHSFDSASNKNFSQCLESKLENSPVENVTAASTLLSQAKIDTGENKFPGSAPQQHSILSNQTSKSSDNRETPRNHSLPKCNSHLEITIPKDLKLKEAEKTDEKQLIIDAGQKRFGAVSCNVCGMLYTASNPEDETQHLLFHNQFISAVKYVGWKKERILAEYPDGRIIMVLPEDPKYALKKVDEIREMVDNDLGFQQAPLMCYSRTKTLLFISNDKKVVGCLIAEHIQWGYRVIEEKLPVIRSEEEKVRFERQKAWCCSTLPEPAICGISRIWVFSMMRRKKIASRMIECLRSNFIYGSYLSKEEIAFSDPTPDGKLFATQYCGTGQFLVYNFINGQNST
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
function
FUNCTION: Acetyltransferase required for the establishment of sister chromatid cohesion (PubMed:15958495, PubMed:18614053). Couples the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during S phase. Acts by mediating the acetylation of cohesin component SMC3 (PubMed:18614053). {ECO:0000269|PubMed:14576321, ECO:0000269|PubMed:15958495, ECO:0000269|PubMed:18614053, ECO:0000269|PubMed:19907496, ECO:0000269|PubMed:27112597, ECO:0000269|PubMed:27803161}.
uniprot
proteins
mass_dalton
94983
uniprot
proteins
mutagenesis
MUTAGEN 622; /note="C->G: No effect on association with chromosomes."; /evidence="ECO:0000269|PubMed:15958495"; MUTAGEN 640; /note="F->A: Strongly decreased enzyme activity."; /evidence="ECO:0000269|PubMed:27803161"; MUTAGEN 643; /note="Q->A: Strongly decreased enzyme activity."; /evidence="ECO:0000269|PubMed:27803161"; MUTAGEN 644; /note="F->A: Strongly decreased enzyme activity."; /evidence="ECO:0000269|PubMed:27803161"; MUTAGEN 690; /note="D->N: Strongly decreased enzyme activity."; /evidence="ECO:0000269|PubMed:27803161"; MUTAGEN 725; /note="E->A: Strongly decreased enzyme activity."; /evidence="ECO:0000269|PubMed:27803161"; MUTAGEN 732; /note="R->A: Strongly decreased enzyme activity."; /evidence="ECO:0000269|PubMed:27803161"; MUTAGEN 735; /note="E->A: Strongly decreased enzyme activity."; /evidence="ECO:0000269|PubMed:27803161"; MUTAGEN 736; /note="E->A: Strongly decreased enzyme activity."; /evidence="ECO:0000269|PubMed:27803161"; MUTAGEN 756; /note="W->A: Strongly decreased enzyme activity."; /evidence="ECO:0000269|PubMed:27803161"; MUTAGEN 768; /note="G->D: Loss of autoacetylation."; /evidence="ECO:0000269|PubMed:15958495, ECO:0000269|PubMed:27112597"; MUTAGEN 770; /note="S->A: Strongly decreased enzyme activity."; /evidence="ECO:0000269|PubMed:27803161"; MUTAGEN 771; /note="R->A: Strongly decreased enzyme activity."; /evidence="ECO:0000269|PubMed:27803161"; MUTAGEN 773; /note="W->G: Decreased thermal stability. Strongly decreased enzyme activity."; /evidence="ECO:0000269|PubMed:27803161"; MUTAGEN 779..780; /note="RR->GG: Significant reduction in autoacetylation."; /evidence="ECO:0000269|PubMed:15958495"; MUTAGEN 780; /note="R->A: Nearly abolishes autoacetylation."; /evidence="ECO:0000269|PubMed:27112597"; MUTAGEN 782..783; /note="KI->EV: Significant reduction in autoacetylation."; /evidence="ECO:0000269|PubMed:15958495"; MUTAGEN 786; /note="R->C: Decreased thermal stability. Strongly decreased enzyme activity."; /evidence="ECO:0000269|PubMed:27803161"; MUTAGEN 789; /note="E->A: Reduced autoacetylation."; /evidence="ECO:0000269|PubMed:15958495, ECO:0000269|PubMed:27112597"; MUTAGEN 803; /note="K->A: Strongly reduced autoacetylation."; /evidence="ECO:0000269|PubMed:27112597"; MUTAGEN 809; /note="S->A: Strongly decreased enzyme activity."; /evidence="ECO:0000269|PubMed:27803161"; MUTAGEN 815; /note="G->R: Strongly decreased enzyme activity. No effect on thermal stability."; /evidence="ECO:0000269|PubMed:27803161
uniprot
proteins
post_translational_modification
PTM: Phosphorylated during mitosis, when associated with chromosomes. {ECO:0000269|PubMed:15958495}.
uniprot
proteins
protein_family
Acetyltransferase family
uniprot
proteins
protein_family
ECO subfamily
uniprot
proteins
pubmed
11572484
uniprot
proteins
pubmed
14576321
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15958495
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18614053
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19907496
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
27112597
uniprot
proteins
pubmed
27803161
uniprot
proteins
sequence_length
840
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14576321, ECO:0000269|PubMed:15958495}. Chromosome {ECO:0000269|PubMed:15958495}. Note=Nuclear at interphase, associated with chromosomes during mitosis. {ECO:0000269|PubMed:15958495}.
uniprot
proteins