PIAS1
entrez
8554
canonical
uniprot
O75925
canonical
ensembl
ENSG00000033800
resolver
ensp
ENSP00000249636
resolver
ensp
ENSP00000438574
resolver
genesymbol
PIAS1
resolver
genesymbol_syn
DDXBP1
resolver
hgnc
HGNC:2752
resolver
uniprot
B2RB67
resolver
uniprot
B3KSY9
resolver
uniprot
C5J4B4
resolver
uniprot
Q147X4
resolver
uniprot
Q99751
resolver
uniprot
Q9UN02
resolver
uniprot_entry
PIAS1_HUMAN
resolver
uniprot_sec
B2RB67
resolver
uniprot_sec
B3KSY9
resolver
uniprot_sec
C5J4B4
resolver
uniprot_sec
Q147X4
resolver
uniprot_sec
Q99751
resolver
uniprot_sec
Q9UN02
resolver
amino_acid_sequence
MADSAELKQMVMSLRVSELQVLLGYAGRNKHGRKHELLTKALHLLKAGCSPAVQMKIKELYRRRFPQKIMTPADLSIPNVHSSPMPATLSPSTIPQLTYDGHPASSPLLPVSLLGPKHELELPHLTSALHPVHPDIKLQKLPFYDLLDELIKPTSLASDNSQRFRETCFAFALTPQQVQQISSSMDISGTKCDFTVQVQLRFCLSETSCPQEDHFPPNLCVKVNTKPCSLPGYLPPTKNGVEPKRPSRPINITSLVRLSTTVPNTIVVSWTAEIGRNYSMAVYLVKQLSSTVLLQRLRAKGIRNPDHSRALIKEKLTADPDSEIATTSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHLIIDGLFMEILKYCTDCDEIQFKEDGTWAPMRSKKEVQEVSASYNGVDGCLSSTLEHQVASHHQSSNKNKKVEVIDLTIDSSSDEEEEEPSAKRTCPSLSPTSPLNNKGILSLPHQASPVSRTPSLPAVDTSYINTSLIQDYRHPFHMTPMPYDLQGLDFFPFLSGDNQHYNTSLLAAAAAAVSDDQDLLHSSRFFPYTSSQMFLDQLSAGGSTSLPTTNGSSSGSNSSLVSSNSLRESHSHTVTNRSSTDTASIFGIIPDIISLD
uniprot
proteins
ec_number
2.3.2.-
uniprot
proteins
function
FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor (PubMed:11583632, PubMed:11867732, PubMed:14500712, PubMed:15280358, PubMed:21965678, PubMed:36050397). Catalyzes sumoylation of various proteins, such as CEBPB, MRE11, MTA1, PTK2, PML and ZNF76 (PubMed:11583632, PubMed:11867732, PubMed:14500712, PubMed:15280358, PubMed:21965678, PubMed:36050397). Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway (PubMed:11583632, PubMed:11867732). In vitro, binds A/T-rich DNA (PubMed:15133049). The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context (PubMed:11583632, PubMed:11867732, PubMed:14500712, PubMed:21965678, PubMed:36050397). Mediates sumoylation of MRE11, stabilizing MRE11 on chromatin during end resection (PubMed:36050397). Sumoylates PML (at 'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation (By similarity). PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation (By similarity). Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation (PubMed:21965678). Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB (By similarity). Mediates the nuclear mobility and localization of MSX1 to the nuclear periphery, whereby MSX1 is brought into the proximity of target myoblast differentiation factor genes (By similarity). Also required for the binding of MSX1 to the core enhancer region in target gene promoter regions, independent of its sumoylation activity (By similarity). Capable of binding to the core enhancer region TAAT box in the MYOD1 gene promoter (By similarity). {ECO:0000250|UniProtKB:O88907, ECO:0000269|PubMed:11583632, ECO:0000269|PubMed:11867732, ECO:0000269|PubMed:14500712, ECO:0000269|PubMed:15133049, ECO:0000269|PubMed:15280358, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:36050397}.; FUNCTION: (Microbial infection) Restricts Epstein-Barr virus (EBV) lytic replication by acting as an inhibitor for transcription factors involved in lytic gene expression (PubMed:29262325). The virus can use apoptotic caspases to antagonize PIAS1-mediated restriction and express its lytic genes (PubMed:29262325). {ECO:0000269|PubMed:29262325}.
uniprot
proteins
mass_dalton
71836
uniprot
proteins
mutagenesis
MUTAGEN 100; /note="D->A: Completely blocks cleavage by caspase-3, -6, and -8 and dramatic suppression of EBVDNA replication; when associated with A-433."; /evidence="ECO:0000269|PubMed:29262325"; MUTAGEN 148; /note="D->A: No effect on cleavages by caspase-6 and -8."; /evidence="ECO:0000269|PubMed:29262325"; MUTAGEN 351; /note="C->A,S: Loss of UBE2I-binding; almost complete loss of promotion of TP53 sumoylation; no loss of SUMO1- and TP53-binding."; /evidence="ECO:0000269|PubMed:11583632"; MUTAGEN 433; /note="D->A: Completely blocks cleavage by caspase-3, -6, and -8 and dramatic suppression of EBVDNA replication; when associated with A-100."; /evidence="ECO:0000269|PubMed:29262325
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein sumoylation.
uniprot
proteins
post_translational_modification
PTM: Sumoylated. {ECO:0000269|PubMed:11867732, ECO:0000269|PubMed:12393906}.
uniprot
proteins
protein_family
PIAS family
uniprot
proteins
pubmed
10628744
uniprot
proteins
pubmed
11439351
uniprot
proteins
pubmed
11583632
uniprot
proteins
pubmed
11672422
uniprot
proteins
pubmed
11867732
uniprot
proteins
pubmed
12223491
uniprot
proteins
pubmed
12356736
uniprot
proteins
pubmed
12393906
uniprot
proteins
pubmed
14500712
uniprot
proteins
pubmed
14701874
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15133049
uniprot
proteins
pubmed
15208321
uniprot
proteins
pubmed
15280358
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16572171
uniprot
proteins
pubmed
16600910
uniprot
proteins
pubmed
16617055
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17369852
uniprot
proteins
pubmed
17540171
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19136629
uniprot
proteins
pubmed
19557165
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19906316
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21724836
uniprot
proteins
pubmed
21965678
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
27211601
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28842558
uniprot
proteins
pubmed
29262325
uniprot
proteins
pubmed
36050397
uniprot
proteins
pubmed
9177271
uniprot
proteins
pubmed
9724754
uniprot
proteins
sequence_length
651
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O88907}. Nucleus speckle {ECO:0000269|PubMed:12393906, ECO:0000269|PubMed:9177271}. Nucleus, PML body {ECO:0000250|UniProtKB:O88907}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11672422}. Note=Interaction with CSRP2 may induce a partial redistribution along the cytoskeleton (PubMed:11672422). Interaction with MSX1 is required for localization to the nuclear periphery (By similarity). {ECO:0000250|UniProtKB:O88907, ECO:0000269|PubMed:11672422}.
uniprot
proteins