PIAS4
entrez
51588
canonical
uniprot
Q8N2W9
canonical
ensembl
ENSG00000105229
resolver
ensp
ENSP00000262971
resolver
enst
ENST00000262971
resolver
genesymbol
PIAS4
resolver
genesymbol_syn
PIASG
resolver
hgnc
HGNC:17002
resolver
uniprot
B3KMR4
resolver
uniprot
O75926
resolver
uniprot
Q96G19
resolver
uniprot
Q9UN16
resolver
uniprot_entry
B3KMR4_HUMAN
resolver
uniprot_entry
PIAS4_HUMAN
resolver
uniprot_sec
O75926
resolver
uniprot_sec
Q96G19
resolver
uniprot_sec
Q9UN16
resolver
amino_acid_sequence
MAAELVEAKNMVMSFRVSDLQMLLGFVGRSKSGLKHELVTRALQLVQFDCSPELFKKIKELYETRYAKKNSEPAPQPHRPLDPLTMHSTYDRAGAVPRTPLAGPNIDYPVLYGKYLNGLGRLPAKTLKPEVRLVKLPFFNMLDELLKPTELVPQNNEKLQESPCIFALTPRQVELIRNSRELQPGVKAVQVVLRICYSDTSCPQEDQYPPNIAVKVNHSYCSVPGYYPSNKPGVEPKRPCRPINLTHLMYLSSATNRITVTWGNYGKSYSVALYLVRQLTSSELLQRLKTIGVKHPELCKALVKEKLRLDPDSEIATTGVRVSLICPLVKMRLSVPCRAETCAHLQCFDAVFYLQMNEKKPTWMCPVCDKPAPYDQLIIDGLLSKILSECEDADEIEYLVDGSWCPIRAEKERSCSPQGAILVLGPSDANGLLPAPSVNGSGALGSTGGGGPVGSMENGKPGADVVDLTLDSSSSSEDEEEEEEEEEDEDEEGPRPKRRCPFQKGLVPAC
uniprot
proteins
ec_number
2.3.2.27
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:12511558, PubMed:12631292, PubMed:12727872, PubMed:15831457, PubMed:15976810, PubMed:22508508, PubMed:32832608). Mediates sumoylation of ALKBH5, AXIN1, CEBPA, KLF8, GATA2, PARK7, HERC2, MYB, TCF4 and RNF168 (PubMed:12223491, PubMed:12511558, PubMed:12631292, PubMed:12727872, PubMed:12750312, PubMed:15831457, PubMed:15976810, PubMed:16617055, PubMed:22508508, PubMed:34048572). Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53/TP53 pathway, the Wnt pathway and the steroid hormone signaling pathway (PubMed:11388671). Involved in gene silencing (PubMed:11248056). In Wnt signaling, represses LEF1 and enhances TCF4 transcriptional activities through promoting their sumoylations (PubMed:12727872, PubMed:15831457). Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation (PubMed:21965678). Binds to AT-rich DNA sequences, known as matrix or scaffold attachment regions (MARs/SARs) (By similarity). Catalyzes conjugation of SUMO2 to KAT5 in response to DNA damage, facilitating repair of DNA double-strand breaks (DSBs) via homologous recombination (HR) (PubMed:32832608). Mediates sumoylation of PARP1 in response to PARP1 trapping to chromatin (PubMed:35013556). Mediates sumoylation of KLF8, repressing KLF8 transcriptional activity and cell cycle progression into G(1) phase (PubMed:16617055). Sumoylates ALKBH5 downstream of MAPK8/JNK1 and MAPK9/JNK2 in response to reactive oxygen species (ROS), inhibiting ALKBH5 RNA demethylase activity (PubMed:34048572). {ECO:0000250|UniProtKB:Q9JM05, ECO:0000269|PubMed:11248056, ECO:0000269|PubMed:11388671, ECO:0000269|PubMed:12223491, ECO:0000269|PubMed:12511558, ECO:0000269|PubMed:12631292, ECO:0000269|PubMed:12727872, ECO:0000269|PubMed:12750312, ECO:0000269|PubMed:15831457, ECO:0000269|PubMed:15976810, ECO:0000269|PubMed:16617055, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:22508508, ECO:0000269|PubMed:32832608, ECO:0000269|PubMed:34048572, ECO:0000269|PubMed:35013556}.
uniprot
proteins
mass_dalton
56504
uniprot
proteins
mutagenesis
MUTAGEN 23..24; /note="LL->AA: Loss of repression of AR- and STAT1-induced transcription; no effect on AR- and STAT1-binding."; /evidence="ECO:0000269|PubMed:11248056, ECO:0000269|PubMed:11439351"; MUTAGEN 35; /note="K->R: Complete loss of sumoylation. No enhancement of TCF4 sumoylation. No effect on interaction with TCF4. Colocalizes with SUMO1 in nucleus but concentrated into nuclear granules."; /evidence="ECO:0000269|PubMed:12727872, ECO:0000269|PubMed:15831457"; MUTAGEN 128; /note="K->R: Some loss of sumoylation."; /evidence="ECO:0000269|PubMed:12727872, ECO:0000269|PubMed:15831457"; MUTAGEN 342; /note="C->A: Abolished SUMO ligase activity. Inhibits TCF4 sumoylation. Inhibits beta-catenin-mediated TCF7L2/TCF4 activity. No colocalization with TCF7L2/TCF4 in nuclear punctate structures; when associated with A-347."; /evidence="ECO:0000269|PubMed:12727872, ECO:0000269|PubMed:35013556"; MUTAGEN 347; /note="C->A: Inhibits TCF4 sumoylation. Inhibits beta-catenin-mediated TCF7L2/TCF4 activity. No colocalization with TCF7L2/TCF4 in nuclear punctate structures; when associated with A-342. AR- and STAT1-binding."; /evidence="ECO:0000269|PubMed:12727872
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein sumoylation. {ECO:0000269|PubMed:12511558, ECO:0000269|PubMed:12631292, ECO:0000269|PubMed:12727872, ECO:0000269|PubMed:15831457, ECO:0000269|PubMed:15976810, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:22508508, ECO:0000269|PubMed:32832608, ECO:0000269|PubMed:34048572, ECO:0000269|PubMed:35013556}.
uniprot
proteins
post_translational_modification
PTM: Sumoylated. Lys-35 is the main site of sumoylation. Sumoylation is required for TCF4 sumoylation and transcriptional activation. Represses LEF1 transcriptional activity. SUMO1 is the preferred conjugate. {ECO:0000269|PubMed:15831457}.
uniprot
proteins
protein_family
PIAS family
uniprot
proteins
pubmed
11248056
uniprot
proteins
pubmed
11388671
uniprot
proteins
pubmed
11439351
uniprot
proteins
pubmed
12223491
uniprot
proteins
pubmed
12511558
uniprot
proteins
pubmed
12631292
uniprot
proteins
pubmed
12727872
uniprot
proteins
pubmed
12750312
uniprot
proteins
pubmed
15251447
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15831457
uniprot
proteins
pubmed
15976810
uniprot
proteins
pubmed
16617055
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21965678
uniprot
proteins
pubmed
22508508
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28842558
uniprot
proteins
pubmed
32832608
uniprot
proteins
pubmed
34048572
uniprot
proteins
pubmed
35013556
uniprot
proteins
pubmed
9724754
uniprot
proteins
sequence_length
510
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000269|PubMed:11248056, ECO:0000269|PubMed:12727872, ECO:0000269|PubMed:15831457}. Note=Colocalizes with SUMO1 and TCF7L2/TCF4 and LEF1 in a subset of PML (promyelocytic leukemia) nuclear bodies. {ECO:0000269|PubMed:12727872, ECO:0000269|PubMed:15831457}.
uniprot
proteins