DAZAP2
entrez
9802
canonical
uniprot
Q15038
canonical
ensembl
ENSG00000183283
resolver
ensp
ENSP00000394699
resolver
ensp
ENSP00000398804
resolver
ensp
ENSP00000408251
resolver
ensp
ENSP00000412812
resolver
ensp
ENSP00000446554
resolver
ensp
ENSP00000448051
resolver
genesymbol
DAZAP2
resolver
genesymbol_syn
KIAA0058
resolver
genesymbol_syn
PRTB
resolver
hgnc
HGNC:2684
resolver
uniprot
A8K254
resolver
uniprot
B4DDT5
resolver
uniprot
B4E1G3
resolver
uniprot
C9JA96
resolver
uniprot
C9JP84
resolver
uniprot
E9PB45
resolver
uniprot
F8VU62
resolver
uniprot_entry
DAZP2_HUMAN
resolver
uniprot_sec
A8K254
resolver
uniprot_sec
B4DDT5
resolver
uniprot_sec
B4E1G3
resolver
uniprot_sec
C9JA96
resolver
uniprot_sec
C9JP84
resolver
uniprot_sec
E9PB45
resolver
uniprot_sec
F8VU62
resolver
amino_acid_sequence
MNSKGQYPTQPTYPVQPPGNPVYPQTLHLPQAPPYTDAPPAYSELYRPSFVHPGAATVPTMSAAFPGASLYLPMAQSVAVGPLGSTIPMAYYPVGPIYPPGSTVLVEGGYDAGARFGAGATAGNIPPPPPGCPPNAAQLAVMQGANVLVTQRKGNFFMGGSDGGYTIW
uniprot
proteins
function
FUNCTION: In unstressed cells, promotes SIAH1-mediated polyubiquitination and degradation of the serine/threonine-protein kinase HIPK2, probably by acting as a loading factor that potentiates complex formation between HIPK2 and ubiquitin ligase SIAH1 (PubMed:33591310). In response to DNA damage, localizes to the nucleus following phosphorylation by HIPK2 and modulates the expression of a subset of TP53/p53 target genes by binding to TP53 at target gene promoters (PubMed:33591310). This limits the expression of a number of cell death-mediating TP53 target genes, reducing DNA damage-induced cell death (PubMed:33591310). Enhances the binding of transcription factor TCF7L2/TCF4, a Wnt signaling pathway effector, to the promoters of target genes (By similarity). Plays a role in stress granule formation (PubMed:17984221). {ECO:0000250|UniProtKB:Q9DCP9, ECO:0000269|PubMed:17984221, ECO:0000269|PubMed:33591310}.
uniprot
proteins
mass_dalton
17319
uniprot
proteins
mutagenesis
MUTAGEN 4; /note="K->A: Does not affect ubiquitin-mediated degradation. Abolishes nuclear localization with the protein located in the cytoplasm."; /evidence="ECO:0000269|PubMed:21274613"; MUTAGEN 40..42; /note="PAY->AAA: Abolishes interaction with NEDD4. Abolishes NEDD4-mediated ubiquitination."; /evidence="ECO:0000269|PubMed:11342538"; MUTAGEN 77; /note="S->A: Loss of phosphorylation by HIPK2."; /evidence="ECO:0000269|PubMed:33591310"; MUTAGEN 153; /note="K->A: Abolishes ubiquitin-mediated degradation. Does not affect nuclear localization."; /evidence="ECO:0000269|PubMed:21274613
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated (PubMed:11342538, PubMed:21274613, PubMed:22070932). Ubiquitinated by SMURF2, leading to proteasomal degradation (PubMed:22070932). Ubiquitinated by NEDD4, leading to proteasomal degradation (PubMed:11342538). {ECO:0000269|PubMed:11342538, ECO:0000269|PubMed:21274613, ECO:0000269|PubMed:22070932}.; PTM: Following DNA damage, phosphorylated by HIPK2 which promotes DAZAP2 localization to the nucleus, reduces interaction of DAZAP2 with HIPK2 and SIAH1, and prevents DAZAP2-dependent ubiquitination of HIPK2 by E3 ubiquitin-protein ligase SIAH1 and subsequent HIPK2 proteasomal degradation. {ECO:0000269|PubMed:33591310}.
uniprot
proteins
pubmed
10857750
uniprot
proteins
pubmed
11342538
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
17935665
uniprot
proteins
pubmed
17984221
uniprot
proteins
pubmed
19304756
uniprot
proteins
pubmed
21274613
uniprot
proteins
pubmed
21750715
uniprot
proteins
pubmed
22070932
uniprot
proteins
pubmed
22771904
uniprot
proteins
pubmed
33591310
uniprot
proteins
pubmed
7584044
uniprot
proteins
sequence_length
168
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17935665, ECO:0000269|PubMed:17984221, ECO:0000269|PubMed:19304756, ECO:0000269|PubMed:22070932, ECO:0000269|PubMed:33591310}. Nucleus {ECO:0000269|PubMed:17984221, ECO:0000269|PubMed:19304756, ECO:0000269|PubMed:21274613, ECO:0000269|PubMed:22070932, ECO:0000269|PubMed:33591310}. Nucleus speckle {ECO:0000269|PubMed:11342538}. Nucleus, nuclear body {ECO:0000269|PubMed:33591310}. Cytoplasm, Stress granule {ECO:0000269|PubMed:17984221, ECO:0000269|PubMed:33591310}. Note=Predominantly nuclear in macrophages, stimulation of IL17RB with its ligand IL17E induces accumulation in the cytoplasm (PubMed:22070932). Predominantly cytoplasmic when unphosphorylated and localizes to the nucleus following phosphorylation by HIPK2 (PubMed:33591310). Localizes to stress granules under cellular stress conditions (PubMed:17984221). {ECO:0000269|PubMed:17984221, ECO:0000269|PubMed:22070932, ECO:0000269|PubMed:33591310}.
uniprot
proteins