Hipk2
entrez
15258
canonical
uniprot
Q9QZR5
canonical
ensembl
ENSMUSG00000061436
resolver
ensp
ENSMUSP00000124133
resolver
ensp
ENSMUSP00000125150
resolver
ensp
ENSMUSP00000125500
resolver
ensp
ENSMUSP00000125572
resolver
ensp
ENSMUSP00000306351
resolver
enst
ENSMUST00000160360
resolver
enst
ENSMUST00000160962
resolver
genesymbol
Hipk2
resolver
genesymbol_syn
Nbak1
resolver
genesymbol_syn
Stank
resolver
uniprot
A0A0R4J202
resolver
uniprot
A0A0R4J204
resolver
uniprot
O88905
resolver
uniprot
Q5D0E9
resolver
uniprot
Q99P45
resolver
uniprot
Q99P46
resolver
uniprot
Q9D2E6
resolver
uniprot
Q9D474
resolver
uniprot
Q9EQL2
resolver
uniprot
Q9QZR4
resolver
uniprot_entry
A0A0R4J202_MOUSE
resolver
uniprot_entry
A0A0R4J204_MOUSE
resolver
uniprot_entry
HIPK2_MOUSE
resolver
uniprot_entry
Q5D0E9_MOUSE
resolver
uniprot_sec
O88905
resolver
uniprot_sec
Q99P45
resolver
uniprot_sec
Q99P46
resolver
uniprot_sec
Q9D2E6
resolver
uniprot_sec
Q9D474
resolver
uniprot_sec
Q9EQL2
resolver
uniprot_sec
Q9QZR4
resolver
amino_acid_sequence
MAPVYEGMASHVQVFSPHTLQSSAFCSVKKLKVEPSSNWDMTGYGSHSKVYSQSKNIPPSQPASTTVSTSLPIPNPSLPYEQTIIFPGSTGHIVVTSASSTSVTGQVLGGPHNLMRRSTVSLLDTYQKCGLKRKSEEIENTSSVQIIEEHPPMIQNNASGATVATATTSTATSKNSGSNSEGDYQLVQHEVLCSMTNTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTESADDYNFVRAYECFQHKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPVLQQVATALMKLKSLGLIHADLKPENIMLVDPSRQPYRVKVIDFGSASHVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLSAGTKTTRFFNRDTDSPYPLWRLKTPDDHEAETGIKSKEARKYIFNCLDDMAQVNMTTDLEGSDMLVEKADRREFIDLLKKMLTIDADKRVTPIETLNHPFVTMTHLLDFPHSAHVKSCFQNMEICKRRVNMYDTVNQSKTPFITHVAPSTSTNLTMTFNNQLTTVHNQAPTTSSATLSLANPEVSILNYQSALYQPSAASMAAVAPRSMPLQTGTAQICARPDPFQQALIVCPPGFQGLQASPSKHAGYSVRMENAVPIVTQAPGAQPLQIQPGLLAQQAWPGGAQQILLPPAWQQLTGVATHTSVQHAAVIPETMAGTQQLADWRNTHAHGSHYNPIMQQPALLTGHVTLPAAQPLNVGVAHVMRQQPTSTTSSRKSKQHQSSVRNVSTCEVTSSQAISSPQRSKRVKENTPPRCAMVHSSPACSTSVTCGWGDVASSTTRERQRQTIVIPDTPSPTVSVITISSDTDEEEEQKHAPTSTVSKQRKNVISCVTVHDSPYSDSSSNTSPYSVQQRTGHNGTNTLDTKGGLENHCTGNPRTIIVPPLKTQASEVLVECDSLGPAISASHHSSSFKSKSSSTVTSTSGHSSGSSSGAIAYRQQRPGPHFQQQQPLNLSQAQQHMAADRTGSHRRQQAYITPTMAQAPYTFPHNSPSHGTVHPHLAAAAHLPTQPHLYTYTAPTALGSTGTVAHLVASQGSARHTVQHTAYPASIVHQVPVSMGPRVLPSPTIHPSQYPAQFAHQTYISASPASTVYTGYPLSPAKVNQYPYI
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Serine/threonine-protein kinase involved in transcription regulation, p53/TP53-mediated cellular apoptosis and regulation of the cell cycle. Acts as a corepressor of several transcription factors, including SMAD1 and POU4F1/Brn3a and probably NK homeodomain transcription factors. Phosphorylates PDX1, ATF1, PML, p53/TP53, CREB1, CTBP1, CBX4, RUNX1, EP300, CTNNB1, HMGA1, ZBTB4 and DAZAP2. Inhibits cell growth and promotes apoptosis through the activation of p53/TP53 both at the transcription level and at the protein level (by phosphorylation and indirect acetylation). The phosphorylation of p53/TP53 may be mediated by a p53/TP53-HIPK2-AXIN1 complex. Involved in the response to hypoxia by acting as a transcriptional co-suppressor of HIF1A. Mediates transcriptional activation of TP73. In response to TGFB, cooperates with DAXX to activate JNK. Negative regulator through phosphorylation and subsequent proteasomal degradation of CTNNB1 and the antiapoptotic factor CTBP1. In the Wnt/beta-catenin signaling pathway acts as an intermediate kinase between MAP3K7/TAK1 and NLK to promote the proteasomal degradation of MYB. Phosphorylates CBX4 upon DNA damage and promotes its E3 SUMO-protein ligase activity. Activates CREB1 and ATF1 transcription factors by phosphorylation in response to genotoxic stress. In response to DNA damage, stabilizes PML by phosphorylation. PML, HIPK2 and FBXO3 may act synergically to activate p53/TP53-dependent transactivation. Promotes angiogenesis, and is involved in erythroid differentiation, especially during fetal liver erythropoiesis. Phosphorylation of RUNX1 and EP300 stimulates EP300 transcription regulation activity. Triggers ZBTB4 protein degradation in response to DNA damage. In response to DNA damage, phosphorylates DAZAP2 which localizes DAZAP2 to the nucleus, reduces interaction of DAZAP2 with HIPK2 and prevents DAZAP2-dependent ubiquitination of HIPK2 by E3 ubiquitin-protein ligase SIAH1 and subsequent proteasomal degradation (By similarity). Modulates HMGA1 DNA-binding affinity. In response to high glucose, triggers phosphorylation-mediated subnuclear localization shifting of PDX1. Involved in the regulation of eye size, lens formation and retinal lamination during late embryogenesis. {ECO:0000250|UniProtKB:Q9H2X6, ECO:0000269|PubMed:11593421, ECO:0000269|PubMed:11780126, ECO:0000269|PubMed:14567915, ECO:0000269|PubMed:15082531, ECO:0000269|PubMed:15492043, ECO:0000269|PubMed:16917507, ECO:0000269|PubMed:20231426, ECO:0000269|PubMed:20307497, ECO:0000269|PubMed:20579985, ECO:0000269|PubMed:20637728}.
uniprot
proteins
mass_dalton
130498
uniprot
proteins
mutagenesis
MUTAGEN 228; /note="K->R: No enzymatic activity, but still interacts with TP53 and NLK. Blocks the ability to induce cell growth arrest. Decreases corepressor activity."; /evidence="ECO:0000269|PubMed:11593421, ECO:0000269|PubMed:11780126, ECO:0000269|PubMed:15082531, ECO:0000269|PubMed:9748262"; MUTAGEN 361; /note="Y->A: Strongly reduced nuclear localization."; /evidence="ECO:0000269|PubMed:23485397"; MUTAGEN 1189; /note="K->R: Inhibits localization to nuclear speckles."; /evidence="ECO:0000269|PubMed:10535925
uniprot
proteins
post_translational_modification
PTM: Sumoylated. When conjugated it is directed to nuclear speckles. Desumoylated by SENP1. Sumoylation on Lys-32 is promoted by the E3 SUMO-protein ligase CBX4 (By similarity). {ECO:0000250}.; PTM: Autophosphorylation at Tyr-361 in the activation loop activates the kinase and promotes nuclear localization. {ECO:0000269|PubMed:23485397}.; PTM: Ubiquitinated by FBXO3, WSB1 and SIAH1, leading to rapid proteasome-dependent degradation. The degradation mediated by FBXO3, but not ubiquitination, is prevented in the presence of PML. The degradation mediated by WSB1 and SIAH1 is reversibly reduced upon DNA damage. {ECO:0000250|UniProtKB:Q9H2X6}.; PTM: Cleaved at Asp-923 and Asp-984 by CASP6 in a p53/TP53-dependent manner. The cleaved form lacks the autoinhibitory C-terminal domain (AID), resulting in a hyperactive kinase, which potentiates p53/TP53 Ser-46 phosphorylation and subsequent activation of the cell death machinery.
uniprot
proteins
protein_family
CMGC Ser/Thr protein kinase family
uniprot
proteins
protein_family
HIPK subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
10535925
uniprot
proteins
pubmed
11078605
uniprot
proteins
pubmed
11267674
uniprot
proteins
pubmed
11593421
uniprot
proteins
pubmed
11780126
uniprot
proteins
pubmed
11798164
uniprot
proteins
pubmed
14567915
uniprot
proteins
pubmed
14990717
uniprot
proteins
pubmed
15082531
uniprot
proteins
pubmed
15492043
uniprot
proteins
pubmed
15526030
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16917507
uniprot
proteins
pubmed
19714248
uniprot
proteins
pubmed
20231426
uniprot
proteins
pubmed
20307497
uniprot
proteins
pubmed
20579985
uniprot
proteins
pubmed
20637728
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23485397
uniprot
proteins
pubmed
9748262
uniprot
proteins
sequence_length
1196
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000269|PubMed:10535925, ECO:0000269|PubMed:11078605, ECO:0000269|PubMed:14990717, ECO:0000269|PubMed:20579985, ECO:0000269|PubMed:9748262}. Cytoplasm {ECO:0000250|UniProtKB:Q9H2X6}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:11078605}. Cytoplasm {ECO:0000269|PubMed:11078605}. Note=Isoform 2 seems to be both nuclear and cytoplasmic.
uniprot
proteins