HIPK1
entrez
204851
canonical
uniprot
Q86Z02
canonical
ensembl
ENSG00000163349
resolver
ensp
ENSP00000340956
resolver
ensp
ENSP00000358566
resolver
ensp
ENSP00000358571
resolver
ensp
ENSP00000358572
resolver
ensp
ENSP00000358574
resolver
ensp
ENSP00000407442
resolver
ensp
ENSP00000571127
resolver
ensp
ENSP00000571129
resolver
ensp
ENSP00000601300
resolver
ensp
ENSP00000601301
resolver
ensp
ENSP00000601303
resolver
enst
ENST00000369561
resolver
genesymbol
HIPK1
resolver
genesymbol_syn
KIAA0630
resolver
genesymbol_syn
MYAK
resolver
genesymbol_syn
NBAK2
resolver
hgnc
HGNC:19006
resolver
uniprot
A6NJ34
resolver
uniprot
B4DZ33
resolver
uniprot
J3KP92
resolver
uniprot
O75125
resolver
uniprot
Q5SQL2
resolver
uniprot
Q5SQL4
resolver
uniprot
Q5SQL5
resolver
uniprot
Q8IYD7
resolver
uniprot
Q8NDN5
resolver
uniprot
Q8NEB6
resolver
uniprot
Q8TBZ1
resolver
uniprot_entry
B4DZ33_HUMAN
resolver
uniprot_entry
HIPK1_HUMAN
resolver
uniprot_entry
J3KP92_HUMAN
resolver
uniprot_sec
A6NJ34
resolver
uniprot_sec
O75125
resolver
uniprot_sec
Q5SQL2
resolver
uniprot_sec
Q5SQL4
resolver
uniprot_sec
Q5SQL5
resolver
uniprot_sec
Q8IYD7
resolver
uniprot_sec
Q8NDN5
resolver
uniprot_sec
Q8NEB6
resolver
uniprot_sec
Q8TBZ1
resolver
amino_acid_sequence
MASQLQVFSPPSVSSSAFCSAKKLKIEPSGWDVSGQSSNDKYYTHSKTLPATQGQANSSHQVANFNIPAYDQGLLLPAPAVEHIVVTAADSSGSAATSTFQSSQTLTHRSNVSLLEPYQKCGLKRKSEEVDSNGSVQIIEEHPPLMLQNRTVVGAAATTTTVTTKSSSSSGEGDYQLVQHEILCSMTNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSENADEYNFVRSYECFQHKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPVRQPYRVKVIDFGSASHVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLSAGTKTTRFFNRDPNLGYPLWRLKTPEEHELETGIKSKEARKYIFNCLDDMAQVNMSTDLEGTDMLAEKADRREYIDLLKKMLTIDADKRITPLKTLNHQFVTMTHLLDFPHSNHVKSCFQNMEICKRRVHMYDTVSQIKSPFTTHVAPNTSTNLTMSFSNQLNTVHNQASVLASSSTAAAATLSLANSDVSLLNYQSALYPSSAAPVPGVAQQGVSLQPGTTQICTQTDPFQQTFIVCPPAFQTGLQATTKHSGFPVRMDNAVPIVPQAPAAQPLQIQSGVLTQGSCTPLMVATLHPQVATITPQYAVPFTLSCAAGRPALVEQTAAVLQAWPGGTQQILLPSTWQQLPGVALHNSVQPTAMIPEAMGSGQQLADWRNAHSHGNQYSTIMQQPSLLTNHVTLATAQPLNVGVAHVVRQQQSSSLPSKKNKQSAPVSSKSSLDVLPSQVYSLVGSSPLRTTSSYNSLVPVQDQHQPIIIPDTPSPPVSVITIRSDTDEEEDNKYKPSSSGLKPRSNVISYVTVNDSPDSDSSLSSPYSTDTLSALRGNSGSVLEGPGRVVADGTGTRTIIVPPLKTQLGDCTVATQASGLLSNKTKPVASVSGQSSGCCITPTGYRAQRGGTSAAQPLNLSQNQQSSAAPTSQERSSNPAPRRQQAFVAPLSQAPYTFQHGSPLHSTGHPHLAPAPAHLPSQAHLYTYAAPTSAAALGSTSSIAHLFSPQGSSRHAAAYTTHPSTLVHQVPVSVGPSLLTSASVAPAQYQHQFATQSYIGSSRGSTIYTGYPLSPTKISQYSYL
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Serine/threonine-protein kinase involved in transcription regulation and TNF-mediated cellular apoptosis. Plays a role as a corepressor for homeodomain transcription factors. Phosphorylates DAXX and MYB. Phosphorylates DAXX in response to stress, and mediates its translocation from the nucleus to the cytoplasm. Inactivates MYB transcription factor activity by phosphorylation. Prevents MAP3K5-JNK activation in the absence of TNF. TNF triggers its translocation to the cytoplasm in response to stress stimuli, thus activating nuclear MAP3K5-JNK by derepression and promoting apoptosis. May be involved in anti-oxidative stress responses. Involved in the regulation of eye size, lens formation and retinal lamination during late embryogenesis. Promotes angiogenesis and to be involved in erythroid differentiation. May be involved in malignant squamous cell tumor formation. Phosphorylates PAGE4 at 'Thr-51' which is critical for the ability of PAGE4 to potentiate the transcriptional activator activity of JUN (PubMed:24559171). {ECO:0000269|PubMed:12702766, ECO:0000269|PubMed:12968034, ECO:0000269|PubMed:15701637, ECO:0000269|PubMed:16390825, ECO:0000269|PubMed:19646965, ECO:0000269|PubMed:24559171}.
uniprot
proteins
mass_dalton
130843
uniprot
proteins
mutagenesis
MUTAGEN 25; /note="K->R: Reduced sumoylation and cytoplasmic subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-317; R-440; R-556 and R-1203."; /evidence="ECO:0000269|PubMed:15701637"; MUTAGEN 219; /note="K->A: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:19646965"; MUTAGEN 315; /note="D->N: Loss of kinase activity and impaired MAP3K5-JNK inactivation."; /evidence="ECO:0000269|PubMed:15701637"; MUTAGEN 317; /note="K->R: Nuclear subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-25; R-440; R-556 and R-1203."; /evidence="ECO:0000269|PubMed:15701637"; MUTAGEN 440; /note="K->R: Nuclear subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-25; R-317; R-556 and R-1203."; /evidence="ECO:0000269|PubMed:15701637"; MUTAGEN 556; /note="K->R: Nuclear subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-25; R-317; R-440 and R-1203."; /evidence="ECO:0000269|PubMed:15701637"; MUTAGEN 1203; /note="K->R: Nuclear subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-25; R-317; R-440 and R-556."; /evidence="ECO:0000269|PubMed:15701637
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated. Phosphorylated and activated by JNK1. {ECO:0000269|PubMed:12968034}.; PTM: Degraded by PARK7 at the protein level.; PTM: Sumoylated. When conjugated it is directed to nuclear speckles. SENP1-mediated desumoylation is mediated by TNF in response to stress stimuli, triggering transient translocation from nucleus to cytoplasm. {ECO:0000269|PubMed:15701637, ECO:0000269|PubMed:18219322}.
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
12529400
uniprot
proteins
pubmed
12702766
uniprot
proteins
pubmed
12968034
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15701637
uniprot
proteins
pubmed
16390825
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18219322
uniprot
proteins
pubmed
19646965
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24559171
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28289210
uniprot
proteins
pubmed
9734811
uniprot
proteins
sequence_length
1210
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15701637, ECO:0000269|PubMed:16390825, ECO:0000269|PubMed:18219322, ECO:0000269|PubMed:19646965, ECO:0000269|PubMed:28289210}. Cytoplasm {ECO:0000269|PubMed:15701637, ECO:0000269|PubMed:18219322, ECO:0000269|PubMed:19646965, ECO:0000269|PubMed:28289210}. Nucleus speckle {ECO:0000269|PubMed:16390825}. Note=Predominantly nuclear. Translocates from nucleus to cytoplasm in response to stress stimuli via SENP1-mediated desumoylation. {ECO:0000269|PubMed:15701637, ECO:0000269|PubMed:18219322}.
uniprot
proteins