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Homeodomain-interacting protein kinase 1 (EC 2.7.11.1) (Nuclear body-associated kinase 2)

 HIPK1_HUMAN             Reviewed;        1210 AA.
Q86Z02; A6NJ34; O75125; Q5SQL2; Q5SQL4; Q5SQL5; Q8IYD7; Q8NDN5;
Q8NEB6; Q8TBZ1;
29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
12-SEP-2018, entry version 148.
RecName: Full=Homeodomain-interacting protein kinase 1;
EC=2.7.11.1;
AltName: Full=Nuclear body-associated kinase 2;
Name=HIPK1; Synonyms=KIAA0630, MYAK, NBAK2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Miyata Y.;
"Molecular cloning of human HIPK1.";
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 318-1210 (ISOFORM 1).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 720-1210 (ISOFORMS 1/3/4).
TISSUE=Brain;
PubMed=9734811; DOI=10.1093/dnares/5.3.169;
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. X.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:169-176(1998).
[7]
FUNCTION, AND PHOSPHORYLATION BY JNK1.
PubMed=12968034; DOI=10.1074/jbc.M213201200;
Song J.J., Lee Y.J.;
"Role of the ASK1-SEK1-JNK1-HIPK1 signal in Daxx trafficking and ASK1
oligomerization.";
J. Biol. Chem. 278:47245-47252(2003).
[8]
TISSUE SPECIFICITY, AND INTERACTION WITH DAXX.
PubMed=12529400; DOI=10.1128/MCB.23.3.950-960.2003;
Ecsedy J.A., Michaelson J.S., Leder P.;
"Homeodomain-interacting protein kinase 1 modulates Daxx localization,
phosphorylation, and transcriptional activity.";
Mol. Cell. Biol. 23:950-960(2003).
[9]
INTERACTION WITH TP53, TISSUE SPECIFICITY, AND FUNCTION.
PubMed=12702766; DOI=10.1073/pnas.0530308100;
Kondo S., Lu Y., Debbas M., Lin A.W., Sarosi I., Itie A., Wakeham A.,
Tuan J., Saris C., Elliott G., Ma W., Benchimol S., Lowe S.W.,
Mak T.W., Thukral S.K.;
"Characterization of cells and gene-targeted mice deficient for the
p53-binding kinase homeodomain-interacting protein kinase 1 (HIPK1).";
Proc. Natl. Acad. Sci. U.S.A. 100:5431-5436(2003).
[10]
FUNCTION, INTERACTION WITH DAB2IP AND MAP3K5, SUBCELLULAR LOCATION,
SUMOYLATION AT LYS-25 AND LYS-1203, DESUMOYLATION MEDIATED BY TNF, AND
MUTAGENESIS OF LYS-25; ASP-315; LYS-317; LYS-440; LYS-556 AND
LYS-1203.
PubMed=15701637; DOI=10.1074/jbc.M414262200;
Li X., Zhang R., Luo D., Park S.-J., Wang Q., Kim Y., Min W.;
"Tumor necrosis factor alpha-induced desumoylation and cytoplasmic
translocation of homeodomain-interacting protein kinase 1 are critical
for apoptosis signal-regulating kinase 1-JNK/p38 activation.";
J. Biol. Chem. 280:15061-15070(2005).
[11]
FUNCTION IN ANTI-OXIDATIVE STRESS, INTERACTION WITH PARK7, SUBCELLULAR
LOCATION, AND DEGRADATION BY PARK7.
PubMed=16390825; DOI=10.1080/10715760500456847;
Sekito A., Koide-Yoshida S., Niki T., Taira T., Iguchi-Ariga S.M.M.,
Ariga H.;
"DJ-1 interacts with HIPK1 and affects H2O2-induced cell death.";
Free Radic. Res. 40:155-165(2006).
[12]
DESUMOYLATION BY SENP1, AND SUBCELLULAR LOCATION.
PubMed=18219322; DOI=10.1038/sj.cdd.4402303;
Li X., Luo Y., Yu L., Lin Y., Luo D., Zhang H., He Y., Kim Y.-O.,
Kim Y., Tang S., Min W.;
"SENP1 mediates TNF-induced desumoylation and cytoplasmic
translocation of HIPK1 to enhance ASK1-dependent apoptosis.";
Cell Death Differ. 15:739-750(2008).
[13]
FUNCTION AS MYB KINASE, INTERACTION WITH MYB, MUTAGENESIS OF LYS-219,
AND SUBCELLULAR LOCATION.
PubMed=19646965; DOI=10.1016/j.bbrc.2009.07.139;
Matre V., Nordgaard O., Alm-Kristiansen A.H., Ledsaak M.,
Gabrielsen O.S.;
"HIPK1 interacts with c-Myb and modulates its activity through
phosphorylation.";
Biochem. Biophys. Res. Commun. 388:150-154(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-872, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-967 AND SER-1200, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-25, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-25, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-25; LYS-120; LYS-124 AND
LYS-991, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[19]
VARIANTS [LARGE SCALE ANALYSIS] CYS-310 AND VAL-1165.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- 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. {ECO:0000269|PubMed:12702766,
ECO:0000269|PubMed:12968034, ECO:0000269|PubMed:15701637,
ECO:0000269|PubMed:16390825, ECO:0000269|PubMed:19646965}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Interacts with Nkx1-2, Nkx2-5, MYB, PARK7, DAXX and
p53/TP53. Part of a cytoplasmic complex made of HIPK1, DAB2IP and
MAP3K5 in response to TNF. This complex formation promotes MAP3K5-
JNK activation and subsequent apoptosis.
{ECO:0000269|PubMed:12529400, ECO:0000269|PubMed:12702766,
ECO:0000269|PubMed:15701637, ECO:0000269|PubMed:16390825,
ECO:0000269|PubMed:19646965}.
-!- INTERACTION:
Q13643:FHL3; NbExp=3; IntAct=EBI-692891, EBI-741101;
P04637:TP53; NbExp=2; IntAct=EBI-692891, EBI-366083;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly
nuclear. Translocates from nucleus to cytoplasm in response to
stress stimuli via SENP1-mediated desumoylation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=HIPK1-alpha;
IsoId=Q86Z02-1; Sequence=Displayed;
Name=2; Synonyms=HIPK1-beta;
IsoId=Q86Z02-2; Sequence=VSP_013130, VSP_013131;
Name=3;
IsoId=Q86Z02-3; Sequence=VSP_013128;
Name=4;
IsoId=Q86Z02-4; Sequence=VSP_013127, VSP_013129;
-!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in
skeletal muscle and heart. Overexpressed in breast cancer cell
lines. Isoform 2 is highly expressed in testis.
{ECO:0000269|PubMed:12529400, ECO:0000269|PubMed:12702766}.
-!- 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}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. HIPK subfamily. {ECO:0000305}.
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EMBL; AB089957; BAC57075.1; -; mRNA.
EMBL; AL731797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL137856; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471122; EAW56590.1; -; Genomic_DNA.
EMBL; BC028408; AAH28408.1; -; mRNA.
EMBL; BC033012; AAH33012.1; -; mRNA.
EMBL; BC036057; AAH36057.1; -; mRNA.
EMBL; AL833829; CAD38689.1; -; mRNA.
EMBL; AB014530; BAA31605.1; -; mRNA.
CCDS; CCDS41370.1; -. [Q86Z02-3]
CCDS; CCDS867.1; -. [Q86Z02-1]
CCDS; CCDS868.1; -. [Q86Z02-2]
CCDS; CCDS869.1; -. [Q86Z02-4]
RefSeq; NP_689909.2; NM_152696.3. [Q86Z02-2]
RefSeq; NP_852003.1; NM_181358.2. [Q86Z02-4]
RefSeq; NP_938009.1; NM_198268.2. [Q86Z02-1]
RefSeq; NP_938010.1; NM_198269.2. [Q86Z02-3]
RefSeq; XP_005270669.1; XM_005270612.4. [Q86Z02-1]
RefSeq; XP_005270670.1; XM_005270613.4. [Q86Z02-1]
UniGene; Hs.532363; -.
ProteinModelPortal; Q86Z02; -.
SMR; Q86Z02; -.
BioGrid; 128490; 17.
ELM; Q86Z02; -.
IntAct; Q86Z02; 17.
MINT; Q86Z02; -.
STRING; 9606.ENSP00000358571; -.
BindingDB; Q86Z02; -.
ChEMBL; CHEMBL5427; -.
GuidetoPHARMACOLOGY; 2033; -.
iPTMnet; Q86Z02; -.
PhosphoSitePlus; Q86Z02; -.
BioMuta; HIPK1; -.
DMDM; 34395641; -.
EPD; Q86Z02; -.
MaxQB; Q86Z02; -.
PaxDb; Q86Z02; -.
PeptideAtlas; Q86Z02; -.
PRIDE; Q86Z02; -.
ProteomicsDB; 70492; -.
ProteomicsDB; 70493; -. [Q86Z02-2]
ProteomicsDB; 70494; -. [Q86Z02-3]
ProteomicsDB; 70495; -. [Q86Z02-4]
Ensembl; ENST00000340480; ENSP00000340956; ENSG00000163349. [Q86Z02-3]
Ensembl; ENST00000369553; ENSP00000358566; ENSG00000163349. [Q86Z02-4]
Ensembl; ENST00000369558; ENSP00000358571; ENSG00000163349. [Q86Z02-1]
Ensembl; ENST00000369559; ENSP00000358572; ENSG00000163349. [Q86Z02-2]
Ensembl; ENST00000426820; ENSP00000407442; ENSG00000163349. [Q86Z02-1]
GeneID; 204851; -.
KEGG; hsa:204851; -.
UCSC; uc001eel.4; human. [Q86Z02-1]
CTD; 204851; -.
DisGeNET; 204851; -.
EuPathDB; HostDB:ENSG00000163349.21; -.
GeneCards; HIPK1; -.
HGNC; HGNC:19006; HIPK1.
HPA; HPA016664; -.
MIM; 608003; gene.
neXtProt; NX_Q86Z02; -.
OpenTargets; ENSG00000163349; -.
PharmGKB; PA134897980; -.
eggNOG; KOG0667; Eukaryota.
eggNOG; ENOG410XPET; LUCA.
GeneTree; ENSGT00760000119032; -.
HOVERGEN; HBG051908; -.
InParanoid; Q86Z02; -.
KO; K08826; -.
OMA; TDWRNAH; -.
OrthoDB; EOG091G0UMX; -.
PhylomeDB; Q86Z02; -.
TreeFam; TF105417; -.
Reactome; R-HSA-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
Reactome; R-HSA-5578768; Physiological factors.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
SignaLink; Q86Z02; -.
ChiTaRS; HIPK1; human.
GeneWiki; HIPK1; -.
GenomeRNAi; 204851; -.
PRO; PR:Q86Z02; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000163349; Expressed in 239 organ(s), highest expression level in oviduct epithelium.
CleanEx; HS_HIPK1; -.
ExpressionAtlas; Q86Z02; baseline and differential.
Genevisible; Q86Z02; HS.
GO; GO:0005813; C:centrosome; IDA:HPA.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0034333; P:adherens junction assembly; IEA:Ensembl.
GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
GO; GO:0060216; P:definitive hemopoiesis; ISS:UniProtKB.
GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IEA:Ensembl.
GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IEA:Ensembl.
GO; GO:0072577; P:endothelial cell apoptotic process; IDA:UniProtKB.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0001654; P:eye development; ISS:UniProtKB.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
GO; GO:0061072; P:iris morphogenesis; IEA:Ensembl.
GO; GO:0060235; P:lens induction in camera-type eye; IEA:Ensembl.
GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0010842; P:retina layer formation; IEA:Ensembl.
GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
Isopeptide bond; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Serine/threonine-protein kinase;
Transcription; Transcription regulation; Transferase; Ubl conjugation.
CHAIN 1 1210 Homeodomain-interacting protein kinase 1.
/FTId=PRO_0000085993.
DOMAIN 190 518 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 196 204 ATP. {ECO:0000305}.
REGION 885 1093 Interaction with TP53.
{ECO:0000269|PubMed:12702766}.
REGION 891 998 Required for localization to nuclear
speckles. {ECO:0000250}.
REGION 902 926 SUMO interaction motifs (SIM); required
for nuclear localization and kinase
activity. {ECO:0000250}.
MOTIF 844 847 Nuclear localization signal 1 (NLS1).
{ECO:0000250}.
ACT_SITE 315 315 Proton acceptor. {ECO:0000305}.
BINDING 219 219 ATP. {ECO:0000305}.
MOD_RES 872 872 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 967 967 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1200 1200 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 25 25 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
CROSSLNK 25 25 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 120 120 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 124 124 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 991 991 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1203 1203 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:15701637}.
VAR_SEQ 1 394 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013127.
VAR_SEQ 1 374 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013128.
VAR_SEQ 395 399 ASEYD -> MVLMF (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013129.
VAR_SEQ 1049 1075 NQQSSAAPTSQERSSNPAPRRQQAFVA -> VSAMGYCLLF
GPCTVVTFWRTLLLAGC (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013130.
VAR_SEQ 1076 1210 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013131.
VARIANT 6 6 Q -> R (in dbSNP:rs35324789).
/FTId=VAR_051626.
VARIANT 310 310 G -> C (in dbSNP:rs34335651).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040546.
VARIANT 1165 1165 L -> V. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_046047.
MUTAGEN 25 25 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.
{ECO:0000269|PubMed:15701637}.
MUTAGEN 219 219 K->A: Loss of kinase activity.
{ECO:0000269|PubMed:19646965}.
MUTAGEN 315 315 D->N: Loss of kinase activity and
impaired MAP3K5-JNK inactivation.
{ECO:0000269|PubMed:15701637}.
MUTAGEN 317 317 K->R: Nuclear subcellular location.
Impaired sumoylation and cytoplasmic
subcellular location; when associated
with R-25; R-440; R-556 and R-1203.
{ECO:0000269|PubMed:15701637}.
MUTAGEN 440 440 K->R: Nuclear subcellular location.
Impaired sumoylation and cytoplasmic
subcellular location; when associated
with R-25; R-317; R-556 and R-1203.
{ECO:0000269|PubMed:15701637}.
MUTAGEN 556 556 K->R: Nuclear subcellular location.
Impaired sumoylation and cytoplasmic
subcellular location; when associated
with R-25; R-317; R-440 and R-1203.
{ECO:0000269|PubMed:15701637}.
MUTAGEN 1203 1203 K->R: Nuclear subcellular location.
Impaired sumoylation and cytoplasmic
subcellular location; when associated
with R-25; R-317; R-440 and R-556.
{ECO:0000269|PubMed:15701637}.
CONFLICT 721 721 P -> Q (in Ref. 4; AAH33012).
{ECO:0000305}.
CONFLICT 747 747 Missing (in Ref. 6; BAA31605).
{ECO:0000305}.
CONFLICT 799 799 H -> Y (in Ref. 5; CAD38689).
{ECO:0000305}.
CONFLICT 1054 1054 A -> V (in Ref. 4; AAH36057).
{ECO:0000305}.
SEQUENCE 1210 AA; 130843 MW; DB0BBFA6DF152909 CRC64;
MASQLQVFSP PSVSSSAFCS AKKLKIEPSG WDVSGQSSND KYYTHSKTLP ATQGQANSSH
QVANFNIPAY DQGLLLPAPA VEHIVVTAAD SSGSAATSTF QSSQTLTHRS NVSLLEPYQK
CGLKRKSEEV DSNGSVQIIE EHPPLMLQNR TVVGAAATTT TVTTKSSSSS GEGDYQLVQH
EILCSMTNSY EVLEFLGRGT FGQVAKCWKR STKEIVAIKI LKNHPSYARQ GQIEVSILSR
LSSENADEYN FVRSYECFQH KNHTCLVFEM LEQNLYDFLK QNKFSPLPLK YIRPILQQVA
TALMKLKSLG LIHADLKPEN IMLVDPVRQP YRVKVIDFGS ASHVSKAVCS TYLQSRYYRA
PEIILGLPFC EAIDMWSLGC VIAELFLGWP LYPGASEYDQ IRYISQTQGL PAEYLLSAGT
KTTRFFNRDP NLGYPLWRLK TPEEHELETG IKSKEARKYI FNCLDDMAQV NMSTDLEGTD
MLAEKADRRE YIDLLKKMLT IDADKRITPL KTLNHQFVTM THLLDFPHSN HVKSCFQNME
ICKRRVHMYD TVSQIKSPFT THVAPNTSTN LTMSFSNQLN TVHNQASVLA SSSTAAAATL
SLANSDVSLL NYQSALYPSS AAPVPGVAQQ GVSLQPGTTQ ICTQTDPFQQ TFIVCPPAFQ
TGLQATTKHS GFPVRMDNAV PIVPQAPAAQ PLQIQSGVLT QGSCTPLMVA TLHPQVATIT
PQYAVPFTLS CAAGRPALVE QTAAVLQAWP GGTQQILLPS TWQQLPGVAL HNSVQPTAMI
PEAMGSGQQL ADWRNAHSHG NQYSTIMQQP SLLTNHVTLA TAQPLNVGVA HVVRQQQSSS
LPSKKNKQSA PVSSKSSLDV LPSQVYSLVG SSPLRTTSSY NSLVPVQDQH QPIIIPDTPS
PPVSVITIRS DTDEEEDNKY KPSSSGLKPR SNVISYVTVN DSPDSDSSLS SPYSTDTLSA
LRGNSGSVLE GPGRVVADGT GTRTIIVPPL KTQLGDCTVA TQASGLLSNK TKPVASVSGQ
SSGCCITPTG YRAQRGGTSA AQPLNLSQNQ QSSAAPTSQE RSSNPAPRRQ QAFVAPLSQA
PYTFQHGSPL HSTGHPHLAP APAHLPSQAH LYTYAAPTSA AALGSTSSIA HLFSPQGSSR
HAAAYTTHPS TLVHQVPVSV GPSLLTSASV APAQYQHQFA TQSYIGSSRG STIYTGYPLS
PTKISQYSYL


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