Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q86Z02 (HIPK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Homeodomain-interacting protein kinase 1

EC=2.7.11.1
Alternative name(s):
Nuclear body-associated kinase 2
Gene names
Name:HIPK1
Synonyms:KIAA0630, MYAK, NBAK2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1210 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.7 Ref.9 Ref.10 Ref.11 Ref.13

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.13

Subcellular location

Nucleus. Cytoplasm. Note: Predominantly nuclear. Translocates from nucleus to cytoplasm in response to stress stimuli via SENP1-mediated desumoylation. Ref.10 Ref.11 Ref.12 Ref.13

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. Ref.8 Ref.9

Post-translational modification

Autophosphorylated. Phosphorylated and activated by JNK1. Ref.7

Degraded by PARK7 at the protein level.

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. Ref.10 Ref.12

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. HIPK subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanterior/posterior pattern specification

Inferred from electronic annotation. Source: Ensembl

definitive hemopoiesis

Inferred from sequence or structural similarity PubMed 20231426. Source: UniProtKB

embryonic camera-type eye morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic retina morphogenesis in camera-type eye

Inferred from electronic annotation. Source: Ensembl

endothelial cell apoptotic process

Inferred from direct assay Ref.10. Source: UniProtKB

extrinsic apoptotic signaling pathway

Inferred from direct assay Ref.10. Source: UniProtKB

eye development

Inferred from sequence or structural similarity PubMed 20579985. Source: UniProtKB

intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from electronic annotation. Source: Ensembl

iris morphogenesis

Inferred from electronic annotation. Source: Ensembl

lens induction in camera-type eye

Inferred from electronic annotation. Source: Ensembl

neuron differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of angiogenesis

Inferred from sequence or structural similarity PubMed 16917507. Source: UniProtKB

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

protein desumoylation

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of tumor necrosis factor-mediated signaling pathway

Inferred from direct assay Ref.10. Source: UniProtKB

retina layer formation

Inferred from electronic annotation. Source: Ensembl

smoothened signaling pathway

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.10. Source: UniProtKB

nuclear speck

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay Ref.10. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.9. Source: IntAct

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TP53P046372EBI-692891,EBI-366083

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86Z02-1)

Also known as: HIPK1-alpha;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q86Z02-2)

Also known as: HIPK1-beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1049-1075: NQQSSAAPTSQERSSNPAPRRQQAFVA → VSAMGYCLLFGPCTVVTFWRTLLLAGC
     1076-1210: Missing.
Isoform 3 (identifier: Q86Z02-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-374: Missing.
Isoform 4 (identifier: Q86Z02-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-394: Missing.
     395-399: ASEYD → MVLMF

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12101210Homeodomain-interacting protein kinase 1
PRO_0000085993

Regions

Domain190 – 518329Protein kinase
Nucleotide binding196 – 2049ATP Probable
Region844 – 8474Nuclear localization signal 1 (NLS1) By similarity
Region885 – 1093209Interaction with TP53
Region891 – 998108Required for localization to nuclear speckles By similarity
Region902 – 92625SUMO interaction motifs (SIM); required for nuclear localization and kinase activity By similarity

Sites

Active site3151Proton acceptor Probable
Binding site2191ATP Probable

Amino acid modifications

Modified residue8721Phosphoserine Ref.14
Cross-link25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.10
Cross-link1203Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable

Natural variations

Alternative sequence1 – 394394Missing in isoform 4.
VSP_013127
Alternative sequence1 – 374374Missing in isoform 3.
VSP_013128
Alternative sequence395 – 3995ASEYD → MVLMF in isoform 4.
VSP_013129
Alternative sequence1049 – 107527NQQSS…QAFVA → VSAMGYCLLFGPCTVVTFWR TLLLAGC in isoform 2.
VSP_013130
Alternative sequence1076 – 1210135Missing in isoform 2.
VSP_013131
Natural variant61Q → R.
Corresponds to variant rs35324789 [ dbSNP | Ensembl ].
VAR_051626
Natural variant3101G → C. Ref.15
VAR_040546
Natural variant11651L → V. Ref.15
VAR_046047

Experimental info

Mutagenesis251K → 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. Ref.10
Mutagenesis2191K → A: Loss of kinase activity. Ref.13
Mutagenesis3151D → N: Loss of kinase activity and impaired MAP3K5-JNK inactivation. Ref.10
Mutagenesis3171K → R: Nuclear subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-25; R-440; R-556 and R-1203. Ref.10
Mutagenesis4401K → R: Nuclear subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-25; R-317; R-556 and R-1203. Ref.10
Mutagenesis5561K → R: Nuclear subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-25; R-317; R-440 and R-1203. Ref.10
Mutagenesis12031K → R: Nuclear subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-25; R-317; R-440 and R-556. Ref.10
Sequence conflict7211P → Q in AAH33012. Ref.4
Sequence conflict7471Missing in BAA31605. Ref.6
Sequence conflict7991H → Y in CAD38689. Ref.5
Sequence conflict10541A → V in AAH36057. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (HIPK1-alpha) [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: DB0BBFA6DF152909

FASTA1,210130,843
        10         20         30         40         50         60 
MASQLQVFSP PSVSSSAFCS AKKLKIEPSG WDVSGQSSND KYYTHSKTLP ATQGQANSSH 

        70         80         90        100        110        120 
QVANFNIPAY DQGLLLPAPA VEHIVVTAAD SSGSAATSTF QSSQTLTHRS NVSLLEPYQK 

       130        140        150        160        170        180 
CGLKRKSEEV DSNGSVQIIE EHPPLMLQNR TVVGAAATTT TVTTKSSSSS GEGDYQLVQH 

       190        200        210        220        230        240 
EILCSMTNSY EVLEFLGRGT FGQVAKCWKR STKEIVAIKI LKNHPSYARQ GQIEVSILSR 

       250        260        270        280        290        300 
LSSENADEYN FVRSYECFQH KNHTCLVFEM LEQNLYDFLK QNKFSPLPLK YIRPILQQVA 

       310        320        330        340        350        360 
TALMKLKSLG LIHADLKPEN IMLVDPVRQP YRVKVIDFGS ASHVSKAVCS TYLQSRYYRA 

       370        380        390        400        410        420 
PEIILGLPFC EAIDMWSLGC VIAELFLGWP LYPGASEYDQ IRYISQTQGL PAEYLLSAGT 

       430        440        450        460        470        480 
KTTRFFNRDP NLGYPLWRLK TPEEHELETG IKSKEARKYI FNCLDDMAQV NMSTDLEGTD 

       490        500        510        520        530        540 
MLAEKADRRE YIDLLKKMLT IDADKRITPL KTLNHQFVTM THLLDFPHSN HVKSCFQNME 

       550        560        570        580        590        600 
ICKRRVHMYD TVSQIKSPFT THVAPNTSTN LTMSFSNQLN TVHNQASVLA SSSTAAAATL 

       610        620        630        640        650        660 
SLANSDVSLL NYQSALYPSS AAPVPGVAQQ GVSLQPGTTQ ICTQTDPFQQ TFIVCPPAFQ 

       670        680        690        700        710        720 
TGLQATTKHS GFPVRMDNAV PIVPQAPAAQ PLQIQSGVLT QGSCTPLMVA TLHPQVATIT 

       730        740        750        760        770        780 
PQYAVPFTLS CAAGRPALVE QTAAVLQAWP GGTQQILLPS TWQQLPGVAL HNSVQPTAMI 

       790        800        810        820        830        840 
PEAMGSGQQL ADWRNAHSHG NQYSTIMQQP SLLTNHVTLA TAQPLNVGVA HVVRQQQSSS 

       850        860        870        880        890        900 
LPSKKNKQSA PVSSKSSLDV LPSQVYSLVG SSPLRTTSSY NSLVPVQDQH QPIIIPDTPS 

       910        920        930        940        950        960 
PPVSVITIRS DTDEEEDNKY KPSSSGLKPR SNVISYVTVN DSPDSDSSLS SPYSTDTLSA 

       970        980        990       1000       1010       1020 
LRGNSGSVLE GPGRVVADGT GTRTIIVPPL KTQLGDCTVA TQASGLLSNK TKPVASVSGQ 

      1030       1040       1050       1060       1070       1080 
SSGCCITPTG YRAQRGGTSA AQPLNLSQNQ QSSAAPTSQE RSSNPAPRRQ QAFVAPLSQA 

      1090       1100       1110       1120       1130       1140 
PYTFQHGSPL HSTGHPHLAP APAHLPSQAH LYTYAAPTSA AALGSTSSIA HLFSPQGSSR 

      1150       1160       1170       1180       1190       1200 
HAAAYTTHPS TLVHQVPVSV GPSLLTSASV APAQYQHQFA TQSYIGSSRG STIYTGYPLS 

      1210 
PTKISQYSYL 

« Hide

Isoform 2 (HIPK1-beta) [UniParc].

Checksum: DC4EE791F0EEC369
Show »

FASTA1,075116,731
Isoform 3 [UniParc].

Checksum: ED30D5EDCA8D4918
Show »

FASTA83689,481
Isoform 4 [UniParc].

Checksum: 97A2176C8995F038
Show »

FASTA81687,302

References

« Hide 'large scale' references
[1]"Molecular cloning of human HIPK1."
Miyata Y.
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The DNA sequence and biological annotation of human chromosome 1."
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. expand/collapse author list , 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.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
Tissue: Testis.
[5]"The full-ORF clone resource of the German cDNA consortium."
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.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 318-1210 (ISOFORM 1).
Tissue: Testis.
[6]"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."
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 720-1210 (ISOFORMS 1/3/4).
Tissue: Brain.
[7]"Role of the ASK1-SEK1-JNK1-HIPK1 signal in Daxx trafficking and ASK1 oligomerization."
Song J.J., Lee Y.J.
J. Biol. Chem. 278:47245-47252(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION BY JNK1.
[8]"Homeodomain-interacting protein kinase 1 modulates Daxx localization, phosphorylation, and transcriptional activity."
Ecsedy J.A., Michaelson J.S., Leder P.
Mol. Cell. Biol. 23:950-960(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INTERACTION WITH DAXX.
[9]"Characterization of cells and gene-targeted mice deficient for the p53-binding kinase homeodomain-interacting protein kinase 1 (HIPK1)."
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.
Proc. Natl. Acad. Sci. U.S.A. 100:5431-5436(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TP53, TISSUE SPECIFICITY, FUNCTION.
[10]"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."
Li X., Zhang R., Luo D., Park S.-J., Wang Q., Kim Y., Min W.
J. Biol. Chem. 280:15061-15070(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DAB2IP AND MAP3K5, SUBCELLULAR LOCATION, SUMOYLATION AT LYS-25 AND LYS-1203, DESUMOYLATION MEDIATED BY TNF, MUTAGENESIS OF LYS-25; ASP-315; LYS-317; LYS-440; LYS-556 AND LYS-1203.
[11]"DJ-1 interacts with HIPK1 and affects H2O2-induced cell death."
Sekito A., Koide-Yoshida S., Niki T., Taira T., Iguchi-Ariga S.M.M., Ariga H.
Free Radic. Res. 40:155-165(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ANTI-OXIDATIVE STRESS, INTERACTION WITH PARK7, SUBCELLULAR LOCATION, DEGRADATION BY PARK7.
[12]"SENP1 mediates TNF-induced desumoylation and cytoplasmic translocation of HIPK1 to enhance ASK1-dependent apoptosis."
Li X., Luo Y., Yu L., Lin Y., Luo D., Zhang H., He Y., Kim Y.-O., Kim Y., Tang S., Min W.
Cell Death Differ. 15:739-750(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DESUMOYLATION BY SENP1, SUBCELLULAR LOCATION.
[13]"HIPK1 interacts with c-Myb and modulates its activity through phosphorylation."
Matre V., Nordgaard O., Alm-Kristiansen A.H., Ledsaak M., Gabrielsen O.S.
Biochem. Biophys. Res. Commun. 388:150-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS MYB KINASE, INTERACTION WITH MYB, MUTAGENESIS OF LYS-219, SUBCELLULAR LOCATION.
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-872, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Patterns of somatic mutation in human cancer genomes."
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. expand/collapse author list , 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.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-310 AND VAL-1165.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB089957 mRNA. Translation: BAC57075.1.
AL731797 Genomic DNA. Translation: CAI22792.1.
AL731797 Genomic DNA. Translation: CAI22793.1.
AL731797 Genomic DNA. Translation: CAI22795.1.
AL137856 Genomic DNA. No translation available.
CH471122 Genomic DNA. Translation: EAW56590.1.
BC028408 mRNA. Translation: AAH28408.1.
BC033012 mRNA. Translation: AAH33012.1.
BC036057 mRNA. Translation: AAH36057.1.
AL833829 mRNA. Translation: CAD38689.1.
AB014530 mRNA. Translation: BAA31605.1.
CCDSCCDS41370.1. [Q86Z02-3]
CCDS867.1. [Q86Z02-1]
CCDS868.1. [Q86Z02-2]
CCDS869.1. [Q86Z02-4]
RefSeqNP_689909.2. NM_152696.3. [Q86Z02-2]
NP_852003.1. NM_181358.2. [Q86Z02-4]
NP_938009.1. NM_198268.2. [Q86Z02-1]
NP_938010.1. NM_198269.2. [Q86Z02-3]
XP_005270669.1. XM_005270612.2. [Q86Z02-1]
XP_005270670.1. XM_005270613.2. [Q86Z02-1]
UniGeneHs.532363.

3D structure databases

ProteinModelPortalQ86Z02.
SMRQ86Z02. Positions 188-517.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid128490. 16 interactions.
IntActQ86Z02. 14 interactions.
MINTMINT-1187651.

Chemistry

BindingDBQ86Z02.
ChEMBLCHEMBL5427.
GuidetoPHARMACOLOGY2033.

PTM databases

PhosphoSiteQ86Z02.

Polymorphism databases

DMDM34395641.

Proteomic databases

PaxDbQ86Z02.
PRIDEQ86Z02.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340480; ENSP00000340956; ENSG00000163349. [Q86Z02-3]
ENST00000369553; ENSP00000358566; ENSG00000163349. [Q86Z02-4]
ENST00000369558; ENSP00000358571; ENSG00000163349. [Q86Z02-1]
ENST00000369559; ENSP00000358572; ENSG00000163349. [Q86Z02-2]
ENST00000406344; ENSP00000384960; ENSG00000163349. [Q86Z02-4]
ENST00000426820; ENSP00000407442; ENSG00000163349. [Q86Z02-1]
GeneID204851.
KEGGhsa:204851.
UCSCuc001eel.3. human. [Q86Z02-2]
uc001eem.3. human. [Q86Z02-1]
uc001eep.3. human. [Q86Z02-4]

Organism-specific databases

CTD204851.
GeneCardsGC01P114471.
HGNCHGNC:19006. HIPK1.
HPAHPA016664.
MIM608003. gene.
neXtProtNX_Q86Z02.
PharmGKBPA134897980.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG051908.
InParanoidQ86Z02.
KOK08826.
OMANKYKPSS.
PhylomeDBQ86Z02.
TreeFamTF105417.

Enzyme and pathway databases

SignaLinkQ86Z02.

Gene expression databases

ArrayExpressQ86Z02.
BgeeQ86Z02.
CleanExHS_HIPK1.
GenevestigatorQ86Z02.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHIPK1. human.
GeneWikiHIPK1.
GenomeRNAi204851.
NextBio90482.
PROQ86Z02.
SOURCESearch...

Entry information

Entry nameHIPK1_HUMAN
AccessionPrimary (citable) accession number: Q86Z02
Secondary accession number(s): A6NJ34 expand/collapse secondary AC list , O75125, Q5SQL2, Q5SQL4, Q5SQL5, Q8IYD7, Q8NDN5, Q8NEB6, Q8TBZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM