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Q86Z02

- HIPK1_HUMAN

UniProt

Q86Z02 - HIPK1_HUMAN

Protein

Homeodomain-interacting protein kinase 1

Gene

HIPK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    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.5 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei219 – 2191ATPCurated
    Active sitei315 – 3151Proton acceptorCurated

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi196 – 2049ATPCurated

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. anterior/posterior pattern specification Source: Ensembl
    2. definitive hemopoiesis Source: UniProtKB
    3. embryonic camera-type eye morphogenesis Source: Ensembl
    4. embryonic retina morphogenesis in camera-type eye Source: Ensembl
    5. endothelial cell apoptotic process Source: UniProtKB
    6. extrinsic apoptotic signaling pathway Source: UniProtKB
    7. eye development Source: UniProtKB
    8. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: Ensembl
    9. iris morphogenesis Source: Ensembl
    10. lens induction in camera-type eye Source: Ensembl
    11. neuron differentiation Source: Ensembl
    12. positive regulation of angiogenesis Source: UniProtKB
    13. positive regulation of cell proliferation Source: Ensembl
    14. protein desumoylation Source: UniProtKB
    15. regulation of transcription, DNA-templated Source: UniProtKB-KW
    16. regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB
    17. retina layer formation Source: Ensembl
    18. smoothened signaling pathway Source: Ensembl
    19. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ86Z02.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Homeodomain-interacting protein kinase 1 (EC:2.7.11.1)
    Alternative name(s):
    Nuclear body-associated kinase 2
    Gene namesi
    Name:HIPK1
    Synonyms:KIAA0630, MYAK, NBAK2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:19006. HIPK1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nuclear speck Source: Ensembl
    3. nucleus Source: UniProtKB
    4. PML body Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi25 – 251K → 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. 1 Publication
    Mutagenesisi219 – 2191K → A: Loss of kinase activity. 1 Publication
    Mutagenesisi315 – 3151D → N: Loss of kinase activity and impaired MAP3K5-JNK inactivation. 1 Publication
    Mutagenesisi317 – 3171K → R: Nuclear subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-25; R-440; R-556 and R-1203. 1 Publication
    Mutagenesisi440 – 4401K → R: Nuclear subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-25; R-317; R-556 and R-1203. 1 Publication
    Mutagenesisi556 – 5561K → R: Nuclear subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-25; R-317; R-440 and R-1203. 1 Publication
    Mutagenesisi1203 – 12031K → R: Nuclear subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-25; R-317; R-440 and R-556. 1 Publication

    Organism-specific databases

    PharmGKBiPA134897980.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12101210Homeodomain-interacting protein kinase 1PRO_0000085993Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki25 – 25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei872 – 8721Phosphoserine2 Publications
    Cross-linki1203 – 1203Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated

    Post-translational modificationi

    Autophosphorylated. Phosphorylated and activated by JNK1.2 Publications
    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.2 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ86Z02.
    PRIDEiQ86Z02.

    PTM databases

    PhosphoSiteiQ86Z02.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed with highest levels in skeletal muscle and heart. Overexpressed in breast cancer cell lines. Isoform 2 is highly expressed in testis.2 Publications

    Gene expression databases

    ArrayExpressiQ86Z02.
    BgeeiQ86Z02.
    CleanExiHS_HIPK1.
    GenevestigatoriQ86Z02.

    Organism-specific databases

    HPAiHPA016664.

    Interactioni

    Subunit structurei

    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.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TP53P046372EBI-692891,EBI-366083

    Protein-protein interaction databases

    BioGridi128490. 16 interactions.
    IntActiQ86Z02. 15 interactions.
    MINTiMINT-1187651.

    Structurei

    3D structure databases

    ProteinModelPortaliQ86Z02.
    SMRiQ86Z02. Positions 188-517.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini190 – 518329Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni844 – 8474Nuclear localization signal 1 (NLS1)By similarity
    Regioni885 – 1093209Interaction with TP53Add
    BLAST
    Regioni891 – 998108Required for localization to nuclear specklesBy similarityAdd
    BLAST
    Regioni902 – 92625SUMO interaction motifs (SIM); required for nuclear localization and kinase activityBy similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG051908.
    InParanoidiQ86Z02.
    KOiK08826.
    OMAiNKYKPSS.
    PhylomeDBiQ86Z02.
    TreeFamiTF105417.

    Family and domain databases

    InterProiIPR011009. 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]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q86Z02-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MASQLQVFSP PSVSSSAFCS AKKLKIEPSG WDVSGQSSND KYYTHSKTLP     50
    ATQGQANSSH QVANFNIPAY DQGLLLPAPA VEHIVVTAAD SSGSAATSTF 100
    QSSQTLTHRS NVSLLEPYQK CGLKRKSEEV DSNGSVQIIE EHPPLMLQNR 150
    TVVGAAATTT TVTTKSSSSS GEGDYQLVQH EILCSMTNSY EVLEFLGRGT 200
    FGQVAKCWKR STKEIVAIKI LKNHPSYARQ GQIEVSILSR LSSENADEYN 250
    FVRSYECFQH KNHTCLVFEM LEQNLYDFLK QNKFSPLPLK YIRPILQQVA 300
    TALMKLKSLG LIHADLKPEN IMLVDPVRQP YRVKVIDFGS ASHVSKAVCS 350
    TYLQSRYYRA PEIILGLPFC EAIDMWSLGC VIAELFLGWP LYPGASEYDQ 400
    IRYISQTQGL PAEYLLSAGT KTTRFFNRDP NLGYPLWRLK TPEEHELETG 450
    IKSKEARKYI FNCLDDMAQV NMSTDLEGTD MLAEKADRRE YIDLLKKMLT 500
    IDADKRITPL KTLNHQFVTM THLLDFPHSN HVKSCFQNME ICKRRVHMYD 550
    TVSQIKSPFT THVAPNTSTN LTMSFSNQLN TVHNQASVLA SSSTAAAATL 600
    SLANSDVSLL NYQSALYPSS AAPVPGVAQQ GVSLQPGTTQ ICTQTDPFQQ 650
    TFIVCPPAFQ TGLQATTKHS GFPVRMDNAV PIVPQAPAAQ PLQIQSGVLT 700
    QGSCTPLMVA TLHPQVATIT PQYAVPFTLS CAAGRPALVE QTAAVLQAWP 750
    GGTQQILLPS TWQQLPGVAL HNSVQPTAMI PEAMGSGQQL ADWRNAHSHG 800
    NQYSTIMQQP SLLTNHVTLA TAQPLNVGVA HVVRQQQSSS LPSKKNKQSA 850
    PVSSKSSLDV LPSQVYSLVG SSPLRTTSSY NSLVPVQDQH QPIIIPDTPS 900
    PPVSVITIRS DTDEEEDNKY KPSSSGLKPR SNVISYVTVN DSPDSDSSLS 950
    SPYSTDTLSA LRGNSGSVLE GPGRVVADGT GTRTIIVPPL KTQLGDCTVA 1000
    TQASGLLSNK TKPVASVSGQ SSGCCITPTG YRAQRGGTSA AQPLNLSQNQ 1050
    QSSAAPTSQE RSSNPAPRRQ QAFVAPLSQA PYTFQHGSPL HSTGHPHLAP 1100
    APAHLPSQAH LYTYAAPTSA AALGSTSSIA HLFSPQGSSR HAAAYTTHPS 1150
    TLVHQVPVSV GPSLLTSASV APAQYQHQFA TQSYIGSSRG STIYTGYPLS 1200
    PTKISQYSYL 1210
    Length:1,210
    Mass (Da):130,843
    Last modified:June 1, 2003 - v1
    Checksum:iDB0BBFA6DF152909
    GO
    Isoform 2 (identifier: Q86Z02-2) [UniParc]FASTAAdd to Basket

    Also known as: HIPK1-beta

    The sequence of this isoform differs from the canonical sequence as follows:
         1049-1075: NQQSSAAPTSQERSSNPAPRRQQAFVA → VSAMGYCLLFGPCTVVTFWRTLLLAGC
         1076-1210: Missing.

    Show »
    Length:1,075
    Mass (Da):116,731
    Checksum:iDC4EE791F0EEC369
    GO
    Isoform 3 (identifier: Q86Z02-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-374: Missing.

    Show »
    Length:836
    Mass (Da):89,481
    Checksum:iED30D5EDCA8D4918
    GO
    Isoform 4 (identifier: Q86Z02-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:816
    Mass (Da):87,302
    Checksum:i97A2176C8995F038
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti721 – 7211P → Q in AAH33012. (PubMed:15489334)Curated
    Sequence conflicti747 – 7471Missing in BAA31605. (PubMed:9734811)Curated
    Sequence conflicti799 – 7991H → Y in CAD38689. (PubMed:17974005)Curated
    Sequence conflicti1054 – 10541A → V in AAH36057. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti6 – 61Q → R.
    Corresponds to variant rs35324789 [ dbSNP | Ensembl ].
    VAR_051626
    Natural varianti310 – 3101G → C.1 Publication
    VAR_040546
    Natural varianti1165 – 11651L → V.1 Publication
    VAR_046047

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 394394Missing in isoform 4. 1 PublicationVSP_013127Add
    BLAST
    Alternative sequencei1 – 374374Missing in isoform 3. 1 PublicationVSP_013128Add
    BLAST
    Alternative sequencei395 – 3995ASEYD → MVLMF in isoform 4. 1 PublicationVSP_013129
    Alternative sequencei1049 – 107527NQQSS…QAFVA → VSAMGYCLLFGPCTVVTFWR TLLLAGC in isoform 2. 1 PublicationVSP_013130Add
    BLAST
    Alternative sequencei1076 – 1210135Missing in isoform 2. 1 PublicationVSP_013131Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS41370.1. [Q86Z02-3]
    CCDS867.1. [Q86Z02-1]
    CCDS868.1. [Q86Z02-2]
    CCDS869.1. [Q86Z02-4]
    RefSeqiNP_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]
    UniGeneiHs.532363.

    Genome annotation databases

    EnsembliENST00000340480; ENSP00000340956; ENSG00000163349. [Q86Z02-3]
    ENST00000369553; ENSP00000358566; ENSG00000163349. [Q86Z02-4]
    ENST00000369558; ENSP00000358571; ENSG00000163349. [Q86Z02-1]
    ENST00000369559; ENSP00000358572; ENSG00000163349. [Q86Z02-2]
    ENST00000426820; ENSP00000407442; ENSG00000163349. [Q86Z02-1]
    GeneIDi204851.
    KEGGihsa:204851.
    UCSCiuc001eel.3. human. [Q86Z02-2]
    uc001eem.3. human. [Q86Z02-1]
    uc001eep.3. human. [Q86Z02-4]

    Polymorphism databases

    DMDMi34395641.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS41370.1. [Q86Z02-3 ]
    CCDS867.1. [Q86Z02-1 ]
    CCDS868.1. [Q86Z02-2 ]
    CCDS869.1. [Q86Z02-4 ]
    RefSeqi NP_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 ]
    UniGenei Hs.532363.

    3D structure databases

    ProteinModelPortali Q86Z02.
    SMRi Q86Z02. Positions 188-517.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 128490. 16 interactions.
    IntActi Q86Z02. 15 interactions.
    MINTi MINT-1187651.

    Chemistry

    BindingDBi Q86Z02.
    ChEMBLi CHEMBL5427.
    GuidetoPHARMACOLOGYi 2033.

    PTM databases

    PhosphoSitei Q86Z02.

    Polymorphism databases

    DMDMi 34395641.

    Proteomic databases

    PaxDbi Q86Z02.
    PRIDEi Q86Z02.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000340480 ; ENSP00000340956 ; ENSG00000163349 . [Q86Z02-3 ]
    ENST00000369553 ; ENSP00000358566 ; ENSG00000163349 . [Q86Z02-4 ]
    ENST00000369558 ; ENSP00000358571 ; ENSG00000163349 . [Q86Z02-1 ]
    ENST00000369559 ; ENSP00000358572 ; ENSG00000163349 . [Q86Z02-2 ]
    ENST00000426820 ; ENSP00000407442 ; ENSG00000163349 . [Q86Z02-1 ]
    GeneIDi 204851.
    KEGGi hsa:204851.
    UCSCi uc001eel.3. human. [Q86Z02-2 ]
    uc001eem.3. human. [Q86Z02-1 ]
    uc001eep.3. human. [Q86Z02-4 ]

    Organism-specific databases

    CTDi 204851.
    GeneCardsi GC01P114471.
    HGNCi HGNC:19006. HIPK1.
    HPAi HPA016664.
    MIMi 608003. gene.
    neXtProti NX_Q86Z02.
    PharmGKBi PA134897980.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG051908.
    InParanoidi Q86Z02.
    KOi K08826.
    OMAi NKYKPSS.
    PhylomeDBi Q86Z02.
    TreeFami TF105417.

    Enzyme and pathway databases

    SignaLinki Q86Z02.

    Miscellaneous databases

    ChiTaRSi HIPK1. human.
    GeneWikii HIPK1.
    GenomeRNAii 204851.
    NextBioi 90482.
    PROi Q86Z02.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q86Z02.
    Bgeei Q86Z02.
    CleanExi HS_HIPK1.
    Genevestigatori Q86Z02.

    Family and domain databases

    InterProi IPR011009. 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 ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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.
      , 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.

    Entry informationi

    Entry nameiHIPK1_HUMAN
    AccessioniPrimary (citable) accession number: Q86Z02
    Secondary accession number(s): A6NJ34
    , O75125, Q5SQL2, Q5SQL4, Q5SQL5, Q8IYD7, Q8NDN5, Q8NEB6, Q8TBZ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 29, 2003
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3