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Q9H2X6

- HIPK2_HUMAN

UniProt

Q9H2X6 - HIPK2_HUMAN

Protein

Homeodomain-interacting protein kinase 2

Gene

HIPK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (06 Jun 2002)
      Previous versions | rss
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    Functioni

    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 and ZBTB4. 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. 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.18 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei228 – 2281ATPCurated
    Active sitei324 – 3241Proton acceptorCurated
    Sitei923 – 9242Cleavage; by CASP6
    Sitei984 – 9852Cleavage; by CASP6

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi205 – 2139ATPCurated

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein kinase activity Source: UniProtKB
    4. protein serine/threonine kinase activity Source: BHF-UCL
    5. RNA polymerase II activating transcription factor binding Source: BHF-UCL
    6. RNA polymerase II transcription coactivator activity Source: Ensembl
    7. SMAD binding Source: UniProtKB
    8. transcription corepressor activity Source: UniProtKB
    9. virion binding Source: UniProtKB

    GO - Biological processi

    1. adult walking behavior Source: Ensembl
    2. anterior/posterior pattern specification Source: Ensembl
    3. cellular response to hypoxia Source: UniProtKB
    4. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: BHF-UCL
    5. embryonic camera-type eye morphogenesis Source: Ensembl
    6. embryonic retina morphogenesis in camera-type eye Source: Ensembl
    7. erythrocyte differentiation Source: UniProtKB
    8. eye development Source: UniProtKB
    9. intrinsic apoptotic signaling pathway Source: UniProtKB
    10. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
    11. iris morphogenesis Source: Ensembl
    12. lens induction in camera-type eye Source: Ensembl
    13. modulation by virus of host morphology or physiology Source: UniProtKB
    14. negative regulation of BMP signaling pathway Source: UniProtKB
    15. negative regulation of neuron apoptotic process Source: Ensembl
    16. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    17. neuron differentiation Source: Ensembl
    18. peptidyl-serine phosphorylation Source: BHF-UCL
    19. peptidyl-threonine phosphorylation Source: BHF-UCL
    20. PML body organization Source: UniProtKB
    21. positive regulation of angiogenesis Source: UniProtKB
    22. positive regulation of cell proliferation Source: Ensembl
    23. positive regulation of DNA binding Source: Ensembl
    24. positive regulation of JNK cascade Source: UniProtKB
    25. positive regulation of protein binding Source: BHF-UCL
    26. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    27. positive regulation of transcription, DNA-templated Source: BHF-UCL
    28. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    29. positive regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
    30. protein phosphorylation Source: UniProtKB
    31. regulation of cell cycle Source: UniProtKB
    32. retina layer formation Source: Ensembl
    33. SMAD protein signal transduction Source: UniProtKB
    34. smoothened signaling pathway Source: Ensembl
    35. transforming growth factor beta receptor signaling pathway Source: Ensembl
    36. voluntary musculoskeletal movement Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, DNA damage, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    SignaLinkiQ9H2X6.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Homeodomain-interacting protein kinase 2 (EC:2.7.11.1)
    Short name:
    hHIPk2
    Gene namesi
    Name:HIPK2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:14402. HIPK2.

    Subcellular locationi

    NucleusPML body. Cytoplasm
    Note: Concentrated in PML/POD/ND10 nuclear bodies. Small amounts are cytoplasmic.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nuclear body Source: UniProtKB
    3. nucleus Source: UniProtKB
    4. PML body Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi228 – 2281K → A: Locates in the nucleoplasm, no effect on interaction with RANBP9, but loss of kinase activity toward PML, RUNX1 and EP300. 10 Publications
    Mutagenesisi228 – 2281K → R: Abolishes enzymatic activity, no effect on interaction with TP53 and TP73 or on BMP-induced transcriptional activation. Enhances BMP-induced transcriptional activation; when associated with 359-AAF-361. 10 Publications
    Mutagenesisi359 – 3613STY → AAF: Enhances BMP-induced transcriptional activation; when associated with R-228. 1 Publication
    Mutagenesisi803 – 8031K → A: Impaired nuclear localization; when associated with A-805. 2 Publications
    Mutagenesisi805 – 8051K → A: Impaired nuclear localization; when associated with A-803. 2 Publications
    Mutagenesisi833 – 8331R → A: Impaired nuclear localization. 2 Publications
    Mutagenesisi835 – 8351K → E: Impaired nuclear localization. 2 Publications
    Mutagenesisi885 – 8928VSVITISS → KFMHFHRM: Loss of SUMO and CBX4 interaction, and impaired nuclear and PML-nuclear bodies localization. 1 Publication
    Mutagenesisi885 – 8884VSVI → KSAK: Loss of SUMO interaction, and impaired nuclear and PML-nuclear bodies localization. 1 Publication
    Mutagenesisi892 – 8954SDTD → ADTA: Loss of SUMO interaction, and impaired nuclear and PML-nuclear bodies localization. 1 Publication
    Mutagenesisi893 – 8997DTDEEEE → NFNQQQQ: Loss of SUMO and CBX4 interaction, and impaired nuclear and PML-nuclear bodies localization. 1 Publication

    Organism-specific databases

    PharmGKBiPA29291.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11981198Homeodomain-interacting protein kinase 2PRO_0000085995Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei16 – 161PhosphoserineBy similarity
    Cross-linki32 – 32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei118 – 1181PhosphoserineBy similarity
    Modified residuei135 – 1351PhosphoserineBy similarity
    Modified residuei141 – 1411PhosphothreonineBy similarity
    Modified residuei252 – 2521PhosphothreonineBy similarity
    Modified residuei273 – 2731PhosphothreonineBy similarity
    Modified residuei361 – 3611PhosphotyrosineBy similarity
    Modified residuei361 – 3611Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei441 – 4411PhosphoserineBy similarity
    Modified residuei482 – 4821PhosphothreonineBy similarity
    Modified residuei517 – 5171PhosphothreonineBy similarity
    Modified residuei566 – 5661PhosphothreonineBy similarity
    Modified residuei634 – 6341PhosphoserineBy similarity
    Modified residuei668 – 6681PhosphoserineBy similarity
    Modified residuei687 – 6871PhosphothreonineBy similarity
    Modified residuei815 – 8151PhosphoserineBy similarity
    Modified residuei827 – 8271PhosphoserineBy similarity
    Modified residuei934 – 9341PhosphoserineBy similarity
    Modified residuei992 – 9921PhosphoserineBy similarity
    Modified residuei1041 – 10411PhosphoserineBy similarity
    Modified residuei1155 – 11551PhosphoserineBy similarity
    Modified residuei1188 – 11881PhosphoserineBy similarity
    Cross-linki1191 – 1191Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

    Post-translational modificationi

    Autophosphorylation at Tyr-361 in the activation loop activates the kinase and promotes nuclear localization.By similarity
    Sumoylated. When conjugated it is directed to nuclear speckles. Desumoylated by SENP1 By similarity. Sumoylation on Lys-32 is promoted by the E3 SUMO-protein ligase CBX4.By similarity4 Publications
    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.3 Publications
    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.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9H2X6.
    PaxDbiQ9H2X6.
    PRIDEiQ9H2X6.

    PTM databases

    PhosphoSiteiQ9H2X6.

    Miscellaneous databases

    PMAP-CutDBQ9H2X6.

    Expressioni

    Tissue specificityi

    Highly expressed in heart, muscle and kidney. Weakly expressed in a ubiquitous way. Down-regulated in several thyroid and breast tumors.2 Publications

    Inductioni

    Unstable in unstressed cells but stabilized upon DNA damage. Induced by UV irradiation and other genotoxic agents (adriamycin ADR, cisplatin CDDP, etoposide, IR, roscovitin), thus triggering p53/TP53 apoptotic response. Consistutively negatively regulated by SIAH1 and WSB1 through proteasomal degradation. This negative regulation is impaired upon genotoxic stress. Repressed upon hypoxia (often associated with tumors), through MDM2- (an E3 ubiquitin ligases) mediated proteasomal degradation, thus inactivating p53/TP53 apoptotic response. This hypoxia repression is reversed by zinc. The stabilization mediated by DNA damage requires the damage checkpoint kinases ATM and ATR.5 Publications

    Gene expression databases

    ArrayExpressiQ9H2X6.
    BgeeiQ9H2X6.
    CleanExiHS_HIPK2.
    GenevestigatoriQ9H2X6.

    Organism-specific databases

    HPAiHPA007611.

    Interactioni

    Subunit structurei

    Interacts with CREB1, SIAH1, WSB1, CBX4, TRADD, p53/TP53, TP73, TP63, CREBBP, DAXX, P53DINP1, SKI, SMAD1, SMAD2 and SMAD3, but not SMAD4. Interacts with ATF1, PML, RUNX1, EP300, NKX1-2, NKX2-5, SPN/CD43, UBE2I, HMGA1, CTBP1, AXIN1, NLK, MYB, POU4F1, POU4F2, POU4F3, UBE2I, UBL1 and ZBTB4. Probably part of a complex consisting of p53/TP53, HIPK2 and AXIN1. Interacts with SP100; positively regulates TP53-dependent transcription.16 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DCAF7P6196210EBI-348345,EBI-359808
    EP300Q094724EBI-348345,EBI-447295
    MECP2P516082EBI-348345,EBI-1189067
    RUNX1Q011964EBI-348345,EBI-925904

    Protein-protein interaction databases

    BioGridi118815. 55 interactions.
    DIPiDIP-31716N.
    IntActiQ9H2X6. 16 interactions.
    MINTiMINT-234689.
    STRINGi9606.ENSP00000263551.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H2X6.
    SMRiQ9H2X6. Positions 125-554.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini199 – 527329Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni97 – 230134Transcriptional corepressionBy similarityAdd
    BLAST
    Regioni189 – 520332Interaction with DAXXAdd
    BLAST
    Regioni539 – 844306Interaction with SKI and SMAD1Add
    BLAST
    Regioni752 – 897146Interaction with POU4F1By similarityAdd
    BLAST
    Regioni774 – 876103Interaction with CTBP1By similarityAdd
    BLAST
    Regioni787 – 897111Interaction with HMGA1By similarityAdd
    BLAST
    Regioni802 – 8054Nuclear localization signal 1 (NLS1)
    Regioni832 – 8354Nuclear localization signal 2 (NLS2)
    Regioni846 – 94196Interaction with TP53 and TP73Add
    BLAST
    Regioni873 – 980108Required for localization to nuclear specklesBy similarityAdd
    BLAST
    Regioni873 – 90735Interaction with UBE2IBy similarityAdd
    BLAST
    Regioni884 – 90825SUMO interaction motifs (SIM); required for nuclear localization and kinase activityAdd
    BLAST
    Regioni935 – 1049115Interaction with AXIN1By similarityAdd
    BLAST
    Regioni984 – 1198215Autoinhibitory domain (AID)Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1088 – 10947Poly-Ala

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000231785.
    HOVERGENiHBG051908.
    InParanoidiQ9H2X6.
    KOiK08826.
    OMAiYSFPHNS.
    OrthoDBiEOG7034GK.
    PhylomeDBiQ9H2X6.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Experimental confirmation may be lacking for some isoforms.

    Isoform 1 (identifier: Q9H2X6-1) [UniParc]FASTAAdd to Basket

    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

    MAPVYEGMAS HVQVFSPHTL QSSAFCSVKK LKIEPSSNWD MTGYGSHSKV     50
    YSQSKNIPLS QPATTTVSTS LPVPNPSLPY EQTIVFPGST GHIVVTSASS 100
    TSVTGQVLGG PHNLMRRSTV SLLDTYQKCG LKRKSEEIEN TSSVQIIEEH 150
    PPMIQNNASG ATVATATTST ATSKNSGSNS EGDYQLVQHE VLCSMTNTYE 200
    VLEFLGRGTF GQVVKCWKRG TNEIVAIKIL KNHPSYARQG QIEVSILARL 250
    STESADDYNF VRAYECFQHK NHTCLVFEML EQNLYDFLKQ NKFSPLPLKY 300
    IRPVLQQVAT ALMKLKSLGL IHADLKPENI MLVDPSRQPY RVKVIDFGSA 350
    SHVSKAVCST YLQSRYYRAP EIILGLPFCE AIDMWSLGCV IAELFLGWPL 400
    YPGASEYDQI RYISQTQGLP AEYLLSAGTK TTRFFNRDTD SPYPLWRLKT 450
    PDDHEAETGI KSKEARKYIF NCLDDMAQVN MTTDLEGSDM LVEKADRREF 500
    IDLLKKMLTI DADKRITPIE TLNHPFVTMT HLLDFPHSTH VKSCFQNMEI 550
    CKRRVNMYDT VNQSKTPFIT HVAPSTSTNL TMTFNNQLTT VHNQAPSSTS 600
    ATISLANPEV SILNYPSTLY QPSAASMAAV AQRSMPLQTG TAQICARPDP 650
    FQQALIVCPP GFQGLQASPS KHAGYSVRME NAVPIVTQAP GAQPLQIQPG 700
    LLAQQAWPSG TQQILLPPAW QQLTGVATHT SVQHATVIPE TMAGTQQLAD 750
    WRNTHAHGSH YNPIMQQPAL LTGHVTLPAA QPLNVGVAHV MRQQPTSTTS 800
    SRKSKQHQSS VRNVSTCEVS SSQAISSPQR SKRVKENTPP RCAMVHSSPA 850
    CSTSVTCGWG DVASSTTRER QRQTIVIPDT PSPTVSVITI SSDTDEEEEQ 900
    KHAPTSTVSK QRKNVISCVT VHDSPYSDSS SNTSPYSVQQ RAGHNNANAF 950
    DTKGSLENHC TGNPRTIIVP PLKTQASEVL VECDSLVPVN TSHHSSSYKS 1000
    KSSSNVTSTS GHSSGSSSGA ITYRQQRPGP HFQQQQPLNL SQAQQHITTD 1050
    RTGSHRRQQA YITPTMAQAP YSFPHNSPSH GTVHPHLAAA AAAAHLPTQP 1100
    HLYTYTAPAA LGSTGTVAHL VASQGSARHT VQHTAYPASI VHQVPVSMGP 1150
    RVLPSPTIHP SQYPAQFAHQ TYISASPAST VYTGYPLSPA KVNQYPYI 1198
    Length:1,198
    Mass (Da):130,966
    Last modified:June 6, 2002 - v2
    Checksum:i6022D5710E8D2D93
    GO
    Isoform 2 (identifier: Q9H2X6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         808-907: Missing.
         989-1018: VNTSHHSSSYKSKSSSNVTSTSGHSSGSSS → GNLGPGQGRNLSLESGFPAFLLLEMLLYGS
         1019-1198: Missing.

    Show »
    Length:918
    Mass (Da):101,013
    Checksum:iBA34005E15CFC5CD
    GO
    Isoform 3 (identifier: Q9H2X6-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         595-621: Missing.

    Show »
    Length:1,171
    Mass (Da):128,158
    Checksum:iC38A3241948C7D66
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti33 – 331I → V in AAG41236. (PubMed:11267674)Curated
    Sequence conflicti59 – 591L → P in AAG41236. (PubMed:11267674)Curated
    Sequence conflicti64 – 641T → S in AAG41236. (PubMed:11267674)Curated
    Sequence conflicti169 – 1691S → F in AAG35710. 1 PublicationCurated
    Sequence conflicti187 – 1871V → S in AAG35710. 1 PublicationCurated
    Sequence conflicti202 – 2021L → S in AAG35710. 1 PublicationCurated
    Sequence conflicti233 – 2331H → R in AAG41236. (PubMed:11267674)Curated
    Sequence conflicti471 – 4711N → I in AAL37371. 1 PublicationCurated
    Sequence conflicti669 – 6691P → S in AAG35710. 1 PublicationCurated
    Sequence conflicti711 – 7111T → N in AAG35710. 1 PublicationCurated
    Sequence conflicti717 – 7193PPA → SPT in AAG35710. 1 PublicationCurated
    Sequence conflicti724 – 7241T → D in AAG35710. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti792 – 7921R → Q.1 Publication
    VAR_040547
    Natural varianti1027 – 10271R → Q.1 Publication
    VAR_040548

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei595 – 62127Missing in isoform 3. 1 PublicationVSP_004804Add
    BLAST
    Alternative sequencei808 – 907100Missing in isoform 2. 1 PublicationVSP_004805Add
    BLAST
    Alternative sequencei989 – 101830VNTSH…SGSSS → GNLGPGQGRNLSLESGFPAF LLLEMLLYGS in isoform 2. 1 PublicationVSP_004806Add
    BLAST
    Alternative sequencei1019 – 1198180Missing in isoform 2. 1 PublicationVSP_004807Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF208291 mRNA. Translation: AAG41236.1.
    AF326592 mRNA. Translation: AAL37371.1.
    AC005531 Genomic DNA. Translation: AAS00368.1.
    AC073184 Genomic DNA. No translation available.
    AC006021 Genomic DNA. No translation available.
    AC141932 Genomic DNA. No translation available.
    AF207702 mRNA. Translation: AAG35710.1.
    RefSeqiNP_001106710.1. NM_001113239.2. [Q9H2X6-3]
    NP_073577.3. NM_022740.4. [Q9H2X6-1]
    UniGeneiHs.731417.

    Genome annotation databases

    EnsembliENST00000406875; ENSP00000385571; ENSG00000064393. [Q9H2X6-1]
    ENST00000428878; ENSP00000413724; ENSG00000064393. [Q9H2X6-3]
    GeneIDi28996.
    KEGGihsa:28996.
    UCSCiuc003vvd.4. human. [Q9H2X6-3]
    uc003vvf.4. human. [Q9H2X6-1]

    Polymorphism databases

    DMDMi21431782.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF208291 mRNA. Translation: AAG41236.1 .
    AF326592 mRNA. Translation: AAL37371.1 .
    AC005531 Genomic DNA. Translation: AAS00368.1 .
    AC073184 Genomic DNA. No translation available.
    AC006021 Genomic DNA. No translation available.
    AC141932 Genomic DNA. No translation available.
    AF207702 mRNA. Translation: AAG35710.1 .
    RefSeqi NP_001106710.1. NM_001113239.2. [Q9H2X6-3 ]
    NP_073577.3. NM_022740.4. [Q9H2X6-1 ]
    UniGenei Hs.731417.

    3D structure databases

    ProteinModelPortali Q9H2X6.
    SMRi Q9H2X6. Positions 125-554.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118815. 55 interactions.
    DIPi DIP-31716N.
    IntActi Q9H2X6. 16 interactions.
    MINTi MINT-234689.
    STRINGi 9606.ENSP00000263551.

    Chemistry

    BindingDBi Q9H2X6.
    ChEMBLi CHEMBL4576.
    GuidetoPHARMACOLOGYi 2034.

    PTM databases

    PhosphoSitei Q9H2X6.

    Polymorphism databases

    DMDMi 21431782.

    Proteomic databases

    MaxQBi Q9H2X6.
    PaxDbi Q9H2X6.
    PRIDEi Q9H2X6.

    Protocols and materials databases

    DNASUi 28996.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000406875 ; ENSP00000385571 ; ENSG00000064393 . [Q9H2X6-1 ]
    ENST00000428878 ; ENSP00000413724 ; ENSG00000064393 . [Q9H2X6-3 ]
    GeneIDi 28996.
    KEGGi hsa:28996.
    UCSCi uc003vvd.4. human. [Q9H2X6-3 ]
    uc003vvf.4. human. [Q9H2X6-1 ]

    Organism-specific databases

    CTDi 28996.
    GeneCardsi GC07M139246.
    HGNCi HGNC:14402. HIPK2.
    HPAi HPA007611.
    MIMi 606868. gene.
    neXtProti NX_Q9H2X6.
    PharmGKBi PA29291.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000231785.
    HOVERGENi HBG051908.
    InParanoidi Q9H2X6.
    KOi K08826.
    OMAi YSFPHNS.
    OrthoDBi EOG7034GK.
    PhylomeDBi Q9H2X6.
    TreeFami TF105417.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    SignaLinki Q9H2X6.

    Miscellaneous databases

    ChiTaRSi HIPK2. human.
    GeneWikii HIPK2.
    GenomeRNAii 28996.
    NextBioi 51926.
    PMAP-CutDB Q9H2X6.
    PROi Q9H2X6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H2X6.
    Bgeei Q9H2X6.
    CleanExi HS_HIPK2.
    Genevestigatori Q9H2X6.

    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. "Isolation and characterization of cDNAs for the protein kinase HIPK2."
      Wang Y., Hofmann T.G., Runkel L., Haaf T., Schaller H., Debatin K.-M., Hug H.
      Biochim. Biophys. Acta 1518:168-172(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-228.
      Tissue: Liver and Testis.
    2. "Sequencing of hHIPk2, a human homolog of mouse homeodomain interacting protein kinase 2."
      Stukart G.C., Dias-Neto E.
      Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Frontal cortex.
    3. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Pierantoni G.M., Benvenuto G., Chiariotti L., Fusco A.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-1198 (ISOFORM 2).
    5. "The serine/threonine kinase HIPK2 interacts with TRADD, but not with CD95 or TNF-R1 in 293T cells."
      Li X., Wang Y., Debatin K.-M., Hug H.
      Biochem. Biophys. Res. Commun. 277:513-517(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRADD.
    6. "The homeodomain-interacting protein kinase 2 gene is expressed late in embryogenesis and preferentially in retina, muscle, and neural tissues."
      Pierantoni G.M., Bulfone A., Pentimalli F., Fedele M., Iuliano R., Santoro M., Chiariotti L., Ballabio A., Fusco A.
      Biochem. Biophys. Res. Commun. 290:942-947(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. Cited for: INTERACTION WITH RANBP9, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-228.
    8. "Identification and characterization of HIPK2 interacting with p73 and modulating functions of the p53 family in vivo."
      Kim E.-J., Park J.-S., Um S.-J.
      J. Biol. Chem. 277:32020-32028(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TP73; TP53 AND TP63, MUTAGENESIS OF LYS-228, FUNCTION.
    9. "Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2."
      Hofmann T.G., Moeller A., Sirma H., Zentgraf H., Taya Y., Droege W., Will H., Schmitz M.L.
      Nat. Cell Biol. 4:1-10(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, INTERACTION WITH TP53 AND CREBBP, MUTAGENESIS OF LYS-228, FUNCTION, INDUCTION.
    10. "PML is required for homeodomain-interacting protein kinase 2 (HIPK2)-mediated p53 phosphorylation and cell cycle arrest but is dispensable for the formation of HIPK domains."
      Moeller A., Sirma H., Hofmann T.G., Rueffer S., Klimczak E., Droege W., Will H., Schmitz M.L.
      Cancer Res. 63:4310-4314(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-228.
    11. "HIPK2 regulates transforming growth factor-beta-induced c-Jun NH(2)-terminal kinase activation and apoptosis in human hepatoma cells."
      Hofmann T.G., Stollberg N., Schmitz M.L., Will H.
      Cancer Res. 63:8271-8277(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DAXX, MUTAGENESIS OF LYS-228.
    12. "TP53INP1s and homeodomain-interacting protein kinase-2 (HIPK2) are partners in regulating p53 activity."
      Tomasini R., Samir A.A., Carrier A., Isnardon D., Cecchinelli B., Soddu S., Malissen B., Dagorn J.-C., Iovanna J.L., Dusetti N.J.
      J. Biol. Chem. 278:37722-37729(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH P53DINP1.
    13. "Requirement of the co-repressor homeodomain-interacting protein kinase 2 for ski-mediated inhibition of bone morphogenetic protein-induced transcriptional activation."
      Harada J., Kokura K., Kanei-Ishii C., Nomura T., Khan M.M., Kim Y., Ishii S.
      J. Biol. Chem. 278:38998-39005(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SKI; SMAD1; SMAD2 AND SMAD3, MUTAGENESIS OF LYS-228 AND 359-SER--TYR-361.
    14. "Sp100 is important for the stimulatory effect of homeodomain-interacting protein kinase-2 on p53-dependent gene expression."
      Moeller A., Sirma H., Hofmann T.G., Staege H., Gresko E., Luedi K.S., Klimczak E., Droege W., Will H., Schmitz M.L.
      Oncogene 22:8731-8737(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SP100.
    15. "Desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) through the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1."
      Kim Y.H., Sung K.S., Lee S.-J., Kim Y.-O., Choi C.Y., Kim Y.
      FEBS Lett. 579:6272-6278(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: DESUMOYLATION.
    16. "Autoregulatory control of the p53 response by caspase-mediated processing of HIPK2."
      Gresko E., Roscic A., Ritterhoff S., Vichalkovski A., del Sal G., Schmitz M.L.
      EMBO J. 25:1883-1894(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE BY CASP6 AT ASP-923 AND ASP-984.
    17. "Phosphorylation-dependent control of Pc2 SUMO E3 ligase activity by its substrate protein HIPK2."
      Roscic A., Moeller A., Calzado M.A., Renner F., Wimmer V.C., Gresko E., Luedi K.S., Schmitz M.L.
      Mol. Cell 24:77-89(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBX4, SUMOYLATION AT LYS-32, FUNCTION.
    18. "Homeodomain-interacting protein kinase-2 (HIPK2) phosphorylates HMGA1a at Ser-35, Thr-52, and Thr-77 and modulates its DNA binding affinity."
      Zhang Q., Wang Y.
      J. Proteome Res. 6:4711-4719(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS HMGA1 KINASE.
    19. "PEBP2-beta/CBF-beta-dependent phosphorylation of RUNX1 and p300 by HIPK2: implications for leukemogenesis."
      Wee H.-J., Voon D.C.-C., Bae S.-C., Ito Y.
      Blood 112:3777-3787(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS RUNX1 AND EP300 KINASE, MUTAGENESIS OF LYS-228.
    20. "Ubiquitination and degradation of homeodomain-interacting protein kinase 2 by WD40 repeat/SOCS box protein WSB-1."
      Choi D.W., Seo Y.-M., Kim E.-A., Sung K.S., Ahn J.W., Park S.-J., Lee S.-R., Choi C.Y.
      J. Biol. Chem. 283:4682-4689(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WSB1, UBIQUITINATION BY WSB1.
    21. "PML activates transcription by protecting HIPK2 and p300 from SCFFbx3-mediated degradation."
      Shima Y., Shima T., Chiba T., Irimura T., Pandolfi P.P., Kitabayashi I.
      Mol. Cell. Biol. 28:7126-7138(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, UBIQUITINATION BY FBXO3.
    22. "Control of HIPK2 stability by ubiquitin ligase Siah-1 and checkpoint kinases ATM and ATR."
      Winter M., Sombroek D., Dauth I., Moehlenbrink J., Scheuermann K., Crone J., Hofmann T.G.
      Nat. Cell Biol. 10:812-824(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY DNA DAMAGE, INTERACTION WITH SIAH1, UBIQUITINATION BY SIAH1.
    23. "Transcriptional regulation of hypoxia-inducible factor 1alpha by HIPK2 suggests a novel mechanism to restrain tumor growth."
      Nardinocchi L., Puca R., Guidolin D., Belloni A.S., Bossi G., Michiels C., Sacchi A., Onisto M., D'Orazi G.
      Biochim. Biophys. Acta 1793:368-377(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS HIF1A TRANSCRIPTION REGULATOR AND ANGIOGENESIS PROMOTER.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "PML tumor suppressor is regulated by HIPK2-mediated phosphorylation in response to DNA damage."
      Gresko E., Ritterhoff S., Sevilla-Perez J., Roscic A., Froebius K., Kotevic I., Vichalkovski A., Hess D., Hemmings B.A., Schmitz M.L.
      Oncogene 28:698-708(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS PML KINASE, INTERACTION WITH PML, MUTAGENESIS OF LYS-228.
    26. "The human protein kinase HIPK2 phosphorylates and downregulates the methyl-binding transcription factor ZBTB4."
      Yamada D., Perez-Torrado R., Filion G., Caly M., Jammart B., Devignot V., Sasai N., Ravassard P., Mallet J., Sastre-Garau X., Schmitz M.L., Defossez P.A.
      Oncogene 28:2535-2544(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS ZBTB4 KINASE, INTERACTION WITH ZBTB4.
    27. "Targeting hypoxia in cancer cells by restoring homeodomain interacting protein-kinase 2 and p53 activity and suppressing HIF-1alpha."
      Nardinocchi L., Puca R., Sacchi A., Rechavi G., Givol D., D'Orazi G.
      PLoS ONE 4:E6819-E6819(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY ZINC DURING HYPOXIA.
    28. "Pancreatic and duodenal homeobox 1 (PDX1) phosphorylation at serine-269 is HIPK2-dependent and affects PDX1 subnuclear localization."
      An R., da Silva Xavier G., Semplici F., Vakhshouri S., Hao H.X., Rutter J., Pagano M.A., Meggio F., Pinna L.A., Rutter G.A.
      Biochem. Biophys. Res. Commun. 399:155-161(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS PDX1 KINASE.
    29. "Homeodomain-interacting protein kinase 2 (HIPK2) targets beta-catenin for phosphorylation and proteasomal degradation."
      Kim E.-A., Kim J.E., Sung K.S., Choi D.W., Lee B.J., Choi C.Y.
      Biochem. Biophys. Res. Commun. 394:966-971(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS CTNNB1 KINASE.
    30. "Transcriptional regulation of ferritin and antioxidant genes by HIPK2 under genotoxic stress."
      Hailemariam K., Iwasaki K., Huang B.W., Sakamoto K., Tsuji Y.
      J. Cell Sci. 123:3863-3871(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS ATF1 KINASE, INTERACTION WITH ATF1.
    31. "Regulation of genotoxic stress response by homeodomain-interacting protein kinase 2 through phosphorylation of cyclic AMP response element-binding protein at serine 271."
      Sakamoto K., Huang B.-W., Iwasaki K., Hailemariam K., Ninomiya-Tsuji J., Tsuji Y.
      Mol. Biol. Cell 21:2966-2974(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS CREB1 KINASE, INTERACTION WITH CREB1.
    32. "Control of nuclear HIPK2 localization and function by a SUMO interaction motif."
      de la Vega L., Froebius K., Moreno R., Calzado M.A., Geng H., Schmitz M.L.
      Biochim. Biophys. Acta 1813:283-297(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, SUMOYLATION, NUCLEAR LOCALIZATION SIGNALS, MUTAGENESIS OF LYS-803; LYS-805; ARG-833; LYS-835; 885-VAL--SER-892 AND 893-ASP--GLU-899, INTERACTION WITH CBX4.
    33. "Role of the SUMO-interacting motif in HIPK2 targeting to the PML nuclear bodies and regulation of p53."
      Sung K.S., Lee Y.A., Kim E.T., Lee S.R., Ahn J.H., Choi C.Y.
      Exp. Cell Res. 317:1060-1070(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, SUMOYLATION, FUNCTION, MUTAGENESIS OF 885-VAL--ILE-888 AND 892-SER--ASP-895.
    34. Cited for: REVIEW ON DNA DAMAGE SIGNALING, INDUCTION BY GENOTOXIC AGENTS, STABILIZATION BY DNA DAMAGE.
    35. "Apoptosis and autophagy: Regulation of apoptosis by DNA damage signalling - roles of p53, p73 and HIPK2."
      Bitomsky N., Hofmann T.G.
      FEBS J. 276:6074-6083(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    36. "HIPK2-a therapeutical target to be (re)activated for tumor suppression: role in p53 activation and HIF-1? inhibition."
      Nardinocchi L., Puca R., Givol D., D'Orazi G.
      Cell Cycle 9:1270-1275(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW AS HYPOXIA AND TP53 REGULATOR.
    37. "Regulation of p53 activity by HIPK2: molecular mechanisms and therapeutical implications in human cancer cells."
      Puca R., Nardinocchi L., Givol D., D'Orazi G.
      Oncogene 29:4378-4387(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW AS TP53 REGULATOR, INDUCTION BY GENOTOXIC AGENTS AND HYPOXIA.
    38. "DNA damage-induced heterogeneous nuclear ribonucleoprotein K SUMOylation regulates p53 transcriptional activation."
      Pelisch F., Pozzi B., Risso G., Munoz M.J., Srebrow A.
      J. Biol. Chem. 287:30789-30799(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    39. "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] GLN-792 AND GLN-1027.

    Entry informationi

    Entry nameiHIPK2_HUMAN
    AccessioniPrimary (citable) accession number: Q9H2X6
    Secondary accession number(s): Q75MR7, Q8WWI4, Q9H2Y1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: June 6, 2002
    Last modified: October 1, 2014
    This is version 147 of the entry and version 2 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

    Miscellaneous

    Interesting targets for cancer therapy. HIPK2 deregulation would end up in a multifactorial response leading to tumor chemoresistance by affecting p53/TP53 activity on one hand and to angiogenesis and cell proliferation by affecting HIF1A activity on the other hand. May provide important insights in the process of tumor progression, and may also serve as the crucial point in the diagnostic and therapeutical aspects of cancer. Tumor treatment may potential be improved by zinc supplementation in combination with chemotherapy to address hypoxia (PubMed:20514025).1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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