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Q9H2X6

- HIPK2_HUMAN

UniProt

Q9H2X6 - HIPK2_HUMAN

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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

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 kinase activity Source: UniProtKB
  3. protein serine/threonine kinase activity Source: BHF-UCL
  4. RNA polymerase II activating transcription factor binding Source: BHF-UCL
  5. RNA polymerase II transcription coactivator activity Source: Ensembl
  6. SMAD binding Source: UniProtKB
  7. transcription corepressor activity Source: UniProtKB
  8. 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 protein phosphorylation Source: Ensembl
  27. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  28. positive regulation of transcription, DNA-templated Source: BHF-UCL
  29. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  30. positive regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
  31. protein phosphorylation Source: UniProtKB
  32. regulation of cell cycle Source: UniProtKB
  33. retina layer formation Source: Ensembl
  34. SMAD protein signal transduction Source: UniProtKB
  35. smoothened signaling pathway Source: Ensembl
  36. transforming growth factor beta receptor signaling pathway Source: Ensembl
  37. voluntary musculoskeletal movement Source: Ensembl
Complete GO annotation...

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.
ReactomeiREACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
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
Complete GO annotation...

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. 9 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. 9 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. 1 Publication
Mutagenesisi805 – 8051K → A: Impaired nuclear localization; when associated with A-803. 1 Publication
Mutagenesisi833 – 8331R → A: Impaired nuclear localization. 1 Publication
Mutagenesisi835 – 8351K → E: Impaired nuclear localization. 1 Publication
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

BgeeiQ9H2X6.
CleanExiHS_HIPK2.
ExpressionAtlasiQ9H2X6. baseline and differential.
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.
GeneTreeiENSGT00760000119032.
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.
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

        10         20         30         40         50
MAPVYEGMAS HVQVFSPHTL QSSAFCSVKK LKIEPSSNWD MTGYGSHSKV
60 70 80 90 100
YSQSKNIPLS QPATTTVSTS LPVPNPSLPY EQTIVFPGST GHIVVTSASS
110 120 130 140 150
TSVTGQVLGG PHNLMRRSTV SLLDTYQKCG LKRKSEEIEN TSSVQIIEEH
160 170 180 190 200
PPMIQNNASG ATVATATTST ATSKNSGSNS EGDYQLVQHE VLCSMTNTYE
210 220 230 240 250
VLEFLGRGTF GQVVKCWKRG TNEIVAIKIL KNHPSYARQG QIEVSILARL
260 270 280 290 300
STESADDYNF VRAYECFQHK NHTCLVFEML EQNLYDFLKQ NKFSPLPLKY
310 320 330 340 350
IRPVLQQVAT ALMKLKSLGL IHADLKPENI MLVDPSRQPY RVKVIDFGSA
360 370 380 390 400
SHVSKAVCST YLQSRYYRAP EIILGLPFCE AIDMWSLGCV IAELFLGWPL
410 420 430 440 450
YPGASEYDQI RYISQTQGLP AEYLLSAGTK TTRFFNRDTD SPYPLWRLKT
460 470 480 490 500
PDDHEAETGI KSKEARKYIF NCLDDMAQVN MTTDLEGSDM LVEKADRREF
510 520 530 540 550
IDLLKKMLTI DADKRITPIE TLNHPFVTMT HLLDFPHSTH VKSCFQNMEI
560 570 580 590 600
CKRRVNMYDT VNQSKTPFIT HVAPSTSTNL TMTFNNQLTT VHNQAPSSTS
610 620 630 640 650
ATISLANPEV SILNYPSTLY QPSAASMAAV AQRSMPLQTG TAQICARPDP
660 670 680 690 700
FQQALIVCPP GFQGLQASPS KHAGYSVRME NAVPIVTQAP GAQPLQIQPG
710 720 730 740 750
LLAQQAWPSG TQQILLPPAW QQLTGVATHT SVQHATVIPE TMAGTQQLAD
760 770 780 790 800
WRNTHAHGSH YNPIMQQPAL LTGHVTLPAA QPLNVGVAHV MRQQPTSTTS
810 820 830 840 850
SRKSKQHQSS VRNVSTCEVS SSQAISSPQR SKRVKENTPP RCAMVHSSPA
860 870 880 890 900
CSTSVTCGWG DVASSTTRER QRQTIVIPDT PSPTVSVITI SSDTDEEEEQ
910 920 930 940 950
KHAPTSTVSK QRKNVISCVT VHDSPYSDSS SNTSPYSVQQ RAGHNNANAF
960 970 980 990 1000
DTKGSLENHC TGNPRTIIVP PLKTQASEVL VECDSLVPVN TSHHSSSYKS
1010 1020 1030 1040 1050
KSSSNVTSTS GHSSGSSSGA ITYRQQRPGP HFQQQQPLNL SQAQQHITTD
1060 1070 1080 1090 1100
RTGSHRRQQA YITPTMAQAP YSFPHNSPSH GTVHPHLAAA AAAAHLPTQP
1110 1120 1130 1140 1150
HLYTYTAPAA LGSTGTVAHL VASQGSARHT VQHTAYPASI VHQVPVSMGP
1160 1170 1180 1190
RVLPSPTIHP SQYPAQFAHQ TYISASPAST VYTGYPLSPA KVNQYPYI
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:
EMBLi
GenBanki
DDBJi
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.
CCDSiCCDS75666.1. [Q9H2X6-3]
CCDS75667.1. [Q9H2X6-1]
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:
EMBLi
GenBanki
DDBJi
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 .
CCDSi CCDS75666.1. [Q9H2X6-3 ]
CCDS75667.1. [Q9H2X6-1 ]
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.
GeneTreei ENSGT00760000119032.
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.
Reactomei REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
SignaLinki Q9H2X6.

Miscellaneous databases

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

Gene expression databases

Bgeei Q9H2X6.
CleanExi HS_HIPK2.
ExpressionAtlasi Q9H2X6. baseline and differential.
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.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 149 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

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