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Q9QZR5

- HIPK2_MOUSE

UniProt

Q9QZR5 - HIPK2_MOUSE

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Protein

Homeodomain-interacting protein kinase 2

Gene

Hipk2

Organism
Mus musculus (Mouse)
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.10 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 CASP6By similarity
Sitei984 – 9852Cleavage; by CASP6By similarity

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. transcription corepressor activity Source: UniProtKB
  6. virion binding Source: UniProtKB

GO - Biological processi

  1. adult locomotory behavior Source: MGI
  2. adult walking behavior Source: MGI
  3. anterior/posterior pattern specification Source: MGI
  4. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: Ensembl
  5. embryonic camera-type eye morphogenesis Source: DFLAT
  6. embryonic retina morphogenesis in camera-type eye Source: DFLAT
  7. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: MGI
  8. iris morphogenesis Source: DFLAT
  9. lens induction in camera-type eye Source: DFLAT
  10. negative regulation of BMP signaling pathway Source: Ensembl
  11. negative regulation of neuron apoptotic process Source: MGI
  12. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  13. neuron differentiation Source: DFLAT
  14. peptidyl-serine phosphorylation Source: BHF-UCL
  15. peptidyl-threonine phosphorylation Source: BHF-UCL
  16. positive regulation of angiogenesis Source: Ensembl
  17. positive regulation of cell proliferation Source: MGI
  18. positive regulation of DNA binding Source: UniProtKB
  19. positive regulation of JNK cascade Source: UniProtKB
  20. positive regulation of protein binding Source: BHF-UCL
  21. positive regulation of protein phosphorylation Source: MGI
  22. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  23. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  24. positive regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
  25. protein phosphorylation Source: UniProtKB
  26. retina layer formation Source: DFLAT
  27. SMAD protein signal transduction Source: Ensembl
  28. smoothened signaling pathway Source: MGI
  29. transcription, DNA-templated Source: UniProtKB-KW
  30. transforming growth factor beta receptor signaling pathway Source: MGI
  31. voluntary musculoskeletal movement Source: MGI
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. 3474.
ReactomeiREACT_196516. YAP1- and WWTR1 (TAZ)-stimulated gene expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Homeodomain-interacting protein kinase 2 (EC:2.7.11.1)
Alternative name(s):
Nuclear body-associated kinase 1
Sialophorin tail-associated nuclear serine/threonine-protein kinase
Gene namesi
Name:Hipk2
Synonyms:Nbak1, Stank
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:1314872. Hipk2.

Subcellular locationi

NucleusPML body 5 Publications. Cytoplasm By similarity
Isoform 2 : Nucleus. Cytoplasm
Note: Isoform 2 seems to be both nuclear and cytoplasmic.

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. nucleus Source: UniProtKB
  3. PML body Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Inhibited terminal erythroid cell proliferation and terminal enucleation, as well as reduced accumulation of hemoglobin. Impaired transcription of many genes involved in cell proliferation and apoptosis, and of erythroid-specific genes involved in hemoglobin biosynthesis, such as HBA and SLC25A37/MFRN. Enhanced stability of CTNNB1; accumulation of beta-catenin leading to the potentiation of beta-catenin-mediated cell proliferation and tumor formation. Small eyes with deficient lens, abnormal retinal lamination, and thickened retinas.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi228 – 2281K → R: No enzymatic activity, but still interacts with TP53 and NLK. Blocks the ability to induce cell growth arrest. Decreases corepressor activity. 4 Publications
Mutagenesisi361 – 3611Y → A: Strongly reduced nuclear localization. 1 Publication
Mutagenesisi1189 – 11891K → R: Inhibits localization to nuclear speckles. 1 Publication

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11961196Homeodomain-interacting protein kinase 2PRO_0000085997Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161Phosphoserine1 Publication
Cross-linki32 – 32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei118 – 1181Phosphoserine1 Publication
Modified residuei135 – 1351Phosphoserine1 Publication
Modified residuei141 – 1411Phosphothreonine1 Publication
Modified residuei252 – 2521Phosphothreonine1 Publication
Modified residuei273 – 2731Phosphothreonine1 Publication
Modified residuei361 – 3611Phosphotyrosine; by autocatalysis1 Publication
Modified residuei441 – 4411Phosphoserine1 Publication
Modified residuei482 – 4821Phosphothreonine1 Publication
Modified residuei517 – 5171Phosphothreonine1 Publication
Modified residuei566 – 5661Phosphothreonine1 Publication
Modified residuei634 – 6341Phosphoserine1 Publication
Modified residuei668 – 6681Phosphoserine1 Publication
Modified residuei687 – 6871Phosphothreonine1 Publication
Modified residuei815 – 8151Phosphoserine1 Publication
Modified residuei827 – 8271Phosphoserine1 Publication
Modified residuei934 – 9341Phosphoserine1 Publication
Modified residuei991 – 9911Phosphoserine1 Publication
Modified residuei993 – 9931Phosphoserine1 Publication
Modified residuei1042 – 10421Phosphoserine1 Publication
Modified residuei1153 – 11531Phosphoserine1 Publication
Modified residuei1186 – 11861Phosphoserine1 Publication
Cross-linki1189 – 1189Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Post-translational modificationi

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

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9QZR5.
PaxDbiQ9QZR5.
PRIDEiQ9QZR5.

PTM databases

PhosphoSiteiQ9QZR5.

Expressioni

Tissue specificityi

Ubiquitous. Abundant in muscle, heart, small intestine, stomach, kidney and brain; and low in testis, skin and lung.3 Publications

Developmental stagei

At E15-E17, mainly in the developing retina, telencephalon and myoblasts. At E12.5, detected in the developing trigeminal and dorsal root ganglia, and in the developing spinal cord (at protein level). Highly induced during primary fetal liver erythropoiesis. Expressed in the inner retina during late embryogenesis, in nucleus. Highest levels at E14.5 for isoform 2 and P12.5 for isoform 1.4 Publications

Inductioni

During T-cell activation.2 Publications

Gene expression databases

BgeeiQ9QZR5.
CleanExiMM_HIPK2.
ExpressionAtlasiQ9QZR5. baseline and differential.
GenevestigatoriQ9QZR5.

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 SP100; positively regulates TP53-dependent transcription (By similarity). 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.By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MECP2P516083EBI-366905,EBI-1189067From a different organism.
MybP068762EBI-366905,EBI-366934
NlkO549492EBI-366905,EBI-366894
WSB1Q9Y6I75EBI-366905,EBI-1171494From a different organism.

Protein-protein interaction databases

BioGridi200307. 5 interactions.
DIPiDIP-31712N.
IntActiQ9QZR5. 8 interactions.
STRINGi10090.ENSMUSP00000045457.

Structurei

3D structure databases

ProteinModelPortaliQ9QZR5.
SMRiQ9QZR5. 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 corepressionAdd
BLAST
Regioni189 – 520332Interaction with DAXXBy similarityAdd
BLAST
Regioni539 – 844306Interaction with SKI and SMAD1By similarityAdd
BLAST
Regioni752 – 897146Interaction with POU4F1Add
BLAST
Regioni774 – 876103Interaction with CTBP1Add
BLAST
Regioni787 – 897111Interaction with HMGA1Add
BLAST
Regioni802 – 8054Nuclear localization signal 1 (NLS1)By similarity
Regioni832 – 8354Nuclear localization signal 2 (NLS2)By similarity
Regioni839 – 93496Interaction with TP53 and TP73Add
BLAST
Regioni873 – 980108Localization to nuclear specklesAdd
BLAST
Regioni873 – 980108Required for localization to nuclear specklesBy similarityAdd
BLAST
Regioni873 – 90735Interaction with UBE2IAdd
BLAST
Regioni884 – 90825SUMO interaction motifs (SIM); required for nuclear localization and kinase activityBy similarityAdd
BLAST
Regioni935 – 1050116Interaction with AXIN1Add
BLAST
Regioni984 – 1196213Autoinhibitory domain (AID)By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1089 – 10924Poly-Ala

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119032.
HOVERGENiHBG051908.
InParanoidiQ9QZR5.
KOiK08826.
OMAiYSFPHNS.
OrthoDBiEOG7034GK.
PhylomeDBiQ9QZR5.
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 (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9QZR5-1) [UniParc]FASTAAdd to Basket

Also known as: Nbak1b, b

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 LKVEPSSNWD MTGYGSHSKV
60 70 80 90 100
YSQSKNIPPS QPASTTVSTS LPIPNPSLPY EQTIIFPGST 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 DADKRVTPIE TLNHPFVTMT HLLDFPHSAH VKSCFQNMEI
560 570 580 590 600
CKRRVNMYDT VNQSKTPFIT HVAPSTSTNL TMTFNNQLTT VHNQAPTTSS
610 620 630 640 650
ATLSLANPEV SILNYQSALY QPSAASMAAV APRSMPLQTG TAQICARPDP
660 670 680 690 700
FQQALIVCPP GFQGLQASPS KHAGYSVRME NAVPIVTQAP GAQPLQIQPG
710 720 730 740 750
LLAQQAWPGG AQQILLPPAW QQLTGVATHT SVQHAAVIPE TMAGTQQLAD
760 770 780 790 800
WRNTHAHGSH YNPIMQQPAL LTGHVTLPAA QPLNVGVAHV MRQQPTSTTS
810 820 830 840 850
SRKSKQHQSS VRNVSTCEVT SSQAISSPQR SKRVKENTPP RCAMVHSSPA
860 870 880 890 900
CSTSVTCGWG DVASSTTRER QRQTIVIPDT PSPTVSVITI SSDTDEEEEQ
910 920 930 940 950
KHAPTSTVSK QRKNVISCVT VHDSPYSDSS SNTSPYSVQQ RTGHNGTNTL
960 970 980 990 1000
DTKGGLENHC TGNPRTIIVP PLKTQASEVL VECDSLGPAI SASHHSSSFK
1010 1020 1030 1040 1050
SKSSSTVTST SGHSSGSSSG AIAYRQQRPG PHFQQQQPLN LSQAQQHMAA
1060 1070 1080 1090 1100
DRTGSHRRQQ AYITPTMAQA PYTFPHNSPS HGTVHPHLAA AAHLPTQPHL
1110 1120 1130 1140 1150
YTYTAPTALG STGTVAHLVA SQGSARHTVQ HTAYPASIVH QVPVSMGPRV
1160 1170 1180 1190
LPSPTIHPSQ YPAQFAHQTY ISASPASTVY TGYPLSPAKV NQYPYI
Length:1,196
Mass (Da):130,498
Last modified:April 27, 2001 - v2
Checksum:i5C863BE377F3AAEF
GO
Isoform 2 (identifier: Q9QZR5-2) [UniParc]FASTAAdd to Basket

Also known as: Nbak1a, a

The sequence of this isoform differs from the canonical sequence as follows:
     594-620: Missing.

Show »
Length:1,169
Mass (Da):127,676
Checksum:iF8C5ED0ADE4CFE4F
GO
Isoform 3 (identifier: Q9QZR5-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: Missing.
     369-1196: Missing.

Show »
Length:361
Mass (Da):39,990
Checksum:iF1F5B6095C8BCDA5
GO
Isoform 4 (identifier: Q9QZR5-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: Missing.
     594-620: Missing.

Show »
Length:1,162
Mass (Da):126,928
Checksum:i7478F6F1DAF75DE1
GO
Isoform 5 (identifier: Q9QZR5-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-480: Missing.
     595-605: APTTSSATLSL → KSQLIGLSPES
     606-1196: Missing.

Show »
Length:125
Mass (Da):14,279
Checksum:i7052092228D50AD5
GO

Sequence cautioni

The sequence AAC63011.1 differs from that shown. Reason: Frameshift at position 2. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti460 – 4601I → T in AAC63011. (PubMed:9748262)Curated
Sequence conflicti479 – 4791V → G in AAC63011. (PubMed:9748262)Curated
Sequence conflicti705 – 7051Missing in AAG41237. (PubMed:11267674)Curated
Sequence conflicti705 – 7051Missing in AAK07649. (PubMed:14990717)Curated
Sequence conflicti719 – 7191A → T in AAC63011. (PubMed:9748262)Curated
Sequence conflicti1120 – 11201A → R in AAC63011. (PubMed:9748262)Curated
Sequence conflicti1132 – 11321T → A in AAK07650. (PubMed:14990717)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 480480Missing in isoform 5. 1 PublicationVSP_013136Add
BLAST
Alternative sequencei1 – 77Missing in isoform 3 and isoform 4. 2 PublicationsVSP_013135
Alternative sequencei369 – 1196828Missing in isoform 3. 1 PublicationVSP_013137Add
BLAST
Alternative sequencei594 – 62027Missing in isoform 2 and isoform 4. 4 PublicationsVSP_004808Add
BLAST
Alternative sequencei595 – 60511APTTSSATLSL → KSQLIGLSPES in isoform 5. 1 PublicationVSP_013138Add
BLAST
Alternative sequencei606 – 1196591Missing in isoform 5. 1 PublicationVSP_013139Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077659 mRNA. Translation: AAC63011.1. Frameshift.
AF273680 mRNA. Translation: AAG02078.1.
AF208292 mRNA. Translation: AAG41237.1.
AF333791 mRNA. Translation: AAK07649.1.
AF333792 mRNA. Translation: AAK07650.1.
AF170301 mRNA. Translation: AAD52566.1.
AF170302 mRNA. Translation: AAD52567.1.
AK016742 mRNA. Translation: BAB30405.1.
AK019821 mRNA. Translation: BAB31866.1.
CCDSiCCDS20017.2. [Q9QZR5-1]
PIRiT17088.
RefSeqiNP_001129537.1. NM_001136065.2.
NP_001281072.1. NM_001294143.1. [Q9QZR5-2]
NP_001281073.1. NM_001294144.1.
NP_034563.2. NM_010433.2. [Q9QZR5-1]
UniGeneiMm.23790.
Mm.391962.
Mm.486937.

Genome annotation databases

EnsembliENSMUST00000160360; ENSMUSP00000125500; ENSMUSG00000061436.
ENSMUST00000160962; ENSMUSP00000125572; ENSMUSG00000061436.
ENSMUST00000161779; ENSMUSP00000124133; ENSMUSG00000061436. [Q9QZR5-1]
ENSMUST00000162359; ENSMUSP00000125150; ENSMUSG00000061436. [Q9QZR5-2]
GeneIDi15258.
KEGGimmu:15258.
UCSCiuc009bkw.2. mouse. [Q9QZR5-4]
uc009bkx.2. mouse. [Q9QZR5-1]
uc009blb.2. mouse. [Q9QZR5-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077659 mRNA. Translation: AAC63011.1 . Frameshift.
AF273680 mRNA. Translation: AAG02078.1 .
AF208292 mRNA. Translation: AAG41237.1 .
AF333791 mRNA. Translation: AAK07649.1 .
AF333792 mRNA. Translation: AAK07650.1 .
AF170301 mRNA. Translation: AAD52566.1 .
AF170302 mRNA. Translation: AAD52567.1 .
AK016742 mRNA. Translation: BAB30405.1 .
AK019821 mRNA. Translation: BAB31866.1 .
CCDSi CCDS20017.2. [Q9QZR5-1 ]
PIRi T17088.
RefSeqi NP_001129537.1. NM_001136065.2.
NP_001281072.1. NM_001294143.1. [Q9QZR5-2 ]
NP_001281073.1. NM_001294144.1.
NP_034563.2. NM_010433.2. [Q9QZR5-1 ]
UniGenei Mm.23790.
Mm.391962.
Mm.486937.

3D structure databases

ProteinModelPortali Q9QZR5.
SMRi Q9QZR5. Positions 125-554.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200307. 5 interactions.
DIPi DIP-31712N.
IntActi Q9QZR5. 8 interactions.
STRINGi 10090.ENSMUSP00000045457.

PTM databases

PhosphoSitei Q9QZR5.

Proteomic databases

MaxQBi Q9QZR5.
PaxDbi Q9QZR5.
PRIDEi Q9QZR5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000160360 ; ENSMUSP00000125500 ; ENSMUSG00000061436 .
ENSMUST00000160962 ; ENSMUSP00000125572 ; ENSMUSG00000061436 .
ENSMUST00000161779 ; ENSMUSP00000124133 ; ENSMUSG00000061436 . [Q9QZR5-1 ]
ENSMUST00000162359 ; ENSMUSP00000125150 ; ENSMUSG00000061436 . [Q9QZR5-2 ]
GeneIDi 15258.
KEGGi mmu:15258.
UCSCi uc009bkw.2. mouse. [Q9QZR5-4 ]
uc009bkx.2. mouse. [Q9QZR5-1 ]
uc009blb.2. mouse. [Q9QZR5-3 ]

Organism-specific databases

CTDi 28996.
MGIi MGI:1314872. Hipk2.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119032.
HOVERGENi HBG051908.
InParanoidi Q9QZR5.
KOi K08826.
OMAi YSFPHNS.
OrthoDBi EOG7034GK.
PhylomeDBi Q9QZR5.
TreeFami TF105417.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 3474.
Reactomei REACT_196516. YAP1- and WWTR1 (TAZ)-stimulated gene expression.

Miscellaneous databases

ChiTaRSi Hipk2. mouse.
NextBioi 287877.
PROi Q9QZR5.
SOURCEi Search...

Gene expression databases

Bgeei Q9QZR5.
CleanExi MM_HIPK2.
ExpressionAtlasi Q9QZR5. baseline and differential.
Genevestigatori Q9QZR5.

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 ]
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Publicationsi

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  1. "Homeodomain-interacting protein kinases, a novel family of co-repressors for homeodomain transcription factors."
    Kim Y.H., Choi C.Y., Lee S.-J., Conti M.A., Kim Y.
    J. Biol. Chem. 273:25875-25879(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH NKX1-2 AND NKX2-5, MUTAGENESIS OF LYS-228.
    Strain: BALB/c.
  2. "Identification and cloning of a CD43-associated serine/threonine kinase."
    Wang W., Link V., Green J.M.
    Cell. Immunol. 205:34-39(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH SPN, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION.
    Strain: BALB/c.
    Tissue: Heart.
  3. "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 4).
  4. "US11 of herpes simplex virus type 1 interacts with HIPK2 and antagonizes HIPK2-induced cell growth arrest."
    Giraud S., Diaz-Latoud C., Hacot S., Textoris J., Bourette R.P., Diaz J.-J.
    J. Virol. 78:2984-2993(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Heart.
  5. "Protein kinases associated with PML/CBP nuclear bodies and filamentous threads regulate transcription and inhibit cell growth."
    Sather S.L., Johnson N.L., Johnson G.L.
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  6. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
    Strain: C57BL/6J.
    Tissue: Testis.
  7. "Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1."
    Kim Y.H., Choi C.Y., Kim Y.
    Proc. Natl. Acad. Sci. U.S.A. 96:12350-12355(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH UBE2I, SUMOYLATION, MUTAGENESIS OF LYS-1189.
  8. "High mobility group I (Y) proteins bind HIPK2, a serine-threonine kinase protein which inhibits cell growth."
    Pierantoni G.M., Fedele M., Pentimalli F., Benvenuto G., Pero R., Viglietto G., Santoro M., Chiariotti L., Fusco A.
    Oncogene 20:6132-6141(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HMGA1, FUNCTION, PHOSPHORYLATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-228.
  9. "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, DEVELOPMENTAL STAGE.
  10. "Homeodomain-interacting protein kinase-2 phosphorylates p53 at Ser 46 and mediates apoptosis."
    D'Orazi G., Cecchinelli B., Bruno T., Manni I., Higashimoto Y., Saito S., Gostissa M., Coen S., Marchetti A., Del Sal G., Piaggio G., Fanciulli M., Appella E., Soddu S.
    Nat. Cell Biol. 4:11-19(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TP53, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-228.
  11. "Homeodomain interacting protein kinase 2 promotes apoptosis by downregulating the transcriptional corepressor CtBP."
    Zhang Q., Yoshimatsu Y., Hildebrand J., Frisch S.M., Goodman R.H.
    Cell 115:177-186(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CTBP1.
  12. "Axin stimulates p53 functions by activation of HIPK2 kinase through multimeric complex formation."
    Rui Y., Xu Z., Lin S., Li Q., Rui H., Luo W., Zhou H.-M., Cheung P.-Y., Wu Z., Ye Z., Li P., Han J., Lin S.-C.
    EMBO J. 23:4583-4594(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AXIN1, IDENTIFICATION IN A COMPLEX WITH TP53 AND AXIN1.
  13. "Wnt-1 signal induces phosphorylation and degradation of c-Myb protein via TAK1, HIPK2, and NLK."
    Kanei-Ishii C., Ninomiya-Tsuji J., Tanikawa J., Nomura T., Ishitani T., Kishida S., Kokura K., Kurahashi T., Ichikawa-Iwata E., Kim Y., Matsumoto K., Ishii S.
    Genes Dev. 18:816-829(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN WNT SIGNALING, INTERACTION WITH NLK AND MYB, MUTAGENESIS OF LYS-228.
  14. "Interaction of Brn3a and HIPK2 mediates transcriptional repression of sensory neuron survival."
    Wiggins A.K., Wei G., Doxakis E., Wong C., Tang A.A., Zang K., Luo E.J., Neve R.L., Reichardt L.F., Huang E.J.
    J. Cell Biol. 167:257-267(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH POU4F1; POU4F2 AND POU4F3, DEVELOPMENTAL STAGE.
  15. "Roles of HIPK1 and HIPK2 in AML1- and p300-dependent transcription, hematopoiesis and blood vessel formation."
    Aikawa Y., Nguyen L.A., Isono K., Takakura N., Tagata Y., Schmitz M.L., Koseki H., Kitabayashi I.
    EMBO J. 25:3955-3965(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS KINASE AND IN ANGIOGENESIS, INTERACTION WITH RUNX1 AND EP300.
  16. "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.
  17. "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, DISRUPTION PHENOTYPE.
  18. "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.
  19. "Homeodomain-interacting protein kinase 2 plays an important role in normal terminal erythroid differentiation."
    Hattangadi S.M., Burke K.A., Lodish H.F.
    Blood 115:4853-4861(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
  20. "Involvement of the Hipk family in regulation of eyeball size, lens formation and retinal morphogenesis."
    Inoue T., Kagawa T., Inoue-Mochita M., Isono K., Ohtsu N., Nobuhisa I., Fukushima M., Tanihara H., Taga T.
    FEBS Lett. 584:3233-3238(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN EYE DEVELOPMENT, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  21. "HIPK2 catalytic activity and subcellular localization are regulated by activation-loop Y354 autophosphorylation."
    Siepi F., Gatti V., Camerini S., Crescenzi M., Soddu S.
    Biochim. Biophys. Acta 1833:1443-1453(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-16; SER-118; SER-135; THR-141; THR-252; THR-273; TYR-361; SER-441; THR-482; THR-517; THR-566; SER-634; SER-668; THR-687; SER-815; SER-827; SER-934; SER-991; SER-991; SER-1042; SER-1153 AND SER-1186, ENZYME REGULATION, MUTAGENESIS OF TYR-361.

Entry informationi

Entry nameiHIPK2_MOUSE
AccessioniPrimary (citable) accession number: Q9QZR5
Secondary accession number(s): O88905
, Q99P45, Q99P46, Q9D2E6, Q9D474, Q9EQL2, Q9QZR4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: November 26, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

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