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Protein

Homeodomain-interacting protein kinase 2

Gene

Hipk2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei228ATPCurated1
Active sitei324Proton acceptorCurated1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi205 – 213ATPCurated9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein kinase activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: BHF-UCL
  • RNA polymerase II activating transcription factor binding Source: BHF-UCL
  • RNA polymerase II transcription coactivator activity Source: Ensembl
  • SMAD binding Source: MGI
  • transcription corepressor activity Source: UniProtKB
  • virion binding Source: UniProtKB

GO - Biological processi

  • adult locomotory behavior Source: MGI
  • adult walking behavior Source: MGI
  • anterior/posterior pattern specification Source: MGI
  • DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: MGI
  • embryonic camera-type eye morphogenesis Source: DFLAT
  • embryonic retina morphogenesis in camera-type eye Source: DFLAT
  • intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: MGI
  • iris morphogenesis Source: DFLAT
  • lens induction in camera-type eye Source: DFLAT
  • negative regulation of BMP signaling pathway Source: MGI
  • negative regulation of neuron apoptotic process Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • neuron differentiation Source: DFLAT
  • peptidyl-serine phosphorylation Source: BHF-UCL
  • peptidyl-threonine phosphorylation Source: BHF-UCL
  • positive regulation of angiogenesis Source: MGI
  • positive regulation of cell proliferation Source: MGI
  • positive regulation of DNA binding Source: UniProtKB
  • positive regulation of JNK cascade Source: UniProtKB
  • positive regulation of protein binding Source: BHF-UCL
  • positive regulation of protein phosphorylation Source: MGI
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • retina layer formation Source: DFLAT
  • SMAD protein signal transduction Source: MGI
  • smoothened signaling pathway Source: MGI
  • transforming growth factor beta receptor signaling pathway Source: MGI
  • 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.
ReactomeiR-MMU-6804756. Regulation of TP53 Activity through Phosphorylation.

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
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1314872. Hipk2.

Subcellular locationi

Isoform 2 :

GO - Cellular componenti

  • cytoplasm Source: MGI
  • nuclear body Source: MGI
  • nucleus Source: UniProtKB
  • PML body Source: MGI
  • RNA polymerase II transcription factor complex Source: BHF-UCL
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)DescriptionActionsGraphical viewLength
Mutagenesisi228K → R: No enzymatic activity, but still interacts with TP53 and NLK. Blocks the ability to induce cell growth arrest. Decreases corepressor activity. 4 Publications1
Mutagenesisi361Y → A: Strongly reduced nuclear localization. 1 Publication1
Mutagenesisi1189K → R: Inhibits localization to nuclear speckles. 1 Publication1

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000859971 – 1196Homeodomain-interacting protein kinase 2Add BLAST1196

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei16Phosphoserine1 Publication1
Cross-linki32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei118Phosphoserine1 Publication1
Modified residuei135Phosphoserine1 Publication1
Modified residuei141Phosphothreonine1 Publication1
Modified residuei252Phosphothreonine1 Publication1
Modified residuei273Phosphothreonine1 Publication1
Modified residuei361Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei441Phosphoserine1 Publication1
Modified residuei482Phosphothreonine1 Publication1
Modified residuei517Phosphothreonine1 Publication1
Modified residuei566Phosphothreonine1 Publication1
Modified residuei634Phosphoserine1 Publication1
Modified residuei668Phosphoserine1 Publication1
Modified residuei687Phosphothreonine1 Publication1
Modified residuei815Phosphoserine1 Publication1
Modified residuei827PhosphoserineCombined sources1 Publication1
Modified residuei934Phosphoserine1 Publication1
Modified residuei991Phosphoserine1 Publication1
Modified residuei993Phosphoserine1 Publication1
Modified residuei1042Phosphoserine1 Publication1
Modified residuei1153Phosphoserine1 Publication1
Modified residuei1186Phosphoserine1 Publication1
Cross-linki1189Glycyl 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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei923 – 924Cleavage; by CASP6By similarity2
Sitei984 – 985Cleavage; by CASP6By similarity2

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9QZR5.
PRIDEiQ9QZR5.

PTM databases

iPTMnetiQ9QZR5.
PhosphoSitePlusiQ9QZR5.

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

BgeeiENSMUSG00000061436.
CleanExiMM_HIPK2.
ExpressionAtlasiQ9QZR5. baseline and differential.
GenevisibleiQ9QZR5. MM.

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.

GO - Molecular functioni

  • RNA polymerase II activating transcription factor binding Source: BHF-UCL
  • SMAD binding Source: MGI

Protein-protein interaction databases

BioGridi200307. 6 interactors.
DIPiDIP-31712N.
IntActiQ9QZR5. 8 interactors.
STRINGi10090.ENSMUSP00000124133.

Structurei

3D structure databases

ProteinModelPortaliQ9QZR5.
SMRiQ9QZR5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini199 – 527Protein kinasePROSITE-ProRule annotationAdd BLAST329

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni97 – 230Transcriptional corepressionAdd BLAST134
Regioni189 – 520Interaction with DAXXBy similarityAdd BLAST332
Regioni539 – 844Interaction with SKI and SMAD1By similarityAdd BLAST306
Regioni752 – 897Interaction with POU4F11 PublicationAdd BLAST146
Regioni774 – 876Interaction with CTBP11 PublicationAdd BLAST103
Regioni787 – 897Interaction with HMGA11 PublicationAdd BLAST111
Regioni839 – 934Interaction with TP53 and TP731 PublicationAdd BLAST96
Regioni873 – 980Localization to nuclear specklesAdd BLAST108
Regioni873 – 980Required for localization to nuclear specklesBy similarityAdd BLAST108
Regioni873 – 907Interaction with UBE2I1 PublicationAdd BLAST35
Regioni884 – 908SUMO interaction motifs (SIM); required for nuclear localization and kinase activityBy similarityAdd BLAST25
Regioni935 – 1050Interaction with AXIN11 PublicationAdd BLAST116
Regioni984 – 1196Autoinhibitory domain (AID)By similarityAdd BLAST213

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi802 – 805Nuclear localization signal 1 (NLS1)By similarity4
Motifi832 – 835Nuclear localization signal 2 (NLS2)By similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1089 – 1092Poly-Ala4

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0667. Eukaryota.
ENOG410XPET. LUCA.
GeneTreeiENSGT00760000119032.
HOVERGENiHBG051908.
InParanoidiQ9QZR5.
KOiK08826.
OMAiMIQNNAS.
OrthoDBiEOG091G0UMX.
PhylomeDBiQ9QZR5.
TreeFamiTF105417.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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. AlignAdd to basket

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 differs from that shown. Reason: Frameshift at position 2.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti460I → T in AAC63011 (PubMed:9748262).Curated1
Sequence conflicti479V → G in AAC63011 (PubMed:9748262).Curated1
Sequence conflicti705Missing in AAG41237 (PubMed:11267674).Curated1
Sequence conflicti705Missing in AAK07649 (PubMed:14990717).Curated1
Sequence conflicti719A → T in AAC63011 (PubMed:9748262).Curated1
Sequence conflicti1120A → R in AAC63011 (PubMed:9748262).Curated1
Sequence conflicti1132T → A in AAK07650 (PubMed:14990717).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0131361 – 480Missing in isoform 5. 1 PublicationAdd BLAST480
Alternative sequenceiVSP_0131351 – 7Missing in isoform 3 and isoform 4. 2 Publications7
Alternative sequenceiVSP_013137369 – 1196Missing in isoform 3. 1 PublicationAdd BLAST828
Alternative sequenceiVSP_004808594 – 620Missing in isoform 2 and isoform 4. 4 PublicationsAdd BLAST27
Alternative sequenceiVSP_013138595 – 605APTTSSATLSL → KSQLIGLSPES in isoform 5. 1 PublicationAdd BLAST11
Alternative sequenceiVSP_013139606 – 1196Missing in isoform 5. 1 PublicationAdd BLAST591

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]
CCDS80527.1. [Q9QZR5-2]
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

EnsembliENSMUST00000161779; ENSMUSP00000124133; ENSMUSG00000061436. [Q9QZR5-1]
ENSMUST00000162359; ENSMUSP00000125150; ENSMUSG00000061436. [Q9QZR5-2]
GeneIDi15258.
KEGGimmu:15258.
UCSCiuc009bkw.3. mouse. [Q9QZR5-4]
uc009bkx.2. mouse. [Q9QZR5-1]
uc009blb.3. 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.
CCDSiCCDS20017.2. [Q9QZR5-1]
CCDS80527.1. [Q9QZR5-2]
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.

3D structure databases

ProteinModelPortaliQ9QZR5.
SMRiQ9QZR5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200307. 6 interactors.
DIPiDIP-31712N.
IntActiQ9QZR5. 8 interactors.
STRINGi10090.ENSMUSP00000124133.

PTM databases

iPTMnetiQ9QZR5.
PhosphoSitePlusiQ9QZR5.

Proteomic databases

PaxDbiQ9QZR5.
PRIDEiQ9QZR5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000161779; ENSMUSP00000124133; ENSMUSG00000061436. [Q9QZR5-1]
ENSMUST00000162359; ENSMUSP00000125150; ENSMUSG00000061436. [Q9QZR5-2]
GeneIDi15258.
KEGGimmu:15258.
UCSCiuc009bkw.3. mouse. [Q9QZR5-4]
uc009bkx.2. mouse. [Q9QZR5-1]
uc009blb.3. mouse. [Q9QZR5-3]

Organism-specific databases

CTDi28996.
MGIiMGI:1314872. Hipk2.

Phylogenomic databases

eggNOGiKOG0667. Eukaryota.
ENOG410XPET. LUCA.
GeneTreeiENSGT00760000119032.
HOVERGENiHBG051908.
InParanoidiQ9QZR5.
KOiK08826.
OMAiMIQNNAS.
OrthoDBiEOG091G0UMX.
PhylomeDBiQ9QZR5.
TreeFamiTF105417.

Enzyme and pathway databases

BRENDAi2.7.11.1. 3474.
ReactomeiR-MMU-6804756. Regulation of TP53 Activity through Phosphorylation.

Miscellaneous databases

ChiTaRSiHipk2. mouse.
PROiQ9QZR5.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000061436.
CleanExiMM_HIPK2.
ExpressionAtlasiQ9QZR5. baseline and differential.
GenevisibleiQ9QZR5. MM.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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]
ProtoNetiSearch...

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 30, 2016
This is version 165 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.