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Entry version 190 (13 Feb 2019)
Sequence version 2 (06 Jun 2002)
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Protein

Homeodomain-interacting protein kinase 2

Gene

HIPK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei228ATPCurated1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei324Proton acceptorCurated1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi205 – 213ATPCurated9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, DNA damage, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.11.1 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-2032785 YAP1- and WWTR1 (TAZ)-stimulated gene expression
R-HSA-3899300 SUMOylation of transcription cofactors
R-HSA-5578768 Physiological factors
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-8939243 RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known
R-HSA-9022692 Regulation of MECP2 expression and activity

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q9H2X6

SIGNOR Signaling Network Open Resource

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SIGNORi
Q9H2X6

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Homeodomain-interacting protein kinase 2 (EC:2.7.11.1)
Short name:
hHIPk2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:HIPK2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000064393.15

Human Gene Nomenclature Database

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HGNCi
HGNC:14402 HIPK2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
606868 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q9H2X6

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi228K → A: Locates in the nucleoplasm, no effect on interaction with RANBP9, but loss of kinase activity toward PML, RUNX1 and EP300. 9 Publications1
Mutagenesisi228K → 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 Publications1
Mutagenesisi359 – 361STY → AAF: Enhances BMP-induced transcriptional activation; when associated with R-228. 1 Publication3
Mutagenesisi803K → A: Impaired nuclear localization; when associated with A-805. 1 Publication1
Mutagenesisi805K → A: Impaired nuclear localization; when associated with A-803. 1 Publication1
Mutagenesisi833R → A: Impaired nuclear localization. 1 Publication1
Mutagenesisi835K → E: Impaired nuclear localization. 1 Publication1
Mutagenesisi885 – 892VSVITISS → KFMHFHRM: Loss of SUMO and CBX4 interaction, and impaired nuclear and PML-nuclear bodies localization. 1 Publication8
Mutagenesisi885 – 888VSVI → KSAK: Loss of SUMO interaction, and impaired nuclear and PML-nuclear bodies localization. 1 Publication4
Mutagenesisi892 – 895SDTD → ADTA: Loss of SUMO interaction, and impaired nuclear and PML-nuclear bodies localization. 1 Publication4
Mutagenesisi893 – 899DTDEEEE → NFNQQQQ: Loss of SUMO and CBX4 interaction, and impaired nuclear and PML-nuclear bodies localization. 1 Publication7

Organism-specific databases

DisGeNET

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DisGeNETi
28996

Open Targets

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OpenTargetsi
ENSG00000064393

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA29291

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4576

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2034

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
HIPK2

Domain mapping of disease mutations (DMDM)

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DMDMi
21431782

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000859951 – 1198Homeodomain-interacting protein kinase 2Add BLAST1198

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei16PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Cross-linki32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei118PhosphoserineBy similarity1
Modified residuei135PhosphoserineBy similarity1
Modified residuei141PhosphothreonineBy similarity1
Modified residuei252PhosphothreonineBy similarity1
Modified residuei273PhosphothreonineBy similarity1
Modified residuei361Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei441PhosphoserineBy similarity1
Modified residuei482PhosphothreonineBy similarity1
Modified residuei517PhosphothreonineBy similarity1
Modified residuei566PhosphothreonineBy similarity1
Modified residuei634PhosphoserineBy similarity1
Modified residuei668PhosphoserineBy similarity1
Modified residuei687PhosphothreonineBy similarity1
Modified residuei815PhosphoserineBy similarity1
Modified residuei827PhosphoserineBy similarity1
Modified residuei934PhosphoserineBy similarity1
Cross-linki953Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki973Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei992PhosphoserineBy similarity1
Modified residuei1041PhosphoserineBy similarity1
Modified residuei1155PhosphoserineBy similarity1
Modified residuei1188PhosphoserineBy similarity1
Cross-linki1191Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei923 – 924Cleavage; by CASP62
Sitei984 – 985Cleavage; by CASP62

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9H2X6

MaxQB - The MaxQuant DataBase

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MaxQBi
Q9H2X6

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q9H2X6

PeptideAtlas

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PeptideAtlasi
Q9H2X6

PRoteomics IDEntifications database

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PRIDEi
Q9H2X6

ProteomicsDB human proteome resource

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ProteomicsDBi
80628
80629 [Q9H2X6-2]
80630 [Q9H2X6-3]

Consortium for Top Down Proteomics

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TopDownProteomicsi
Q9H2X6-2 [Q9H2X6-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9H2X6

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q9H2X6

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
Q9H2X6

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000064393 Expressed in 239 organ(s), highest expression level in inferior vagus X ganglion

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9H2X6 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9H2X6 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA007611

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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. Interacts with SUMO1P1/SUMO5 (PubMed:27211601).17 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
118815, 67 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q9H2X6

Database of interacting proteins

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DIPi
DIP-31716N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
Q9H2X6

Protein interaction database and analysis system

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IntActi
Q9H2X6, 22 interactors

Molecular INTeraction database

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MINTi
Q9H2X6

STRING: functional protein association networks

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STRINGi
9606.ENSP00000385571

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q9H2X6

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q9H2X6

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q9H2X6

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini199 – 527Protein kinasePROSITE-ProRule annotationAdd BLAST329

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni97 – 230Transcriptional corepressionBy similarityAdd BLAST134
Regioni189 – 520Interaction with DAXX1 PublicationAdd BLAST332
Regioni539 – 844Interaction with SKI and SMAD11 PublicationAdd BLAST306
Regioni752 – 897Interaction with POU4F1By similarityAdd BLAST146
Regioni774 – 876Interaction with CTBP1By similarityAdd BLAST103
Regioni787 – 897Interaction with HMGA1By similarityAdd BLAST111
Regioni846 – 941Interaction with TP53 and TP731 PublicationAdd BLAST96
Regioni873 – 980Required for localization to nuclear specklesBy similarityAdd BLAST108
Regioni873 – 907Interaction with UBE2IBy similarityAdd BLAST35
Regioni884 – 908SUMO interaction motifs (SIM); required for nuclear localization and kinase activityAdd BLAST25
Regioni935 – 1049Interaction with AXIN1By similarityAdd BLAST115
Regioni984 – 1198Autoinhibitory domain (AID)Add BLAST215

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi802 – 805Nuclear localization signal 1 (NLS1)4
Motifi832 – 835Nuclear localization signal 2 (NLS2)4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1088 – 1094Poly-Ala7

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0667 Eukaryota
ENOG410XPET LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157742

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000231785

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG051908

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9H2X6

KEGG Orthology (KO)

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KOi
K08826

Identification of Orthologs from Complete Genome Data

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OMAi
VHNSPAC

Database of Orthologous Groups

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OrthoDBi
547545at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9H2X6

TreeFam database of animal gene trees

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TreeFami
TF105417

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

Pfam protein domain database

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Pfami
View protein in Pfam
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Note: Experimental confirmation may be lacking for some isoforms.

This entry has 3 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H7BXX9H7BXX9_HUMAN
Homeodomain-interacting protein kin...
HIPK2
911Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti33I → V in AAG41236 (PubMed:11267674).Curated1
Sequence conflicti59L → P in AAG41236 (PubMed:11267674).Curated1
Sequence conflicti64T → S in AAG41236 (PubMed:11267674).Curated1
Sequence conflicti169S → F in AAG35710 (Ref. 4) Curated1
Sequence conflicti187V → S in AAG35710 (Ref. 4) Curated1
Sequence conflicti202L → S in AAG35710 (Ref. 4) Curated1
Sequence conflicti233H → R in AAG41236 (PubMed:11267674).Curated1
Sequence conflicti471N → I in AAL37371 (Ref. 2) Curated1
Sequence conflicti669P → S in AAG35710 (Ref. 4) Curated1
Sequence conflicti711T → N in AAG35710 (Ref. 4) Curated1
Sequence conflicti717 – 719PPA → SPT in AAG35710 (Ref. 4) Curated3
Sequence conflicti724T → D in AAG35710 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_040547792R → Q1 PublicationCorresponds to variant dbSNP:rs56132157Ensembl.1
Natural variantiVAR_0405481027R → Q1 PublicationCorresponds to variant dbSNP:rs35255718Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_004804595 – 621Missing in isoform 3. 1 PublicationAdd BLAST27
Alternative sequenceiVSP_004805808 – 907Missing in isoform 2. 1 PublicationAdd BLAST100
Alternative sequenceiVSP_004806989 – 1018VNTSH…SGSSS → GNLGPGQGRNLSLESGFPAF LLLEMLLYGS in isoform 2. 1 PublicationAdd BLAST30
Alternative sequenceiVSP_0048071019 – 1198Missing in isoform 2. 1 PublicationAdd BLAST180

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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

The Consensus CDS (CCDS) project

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CCDSi
CCDS75666.1 [Q9H2X6-3]
CCDS75667.1 [Q9H2X6-1]

NCBI Reference Sequences

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RefSeqi
NP_001106710.1, NM_001113239.2 [Q9H2X6-3]
NP_073577.3, NM_022740.4 [Q9H2X6-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.731417

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000406875; ENSP00000385571; ENSG00000064393 [Q9H2X6-1]
ENST00000428878; ENSP00000413724; ENSG00000064393 [Q9H2X6-3]

Database of genes from NCBI RefSeq genomes

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GeneIDi
28996

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:28996

UCSC genome browser

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UCSCi
uc003vvd.5 human [Q9H2X6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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
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

3D structure databases

ProteinModelPortaliQ9H2X6
SMRiQ9H2X6
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118815, 67 interactors
CORUMiQ9H2X6
DIPiDIP-31716N
ELMiQ9H2X6
IntActiQ9H2X6, 22 interactors
MINTiQ9H2X6
STRINGi9606.ENSP00000385571

Chemistry databases

BindingDBiQ9H2X6
ChEMBLiCHEMBL4576
GuidetoPHARMACOLOGYi2034

PTM databases

iPTMnetiQ9H2X6
PhosphoSitePlusiQ9H2X6

Polymorphism and mutation databases

BioMutaiHIPK2
DMDMi21431782

Proteomic databases

jPOSTiQ9H2X6
MaxQBiQ9H2X6
PaxDbiQ9H2X6
PeptideAtlasiQ9H2X6
PRIDEiQ9H2X6
ProteomicsDBi80628
80629 [Q9H2X6-2]
80630 [Q9H2X6-3]
TopDownProteomicsiQ9H2X6-2 [Q9H2X6-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
28996
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000406875; ENSP00000385571; ENSG00000064393 [Q9H2X6-1]
ENST00000428878; ENSP00000413724; ENSG00000064393 [Q9H2X6-3]
GeneIDi28996
KEGGihsa:28996
UCSCiuc003vvd.5 human [Q9H2X6-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
28996
DisGeNETi28996
EuPathDBiHostDB:ENSG00000064393.15

GeneCards: human genes, protein and diseases

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GeneCardsi
HIPK2
HGNCiHGNC:14402 HIPK2
HPAiHPA007611
MIMi606868 gene
neXtProtiNX_Q9H2X6
OpenTargetsiENSG00000064393
PharmGKBiPA29291

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0667 Eukaryota
ENOG410XPET LUCA
GeneTreeiENSGT00940000157742
HOGENOMiHOG000231785
HOVERGENiHBG051908
InParanoidiQ9H2X6
KOiK08826
OMAiVHNSPAC
OrthoDBi547545at2759
PhylomeDBiQ9H2X6
TreeFamiTF105417

Enzyme and pathway databases

BRENDAi2.7.11.1 2681
ReactomeiR-HSA-2032785 YAP1- and WWTR1 (TAZ)-stimulated gene expression
R-HSA-3899300 SUMOylation of transcription cofactors
R-HSA-5578768 Physiological factors
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-8939243 RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known
R-HSA-9022692 Regulation of MECP2 expression and activity
SignaLinkiQ9H2X6
SIGNORiQ9H2X6

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
HIPK2 human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
HIPK2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
28996
PMAP-CutDBiQ9H2X6

Protein Ontology

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PROi
PR:Q9H2X6

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000064393 Expressed in 239 organ(s), highest expression level in inferior vagus X ganglion
ExpressionAtlasiQ9H2X6 baseline and differential
GenevisibleiQ9H2X6 HS

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHIPK2_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9H2X6
Secondary accession number(s): Q75MR7, Q8WWI4, Q9H2Y1
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: June 6, 2002
Last modified: February 13, 2019
This is version 190 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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