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Entry version 187 (18 Sep 2019)
Sequence version 2 (27 Apr 2001)
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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

<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.10 Publications

<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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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

More...
BRENDAi
2.7.11.1 3474

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-3899300 SUMOylation of transcription cofactors
R-MMU-6804756 Regulation of TP53 Activity through Phosphorylation
R-MMU-8939243 RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known

<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)
Alternative name(s):
Nuclear body-associated kinase 1
Sialophorin tail-associated nuclear serine/threonine-protein kinase
<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
Synonyms:Nbak1, Stank
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 6

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1314872 Hipk2

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>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
<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 → 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

<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_00000859971 – 1196Homeodomain-interacting protein kinase 2Add BLAST1196

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 residuei16Phosphoserine1 Publication1
<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); alternateBy similarity
Cross-linki32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy 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
Cross-linki953Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki973Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
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)

<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

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
<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 CASP6By similarity2
Sitei984 – 985Cleavage; by CASP6By similarity2

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
Q9QZR5

PRoteomics IDEntifications database

More...
PRIDEi
Q9QZR5

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9QZR5

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

More...
PhosphoSitePlusi
Q9QZR5

<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

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

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

At 15 dpc-17 dpc, mainly in the developing retina, telencephalon and myoblasts. At 12.5 dpc, 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 14.5 dpc for isoform 2 and P12.5 for isoform 1.4 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

During T-cell activation.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000061436 Expressed in 325 organ(s), highest expression level in vestibular membrane of cochlear duct

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9QZR5 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9QZR5 MM

<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 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

<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
200307, 6 interactors

Database of interacting proteins

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DIPi
DIP-31712N

Protein interaction database and analysis system

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IntActi
Q9QZR5, 11 interactors

Molecular INTeraction database

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MINTi
Q9QZR5

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000124133

<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

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

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SMRi
Q9QZR5

Database of comparative protein structure models

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ModBasei
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 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
<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)By similarity4
Motifi832 – 835Nuclear localization signal 2 (NLS2)By similarity4

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 biasi1089 – 1092Poly-Ala4

<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

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9QZR5

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
59821at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9QZR5

TreeFam database of animal gene trees

More...
TreeFami
TF105417

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (5+)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 5 <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

This entry has 5 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9QZR5-1) [UniParc]FASTAAdd to basket
Also known as: Nbak1b, b

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<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: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

<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 are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0R4J202A0A0R4J202_MOUSE
Homeodomain interacting protein kin...
Hipk2 mCG_9268
1,168Annotation 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>
A0A0R4J204A0A0R4J204_MOUSE
Homeodomain interacting protein kin...
Hipk2 mCG_9268
1,161Annotation 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

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 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
<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_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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS20017.2 [Q9QZR5-1]
CCDS80527.1 [Q9QZR5-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
T17088

NCBI Reference Sequences

More...
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]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000161779; ENSMUSP00000124133; ENSMUSG00000061436 [Q9QZR5-1]
ENSMUST00000162359; ENSMUSP00000125150; ENSMUSG00000061436 [Q9QZR5-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
15258

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:15258

UCSC genome browser

More...
UCSCi
uc009bkw.3 mouse [Q9QZR5-4]
uc009bkx.2 mouse [Q9QZR5-1]
uc009blb.3 mouse [Q9QZR5-3]

Keywords - Coding sequence diversityi

Alternative splicing

<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

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]

3D structure databases

SMRiQ9QZR5
ModBaseiSearch...

Protein-protein interaction databases

BioGridi200307, 6 interactors
DIPiDIP-31712N
IntActiQ9QZR5, 11 interactors
MINTiQ9QZR5
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

Comparative Toxicogenomics Database

More...
CTDi
28996
MGIiMGI:1314872 Hipk2

Phylogenomic databases

eggNOGiKOG0667 Eukaryota
ENOG410XPET LUCA
GeneTreeiENSGT00940000157742
InParanoidiQ9QZR5
KOiK08826
OMAiVHNSPAC
OrthoDBi59821at2759
PhylomeDBiQ9QZR5
TreeFamiTF105417

Enzyme and pathway databases

BRENDAi2.7.11.1 3474
ReactomeiR-MMU-3899300 SUMOylation of transcription cofactors
R-MMU-6804756 Regulation of TP53 Activity through Phosphorylation
R-MMU-8939243 RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known

Miscellaneous databases

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

More...
ChiTaRSi
Hipk2 mouse

Protein Ontology

More...
PROi
PR:Q9QZR5

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000061436 Expressed in 325 organ(s), highest expression level in vestibular membrane of cochlear duct
ExpressionAtlasiQ9QZR5 baseline and differential
GenevisibleiQ9QZR5 MM

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

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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_MOUSE
<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: Q9QZR5
Secondary accession number(s): O88905
, Q99P45, Q99P46, Q9D2E6, Q9D474, Q9EQL2, Q9QZR4
<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: April 27, 2001
Last modified: September 18, 2019
This is version 187 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

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