Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q62120 (JAK2_MOUSE)

Entry version 205 (11 Dec 2019)
Sequence version 2 (20 May 2008)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Tyrosine-protein kinase JAK2

Gene

Jak2

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

Non-receptor tyrosine kinase involved in various processes such as cell growth, development, differentiation or histone modifications. Mediates essential signaling events in both innate and adaptive immunity. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors such as growth hormone (GHR), prolactin (PRLR), leptin (LEPR), erythropoietin (EPOR), thrombopoietin (THPO); or type II receptors including IFN-alpha, IFN-beta, IFN-gamma and multiple interleukins. Following ligand-binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, cell stimulation with erythropoietin (EPO) during erythropoiesis leads to JAK2 autophosphorylation, activation, and its association with erythropoietin receptor (EPOR) that becomes phosphorylated in its cytoplasmic domain. Then, STAT5 (STAT5A or STAT5B) is recruited, phosphorylated and activated by JAK2. Once activated, dimerized STAT5 translocates into the nucleus and promotes the transcription of several essential genes involved in the modulation of erythropoiesis. Part of a signaling cascade that is activated by increased cellular retinol and that leads to the activation of STAT5 (STAT5A or STAT5B). In addition, JAK2 mediates angiotensin-2-induced ARHGEF1 phosphorylation. Plays a role in cell cycle by phosphorylating CDKN1B. Cooperates with TEC through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. In the nucleus, plays a key role in chromatin by specifically mediating phosphorylation of 'Tyr-41' of histone H3 (H3Y41ph), a specific tag that promotes exclusion of CBX5 (HP1 alpha) from chromatin.9 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

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+CuratedNote: Mn2+ was used in the in vitro kinase assay but Mg2+ is likely to be the in vivo cofactor.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Regulated by autophosphorylation, can both activate or decrease activity (PubMed:8343951, PubMed:20304997, PubMed:21726629). Heme regulates its activity by enhancing the phosphorylation on Tyr-1007 and Tyr-1008 (By similarity).By similarity1 Publication2 Publications

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 sitei882ATPPROSITE-ProRule annotation1
<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 sitei976Proton acceptorPROSITE-ProRule annotation1

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 bindingi855 – 863ATPPROSITE-ProRule annotation9

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionChromatin regulator, Kinase, Transferase, Tyrosine-protein kinase
Biological processAdaptive immunity, Immunity, Innate immunity
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.10.2 3474

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-1059683 Interleukin-6 signaling
R-MMU-110056 MAPK3 (ERK1) activation
R-MMU-112411 MAPK1 (ERK2) activation
R-MMU-1170546 Prolactin receptor signaling
R-MMU-1433557 Signaling by SCF-KIT
R-MMU-512988 Interleukin-3, Interleukin-5 and GM-CSF signaling
R-MMU-5673000 RAF activation
R-MMU-5673001 RAF/MAP kinase cascade
R-MMU-6785807 Interleukin-4 and Interleukin-13 signaling
R-MMU-6788467 IL-6-type cytokine receptor ligand interactions
R-MMU-69231 Cyclin D associated events in G1
R-MMU-877300 Interferon gamma signaling
R-MMU-877312 Regulation of IFNG signaling
R-MMU-8854691 Interleukin-20 family signaling
R-MMU-8984722 Interleukin-35 Signalling
R-MMU-9020591 Interleukin-12 signaling
R-MMU-9020933 Interleukin-23 signaling
R-MMU-9020956 Interleukin-27 signaling
R-MMU-9027276 Erythropoietin activates Phosphoinositide-3-kinase (PI3K)
R-MMU-9027284 Erythropoietin activates RAS
R-MMU-912526 Interleukin receptor SHC signaling
R-MMU-982772 Growth hormone receptor signaling
R-MMU-983231 Factors involved in megakaryocyte development and platelet production

<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:
Tyrosine-protein kinase JAK2 (EC:2.7.10.22 Publications)
Alternative name(s):
Janus kinase 2
Short name:
JAK-2
<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:Jak2
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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: Unplaced

Organism-specific databases

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

More...MGIi		MGI:96629 Jak2

<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, Membrane, 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

Embryos are anemic and die around day 12.5 post-coitum (dpc). Primitive erythrocytes are found, but definitive erythropoiesis is absent. Fetal liver myeloid progenitors, although present based on the expression of lineage specific markers, fail to respond to erythropoietin (Epo), thrombopoietin (Thpo), interleukin-3 (Il3), or granulocyte and macrophage colony-stimulating factor 1 (Csf1 and Csf2). Fetal liver BFU-E and CFU-E colonies are completely absent. However, multilineage hematopoietic stem cells (CD34(low), c-kit(pos)) can be found, and B-lymphopoiesis appears intact.2 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>Mutagenesisi119Y → E: Phosphorylation mimic mutant, leads to dissociation of JAK2 from the erythropoietin receptor complex. 1 Publication1
Mutagenesisi119Y → F: More stably associated with the erythropoietin receptor complex. 1 Publication1
Mutagenesisi372Y → F: About 60% loss of STAT1 phosphorylation by JAK2. 1 Publication1
Mutagenesisi373Y → F: Decreased the ability of JAK2 to autophosphorylate. 1 Publication1
Mutagenesisi868Y → F: Reduced activity in response to growth hormone. 1 Publication1
Mutagenesisi966Y → F: Reduced activity in response to growth hormone. 1 Publication1
Mutagenesisi972Y → F: Reduced activity in response to growth hormone. 1 Publication1
Mutagenesisi1008Y → F: Affects the phosphorylation pattern. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1649049

DrugCentral

More...DrugCentrali		Q62120

<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_00000881131 – 1129Tyrosine-protein kinase JAK2Add BLAST1129

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 residuei119Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei372Phosphotyrosine1 Publication1
Modified residuei373Phosphotyrosine1 Publication1
Modified residuei523PhosphoserineCombined sources1
Modified residuei570PhosphotyrosineBy similarity1
Modified residuei813Phosphotyrosine2 Publications1
Modified residuei868Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei966Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei972Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1007Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1008Phosphotyrosine; by autocatalysis1 Publication1

<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

Autophosphorylated, leading to regulate its activity. Leptin promotes phosphorylation on tyrosine residues, including phosphorylation on Tyr-813 (PubMed:16824542, PubMed:17565041). Autophosphorylation on Tyr-119 in response to EPO down-regulates its kinase activity (PubMed:17024180). Autophosphorylation on Tyr-868, Tyr-966 and Tyr-972 in response to growth hormone (GH) are required for maximal kinase activity (PubMed:20304997). Also phosphorylated by TEC (PubMed:9473212). Phosphorylated on tyrosine residues in response to interferon gamma signaling (By similarity). Phosphorylated on tyrosine residues in response to a signaling cascade that is activated by increased cellular retinol (PubMed:21368206).By similarity8 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q62120

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q62120

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

More...PaxDbi		Q62120

PRoteomics IDEntifications database

More...PRIDEi		Q62120

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q62120

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

More...PhosphoSitePlusi		Q62120

<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

Ubiquitously expressed throughout most tissues.

<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 IL23R, SKB1 and STAM2 (By similarity).

Interacts with EPOR (PubMed:8343951, PubMed:11779507).

Interacts with LYN (PubMed:9573010).

Interacts with SIRPA (PubMed:10842184).

Interacts with SH2B1 (PubMed:17565041, PubMed:16824542).

Interacts with TEC (PubMed:9473212).

Interacts with IFNGR2 (via intracellular domain) (By similarity).

Interacts with LEPR (Isoform B) (PubMed:11923481).

Interacts with HSP90AB1; promotes functional activation in a heat shock-dependent manner.

Interacts with STRA6 (By similarity).

By similarity9 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

Show more details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		200857, 34 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-388 Interleukin-12-receptor complex
CPX-389 Interleukin-23-receptor complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q62120

Database of interacting proteins

More...DIPi		DIP-320N

Protein interaction database and analysis system

More...IntActi		Q62120, 22 interactors

Molecular INTeraction database

More...MINTi		Q62120

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000064394

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q62120

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q62120 protein

<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

More...SMRi		Q62120

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q62120

<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>Domaini37 – 380FERMPROSITE-ProRule annotationAdd BLAST344
Domaini401 – 482SH2; atypicalPROSITE-ProRule annotationAdd BLAST82
Domaini545 – 809Protein kinase 1PROSITE-ProRule annotationAdd BLAST265
Domaini849 – 1124Protein kinase 2PROSITE-ProRule annotationAdd BLAST276

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>Regioni1 – 239Interaction with cytokine/interferon/growth hormone receptorsAdd BLAST239

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Possesses 2 protein kinase domains. The second one probably contains the catalytic domain, while the presence of slight differences suggest a different role for protein kinase 1.

<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

Belongs to the protein kinase superfamily. Tyr protein kinase family. JAK subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH2 domain

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0197 Eukaryota
COG0515 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000049158

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q62120

KEGG Orthology (KO)

More...KOi		K04447

Database of Orthologous Groups

More...OrthoDBi		58906at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q62120

Family and domain databases

Conserved Domains Database

More...CDDi		cd13333 FERM_C_JAK2, 1 hit
cd05078 PTK_Jak2_rpt1, 1 hit
cd14205 PTKc_Jak2_rpt2, 1 hit
cd10379 SH2_Jak2, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.505.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR019749 Band_41_domain
IPR035963 FERM_2
IPR000299 FERM_domain
IPR041155 FERM_F1
IPR041046 FERM_F2
IPR041381 Jak1_PHL_dom
IPR037838 JAK2_FERM_C-lobe
IPR035860 JAK2_SH2
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR035588 PTK_Jak2_rpt1
IPR035589 PTKc_Jak2_rpt2
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR016251 Tyr_kinase_non-rcpt_Jak/Tyk2
IPR020693 Tyr_kinase_non-rcpt_Jak2

Pfam protein domain database

More...Pfami		View protein in Pfam
PF18379 FERM_F1, 1 hit
PF18377 FERM_F2, 1 hit
PF17887 Jak1_Phl, 1 hit
PF07714 Pkinase_Tyr, 2 hits
PF00017 SH2, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000636 TyrPK_Jak, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01823 JANUSKINASE
PR01825 JANUSKINASE2
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00295 B41, 1 hit
SM00252 SH2, 1 hit
SM00219 TyrKc, 2 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47031 SSF47031, 1 hit
SSF55550 SSF55550, 1 hit
SSF56112 SSF56112, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50057 FERM_3, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 2 hits
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS50001 SH2, 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>Sequence (1+)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 has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q62120-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGMACLTMTE MEATSTSPVH QNGDIPGSAN SVKQIEPVLQ VYLYHSLGQA 
        60         70         80         90        100
EGEYLKFPSG EYVAEEICVA ASKACGITPV YHNMFALMSE TERIWYPPNH 
       110        120        130        140        150
VFHIDESTRH DILYRIRFYF PHWYCSGSSR TYRYGVSRGA EAPLLDDFVM 
       160        170        180        190        200
SYLFAQWRHD FVHGWIKVPV THETQEECLG MAVLDMMRIA KEKDQTPLAV 
       210        220        230        240        250
YNSVSYKTFL PKCVRAKIQD YHILTRKRIR YRFRRFIQQF SQCKATARNL 
       260        270        280        290        300
KLKYLINLET LQSAFYTEQF EVKESARGPS GEEIFATIII TGNGGIQWSR 
       310        320        330        340        350
GKHKESETLT EQDVQLYCDF PDIIDVSIKQ ANQECSNESR IVTVHKQDGK 
       360        370        380        390        400
VLEIELSSLK EALSFVSLID GYYRLTADAH HYLCKEVAPP AVLENIHSNC 
       410        420        430        440        450
HGPISMDFAI SKLKKAGNQT GLYVLRCSPK DFNKYFLTFA VERENVIEYK 
       460        470        480        490        500
HCLITKNENG EYNLSGTKRN FSNLKDLLNC YQMETVRSDS IIFQFTKCCP 
       510        520        530        540        550
PKPKDKSNLL VFRTNGISDV QISPTLQRHN NVNQMVFHKI RNEDLIFNES 
       560        570        580        590        600
LGQGTFTKIF KGVRREVGDY GQLHKTEVLL KVLDKAHRNY SESFFEAASM 
       610        620        630        640        650
MSQLSHKHLV LNYGVCVCGE ENILVQEFVK FGSLDTYLKK NKNSINILWK 
       660        670        680        690        700
LGVAKQLAWA MHFLEEKSLI HGNVCAKNIL LIREENRRTG NPPFIKLSDP 
       710        720        730        740        750
GISITVLPKD ILQERIPWVP PECIENPKNL NLATDKWSFG TTLWEICSGG 
       760        770        780        790        800
DKPLSALDSQ RKLQFYEDKH QLPAPKWTEL ANLINNCMDY EPDFRPAFRA 
       810        820        830        840        850
VIRDLNSLFT PDYELLTEND MLPNMRIGAL GFSGAFEDRD PTQFEERHLK 
       860        870        880        890        900
FLQQLGKGNF GSVEMCRYDP LQDNTGEVVA VKKLQHSTEE HLRDFEREIE 
       910        920        930        940        950
ILKSLQHDNI VKYKGVCYSA GRRNLRLIME YLPYGSLRDY LQKHKERIDH 
       960        970        980        990       1000
KKLLQYTSQI CKGMEYLGTK RYIHRDLATR NILVENENRV KIGDFGLTKV 
      1010       1020       1030       1040       1050
LPQDKEYYKV KEPGESPIFW YAPESLTESK FSVASDVWSF GVVLYELFTY 
      1060       1070       1080       1090       1100
IEKSKSPPVE FMRMIGNDKQ GQMIVFHLIE LLKSNGRLPR PEGCPDEIYV 
      1110       1120 
IMTECWNNNV SQRPSFRDLS LRVDQIIAA
Length:1,129
Mass (Da):130,235
Last modified:May 20, 2008 - 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:iDCB90FA000F99631
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
G5E852G5E852_MOUSE
Tyrosine-protein kinase
Jak2
1,132Annotation 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>
A0A494BBB9A0A494BBB9_MOUSE
Tyrosine-protein kinase
Jak2
638Annotation score:

Annotation score:2 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 conflicti155A → V in AAB41327 (PubMed:8378315).Curated1
Sequence conflicti468K → N in AAB41327 (PubMed:8378315).Curated1
Sequence conflicti686N → D in AAB41327 (PubMed:8378315).Curated1
Sequence conflicti1016S → R in AAA40014 (PubMed:2466296).Curated1
Sequence conflicti1024E → Q in AAB41327 (PubMed:8378315).Curated1
Sequence conflicti1042 – 1043VV → IP in AAA40014 (PubMed:2466296).Curated2
Sequence conflicti1121 – 1129LRVDQIIAA → FGWIKCGTV in AAB41327 (PubMed:8378315).Curated9

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
L16956 mRNA Translation: AAB41327.1
BC054807 mRNA Translation: AAH54807.1
BC059834 mRNA Translation: AAH59834.1
M33423 mRNA Translation: AAA40014.1

Protein sequence database of the Protein Information Resource

More...PIRi		A47511
B39577
JH0114

NCBI Reference Sequences

More...RefSeqi		NP_001041642.1, NM_001048177.2
NP_032439.2, NM_008413.3

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		16452

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:16452

<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
L16956 mRNA Translation: AAB41327.1
BC054807 mRNA Translation: AAH54807.1
BC059834 mRNA Translation: AAH59834.1
M33423 mRNA Translation: AAA40014.1
PIRiA47511
B39577
JH0114
RefSeqiNP_001041642.1, NM_001048177.2
NP_032439.2, NM_008413.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HDXX-ray2.35G/H/I/J/K/L810-820[»]
4GL9X-ray3.90A/B/C/D836-1129[»]
SMRiQ62120
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi200857, 34 interactors
ComplexPortaliCPX-388 Interleukin-12-receptor complex
CPX-389 Interleukin-23-receptor complex
CORUMiQ62120
DIPiDIP-320N
IntActiQ62120, 22 interactors
MINTiQ62120
STRINGi10090.ENSMUSP00000064394

Chemistry databases

BindingDBiQ62120
ChEMBLiCHEMBL1649049
DrugCentraliQ62120

PTM databases

iPTMnetiQ62120
PhosphoSitePlusiQ62120

Proteomic databases

jPOSTiQ62120
MaxQBiQ62120
PaxDbiQ62120
PRIDEiQ62120

Genome annotation databases

GeneIDi16452
KEGGimmu:16452

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3717
MGIiMGI:96629 Jak2

Phylogenomic databases

eggNOGiKOG0197 Eukaryota
COG0515 LUCA
HOGENOMiHOG000049158
InParanoidiQ62120
KOiK04447
OrthoDBi58906at2759
PhylomeDBiQ62120

Enzyme and pathway databases

BRENDAi2.7.10.2 3474
ReactomeiR-MMU-1059683 Interleukin-6 signaling
R-MMU-110056 MAPK3 (ERK1) activation
R-MMU-112411 MAPK1 (ERK2) activation
R-MMU-1170546 Prolactin receptor signaling
R-MMU-1433557 Signaling by SCF-KIT
R-MMU-512988 Interleukin-3, Interleukin-5 and GM-CSF signaling
R-MMU-5673000 RAF activation
R-MMU-5673001 RAF/MAP kinase cascade
R-MMU-6785807 Interleukin-4 and Interleukin-13 signaling
R-MMU-6788467 IL-6-type cytokine receptor ligand interactions
R-MMU-69231 Cyclin D associated events in G1
R-MMU-877300 Interferon gamma signaling
R-MMU-877312 Regulation of IFNG signaling
R-MMU-8854691 Interleukin-20 family signaling
R-MMU-8984722 Interleukin-35 Signalling
R-MMU-9020591 Interleukin-12 signaling
R-MMU-9020933 Interleukin-23 signaling
R-MMU-9020956 Interleukin-27 signaling
R-MMU-9027276 Erythropoietin activates Phosphoinositide-3-kinase (PI3K)
R-MMU-9027284 Erythropoietin activates RAS
R-MMU-912526 Interleukin receptor SHC signaling
R-MMU-982772 Growth hormone receptor signaling
R-MMU-983231 Factors involved in megakaryocyte development and platelet production

Miscellaneous databases

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

More...ChiTaRSi		Jak2 mouse
EvolutionaryTraceiQ62120

Protein Ontology

More...PROi		PR:Q62120
RNActiQ62120 protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Family and domain databases

CDDicd13333 FERM_C_JAK2, 1 hit
cd05078 PTK_Jak2_rpt1, 1 hit
cd14205 PTKc_Jak2_rpt2, 1 hit
cd10379 SH2_Jak2, 1 hit
Gene3Di3.30.505.10, 1 hit
InterProiView protein in InterPro
IPR019749 Band_41_domain
IPR035963 FERM_2
IPR000299 FERM_domain
IPR041155 FERM_F1
IPR041046 FERM_F2
IPR041381 Jak1_PHL_dom
IPR037838 JAK2_FERM_C-lobe
IPR035860 JAK2_SH2
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR035588 PTK_Jak2_rpt1
IPR035589 PTKc_Jak2_rpt2
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR016251 Tyr_kinase_non-rcpt_Jak/Tyk2
IPR020693 Tyr_kinase_non-rcpt_Jak2
PfamiView protein in Pfam
PF18379 FERM_F1, 1 hit
PF18377 FERM_F2, 1 hit
PF17887 Jak1_Phl, 1 hit
PF07714 Pkinase_Tyr, 2 hits
PF00017 SH2, 1 hit
PIRSFiPIRSF000636 TyrPK_Jak, 1 hit
PRINTSiPR01823 JANUSKINASE
PR01825 JANUSKINASE2
PR00109 TYRKINASE
SMARTiView protein in SMART
SM00295 B41, 1 hit
SM00252 SH2, 1 hit
SM00219 TyrKc, 2 hits
SUPFAMiSSF47031 SSF47031, 1 hit
SSF55550 SSF55550, 1 hit
SSF56112 SSF56112, 2 hits
PROSITEiView protein in PROSITE
PS50057 FERM_3, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 2 hits
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS50001 SH2, 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 nameiJAK2_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: Q62120
Secondary accession number(s): Q62124, Q7TQD0
<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: November 1, 1997
Last sequence update: May 20, 2008
Last modified: December 11, 2019
This is version 205 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

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again