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UniProtKB - O60674 (JAK2_HUMAN)

Entry version 212 (08 May 2019)
Sequence version 2 (24 Jan 2001)
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Protein

Tyrosine-protein kinase JAK2

Gene

JAK2

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

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 (PubMed:7615558). Following ligand-binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins (PubMed:9618263). 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) (PubMed:21368206). In addition, JAK2 mediates angiotensin-2-induced ARHGEF1 phosphorylation (PubMed:20098430). Plays a role in cell cycle by phosphorylating CDKN1B (PubMed:21423214). 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 (PubMed:19783980).7 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.1 Publication

<p>This subsection of the ‘Function’ 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 (By similarity). Heme regulates its activity by enhancing the phosphorylation on Tyr-1007 and Tyr-1008 (PubMed:21036157).By similarity1 Publication

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 sitei882ATPPROSITE-ProRule annotation1
<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 sitei976Proton acceptorPROSITE-ProRule annotation1

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 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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the 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 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1059683 Interleukin-6 signaling
R-HSA-110056 MAPK3 (ERK1) activation
R-HSA-112411 MAPK1 (ERK2) activation
R-HSA-1170546 Prolactin receptor signaling
R-HSA-1433557 Signaling by SCF-KIT
R-HSA-2586552 Signaling by Leptin
R-HSA-3214858 RMTs methylate histone arginines
R-HSA-512988 Interleukin-3, Interleukin-5 and GM-CSF signaling
R-HSA-5673000 RAF activation
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-6788467 IL-6-type cytokine receptor ligand interactions
R-HSA-6802946 Signaling by moderate kinase activity BRAF mutants
R-HSA-6802949 Signaling by RAS mutants
R-HSA-6802952 Signaling by BRAF and RAF fusions
R-HSA-6802955 Paradoxical activation of RAF signaling by kinase inactive BRAF
R-HSA-69231 Cyclin D associated events in G1
R-HSA-877300 Interferon gamma signaling
R-HSA-877312 Regulation of IFNG signaling
R-HSA-8854691 Interleukin-20 family signaling
R-HSA-8984722 Interleukin-35 Signalling
R-HSA-9006335 Signaling by Erythropoietin
R-HSA-9020591 Interleukin-12 signaling
R-HSA-9020933 Interleukin-23 signaling
R-HSA-9020956 Interleukin-27 signaling
R-HSA-9027276 Erythropoietin activates Phosphoinositide-3-kinase (PI3K)
R-HSA-9027277 Erythropoietin activates Phospholipase C gamma (PLCG)
R-HSA-9027283 Erythropoietin activates STAT5
R-HSA-9027284 Erythropoietin activates RAS
R-HSA-912526 Interleukin receptor SHC signaling
R-HSA-982772 Growth hormone receptor signaling
R-HSA-983231 Factors involved in megakaryocyte development and platelet production

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

More...SignaLinki		O60674

SIGNOR Signaling Network Open Resource

More...SIGNORi		O60674

<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:2.7.10.23 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>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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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 9

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:6192 JAK2

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		147796 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_O60674

<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 provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Chromosomal aberrations involving JAK2 are found in both chronic and acute forms of eosinophilic, lymphoblastic and myeloid leukemia. Translocation t(8;9)(p22;p24) with PCM1 links the protein kinase domain of JAK2 to the major portion of PCM1. Translocation t(9;12)(p24;p13) with ETV6.
Budd-Chiari syndrome (BDCHS)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA syndrome caused by obstruction of hepatic venous outflow involving either the hepatic veins or the terminal segment of the inferior vena cava. Obstructions are generally caused by thrombosis and lead to hepatic congestion and ischemic necrosis. Clinical manifestations observed in the majority of patients include hepatomegaly, right upper quadrant pain and abdominal ascites. Budd-Chiari syndrome is associated with a combination of disease states including primary myeloproliferative syndromes and thrombophilia due to factor V Leiden, protein C deficiency and antithrombin III deficiency. Budd-Chiari syndrome is a rare but typical complication in patients with polycythemia vera.
See also OMIM:600880
Polycythemia vera (PV)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA myeloproliferative disorder characterized by abnormal proliferation of all hematopoietic bone marrow elements, erythroid hyperplasia, an absolute increase in total blood volume, but also by myeloid leukocytosis, thrombocytosis and splenomegaly.
See also OMIM:263300
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_032697617V → F in PV, THCYT3 and AML; associated with susceptibility to Budd-Chiari syndrome; somatic mutation in a high percentage of patients with essential thrombocythemia or myelofibrosis; leads to constitutive tyrosine phosphorylation activity that promotes cytokine hypersensitivity. 6 PublicationsCorresponds to variant dbSNP:rs77375493EnsemblClinVar.1
Thrombocythemia 3 (THCYT3)2 Publications
The disease may be caused by mutations affecting the gene represented in this entry.
Disease descriptionA myeloproliferative disorder characterized by excessive platelet production, resulting in increased numbers of circulating platelets. It can be associated with spontaneous hemorrhages and thrombotic episodes.
See also OMIM:614521
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_067534617V → I in THCYT3. 1 PublicationCorresponds to variant dbSNP:rs77375493EnsemblClinVar.1
Myelofibrosis (MYELOF)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by replacement of the bone marrow by fibrous tissue, occurring in association with a myeloproliferative disorder. Clinical manifestations may include anemia, pallor, splenomegaly, hypermetabolic state, petechiae, ecchymosis, bleeding, lymphadenopathy, hepatomegaly, portal hypertension.
See also OMIM:254450
Leukemia, acute myelogenous (AML)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes.
See also OMIM:601626
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_032696607K → N in AML. 1 PublicationCorresponds to variant dbSNP:rs121912472EnsemblClinVar.1
Natural variantiVAR_032697617V → F in PV, THCYT3 and AML; associated with susceptibility to Budd-Chiari syndrome; somatic mutation in a high percentage of patients with essential thrombocythemia or myelofibrosis; leads to constitutive tyrosine phosphorylation activity that promotes cytokine hypersensitivity. 6 PublicationsCorresponds to variant dbSNP:rs77375493EnsemblClinVar.1

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>Sitei352 – 353Breakpoint for translocation to form PCM1-JAK2 fusion protein2
Sitei442 – 443Breakpoint for translocation to form PCM1-JAK2 fusion protein2
Sitei450 – 451Breakpoint for translocation to form PCM1-JAK2 fusion protein2
Sitei504 – 505Breakpoint for translocation to form PCM1-JAK2 fusion protein2
Sitei710 – 711Breakpoint for translocation to form PCM1-JAK2 fusion protein2

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

DisGeNET

More...DisGeNETi		3717

MalaCards human disease database

More...MalaCardsi		JAK2
MIMi254450 phenotype
263300 phenotype
600880 phenotype
601626 phenotype
614521 phenotype

Open Targets

More...OpenTargetsi		ENSG00000096968

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		131 Budd-Chiari syndrome
3318 Essential thrombocythemia
71493 Familial thrombocytosis
729 Polycythemia vera
824 Primary myelofibrosis

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA29989

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2971

Drug and drug target database

More...DrugBanki		DB07162 4-(3-amino-1H-indazol-5-yl)-N-tert-butylbenzenesulfonamide
DB08067 4-[(2-{4-[(CYCLOPROPYLCARBAMOYL)AMINO]-1H-PYRAZOL-3-YL}-1H-BENZIMIDAZOL-6-YL)METHYL]MORPHOLIN-4-IUM
DB07161 5-phenyl-1H-indazol-3-amine
DB08877 Ruxolitinib
DB08895 Tofacitinib
DB05243 XL019

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2048

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		JAK2

<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_00000881121 – 1132Tyrosine-protein kinase JAK2Add BLAST1132

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 autocatalysisBy similarity1
Modified residuei372PhosphotyrosineBy similarity1
Modified residuei373PhosphotyrosineBy similarity1
Modified residuei523PhosphoserineBy similarity1
Modified residuei570PhosphotyrosineCombined sources1
Modified residuei813PhosphotyrosineBy similarity1
Modified residuei868Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei966Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei972Phosphotyrosine; by autocatalysisBy similarity1
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 (By similarity). Autophosphorylation on Tyr-119 in response to EPO down-regulates its kinase activity (By similarity). Autophosphorylation on Tyr-868, Tyr-966 and Tyr-972 in response to growth hormone (GH) are required for maximal kinase activity (By similarity). Also phosphorylated by TEC (By similarity). Phosphorylated on tyrosine residues in response to interferon gamma signaling (PubMed:7615558, PubMed:7673114). Phosphorylated on tyrosine residues in response to a signaling cascade that is activated by increased cellular retinol (PubMed:21368206).By similarity3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		O60674

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		O60674

MaxQB - The MaxQuant DataBase

More...MaxQBi		O60674

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

More...PaxDbi		O60674

PeptideAtlas

More...PeptideAtlasi		O60674

PRoteomics IDEntifications database

More...PRIDEi		O60674

ProteomicsDB human proteome resource

More...ProteomicsDBi		49519

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O60674

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

More...PhosphoSitePlusi		O60674

<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.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000096968 Expressed in 212 organ(s), highest expression level in popliteal artery

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		O60674 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O60674 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB013089
HPA040820
HPA043870

<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 EPOR, LYN, SIRPA, SH2B1 and TEC (By similarity). Interacts with IL23R (PubMed:12023369). Interacts with SKB1 (PubMed:10531356). Interacts with STAM2 (PubMed:10899310). Interacts with IFNGR2 (via intracellular domain) (PubMed:7673114, PubMed:7615558). Interacts with LEPR (Isoform B) (By similarity). Interacts with HSP90AB1; promotes functional activation in a heat shock-dependent manner (PubMed:20353823). Interacts with STRA6 (PubMed:21368206). Interacts with RHEX; this interaction occurs in a erythropoietin (EPO)-dependent manner (PubMed:25092874).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

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		109920, 110 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-382 Interleukin-12-receptor complex
CPX-383 Interleukin-23-receptor complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		O60674

Database of interacting proteins

More...DIPi		DIP-33880N

Protein interaction database and analysis system

More...IntActi		O60674, 35 interactors

Molecular INTeraction database

More...MINTi		O60674

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000371067

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		O60674

<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

Secondary structure

11132
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
2B7AX-ray2.00A/B840-1132[»]
2W1IX-ray2.60A/B835-1132[»]
2XA4X-ray2.04A/B835-1132[»]
3E62X-ray1.92A839-1131[»]
3E63X-ray1.90A839-1131[»]
3E64X-ray1.80A839-1131[»]
3FUPX-ray2.40A/B840-1132[»]
3IO7X-ray2.60A842-1132[»]
3IOKX-ray2.10A842-1132[»]
3JY9X-ray2.10A842-1130[»]
3KCKX-ray2.20A842-1132[»]
3KRRX-ray1.80A840-1132[»]
3LPBX-ray2.00A/B840-1132[»]
3Q32X-ray2.50A/B839-1132[»]
3RVGX-ray2.50A835-1132[»]
3TJCX-ray2.40A/B837-1132[»]
3TJDX-ray2.90A/B837-1132[»]
3UGCX-ray1.34A840-1132[»]
3ZMMX-ray2.51A/B835-1132[»]
4AQCX-ray1.90A/B835-1132[»]
4BBEX-ray1.90A/B/C/D839-1132[»]
4BBFX-ray2.00A/B/C/D839-1132[»]
4C61X-ray2.45A/B835-1132[»]
4C62X-ray2.75A/B835-1132[»]
4D0WX-ray1.77A835-1132[»]
4D0XX-ray1.82A835-1132[»]
4D1SX-ray1.66A835-1132[»]
4E4MX-ray2.25A/B/D/E833-1132[»]
4E6DX-ray2.22A/B835-1132[»]
4E6QX-ray1.95A/B835-1132[»]
4F08X-ray2.82A/B833-1132[»]
4F09X-ray2.40A833-1132[»]
4FVPX-ray2.01A536-812[»]
4FVQX-ray1.75A536-812[»]
4FVRX-ray2.00A536-812[»]
4GFMX-ray2.30A833-1132[»]
4GMYX-ray2.40A833-1132[»]
4HGEX-ray2.30A/B833-1132[»]
4IVAX-ray1.50A833-1132[»]
4JI9X-ray2.40A/B833-1132[»]
4JIAX-ray1.85A833-1132[»]
4P7EX-ray2.40A/B840-1132[»]
4YTCX-ray2.16A842-1132[»]
4YTFX-ray1.78A842-1132[»]
4YTHX-ray2.04A842-1132[»]
4YTIX-ray2.52A842-1132[»]
4Z32X-ray3.04A/B/C/D/E/F/G/H31-516[»]
4ZIMX-ray2.65A/B839-1132[»]
5AEPX-ray1.95A835-1132[»]
5CF4X-ray2.38A/B839-1132[»]
5CF5X-ray2.45A/B839-1132[»]
5CF6X-ray2.50A/B839-1132[»]
5CF8X-ray1.80A/B839-1132[»]
5HEZX-ray2.66A/B/C/D833-1132[»]
5I4NX-ray1.54A535-812[»]
5L3AX-ray1.98A840-1132[»]
5TQ3X-ray2.69A/B837-1132[»]
5TQ4X-ray2.30A837-1132[»]
5TQ5X-ray2.30A837-1132[»]
5TQ6X-ray2.06A/B837-1132[»]
5TQ7X-ray2.10A/B837-1132[»]
5TQ8X-ray1.59A837-1132[»]
5USYX-ray2.00A/B840-1132[»]
5USZX-ray2.10A536-812[»]
5UT0X-ray2.10A536-812[»]
5UT1X-ray1.95A536-812[»]
5UT2X-ray1.75A536-812[»]
5UT3X-ray1.50A536-812[»]
5UT4X-ray2.00A536-812[»]
5UT5X-ray1.90A536-812[»]
5UT6X-ray1.65A536-812[»]
5WEVX-ray1.85A833-1132[»]
5WIJX-ray2.04A536-812[»]
5WIKX-ray2.60B536-812[»]
5WILX-ray2.20A536-812[»]
5WIMX-ray2.55A536-812[»]
5WINX-ray2.38A536-812[»]
6AAJX-ray2.37A/B834-1132[»]
6BBVX-ray1.80A837-1132[»]
6BRWX-ray2.03A536-812[»]
6BS0X-ray1.54A536-812[»]
6BSSX-ray2.10A536-812[»]
6DRWX-ray2.30A840-1132[»]
6E2PX-ray2.83A/B36-514[»]
6E2QX-ray2.65A/B/C/D36-514[»]
6M9HX-ray1.79A536-812[»]

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

More...SMRi		O60674

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		O60674

<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 receptorsBy similarityAdd 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 (By similarity).By similarity

<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

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155640

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000049158

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O60674

KEGG Orthology (KO)

More...KOi		K04447

Identification of Orthologs from Complete Genome Data

More...OMAi		SQLSYKH

Database of Orthologous Groups

More...OrthoDBi		933071at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O60674

TreeFam database of animal gene trees

More...TreeFami		TF327041

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>.<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

O60674-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGMACLTMTE MEGTSTSSIY QNGDISGNAN SMKQIDPVLQ VYLYHSLGKS 
        60         70         80         90        100
EADYLTFPSG EYVAEEICIA ASKACGITPV YHNMFALMSE TERIWYPPNH 
       110        120        130        140        150
VFHIDESTRH NVLYRIRFYF PRWYCSGSNR AYRHGISRGA EAPLLDDFVM 
       160        170        180        190        200
SYLFAQWRHD FVHGWIKVPV THETQEECLG MAVLDMMRIA KENDQTPLAI 
       210        220        230        240        250
YNSISYKTFL PKCIRAKIQD YHILTRKRIR YRFRRFIQQF SQCKATARNL 
       260        270        280        290        300
KLKYLINLET LQSAFYTEKF EVKEPGSGPS GEEIFATIII TGNGGIQWSR 
       310        320        330        340        350
GKHKESETLT EQDLQLYCDF PNIIDVSIKQ ANQEGSNESR VVTIHKQDGK 
       360        370        380        390        400
NLEIELSSLR EALSFVSLID GYYRLTADAH HYLCKEVAPP AVLENIQSNC 
       410        420        430        440        450
HGPISMDFAI SKLKKAGNQT GLYVLRCSPK DFNKYFLTFA VERENVIEYK 
       460        470        480        490        500
HCLITKNENE EYNLSGTKKN FSSLKDLLNC YQMETVRSDN IIFQFTKCCP 
       510        520        530        540        550
PKPKDKSNLL VFRTNGVSDV PTSPTLQRPT HMNQMVFHKI RNEDLIFNES 
       560        570        580        590        600
LGQGTFTKIF KGVRREVGDY GQLHETEVLL KVLDKAHRNY SESFFEAASM 
       610        620        630        640        650
MSKLSHKHLV LNYGVCVCGD ENILVQEFVK FGSLDTYLKK NKNCINILWK 
       660        670        680        690        700
LEVAKQLAWA MHFLEENTLI HGNVCAKNIL LIREEDRKTG NPPFIKLSDP 
       710        720        730        740        750
GISITVLPKD ILQERIPWVP PECIENPKNL NLATDKWSFG TTLWEICSGG 
       760        770        780        790        800
DKPLSALDSQ RKLQFYEDRH QLPAPKWAEL ANLINNCMDY EPDFRPSFRA 
       810        820        830        840        850
IIRDLNSLFT PDYELLTEND MLPNMRIGAL GFSGAFEDRD PTQFEERHLK 
       860        870        880        890        900
FLQQLGKGNF GSVEMCRYDP LQDNTGEVVA VKKLQHSTEE HLRDFEREIE 
       910        920        930        940        950
ILKSLQHDNI VKYKGVCYSA GRRNLKLIME YLPYGSLRDY LQKHKERIDH 
       960        970        980        990       1000
IKLLQYTSQI CKGMEYLGTK RYIHRDLATR NILVENENRV KIGDFGLTKV 
      1010       1020       1030       1040       1050
LPQDKEYYKV KEPGESPIFW YAPESLTESK FSVASDVWSF GVVLYELFTY 
      1060       1070       1080       1090       1100
IEKSKSPPAE FMRMIGNDKQ GQMIVFHLIE LLKNNGRLPR PDGCPDEIYM 
      1110       1120       1130 
IMTECWNNNV NQRPSFRDLA LRVDQIRDNM AG
Length:1,132
Mass (Da):130,674
Last modified:January 24, 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:iC30669EF1A7DA80C
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
A0A1B0GTR9A0A1B0GTR9_HUMAN
Tyrosine-protein kinase
JAK2
710Annotation score:

Annotation score:3 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>
A0A1B0GVR5A0A1B0GVR5_HUMAN
Tyrosine-protein kinase JAK2
JAK2
26Annotation 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 conflicti321P → S in AAC23982 (PubMed:9618263).Curated1
Sequence conflicti1126I → V in AAC23653 (PubMed:9446644).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_041716127G → D1 PublicationCorresponds to variant dbSNP:rs56118985EnsemblClinVar.1
Natural variantiVAR_041717191K → Q in an ovarian serous carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_041718346K → R1 PublicationCorresponds to variant dbSNP:rs55667734Ensembl.1
Natural variantiVAR_041719377A → E1 PublicationCorresponds to variant dbSNP:rs55953208Ensembl.1
Natural variantiVAR_041720393L → V1 PublicationCorresponds to variant dbSNP:rs2230723EnsemblClinVar.1
Natural variantiVAR_032693537 – 539FHK → L in myeloproliferative disorder with erythrocytosis. 1 Publication3
Natural variantiVAR_032694538 – 539HK → QL in myeloproliferative disorder with erythrocytosis. 2
Natural variantiVAR_032695539K → L in myeloproliferative disorder with erythrocytosis; requires 2 nucleotide substitutions. 1 PublicationCorresponds to variant dbSNP:rs121912473EnsemblClinVar.1
Natural variantiVAR_043129584D → E. Corresponds to variant dbSNP:rs17490221Ensembl.1
Natural variantiVAR_032696607K → N in AML. 1 PublicationCorresponds to variant dbSNP:rs121912472EnsemblClinVar.1
Natural variantiVAR_032697617V → F in PV, THCYT3 and AML; associated with susceptibility to Budd-Chiari syndrome; somatic mutation in a high percentage of patients with essential thrombocythemia or myelofibrosis; leads to constitutive tyrosine phosphorylation activity that promotes cytokine hypersensitivity. 6 PublicationsCorresponds to variant dbSNP:rs77375493EnsemblClinVar.1
Natural variantiVAR_067534617V → I in THCYT3. 1 PublicationCorresponds to variant dbSNP:rs77375493EnsemblClinVar.1
Natural variantiVAR_0417211063R → H1 PublicationCorresponds to variant dbSNP:rs41316003EnsemblClinVar.1

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
AF058925 mRNA Translation: AAC23982.1
AF001362 mRNA Translation: AAC23653.1
AF005216 mRNA Translation: AAB82092.1
AL161450 Genomic DNA No translation available.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS6457.1

Protein sequence database of the Protein Information Resource

More...PIRi		JW0091

NCBI Reference Sequences

More...RefSeqi		NP_001309123.1, NM_001322194.1
NP_001309124.1, NM_001322195.1
NP_001309125.1, NM_001322196.1
NP_001309133.1, NM_001322204.1
NP_004963.1, NM_004972.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000381652; ENSP00000371067; ENSG00000096968

Database of genes from NCBI RefSeq genomes

More...GeneIDi		3717

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:3717

UCSC genome browser

More...UCSCi		uc003ziw.3 human

Keywords - Coding sequence diversityi

Chromosomal rearrangement, 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
AF058925 mRNA Translation: AAC23982.1
AF001362 mRNA Translation: AAC23653.1
AF005216 mRNA Translation: AAB82092.1
AL161450 Genomic DNA No translation available.
CCDSiCCDS6457.1
PIRiJW0091
RefSeqiNP_001309123.1, NM_001322194.1
NP_001309124.1, NM_001322195.1
NP_001309125.1, NM_001322196.1
NP_001309133.1, NM_001322204.1
NP_004963.1, NM_004972.3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B7AX-ray2.00A/B840-1132[»]
2W1IX-ray2.60A/B835-1132[»]
2XA4X-ray2.04A/B835-1132[»]
3E62X-ray1.92A839-1131[»]
3E63X-ray1.90A839-1131[»]
3E64X-ray1.80A839-1131[»]
3FUPX-ray2.40A/B840-1132[»]
3IO7X-ray2.60A842-1132[»]
3IOKX-ray2.10A842-1132[»]
3JY9X-ray2.10A842-1130[»]
3KCKX-ray2.20A842-1132[»]
3KRRX-ray1.80A840-1132[»]
3LPBX-ray2.00A/B840-1132[»]
3Q32X-ray2.50A/B839-1132[»]
3RVGX-ray2.50A835-1132[»]
3TJCX-ray2.40A/B837-1132[»]
3TJDX-ray2.90A/B837-1132[»]
3UGCX-ray1.34A840-1132[»]
3ZMMX-ray2.51A/B835-1132[»]
4AQCX-ray1.90A/B835-1132[»]
4BBEX-ray1.90A/B/C/D839-1132[»]
4BBFX-ray2.00A/B/C/D839-1132[»]
4C61X-ray2.45A/B835-1132[»]
4C62X-ray2.75A/B835-1132[»]
4D0WX-ray1.77A835-1132[»]
4D0XX-ray1.82A835-1132[»]
4D1SX-ray1.66A835-1132[»]
4E4MX-ray2.25A/B/D/E833-1132[»]
4E6DX-ray2.22A/B835-1132[»]
4E6QX-ray1.95A/B835-1132[»]
4F08X-ray2.82A/B833-1132[»]
4F09X-ray2.40A833-1132[»]
4FVPX-ray2.01A536-812[»]
4FVQX-ray1.75A536-812[»]
4FVRX-ray2.00A536-812[»]
4GFMX-ray2.30A833-1132[»]
4GMYX-ray2.40A833-1132[»]
4HGEX-ray2.30A/B833-1132[»]
4IVAX-ray1.50A833-1132[»]
4JI9X-ray2.40A/B833-1132[»]
4JIAX-ray1.85A833-1132[»]
4P7EX-ray2.40A/B840-1132[»]
4YTCX-ray2.16A842-1132[»]
4YTFX-ray1.78A842-1132[»]
4YTHX-ray2.04A842-1132[»]
4YTIX-ray2.52A842-1132[»]
4Z32X-ray3.04A/B/C/D/E/F/G/H31-516[»]
4ZIMX-ray2.65A/B839-1132[»]
5AEPX-ray1.95A835-1132[»]
5CF4X-ray2.38A/B839-1132[»]
5CF5X-ray2.45A/B839-1132[»]
5CF6X-ray2.50A/B839-1132[»]
5CF8X-ray1.80A/B839-1132[»]
5HEZX-ray2.66A/B/C/D833-1132[»]
5I4NX-ray1.54A535-812[»]
5L3AX-ray1.98A840-1132[»]
5TQ3X-ray2.69A/B837-1132[»]
5TQ4X-ray2.30A837-1132[»]
5TQ5X-ray2.30A837-1132[»]
5TQ6X-ray2.06A/B837-1132[»]
5TQ7X-ray2.10A/B837-1132[»]
5TQ8X-ray1.59A837-1132[»]
5USYX-ray2.00A/B840-1132[»]
5USZX-ray2.10A536-812[»]
5UT0X-ray2.10A536-812[»]
5UT1X-ray1.95A536-812[»]
5UT2X-ray1.75A536-812[»]
5UT3X-ray1.50A536-812[»]
5UT4X-ray2.00A536-812[»]
5UT5X-ray1.90A536-812[»]
5UT6X-ray1.65A536-812[»]
5WEVX-ray1.85A833-1132[»]
5WIJX-ray2.04A536-812[»]
5WIKX-ray2.60B536-812[»]
5WILX-ray2.20A536-812[»]
5WIMX-ray2.55A536-812[»]
5WINX-ray2.38A536-812[»]
6AAJX-ray2.37A/B834-1132[»]
6BBVX-ray1.80A837-1132[»]
6BRWX-ray2.03A536-812[»]
6BS0X-ray1.54A536-812[»]
6BSSX-ray2.10A536-812[»]
6DRWX-ray2.30A840-1132[»]
6E2PX-ray2.83A/B36-514[»]
6E2QX-ray2.65A/B/C/D36-514[»]
6M9HX-ray1.79A536-812[»]
SMRiO60674
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109920, 110 interactors
ComplexPortaliCPX-382 Interleukin-12-receptor complex
CPX-383 Interleukin-23-receptor complex
CORUMiO60674
DIPiDIP-33880N
IntActiO60674, 35 interactors
MINTiO60674
STRINGi9606.ENSP00000371067

Chemistry databases

BindingDBiO60674
ChEMBLiCHEMBL2971
DrugBankiDB07162 4-(3-amino-1H-indazol-5-yl)-N-tert-butylbenzenesulfonamide
DB08067 4-[(2-{4-[(CYCLOPROPYLCARBAMOYL)AMINO]-1H-PYRAZOL-3-YL}-1H-BENZIMIDAZOL-6-YL)METHYL]MORPHOLIN-4-IUM
DB07161 5-phenyl-1H-indazol-3-amine
DB08877 Ruxolitinib
DB08895 Tofacitinib
DB05243 XL019
GuidetoPHARMACOLOGYi2048

PTM databases

iPTMnetiO60674
PhosphoSitePlusiO60674

Polymorphism and mutation databases

BioMutaiJAK2

Proteomic databases

EPDiO60674
jPOSTiO60674
MaxQBiO60674
PaxDbiO60674
PeptideAtlasiO60674
PRIDEiO60674
ProteomicsDBi49519

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		3717
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381652; ENSP00000371067; ENSG00000096968
GeneIDi3717
KEGGihsa:3717
UCSCiuc003ziw.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3717
DisGeNETi3717

GeneCards: human genes, protein and diseases

More...GeneCardsi		JAK2
HGNCiHGNC:6192 JAK2
HPAiCAB013089
HPA040820
HPA043870
MalaCardsiJAK2
MIMi147796 gene
254450 phenotype
263300 phenotype
600880 phenotype
601626 phenotype
614521 phenotype
neXtProtiNX_O60674
OpenTargetsiENSG00000096968
Orphaneti131 Budd-Chiari syndrome
3318 Essential thrombocythemia
71493 Familial thrombocytosis
729 Polycythemia vera
824 Primary myelofibrosis
PharmGKBiPA29989

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0197 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000155640
HOGENOMiHOG000049158
InParanoidiO60674
KOiK04447
OMAiSQLSYKH
OrthoDBi933071at2759
PhylomeDBiO60674
TreeFamiTF327041

Enzyme and pathway databases

BRENDAi2.7.10.2 2681
ReactomeiR-HSA-1059683 Interleukin-6 signaling
R-HSA-110056 MAPK3 (ERK1) activation
R-HSA-112411 MAPK1 (ERK2) activation
R-HSA-1170546 Prolactin receptor signaling
R-HSA-1433557 Signaling by SCF-KIT
R-HSA-2586552 Signaling by Leptin
R-HSA-3214858 RMTs methylate histone arginines
R-HSA-512988 Interleukin-3, Interleukin-5 and GM-CSF signaling
R-HSA-5673000 RAF activation
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-6788467 IL-6-type cytokine receptor ligand interactions
R-HSA-6802946 Signaling by moderate kinase activity BRAF mutants
R-HSA-6802949 Signaling by RAS mutants
R-HSA-6802952 Signaling by BRAF and RAF fusions
R-HSA-6802955 Paradoxical activation of RAF signaling by kinase inactive BRAF
R-HSA-69231 Cyclin D associated events in G1
R-HSA-877300 Interferon gamma signaling
R-HSA-877312 Regulation of IFNG signaling
R-HSA-8854691 Interleukin-20 family signaling
R-HSA-8984722 Interleukin-35 Signalling
R-HSA-9006335 Signaling by Erythropoietin
R-HSA-9020591 Interleukin-12 signaling
R-HSA-9020933 Interleukin-23 signaling
R-HSA-9020956 Interleukin-27 signaling
R-HSA-9027276 Erythropoietin activates Phosphoinositide-3-kinase (PI3K)
R-HSA-9027277 Erythropoietin activates Phospholipase C gamma (PLCG)
R-HSA-9027283 Erythropoietin activates STAT5
R-HSA-9027284 Erythropoietin activates RAS
R-HSA-912526 Interleukin receptor SHC signaling
R-HSA-982772 Growth hormone receptor signaling
R-HSA-983231 Factors involved in megakaryocyte development and platelet production
SignaLinkiO60674
SIGNORiO60674

Miscellaneous databases

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

More...ChiTaRSi		JAK2 human
EvolutionaryTraceiO60674

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Janus_kinase_2

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

More...GenomeRNAii		3717

Protein Ontology

More...PROi		PR:O60674

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000096968 Expressed in 212 organ(s), highest expression level in popliteal artery
ExpressionAtlasiO60674 baseline and differential
GenevisibleiO60674 HS

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...

<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_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: O60674
Secondary accession number(s): O14636, O75297
<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: December 15, 1998
Last sequence update: January 24, 2001
Last modified: May 8, 2019
This is version 212 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

3D-structure, Complete proteome, 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. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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