Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 185 (12 Aug 2020)
Sequence version 1 (01 Nov 1997)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Tyrosine-protein kinase JAK2

Gene

Jak2

Organism
Rattus norvegicus (Rat)
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.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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%5Fsection">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. Heme regulates its activity by enhancing the phosphorylation on Tyr-1007 and Tyr-1008.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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%5Fsection">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%5Fsection">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

GO - Biological processi

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

Molecular 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, 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-1059683, Interleukin-6 signaling
R-RNO-110056, MAPK3 (ERK1) activation
R-RNO-112411, MAPK1 (ERK2) activation
R-RNO-1170546, Prolactin receptor signaling
R-RNO-1433557, Signaling by SCF-KIT
R-RNO-512988, Interleukin-3, Interleukin-5 and GM-CSF signaling
R-RNO-5673000, RAF activation
R-RNO-5673001, RAF/MAP kinase cascade
R-RNO-6785807, Interleukin-4 and Interleukin-13 signaling
R-RNO-6788467, IL-6-type cytokine receptor ligand interactions
R-RNO-69231, Cyclin D associated events in G1
R-RNO-877300, Interferon gamma signaling
R-RNO-877312, Regulation of IFNG signaling
R-RNO-8854691, Interleukin-20 family signaling
R-RNO-8984722, Interleukin-35 Signalling
R-RNO-9020591, Interleukin-12 signaling
R-RNO-9020933, Interleukin-23 signaling
R-RNO-9020956, Interleukin-27 signaling
R-RNO-9027276, Erythropoietin activates Phosphoinositide-3-kinase (PI3K)
R-RNO-9027284, Erythropoietin activates RAS
R-RNO-912526, Interleukin receptor SHC signaling
R-RNO-982772, Growth hormone receptor signaling
R-RNO-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%5Fand%5Ftaxonomy%5Fsection">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:2.7.10.2)
Alternative name(s):
Janus kinase 2
Short name:
JAK-2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 1

Organism-specific databases

Rat genome database

More...
RGDi
2939, 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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1075225

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000881141 – 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 residuei523PhosphoserineCombined sources1
Modified residuei570PhosphotyrosineBy similarity1
Modified residuei813PhosphotyrosineBy similarity1
Modified residuei868Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei966Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei972Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1007Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1008Phosphotyrosine; by autocatalysisBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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. Autophosphorylation on Tyr-119 in response to EPO down-regulates its kinase activity. Autophosphorylation on Tyr-868, Tyr-966 and Tyr-972 in response to growth hormone (GH) are required for maximal kinase activity. Also phosphorylated by TEC (By similarity). Phosphorylated on tyrosine residues in response to interferon gamma signaling. Phosphorylated on tyrosine residues in response to a signaling cascade that is activated by increased cellular retinol (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...
PaxDbi
Q62689

PRoteomics IDEntifications database

More...
PRIDEi
Q62689

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q62689

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

More...
PhosphoSitePlusi
Q62689

<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
ENSRNOG00000059968, Expressed in thymus and 21 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q62689, RN

<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%5Fsection">'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%5Fsection">'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.

Interacts with LYN.

Interacts with SIRPA.

Interacts with SH2B1.

Interacts with TEC (By similarity).

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

Interacts with LEPR (Isoform B) (By similarity).

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

Interacts with STRA6 (By similarity).

By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
246670, 9 interactors

Database of interacting proteins

More...
DIPi
DIP-491N

Protein interaction database and analysis system

More...
IntActi
Q62689, 3 interactors

Molecular INTeraction database

More...
MINTi
Q62689

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000021218

<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
Q62689

Database of comparative protein structure models

More...
ModBasei
Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">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 – 1126Protein kinase 2PROSITE-ProRule annotationAdd BLAST278

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

The N-terminal domain of JAKs mediates their interaction with cytokine/interferon/growth hormone receptors. 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

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155640

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_008155_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q62689

KEGG Orthology (KO)

More...
KOi
K04447

Identification of Orthologs from Complete Genome Data

More...
OMAi
HIFHVDE

Database of Orthologous Groups

More...
OrthoDBi
58906at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q62689

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%5Flength">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q62689-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGMACLTMTE MEGTSTSPAH QNGDIPGNAN SVKQTEPVLQ VYLYHSLGQA
60 70 80 90 100
EGDYLKFPNG EYVAEEICVA ASKACGITPV YHNMFALMSE TERIWYPPNH
110 120 130 140 150
VFHIDESTRH NILYRIRFYF PHWYCSGSNR TYRYGVSRGA EAPLLDDFVM
160 170 180 190 200
SYLFAQWRHD FVHGWIKVPV THETQEECLG MAVLDMMRIA KEKDQTPLAV
210 220 230 240 250
YNSISYKTFL PKCVRAKIQD YHILTRKRIR YRFRRFIQQF SQCKATARNL
260 270 280 290 300
KLKYLINLET LQSAFYTEQF EVKESARGPS GEEIFATIII TGNGGIQWSR
310 320 330 340 350
GKHKESETLT EQDLQLYCDF PDIIDVSIKQ ANQECSTESR VVTVHKQDGK
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 FSSLKDLLNC YQMETVRSDS IIFQFTKCCP
510 520 530 540 550
PKPKDKSNLL VFRTNGVSDV QLSPTLQRHN NVNQMVFHKI RNEDLIFNES
560 570 580 590 600
LGQGTFTKIF KGVRREVGDY GQLHETEVLL KVLDKAHRNY SESFFEAASM
610 620 630 640 650
MSQLSHKHLV LNYGVCVCGE ENILVQEFVK FGSLDTYLKK NKNSINILWK
660 670 680 690 700
LGVAKQLAWA MHFLEEKSLI HGNVCAKNIL LIREEDRKTG NPPFIKLSDP
710 720 730 740 750
GISITVLPKD ILQERIPWVP PECIENPKNL TLATDKWSFG TTLWEICSGG
760 770 780 790 800
DKPLSALDSQ RKLQFYEDKH QLPAPKWTEL ANLINTCMDY 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 LLKNNGRLPR PEGCPDEIYV
1110 1120 1130
IMTECWNNNV NQRPSFRDLS LRVDQIRDSM AA
Length:1,132
Mass (Da):130,585
Last modified:November 1, 1997 - v1
<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:iC3AEDF2FECE8B95A
GO

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
U13396 mRNA Translation: AAA79911.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JC4127

NCBI Reference Sequences

More...
RefSeqi
NP_113702.1, NM_031514.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000087011; ENSRNOP00000071877; ENSRNOG00000059968

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
24514

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:24514

UCSC genome browser

More...
UCSCi
RGD:2939, rat

<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
U13396 mRNA Translation: AAA79911.1
PIRiJC4127
RefSeqiNP_113702.1, NM_031514.1

3D structure databases

SMRiQ62689
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi246670, 9 interactors
DIPiDIP-491N
IntActiQ62689, 3 interactors
MINTiQ62689
STRINGi10116.ENSRNOP00000021218

Chemistry databases

ChEMBLiCHEMBL1075225

PTM databases

iPTMnetiQ62689
PhosphoSitePlusiQ62689

Proteomic databases

PaxDbiQ62689
PRIDEiQ62689

Genome annotation databases

EnsembliENSRNOT00000087011; ENSRNOP00000071877; ENSRNOG00000059968
GeneIDi24514
KEGGirno:24514
UCSCiRGD:2939, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3717
RGDi2939, Jak2

Phylogenomic databases

eggNOGiKOG0197, Eukaryota
GeneTreeiENSGT00940000155640
HOGENOMiCLU_008155_1_0_1
InParanoidiQ62689
KOiK04447
OMAiHIFHVDE
OrthoDBi58906at2759
PhylomeDBiQ62689

Enzyme and pathway databases

BRENDAi2.7.10.2, 5301
ReactomeiR-RNO-1059683, Interleukin-6 signaling
R-RNO-110056, MAPK3 (ERK1) activation
R-RNO-112411, MAPK1 (ERK2) activation
R-RNO-1170546, Prolactin receptor signaling
R-RNO-1433557, Signaling by SCF-KIT
R-RNO-512988, Interleukin-3, Interleukin-5 and GM-CSF signaling
R-RNO-5673000, RAF activation
R-RNO-5673001, RAF/MAP kinase cascade
R-RNO-6785807, Interleukin-4 and Interleukin-13 signaling
R-RNO-6788467, IL-6-type cytokine receptor ligand interactions
R-RNO-69231, Cyclin D associated events in G1
R-RNO-877300, Interferon gamma signaling
R-RNO-877312, Regulation of IFNG signaling
R-RNO-8854691, Interleukin-20 family signaling
R-RNO-8984722, Interleukin-35 Signalling
R-RNO-9020591, Interleukin-12 signaling
R-RNO-9020933, Interleukin-23 signaling
R-RNO-9020956, Interleukin-27 signaling
R-RNO-9027276, Erythropoietin activates Phosphoinositide-3-kinase (PI3K)
R-RNO-9027284, Erythropoietin activates RAS
R-RNO-912526, Interleukin receptor SHC signaling
R-RNO-982772, Growth hormone receptor signaling
R-RNO-983231, Factors involved in megakaryocyte development and platelet production

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q62689

Gene expression databases

BgeeiENSRNOG00000059968, Expressed in thymus and 21 other tissues
GenevisibleiQ62689, RN

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_RAT
<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: Q62689
<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%5Fand%5Fisoforms">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: November 1, 1997
Last modified: August 12, 2020
This is version 185 of the entry and version 1 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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