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Q62137 (JAK3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase JAK3

EC=2.7.10.2
Alternative name(s):
Janus kinase 3
Short name=JAK-3
Gene names
Name:Jak3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1100 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-receptor tyrosine kinase involved in various processes such as cell growth, development, or differentiation. Mediates essential signaling events in both innate and adaptive immunity and plays a crucial role in hematopoiesis during T-cells development. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors sharing the common subunit gamma such as IL2R, IL4R, IL7R, IL9R, IL15R and IL21R. 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, upon IL2R activation by IL2, JAK1 and JAK3 molecules bind to IL2R beta (IL2RB) and gamma chain (IL2RG) subunits inducing the tyrosine phosphorylation of both receptor subunits on their cytoplasmic domain. Then, STAT5A AND STAT5B are recruited, phosphorylated and activated by JAK1 and JAK3. Once activated, dimerized STAT5 translocates to the nucleus and promotes the transcription of specific target genes in a cytokine-specific fashion. Ref.8

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Subunit structure

Interacts with STAM2 and MYO18A. Interacts with SHB By similarity. Ref.10

Subcellular location

Endomembrane system; Peripheral membrane protein By similarity. Cytoplasm By similarity.

Tissue specificity

In contrast with the ubiquitous expression of the other JAKs, JAK3 is predominantly expressed in hematopoietic tissues. Ref.2

Domain

Possesses two phosphotransferase domains. The second one contains the catalytic domain, while the presence of a pseudokinase domain is required for suppression of basal activity of JAK3.

Post-translational modification

Autophosphorylated, leading to regulate its activity. IL2 promotes phosphorylation on tyrosine residues, including autophosphorylation on Tyr-781 By similarity. Dephosphorylation of Tyr-976 and Tyr-977 by PTPN2 negatively regulates cytokine-mediated signaling By similarity.

Disruption phenotype

Mice show a severe block in B-cell development at the pre-B stage in the bone marrow. Additionally, they possesses small thymuses revealing a defect in T-cell development. The distribution of developmental subsets is relatively normal, suggesting a block in the expansion of early T-cell progenitors. Peripheral T-cells are present at normal or increased numbers but are functionally incompetent. Ref.6 Ref.7 Ref.9

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. JAK subfamily.

Contains 1 FERM domain.

Contains 2 protein kinase domains.

Contains 1 SH2 domain.

Sequence caution

The sequence AAA21415.1 differs from that shown. Reason: Frameshift at several positions.

The sequence AAA21565.1 differs from that shown. Reason: Frameshift at positions 222 and 232.

Ontologies

Keywords
   Biological processAdaptive immunity
Immunity
Innate immunity
   Cellular componentCytoplasm
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
SH2 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Inferred from mutant phenotype PubMed 9498750. Source: BHF-UCL

T cell homeostasis

Inferred from mutant phenotype PubMed 9498750. Source: BHF-UCL

cytokine-mediated signaling pathway

Inferred from direct assay Ref.3. Source: MGI

enzyme linked receptor protein signaling pathway

Inferred from direct assay Ref.3. Source: MGI

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

interleukin-4-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

intracellular signal transduction

Inferred from direct assay Ref.3. Source: MGI

lymph node development

Traceable author statement PubMed 10687308. Source: MGI

negative regulation of FasL biosynthetic process

Inferred from mutant phenotype PubMed 9498750. Source: BHF-UCL

negative regulation of T cell activation

Inferred from mutant phenotype PubMed 9498750. Source: BHF-UCL

negative regulation of T-helper 1 cell differentiation

Inferred from mutant phenotype PubMed 16020505. Source: BHF-UCL

negative regulation of dendritic cell cytokine production

Inferred from mutant phenotype PubMed 16020505. Source: BHF-UCL

negative regulation of interleukin-10 production

Inferred from mutant phenotype PubMed 16020505. Source: BHF-UCL

negative regulation of interleukin-12 production

Inferred from mutant phenotype PubMed 16020505. Source: BHF-UCL

negative regulation of thymocyte apoptotic process

Inferred from mutant phenotype PubMed 9973401. Source: BHF-UCL

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 10872802. Source: MGI

positive regulation of T cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of activated T cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of calcium ion transport

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cytosolic calcium ion concentration

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of dendritic cell apoptotic process

Inferred from mutant phenotype PubMed 16020505. Source: BHF-UCL

positive regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from mutant phenotype PubMed 16020505. Source: BHF-UCL

positive regulation of immune response

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 10485657. Source: MGI

protein autophosphorylation

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of T cell apoptotic process

Inferred from mutant phenotype PubMed 9498750. Source: BHF-UCL

response to interleukin-15

Traceable author statement PubMed 7594533. Source: BHF-UCL

response to interleukin-2

Traceable author statement PubMed 9973401. Source: BHF-UCL

response to interleukin-4

Inferred from sequence or structural similarity. Source: BHF-UCL

response to interleukin-9

Traceable author statement PubMed 7594533. Source: BHF-UCL

tyrosine phosphorylation of Stat5 protein

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: BHF-UCL

cytoskeleton

Inferred from electronic annotation. Source: InterPro

cytosol

Traceable author statement. Source: Reactome

endomembrane system

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular

Inferred by curator PubMed 10872802. Source: BHF-UCL

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein tyrosine kinase activity

Inferred from direct assay PubMed 10872802Ref.3. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q62137-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q62137-2)

The sequence of this isoform differs from the canonical sequence as follows:
     284-284: E → EVLGLGLRSG...RRYCLSFLPQ
     379-379: L → LGASWGQQWGWGWAARTVLGWTWLLSWPRL
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11001100Tyrosine-protein kinase JAK3
PRO_0000088116

Regions

Domain24 – 353330FERM
Domain372 – 472101SH2; atypical
Domain517 – 777261Protein kinase 1
Domain818 – 1100283Protein kinase 2
Nucleotide binding824 – 8329ATP By similarity
Region1 – 223223Interaction with cytokine/interferon/growth hormone receptors By similarity

Sites

Active site9451Proton acceptor By similarity
Binding site8511ATP By similarity

Amino acid modifications

Modified residue7811Phosphotyrosine; by autocatalysis By similarity
Modified residue9001Phosphotyrosine By similarity
Modified residue9351Phosphotyrosine By similarity
Modified residue9761Phosphotyrosine; by autocatalysis By similarity
Modified residue9771Phosphotyrosine; by autocatalysis By similarity

Natural variations

Alternative sequence2841E → EVLGLGLRSGVRGEAWRLVK KPVRTIRKVASPGRADCTTG QGGGVNLKVGPGMELPQGLT WGVTRRVRLDRGRGRTEGDS MDWISGHDPTRPVFSPLTSS PPPHKWRWEGGRRGGCAGSR SVIPWLLSLFLFFFFNGFAR QGFSYSSGCPGTHFVRPGWP RTQKSACLCLSSAVIKGRVP LRRYCLSFLPQ in isoform 2.
VSP_027575
Alternative sequence3791L → LGASWGQQWGWGWAARTVLG WTWLLSWPRL in isoform 2.
VSP_027576

Experimental info

Mutagenesis8531L → R: Loss of activity. Ref.2
Sequence conflict621G → A in AAA21415. Ref.1
Sequence conflict621G → A in AAA21565. Ref.2
Sequence conflict2771S → P in AAA21565. Ref.2
Sequence conflict281 – 2833GDQ → ND in AAA21565. Ref.2
Sequence conflict3011K → N in AAA21565. Ref.2
Sequence conflict3621P → A in AAA21415. Ref.1
Sequence conflict371 – 3722EL → DV in AAA21565. Ref.2
Sequence conflict3901G → A in AAA21415. Ref.1
Sequence conflict4541Missing in BAC40305. Ref.4
Sequence conflict4671N → Y in AAA21565. Ref.2
Sequence conflict4901T → N in AAA21565. Ref.2
Sequence conflict518 – 5192EW → G in AAA21415. Ref.1
Sequence conflict5351R → S in AAA21565. Ref.2
Sequence conflict6991C → G in BAC40305. Ref.4
Sequence conflict6991C → G in BAC29956. Ref.4
Sequence conflict6991C → G in BAE24964. Ref.4
Sequence conflict6991C → G in BAE33790. Ref.4
Sequence conflict6991C → G in BAE37819. Ref.4
Sequence conflict716 – 7172SG → QR in AAA21565. Ref.2
Sequence conflict8001G → VA in AAA21565. Ref.2
Sequence conflict8261K → N in AAI31647. Ref.5
Sequence conflict8411Missing in AAA21415. Ref.1
Sequence conflict8571G → V in AAA21565. Ref.2
Sequence conflict9091F → L in AAA21565. Ref.2
Sequence conflict915 – 9162AR → G in AAA21565. Ref.2
Sequence conflict9161R → A in AAA21415. Ref.1
Sequence conflict10321R → S in BAC40305. Ref.4
Sequence conflict10321R → S in BAC29956. Ref.4
Sequence conflict10321R → S in BAE24964. Ref.4
Sequence conflict10321R → S in BAE33790. Ref.4
Sequence conflict10321R → S in BAE37819. Ref.4
Sequence conflict10741W → V in AAA21415. Ref.1
Sequence conflict10771S → E in AAA21565. Ref.2
Sequence conflict10851G → A in AAA21565. Ref.2
Sequence conflict10931A → G in AAA21415. Ref.1
Sequence conflict10931A → P in AAA21565. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 21, 2007. Version 2.
Checksum: 979A120861ED37C1

FASTA1,100122,641
        10         20         30         40         50         60 
MAPPSEETPL IPQRSCSLSS SEAGALHVLL PPRGPGPPQR LSFSFGDYLA EDLCVRAAKA 

        70         80         90        100        110        120 
CGILPVYHSL FALATEDFSC WFPPSHIFCI EDVDTQVLVY RLRFYFPDWF GLETCHRFGL 

       130        140        150        160        170        180 
RKDLTSAILD LHVLEHLFAQ HRSDLVSGRL PVGLSMKEQG EFLSLAVLDL AQMAREQAQR 

       190        200        210        220        230        240 
PGELLKTVSY KACLPPSLRD VIQGQNFVTR RRIRRTVVLA LRRVVACQAD RYALMAKYIL 

       250        260        270        280        290        300 
DLERLHPAAT TETFRVGLPG AQEEPGLLRV AGDNGISWSS GDQELFQTFC DFPEIVDVSI 

       310        320        330        340        350        360 
KQAPRVGPAG EHRLVTVTRM DGHILEAEFP GLPEALSFVA LVDGYFRLIC DSRHYFCKEV 

       370        380        390        400        410        420 
APPRLLEEEA ELCHGPITLD FAIHKLKAAG SLPGTYILRR SPQDYDSFLL TACVQTPLGP 

       430        440        450        460        470        480 
DYKGCLIRQD PSGAFSLVGL SQPHRSLREL LAACWNSGLR VDGAALNLTS CCAPRPKEKS 

       490        500        510        520        530        540 
NLIVVRRGCT PAPAPGCSPS CCALTQLSFH TIPTDSLEWH ENLGHGSFTK IFRGRRREVV 

       550        560        570        580        590        600 
DGETHDSEVL LKVMDSRHRN CMESFLEAAS LMSQVSYPHL VLLHGVCMAG DSIMVQEFVY 

       610        620        630        640        650        660 
LGAIDMYLRK RGHLVSASWK LQVTKQLAYA LNYLEDKGLP HGNVSARKVL LAREGGDGNP 

       670        680        690        700        710        720 
PFIKLSDPGV SPTVLSLEML TDRIPWVAPE CLQEAQTLCL EADKWGFGAT TWEVFSGGPA 

       730        740        750        760        770        780 
HITSLEPAKK LKFYEDQGQL PALKWTELAG LITQCMAYDP GRRPSFRAIL RDLNGLITSD 

       790        800        810        820        830        840 
YELLSDPTPG IPSPRDELCG GAQLYACQDP AIFEERHLKY ISLLGKGNFG SVELCRYDPL 

       850        860        870        880        890        900 
GDNTGPLVAV KQLQHSGPDQ QRDFQREIQI LKALHSDFIV KYRGVSYGPG RQSLRLVMEY 

       910        920        930        940        950        960 
LPSGCLRDFL QRHRARLHTD RLLLFAWQIC KGMEYLGARR CVHRDLAARN ILVESEAHVK 

       970        980        990       1000       1010       1020 
IADFGLAKLL PLGKDYYVVR EPGQSPIFWY APESLSDNIF SRQSDVWSFG VVLYELFTYC 

      1030       1040       1050       1060       1070       1080 
DKSCSPSAEF LRMMGPEREG PPLCRLLELL AEGRRLPPPP TCPTEVQELM QLCWAPSPHD 

      1090       1100 
RPAFGTLSPQ LDALWRGRPG 

« Hide

Isoform 2 [UniParc].

Checksum: CC2DDD3C6F824439
Show »

FASTA1,319146,899

References

« Hide 'large scale' references
[1]"JAK3: a novel JAK kinase associated with terminal differentiation of hematopoietic cells."
Rane S.G., Reddy E.P.
Oncogene 9:2415-2423(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Murine JAK3 is preferentially expressed in hematopoietic tissues and lymphocyte precursor cells."
Gurniak C.B., Berg L.J.
Blood 87:3151-3160(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, MUTAGENESIS OF LEU-853.
Strain: BALB/C X 129.
Tissue: Thymus.
[3]"Involvement of the Jak-3 Janus kinase in signalling by interleukins 2 and 4 in lymphoid and myeloid cells."
Witthuhn B.A., Silvennoinen O., Miura O., Lai K.S., Cwik C., Liu E.T., Ihle J.N.
Nature 370:153-157(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: BALB/c.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J and NOD.
Tissue: Heart, Spleen and Thymus.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: FVB/N.
Tissue: Mammary tumor.
[6]"Defects in B lymphocyte maturation and T lymphocyte activation in mice lacking Jak3."
Thomis D.C., Gurniak C.B., Tivol E., Sharpe A.H., Berg L.J.
Science 270:794-797(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[7]"Defective lymphoid development in mice lacking Jak3."
Nosaka T., van Deursen J.M., Tripp R.A., Thierfelder W.E., Witthuhn B.A., McMickle A.P., Doherty P.C., Grosveld G.C., Ihle J.N.
Science 270:800-802(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[8]"Peripheral expression of Jak3 is required to maintain T lymphocyte function."
Thomis D.C., Berg L.J.
J. Exp. Med. 185:197-206(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"T cell development and activation in Jak3-deficient mice."
Baird A.M., Thomis D.C., Berg L.J.
J. Leukoc. Biol. 63:669-677(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[10]"A novel protein MAJN binds to Jak3 and inhibits apoptosis induced by IL-2 deprival."
Ji H., Zhai Q., Zhu J., Yan M., Sun L., Liu X., Zheng Z.
Biochem. Biophys. Res. Commun. 270:267-271(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYO18A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L33768 mRNA. Translation: AAA21415.1. Frameshift.
L40172 mRNA. Translation: AAC42085.1.
L32955 mRNA. Translation: AAA21565.1. Frameshift.
AK038268 mRNA. Translation: BAC29956.1.
AK142178 mRNA. Translation: BAE24964.1.
AK156646 mRNA. Translation: BAE33790.1.
AK164520 mRNA. Translation: BAE37819.1.
AK088365 mRNA. Translation: BAC40305.1.
BC105577 mRNA. Translation: AAI05578.1.
BC131646 mRNA. Translation: AAI31647.1.
BC131647 mRNA. Translation: AAI31648.1.
PIRI58401.
S48053.
RefSeqNP_001177759.1. NM_001190830.1.
NP_034719.2. NM_010589.6.
UniGeneMm.249645.
Mm.476857.

3D structure databases

ProteinModelPortalQ62137.
SMRQ62137. Positions 360-1094.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200858. 5 interactions.
IntActQ62137. 2 interactions.
MINTMINT-1523453.

Chemistry

BindingDBQ62137.
ChEMBLCHEMBL5250.

PTM databases

PhosphoSiteQ62137.

Proteomic databases

PRIDEQ62137.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000051995; ENSMUSP00000060073; ENSMUSG00000031805.
ENSMUST00000110012; ENSMUSP00000105639; ENSMUSG00000031805.
ENSMUST00000110013; ENSMUSP00000105640; ENSMUSG00000031805.
GeneID16453.
KEGGmmu:16453.
UCSCuc009mel.2. mouse. [Q62137-1]

Organism-specific databases

CTD3718.
MGIMGI:99928. Jak3.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00710000106680.
HOVERGENHBG006195.
KOK11218.
OrthoDBEOG7BW0HM.
PhylomeDBQ62137.
TreeFamTF327041.

Enzyme and pathway databases

BRENDA2.7.10.2. 3474.
ReactomeREACT_98458. Immune System.

Gene expression databases

BgeeQ62137.
CleanExMM_JAK3.
GenevestigatorQ62137.

Family and domain databases

InterProIPR019749. Band_41_domain.
IPR000299. FERM_domain.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016251. Tyr_kinase_non-rcpt_Jak/Tyk2.
IPR020775. Tyr_kinase_non-rcpt_Jak3.
[Graphical view]
PfamPF07714. Pkinase_Tyr. 2 hits.
[Graphical view]
PIRSFPIRSF000636. TyrPK_Jak. 1 hit.
PRINTSPR01823. JANUSKINASE.
PR01826. JANUSKINASE3.
PR00109. TYRKINASE.
SMARTSM00295. B41. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 2 hits.
[Graphical view]
SUPFAMSSF55550. SSF55550. 2 hits.
SSF56112. SSF56112. 2 hits.
PROSITEPS50057. FERM_3. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio289723.
PROQ62137.
SOURCESearch...

Entry information

Entry nameJAK3_MOUSE
AccessionPrimary (citable) accession number: Q62137
Secondary accession number(s): A2RRI3 expand/collapse secondary AC list , Q0D2M8, Q61746, Q61747, Q8BTY6, Q8BYU2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 21, 2007
Last modified: April 16, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot