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Q62137

- JAK3_MOUSE

UniProt

Q62137 - JAK3_MOUSE

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Protein
Tyrosine-protein kinase JAK3
Gene
Jak3
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei851 – 8511ATP By similarity
Active sitei945 – 9451Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi824 – 8329ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  3. protein binding Source: MGI
  4. protein tyrosine kinase activity Source: MGI

GO - Biological processi

  1. B cell differentiation Source: BHF-UCL
  2. T cell homeostasis Source: BHF-UCL
  3. cytokine-mediated signaling pathway Source: MGI
  4. enzyme linked receptor protein signaling pathway Source: MGI
  5. innate immune response Source: UniProtKB-KW
  6. interleukin-4-mediated signaling pathway Source: Ensembl
  7. intracellular signal transduction Source: MGI
  8. lymph node development Source: MGI
  9. negative regulation of FasL biosynthetic process Source: BHF-UCL
  10. negative regulation of T cell activation Source: BHF-UCL
  11. negative regulation of T-helper 1 cell differentiation Source: BHF-UCL
  12. negative regulation of dendritic cell cytokine production Source: BHF-UCL
  13. negative regulation of interleukin-10 production Source: BHF-UCL
  14. negative regulation of interleukin-12 production Source: BHF-UCL
  15. negative regulation of thymocyte apoptotic process Source: BHF-UCL
  16. peptidyl-tyrosine phosphorylation Source: MGI
  17. positive regulation of T cell proliferation Source: BHF-UCL
  18. positive regulation of activated T cell proliferation Source: BHF-UCL
  19. positive regulation of calcium ion transport Source: BHF-UCL
  20. positive regulation of cytosolic calcium ion concentration Source: BHF-UCL
  21. positive regulation of dendritic cell apoptotic process Source: BHF-UCL
  22. positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
  23. positive regulation of immune response Source: BHF-UCL
  24. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  25. protein autophosphorylation Source: BHF-UCL
  26. regulation of T cell apoptotic process Source: BHF-UCL
  27. response to interleukin-15 Source: BHF-UCL
  28. response to interleukin-2 Source: BHF-UCL
  29. response to interleukin-4 Source: BHF-UCL
  30. response to interleukin-9 Source: BHF-UCL
  31. tyrosine phosphorylation of Stat5 protein Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Adaptive immunity, Immunity, Innate immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiREACT_198701. Interleukin-7 signaling.
REACT_210793. Interleukin receptor SHC signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase JAK3 (EC:2.7.10.2)
Alternative name(s):
Janus kinase 3
Short name:
JAK-3
Gene namesi
Name:Jak3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:99928. Jak3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytoskeleton Source: InterPro
  3. cytosol Source: Reactome
  4. endomembrane system Source: UniProtKB-SubCell
  5. intracellular Source: BHF-UCL
  6. membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

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.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi853 – 8531L → R: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11001100Tyrosine-protein kinase JAK3
PRO_0000088116Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei781 – 7811Phosphotyrosine; by autocatalysis By similarity
Modified residuei900 – 9001Phosphotyrosine By similarity
Modified residuei935 – 9351Phosphotyrosine By similarity
Modified residuei976 – 9761Phosphotyrosine; by autocatalysis By similarity
Modified residuei977 – 9771Phosphotyrosine; by autocatalysis By similarity

Post-translational modificationi

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.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ62137.

PTM databases

PhosphoSiteiQ62137.

Expressioni

Tissue specificityi

In contrast with the ubiquitous expression of the other JAKs, JAK3 is predominantly expressed in hematopoietic tissues.1 Publication

Gene expression databases

BgeeiQ62137.
CleanExiMM_JAK3.
GenevestigatoriQ62137.

Interactioni

Subunit structurei

Interacts with STAM2 and MYO18A. Interacts with SHB By similarity.1 Publication

Protein-protein interaction databases

BioGridi200858. 5 interactions.
IntActiQ62137. 2 interactions.
MINTiMINT-1523453.

Structurei

3D structure databases

ProteinModelPortaliQ62137.
SMRiQ62137. Positions 24-1094.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 353330FERM
Add
BLAST
Domaini372 – 472101SH2; atypical
Add
BLAST
Domaini517 – 777261Protein kinase 1
Add
BLAST
Domaini818 – 1100283Protein kinase 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 223223Interaction with cytokine/interferon/growth hormone receptors By similarity
Add
BLAST

Domaini

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.

Sequence similaritiesi

Contains 1 FERM domain.
Contains 1 SH2 domain.

Keywords - Domaini

Repeat, SH2 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00710000106680.
HOVERGENiHBG006195.
KOiK11218.
OrthoDBiEOG7BW0HM.
PhylomeDBiQ62137.
TreeFamiTF327041.

Family and domain databases

InterProiIPR019749. 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]
PfamiPF07714. Pkinase_Tyr. 2 hits.
[Graphical view]
PIRSFiPIRSF000636. TyrPK_Jak. 1 hit.
PRINTSiPR01823. JANUSKINASE.
PR01826. JANUSKINASE3.
PR00109. TYRKINASE.
SMARTiSM00295. B41. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 2 hits.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 2 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50057. FERM_3. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q62137-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAPPSEETPL IPQRSCSLSS SEAGALHVLL PPRGPGPPQR LSFSFGDYLA     50
EDLCVRAAKA CGILPVYHSL FALATEDFSC WFPPSHIFCI EDVDTQVLVY 100
RLRFYFPDWF GLETCHRFGL RKDLTSAILD LHVLEHLFAQ HRSDLVSGRL 150
PVGLSMKEQG EFLSLAVLDL AQMAREQAQR PGELLKTVSY KACLPPSLRD 200
VIQGQNFVTR RRIRRTVVLA LRRVVACQAD RYALMAKYIL DLERLHPAAT 250
TETFRVGLPG AQEEPGLLRV AGDNGISWSS GDQELFQTFC DFPEIVDVSI 300
KQAPRVGPAG EHRLVTVTRM DGHILEAEFP GLPEALSFVA LVDGYFRLIC 350
DSRHYFCKEV APPRLLEEEA ELCHGPITLD FAIHKLKAAG SLPGTYILRR 400
SPQDYDSFLL TACVQTPLGP DYKGCLIRQD PSGAFSLVGL SQPHRSLREL 450
LAACWNSGLR VDGAALNLTS CCAPRPKEKS NLIVVRRGCT PAPAPGCSPS 500
CCALTQLSFH TIPTDSLEWH ENLGHGSFTK IFRGRRREVV DGETHDSEVL 550
LKVMDSRHRN CMESFLEAAS LMSQVSYPHL VLLHGVCMAG DSIMVQEFVY 600
LGAIDMYLRK RGHLVSASWK LQVTKQLAYA LNYLEDKGLP HGNVSARKVL 650
LAREGGDGNP PFIKLSDPGV SPTVLSLEML TDRIPWVAPE CLQEAQTLCL 700
EADKWGFGAT TWEVFSGGPA HITSLEPAKK LKFYEDQGQL PALKWTELAG 750
LITQCMAYDP GRRPSFRAIL RDLNGLITSD YELLSDPTPG IPSPRDELCG 800
GAQLYACQDP AIFEERHLKY ISLLGKGNFG SVELCRYDPL GDNTGPLVAV 850
KQLQHSGPDQ QRDFQREIQI LKALHSDFIV KYRGVSYGPG RQSLRLVMEY 900
LPSGCLRDFL QRHRARLHTD RLLLFAWQIC KGMEYLGARR CVHRDLAARN 950
ILVESEAHVK IADFGLAKLL PLGKDYYVVR EPGQSPIFWY APESLSDNIF 1000
SRQSDVWSFG VVLYELFTYC DKSCSPSAEF LRMMGPEREG PPLCRLLELL 1050
AEGRRLPPPP TCPTEVQELM QLCWAPSPHD RPAFGTLSPQ LDALWRGRPG 1100
Length:1,100
Mass (Da):122,641
Last modified:August 21, 2007 - v2
Checksum:i979A120861ED37C1
GO
Isoform 2 (identifier: Q62137-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,319
Mass (Da):146,899
Checksum:iCC2DDD3C6F824439
GO

Sequence cautioni

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei284 – 2841E → EVLGLGLRSGVRGEAWRLVK KPVRTIRKVASPGRADCTTG QGGGVNLKVGPGMELPQGLT WGVTRRVRLDRGRGRTEGDS MDWISGHDPTRPVFSPLTSS PPPHKWRWEGGRRGGCAGSR SVIPWLLSLFLFFFFNGFAR QGFSYSSGCPGTHFVRPGWP RTQKSACLCLSSAVIKGRVP LRRYCLSFLPQ in isoform 2.
VSP_027575
Alternative sequencei379 – 3791L → LGASWGQQWGWGWAARTVLG WTWLLSWPRL in isoform 2.
VSP_027576

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621G → A in AAA21415. 1 Publication
Sequence conflicti62 – 621G → A in AAA21565. 1 Publication
Sequence conflicti277 – 2771S → P in AAA21565. 1 Publication
Sequence conflicti281 – 2833GDQ → ND in AAA21565. 1 Publication
Sequence conflicti301 – 3011K → N in AAA21565. 1 Publication
Sequence conflicti362 – 3621P → A in AAA21415. 1 Publication
Sequence conflicti371 – 3722EL → DV in AAA21565. 1 Publication
Sequence conflicti390 – 3901G → A in AAA21415. 1 Publication
Sequence conflicti454 – 4541Missing in BAC40305. 1 Publication
Sequence conflicti467 – 4671N → Y in AAA21565. 1 Publication
Sequence conflicti490 – 4901T → N in AAA21565. 1 Publication
Sequence conflicti518 – 5192EW → G in AAA21415. 1 Publication
Sequence conflicti535 – 5351R → S in AAA21565. 1 Publication
Sequence conflicti699 – 6991C → G in BAC40305. 1 Publication
Sequence conflicti699 – 6991C → G in BAC29956. 1 Publication
Sequence conflicti699 – 6991C → G in BAE24964. 1 Publication
Sequence conflicti699 – 6991C → G in BAE33790. 1 Publication
Sequence conflicti699 – 6991C → G in BAE37819. 1 Publication
Sequence conflicti716 – 7172SG → QR in AAA21565. 1 Publication
Sequence conflicti800 – 8001G → VA in AAA21565. 1 Publication
Sequence conflicti826 – 8261K → N in AAI31647. 1 Publication
Sequence conflicti841 – 8411Missing in AAA21415. 1 Publication
Sequence conflicti857 – 8571G → V in AAA21565. 1 Publication
Sequence conflicti909 – 9091F → L in AAA21565. 1 Publication
Sequence conflicti915 – 9162AR → G in AAA21565. 1 Publication
Sequence conflicti916 – 9161R → A in AAA21415. 1 Publication
Sequence conflicti1032 – 10321R → S in BAC40305. 1 Publication
Sequence conflicti1032 – 10321R → S in BAC29956. 1 Publication
Sequence conflicti1032 – 10321R → S in BAE24964. 1 Publication
Sequence conflicti1032 – 10321R → S in BAE33790. 1 Publication
Sequence conflicti1032 – 10321R → S in BAE37819. 1 Publication
Sequence conflicti1074 – 10741W → V in AAA21415. 1 Publication
Sequence conflicti1077 – 10771S → E in AAA21565. 1 Publication
Sequence conflicti1085 – 10851G → A in AAA21565. 1 Publication
Sequence conflicti1093 – 10931A → G in AAA21415. 1 Publication
Sequence conflicti1093 – 10931A → P in AAA21565. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS22403.1. [Q62137-1]
PIRiI58401.
S48053.
RefSeqiNP_001177759.1. NM_001190830.1.
NP_034719.2. NM_010589.6.
UniGeneiMm.249645.
Mm.476857.

Genome annotation databases

EnsembliENSMUST00000051995; ENSMUSP00000060073; ENSMUSG00000031805.
ENSMUST00000110012; ENSMUSP00000105639; ENSMUSG00000031805.
ENSMUST00000110013; ENSMUSP00000105640; ENSMUSG00000031805.
GeneIDi16453.
KEGGimmu:16453.
UCSCiuc009mel.2. mouse. [Q62137-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS22403.1. [Q62137-1 ]
PIRi I58401.
S48053.
RefSeqi NP_001177759.1. NM_001190830.1.
NP_034719.2. NM_010589.6.
UniGenei Mm.249645.
Mm.476857.

3D structure databases

ProteinModelPortali Q62137.
SMRi Q62137. Positions 24-1094.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200858. 5 interactions.
IntActi Q62137. 2 interactions.
MINTi MINT-1523453.

Chemistry

BindingDBi Q62137.
ChEMBLi CHEMBL5250.

PTM databases

PhosphoSitei Q62137.

Proteomic databases

PRIDEi Q62137.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000051995 ; ENSMUSP00000060073 ; ENSMUSG00000031805 .
ENSMUST00000110012 ; ENSMUSP00000105639 ; ENSMUSG00000031805 .
ENSMUST00000110013 ; ENSMUSP00000105640 ; ENSMUSG00000031805 .
GeneIDi 16453.
KEGGi mmu:16453.
UCSCi uc009mel.2. mouse. [Q62137-1 ]

Organism-specific databases

CTDi 3718.
MGIi MGI:99928. Jak3.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00710000106680.
HOVERGENi HBG006195.
KOi K11218.
OrthoDBi EOG7BW0HM.
PhylomeDBi Q62137.
TreeFami TF327041.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 3474.
Reactomei REACT_198701. Interleukin-7 signaling.
REACT_210793. Interleukin receptor SHC signaling.

Miscellaneous databases

NextBioi 289723.
PROi Q62137.
SOURCEi Search...

Gene expression databases

Bgeei Q62137.
CleanExi MM_JAK3.
Genevestigatori Q62137.

Family and domain databases

InterProi IPR019749. 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 ]
Pfami PF07714. Pkinase_Tyr. 2 hits.
[Graphical view ]
PIRSFi PIRSF000636. TyrPK_Jak. 1 hit.
PRINTSi PR01823. JANUSKINASE.
PR01826. JANUSKINASE3.
PR00109. TYRKINASE.
SMARTi SM00295. B41. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 2 hits.
[Graphical view ]
SUPFAMi SSF55550. SSF55550. 2 hits.
SSF56112. SSF56112. 2 hits.
PROSITEi PS50057. FERM_3. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiJAK3_MOUSE
AccessioniPrimary (citable) accession number: Q62137
Secondary accession number(s): A2RRI3
, Q0D2M8, Q61746, Q61747, Q8BTY6, Q8BYU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 21, 2007
Last modified: September 3, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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