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P23458

- JAK1_HUMAN

UniProt

P23458 - JAK1_HUMAN

Protein

Tyrosine-protein kinase JAK1

Gene

JAK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway. Kinase partner for the interleukin (IL)-2 receptor.1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei908 – 9081ATPPROSITE-ProRule annotation
    Active sitei1003 – 10031Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi881 – 8899ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. growth hormone receptor binding Source: BHF-UCL
    3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    4. protein binding Source: UniProtKB
    5. protein phosphatase binding Source: UniProtKB
    6. protein tyrosine kinase activity Source: Reactome

    GO - Biological processi

    1. cytokine-mediated signaling pathway Source: Reactome
    2. enzyme linked receptor protein signaling pathway Source: Ensembl
    3. interferon-gamma-mediated signaling pathway Source: Reactome
    4. interleukin-2-mediated signaling pathway Source: UniProtKB
    5. intracellular signal transduction Source: ProtInc
    6. protein autophosphorylation Source: Ensembl
    7. protein phosphorylation Source: ProtInc
    8. regulation of interferon-gamma-mediated signaling pathway Source: Reactome
    9. regulation of type I interferon-mediated signaling pathway Source: Reactome
    10. response to antibiotic Source: MGI
    11. type I interferon signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 2681.
    ReactomeiREACT_115529. Interleukin-7 signaling.
    REACT_115831. ISG15 antiviral mechanism.
    REACT_23891. Interleukin receptor SHC signaling.
    REACT_24980. Regulation of IFNG signaling.
    REACT_25078. Interferon gamma signaling.
    REACT_25162. Interferon alpha/beta signaling.
    REACT_25216. Regulation of IFNA signaling.
    REACT_27283. Interleukin-2 signaling.
    REACT_27307. Interleukin-6 signaling.
    SignaLinkiP23458.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase JAK1 (EC:2.7.10.2)
    Alternative name(s):
    Janus kinase 1
    Short name:
    JAK-1
    Gene namesi
    Name:JAK1
    Synonyms:JAK1A, JAK1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6190. JAK1.

    Subcellular locationi

    Endomembrane system; Peripheral membrane protein
    Note: Wholly intracellular, possibly membrane associated.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29988.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11541154Tyrosine-protein kinase JAK1PRO_0000088108Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei3 – 31Phosphotyrosine1 Publication
    Modified residuei228 – 2281Phosphoserine1 Publication
    Modified residuei1034 – 10341Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei1035 – 10351Phosphotyrosine; by autocatalysis1 Publication

    Post-translational modificationi

    Phosphorylated. Dephosphorylation of Tyr-1034 and Tyr-1035 by PTPN2 negatively regulates cytokine-mediated signaling.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP23458.
    PaxDbiP23458.
    PRIDEiP23458.

    PTM databases

    PhosphoSiteiP23458.

    Expressioni

    Tissue specificityi

    Expressed at higher levels in primary colon tumors than in normal colon tissue. The expression level in metastatic colon tumors is comparable to the expression level in normal colon tissue.1 Publication

    Gene expression databases

    BgeeiP23458.
    CleanExiHS_JAK1.
    GenevestigatoriP23458.

    Organism-specific databases

    HPAiCAB013088.

    Interactioni

    Subunit structurei

    Interacts with FER By similarity. Interacts with IL31RA, IFNAR2, JAKMIP1 and SHB.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ERBB2P046262EBI-1383438,EBI-641062
    IFNAR2P485513EBI-1383438,EBI-958408

    Protein-protein interaction databases

    BioGridi109919. 71 interactions.
    DIPiDIP-133N.
    IntActiP23458. 20 interactions.
    MINTiMINT-145830.
    STRINGi9606.ENSP00000343204.

    Structurei

    Secondary structure

    1
    1154
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi569 – 5724
    Beta strandi575 – 5784
    Helixi580 – 5823
    Beta strandi583 – 59210
    Beta strandi595 – 6039
    Beta strandi616 – 6249
    Helixi629 – 64416
    Beta strandi653 – 6597
    Beta strandi662 – 6687
    Helixi675 – 6828
    Turni683 – 6853
    Helixi688 – 70720
    Helixi717 – 7193
    Beta strandi720 – 7245
    Beta strandi727 – 7315
    Beta strandi734 – 7374
    Helixi744 – 7463
    Helixi749 – 7546
    Turni755 – 7584
    Helixi761 – 7655
    Helixi767 – 7693
    Helixi774 – 78714
    Turni788 – 7903
    Turni793 – 7964
    Helixi799 – 8079
    Helixi818 – 82710
    Helixi832 – 8343
    Helixi838 – 84811
    Helixi872 – 8743
    Beta strandi875 – 8839
    Beta strandi885 – 89410
    Beta strandi898 – 9003
    Beta strandi902 – 9109
    Helixi919 – 93012
    Beta strandi940 – 9456
    Beta strandi952 – 9576
    Helixi964 – 9718
    Turni972 – 9743
    Helixi977 – 99620
    Beta strandi998 – 10003
    Helixi1006 – 10083
    Beta strandi1009 – 10135
    Beta strandi1016 – 10194
    Beta strandi1034 – 10363
    Helixi1045 – 10473
    Helixi1050 – 10556
    Beta strandi1057 – 10593
    Helixi1060 – 107516
    Turni1076 – 10783
    Helixi1080 – 10823
    Helixi1084 – 10929
    Helixi1097 – 10993
    Helixi1100 – 110910
    Helixi1122 – 11309
    Helixi1136 – 11383
    Helixi1142 – 115312

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EYGX-ray1.90A865-1154[»]
    3EYHX-ray2.00A865-1154[»]
    4E4LX-ray2.00A/B/D/E854-1154[»]
    4E4NX-ray1.90A/B854-1154[»]
    4E5WX-ray1.86A/B854-1154[»]
    4EHZX-ray2.17A/B/C/D854-1154[»]
    4EI4X-ray2.22A/B854-1154[»]
    4FK6X-ray2.20A/B854-1154[»]
    4GS0X-ray1.80C1033-1036[»]
    4I5CX-ray2.10A/B854-1154[»]
    4IVBX-ray1.90A/B854-1154[»]
    4IVCX-ray2.35A/B854-1154[»]
    4IVDX-ray1.93A/B854-1154[»]
    4K6ZX-ray2.73A854-1154[»]
    4K77X-ray2.40A/B854-1154[»]
    4L00X-ray1.80A/B561-860[»]
    4L01X-ray1.90A/B561-860[»]
    ProteinModelPortaliP23458.
    SMRiP23458. Positions 56-1154.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23458.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini34 – 420387FERMPROSITE-ProRule annotationAdd
    BLAST
    Domaini439 – 544106SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini583 – 855273Protein kinase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini875 – 1153279Protein kinase 2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    Possesses two phosphotransferase domains. The second one probably contains the catalytic domain By similarity, while the presence of slight differences suggest a different role for domain 1.
    The FERM domain mediates interaction with JAKMIP1.

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. JAK subfamily.PROSITE-ProRule annotation
    Contains 1 FERM domain.PROSITE-ProRule annotation
    Contains 2 protein kinase domains.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH2 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000049158.
    HOVERGENiHBG006195.
    InParanoidiP23458.
    KOiK11217.
    OMAiIMRDINK.
    OrthoDBiEOG7BW0HM.
    PhylomeDBiP23458.
    TreeFamiTF327041.

    Family and domain databases

    Gene3Di3.30.505.10. 1 hit.
    InterProiIPR019749. Band_41_domain.
    IPR019748. FERM_central.
    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.
    IPR020776. Tyr_kinase_non-rcpt_Jak1.
    [Graphical view]
    PfamiPF07714. Pkinase_Tyr. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000636. TyrPK_Jak. 1 hit.
    PRINTSiPR01823. JANUSKINASE.
    PR01824. JANUSKINASE1.
    PR00109. TYRKINASE.
    SMARTiSM00295. B41. 1 hit.
    SM00252. SH2. 1 hit.
    SM00219. TyrKc. 2 hits.
    [Graphical view]
    SUPFAMiSSF47031. SSF47031. 1 hit.
    SSF55550. SSF55550. 1 hit.
    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.
    PS50001. SH2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P23458-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQYLNIKEDC NAMAFCAKMR SSKKTEVNLE APEPGVEVIF YLSDREPLRL     50
    GSGEYTAEEL CIRAAQACRI SPLCHNLFAL YDENTKLWYA PNRTITVDDK 100
    MSLRLHYRMR FYFTNWHGTN DNEQSVWRHS PKKQKNGYEK KKIPDATPLL 150
    DASSLEYLFA QGQYDLVKCL APIRDPKTEQ DGHDIENECL GMAVLAISHY 200
    AMMKKMQLPE LPKDISYKRY IPETLNKSIR QRNLLTRMRI NNVFKDFLKE 250
    FNNKTICDSS VSTHDLKVKY LATLETLTKH YGAEIFETSM LLISSENEMN 300
    WFHSNDGGNV LYYEVMVTGN LGIQWRHKPN VVSVEKEKNK LKRKKLENKH 350
    KKDEEKNKIR EEWNNFSYFP EITHIVIKES VVSINKQDNK KMELKLSSHE 400
    EALSFVSLVD GYFRLTADAH HYLCTDVAPP LIVHNIQNGC HGPICTEYAI 450
    NKLRQEGSEE GMYVLRWSCT DFDNILMTVT CFEKSEQVQG AQKQFKNFQI 500
    EVQKGRYSLH GSDRSFPSLG DLMSHLKKQI LRTDNISFML KRCCQPKPRE 550
    ISNLLVATKK AQEWQPVYPM SQLSFDRILK KDLVQGEHLG RGTRTHIYSG 600
    TLMDYKDDEG TSEEKKIKVI LKVLDPSHRD ISLAFFEAAS MMRQVSHKHI 650
    VYLYGVCVRD VENIMVEEFV EGGPLDLFMH RKSDVLTTPW KFKVAKQLAS 700
    ALSYLEDKDL VHGNVCTKNL LLAREGIDSE CGPFIKLSDP GIPITVLSRQ 750
    ECIERIPWIA PECVEDSKNL SVAADKWSFG TTLWEICYNG EIPLKDKTLI 800
    EKERFYESRC RPVTPSCKEL ADLMTRCMNY DPNQRPFFRA IMRDINKLEE 850
    QNPDIVSEKK PATEVDPTHF EKRFLKRIRD LGEGHFGKVE LCRYDPEGDN 900
    TGEQVAVKSL KPESGGNHIA DLKKEIEILR NLYHENIVKY KGICTEDGGN 950
    GIKLIMEFLP SGSLKEYLPK NKNKINLKQQ LKYAVQICKG MDYLGSRQYV 1000
    HRDLAARNVL VESEHQVKIG DFGLTKAIET DKEYYTVKDD RDSPVFWYAP 1050
    ECLMQSKFYI ASDVWSFGVT LHELLTYCDS DSSPMALFLK MIGPTHGQMT 1100
    VTRLVNTLKE GKRLPCPPNC PDEVYQLMRK CWEFQPSNRT SFQNLIEGFE 1150
    ALLK 1154
    Length:1,154
    Mass (Da):133,277
    Last modified:November 25, 2008 - v2
    Checksum:iA2C4BE27851ACABB
    GO

    Sequence cautioni

    The sequence AAA36527.1 differs from that shown. Reason: Frameshift at positions 858 and 862.
    The sequence AAA36527.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti350 – 3501H → D in AAA36527. (PubMed:1848670)Curated
    Sequence conflicti368 – 3681Y → F in AAA36527. (PubMed:1848670)Curated
    Sequence conflicti898 – 8981Missing in AAA36527. (PubMed:1848670)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti973 – 9731N → K.1 Publication
    Corresponds to variant rs34680086 [ dbSNP | Ensembl ].
    VAR_041715

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64174 mRNA. Translation: AAA36527.1. Sequence problems.
    AB209057 mRNA. Translation: BAD92294.1.
    AC093427 Genomic DNA. No translation available.
    CH471059 Genomic DNA. Translation: EAX06547.1.
    BC132729 mRNA. Translation: AAI32730.1.
    CCDSiCCDS41346.1.
    PIRiA39577.
    RefSeqiNP_002218.2. NM_002227.2.
    XP_005270898.1. XM_005270841.1.
    XP_006710687.1. XM_006710624.1.
    UniGeneiHs.207538.

    Genome annotation databases

    EnsembliENST00000342505; ENSP00000343204; ENSG00000162434.
    GeneIDi3716.
    KEGGihsa:3716.
    UCSCiuc001dbu.1. human.

    Polymorphism databases

    DMDMi215274013.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64174 mRNA. Translation: AAA36527.1 . Sequence problems.
    AB209057 mRNA. Translation: BAD92294.1 .
    AC093427 Genomic DNA. No translation available.
    CH471059 Genomic DNA. Translation: EAX06547.1 .
    BC132729 mRNA. Translation: AAI32730.1 .
    CCDSi CCDS41346.1.
    PIRi A39577.
    RefSeqi NP_002218.2. NM_002227.2.
    XP_005270898.1. XM_005270841.1.
    XP_006710687.1. XM_006710624.1.
    UniGenei Hs.207538.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3EYG X-ray 1.90 A 865-1154 [» ]
    3EYH X-ray 2.00 A 865-1154 [» ]
    4E4L X-ray 2.00 A/B/D/E 854-1154 [» ]
    4E4N X-ray 1.90 A/B 854-1154 [» ]
    4E5W X-ray 1.86 A/B 854-1154 [» ]
    4EHZ X-ray 2.17 A/B/C/D 854-1154 [» ]
    4EI4 X-ray 2.22 A/B 854-1154 [» ]
    4FK6 X-ray 2.20 A/B 854-1154 [» ]
    4GS0 X-ray 1.80 C 1033-1036 [» ]
    4I5C X-ray 2.10 A/B 854-1154 [» ]
    4IVB X-ray 1.90 A/B 854-1154 [» ]
    4IVC X-ray 2.35 A/B 854-1154 [» ]
    4IVD X-ray 1.93 A/B 854-1154 [» ]
    4K6Z X-ray 2.73 A 854-1154 [» ]
    4K77 X-ray 2.40 A/B 854-1154 [» ]
    4L00 X-ray 1.80 A/B 561-860 [» ]
    4L01 X-ray 1.90 A/B 561-860 [» ]
    ProteinModelPortali P23458.
    SMRi P23458. Positions 56-1154.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109919. 71 interactions.
    DIPi DIP-133N.
    IntActi P23458. 20 interactions.
    MINTi MINT-145830.
    STRINGi 9606.ENSP00000343204.

    Chemistry

    BindingDBi P23458.
    ChEMBLi CHEMBL2835.
    GuidetoPHARMACOLOGYi 2047.

    PTM databases

    PhosphoSitei P23458.

    Polymorphism databases

    DMDMi 215274013.

    Proteomic databases

    MaxQBi P23458.
    PaxDbi P23458.
    PRIDEi P23458.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000342505 ; ENSP00000343204 ; ENSG00000162434 .
    GeneIDi 3716.
    KEGGi hsa:3716.
    UCSCi uc001dbu.1. human.

    Organism-specific databases

    CTDi 3716.
    GeneCardsi GC01M065247.
    HGNCi HGNC:6190. JAK1.
    HPAi CAB013088.
    MIMi 147795. gene.
    neXtProti NX_P23458.
    PharmGKBi PA29988.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000049158.
    HOVERGENi HBG006195.
    InParanoidi P23458.
    KOi K11217.
    OMAi IMRDINK.
    OrthoDBi EOG7BW0HM.
    PhylomeDBi P23458.
    TreeFami TF327041.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    Reactomei REACT_115529. Interleukin-7 signaling.
    REACT_115831. ISG15 antiviral mechanism.
    REACT_23891. Interleukin receptor SHC signaling.
    REACT_24980. Regulation of IFNG signaling.
    REACT_25078. Interferon gamma signaling.
    REACT_25162. Interferon alpha/beta signaling.
    REACT_25216. Regulation of IFNA signaling.
    REACT_27283. Interleukin-2 signaling.
    REACT_27307. Interleukin-6 signaling.
    SignaLinki P23458.

    Miscellaneous databases

    ChiTaRSi JAK1. human.
    EvolutionaryTracei P23458.
    GeneWikii Janus_kinase_1.
    GenomeRNAii 3716.
    NextBioi 14563.
    PROi P23458.
    SOURCEi Search...

    Gene expression databases

    Bgeei P23458.
    CleanExi HS_JAK1.
    Genevestigatori P23458.

    Family and domain databases

    Gene3Di 3.30.505.10. 1 hit.
    InterProi IPR019749. Band_41_domain.
    IPR019748. FERM_central.
    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.
    IPR020776. Tyr_kinase_non-rcpt_Jak1.
    [Graphical view ]
    Pfami PF07714. Pkinase_Tyr. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF000636. TyrPK_Jak. 1 hit.
    PRINTSi PR01823. JANUSKINASE.
    PR01824. JANUSKINASE1.
    PR00109. TYRKINASE.
    SMARTi SM00295. B41. 1 hit.
    SM00252. SH2. 1 hit.
    SM00219. TyrKc. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47031. SSF47031. 1 hit.
    SSF55550. SSF55550. 1 hit.
    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.
    PS50001. SH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Two novel protein-tyrosine kinases, each with a second phosphotransferase-related catalytic domain, define a new class of protein kinase."
      Wilks A.F., Harpur A.G., Kurban R.R., Ralph S.J., Zuercher G., Ziemiecki A.
      Mol. Cell. Biol. 11:2057-2065(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Brain.
    6. "A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes."
      Lee S.-T., Strunk K.M., Spritz R.A.
      Oncogene 8:3403-3410(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1005-1062.
    7. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1008-1062, TISSUE SPECIFICITY.
      Tissue: Colon tumor.
    8. "Soluble and membrane-anchored forms of the human IFN-alpha/beta receptor."
      Novick D., Cohen B., Tal N., Rubinstein M.
      J. Leukoc. Biol. 57:712-718(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IFNAR2.
    9. "IL-2 receptor signaling through the Shb adapter protein in T and NK cells."
      Lindholm C.K.
      Biochem. Biophys. Res. Commun. 296:929-936(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHB.
    10. "The T cell protein tyrosine phosphatase is a negative regulator of janus family kinases 1 and 3."
      Simoncic P.D., Lee-Loy A., Barber D.L., Tremblay M.L., McGlade C.J.
      Curr. Biol. 12:446-453(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CYTOKINE SIGNALING, PHOSPHORYLATION AT TYR-1034 AND TYR-1035, DEPHOSPHORYLATION AT TYR-1034 AND TYR-1035 BY PTPN2.
    11. "Characterization of the signaling capacities of the novel gp130-like cytokine receptor."
      Dreuw A., Radtke S., Pflanz S., Lippok B.E., Heinrich P.C., Hermanns H.M.
      J. Biol. Chem. 279:36112-36120(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IL31RA.
    12. "Jamip1 (marlin-1) defines a family of proteins interacting with Janus kinases and microtubules."
      Steindler C., Li Z., Algarte M., Alcover A., Libri V., Ragimbeau J., Pellegrini S.
      J. Biol. Chem. 279:43168-43177(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH JAKMIP1.
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-3 AND SER-228, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Dissecting specificity in the Janus kinases: the structures of JAK-specific inhibitors complexed to the JAK1 and JAK2 protein tyrosine kinase domains."
      Williams N.K., Bamert R.S., Patel O., Wang C., Walden P.M., Wilks A.F., Fantino E., Rossjohn J., Lucet I.S.
      J. Mol. Biol. 387:219-232(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 865-1154 IN COMPLEXES WITH SYNTHETIC INHIBITORS CMP6 AND CP-690,550.
    16. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-973.

    Entry informationi

    Entry nameiJAK1_HUMAN
    AccessioniPrimary (citable) accession number: P23458
    Secondary accession number(s): Q59GQ2, Q9UD26
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 161 of the entry and version 2 of the sequence. [Complete history]
    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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3