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P23458 (JAK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase JAK1

EC=2.7.10.2
Alternative name(s):
Janus kinase 1
Short name=JAK-1
Gene names
Name:JAK1
Synonyms:JAK1A, JAK1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1154 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway. Kinase partner for the interleukin (IL)-2 receptor. Ref.10

Catalytic activity

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

Subunit structure

Interacts with FER By similarity. Interacts with IL31RA, IFNAR2, JAKMIP1 and SHB. Ref.8 Ref.9 Ref.11 Ref.12

Subcellular location

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

Tissue specificity

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. Ref.7

Domain

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.

Post-translational modification

Phosphorylated. Dephosphorylation of Tyr-1034 and Tyr-1035 by PTPN2 negatively regulates cytokine-mediated signaling. Ref.10

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 AAA36527.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAA36527.1 differs from that shown. Reason: Frameshift at positions 858 and 862.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainRepeat
SH2 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

enzyme linked receptor protein signaling pathway

Inferred from electronic annotation. Source: Ensembl

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

interleukin-2-mediated signaling pathway

Inferred from direct assay Ref.10. Source: UniProtKB

intracellular signal transduction

Traceable author statement PubMed 8232552. Source: ProtInc

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Traceable author statement Ref.1. Source: ProtInc

regulation of interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

regulation of type I interferon-mediated signaling pathway

Traceable author statement. Source: Reactome

response to antibiotic

Inferred from direct assay PubMed 16280321. Source: MGI

type I interferon signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 10502458. 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

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from direct assay PubMed 10502458. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

growth hormone receptor binding

Inferred from sequence or structural similarity PubMed 10502458. Source: BHF-UCL

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

protein phosphatase binding

Inferred from physical interaction Ref.10. Source: UniProtKB

protein tyrosine kinase activity

Inferred from experiment. Source: Reactome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ERBB2P046262EBI-1383438,EBI-641062
IFNAR2P485513EBI-1383438,EBI-958408

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11541154Tyrosine-protein kinase JAK1
PRO_0000088108

Regions

Domain34 – 420387FERM
Domain439 – 544106SH2
Domain583 – 855273Protein kinase 1
Domain875 – 1153279Protein kinase 2
Nucleotide binding881 – 8899ATP By similarity

Sites

Active site10031Proton acceptor By similarity
Binding site9081ATP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.13
Modified residue31Phosphotyrosine Ref.13
Modified residue2281Phosphoserine Ref.13
Modified residue10341Phosphotyrosine; by autocatalysis Ref.10
Modified residue10351Phosphotyrosine; by autocatalysis Ref.10

Natural variations

Natural variant9731N → K. Ref.16
Corresponds to variant rs34680086 [ dbSNP | Ensembl ].
VAR_041715

Experimental info

Sequence conflict3501H → D in AAA36527. Ref.1
Sequence conflict3681Y → F in AAA36527. Ref.1
Sequence conflict8981Missing in AAA36527. Ref.1

Secondary structure

...................................................................................................... 1154
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23458 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: A2C4BE27851ACABB

FASTA1,154133,277
        10         20         30         40         50         60 
MQYLNIKEDC NAMAFCAKMR SSKKTEVNLE APEPGVEVIF YLSDREPLRL GSGEYTAEEL 

        70         80         90        100        110        120 
CIRAAQACRI SPLCHNLFAL YDENTKLWYA PNRTITVDDK MSLRLHYRMR FYFTNWHGTN 

       130        140        150        160        170        180 
DNEQSVWRHS PKKQKNGYEK KKIPDATPLL DASSLEYLFA QGQYDLVKCL APIRDPKTEQ 

       190        200        210        220        230        240 
DGHDIENECL GMAVLAISHY AMMKKMQLPE LPKDISYKRY IPETLNKSIR QRNLLTRMRI 

       250        260        270        280        290        300 
NNVFKDFLKE FNNKTICDSS VSTHDLKVKY LATLETLTKH YGAEIFETSM LLISSENEMN 

       310        320        330        340        350        360 
WFHSNDGGNV LYYEVMVTGN LGIQWRHKPN VVSVEKEKNK LKRKKLENKH KKDEEKNKIR 

       370        380        390        400        410        420 
EEWNNFSYFP EITHIVIKES VVSINKQDNK KMELKLSSHE EALSFVSLVD GYFRLTADAH 

       430        440        450        460        470        480 
HYLCTDVAPP LIVHNIQNGC HGPICTEYAI NKLRQEGSEE GMYVLRWSCT DFDNILMTVT 

       490        500        510        520        530        540 
CFEKSEQVQG AQKQFKNFQI EVQKGRYSLH GSDRSFPSLG DLMSHLKKQI LRTDNISFML 

       550        560        570        580        590        600 
KRCCQPKPRE ISNLLVATKK AQEWQPVYPM SQLSFDRILK KDLVQGEHLG RGTRTHIYSG 

       610        620        630        640        650        660 
TLMDYKDDEG TSEEKKIKVI LKVLDPSHRD ISLAFFEAAS MMRQVSHKHI VYLYGVCVRD 

       670        680        690        700        710        720 
VENIMVEEFV EGGPLDLFMH RKSDVLTTPW KFKVAKQLAS ALSYLEDKDL VHGNVCTKNL 

       730        740        750        760        770        780 
LLAREGIDSE CGPFIKLSDP GIPITVLSRQ ECIERIPWIA PECVEDSKNL SVAADKWSFG 

       790        800        810        820        830        840 
TTLWEICYNG EIPLKDKTLI EKERFYESRC RPVTPSCKEL ADLMTRCMNY DPNQRPFFRA 

       850        860        870        880        890        900 
IMRDINKLEE QNPDIVSEKK PATEVDPTHF EKRFLKRIRD LGEGHFGKVE LCRYDPEGDN 

       910        920        930        940        950        960 
TGEQVAVKSL KPESGGNHIA DLKKEIEILR NLYHENIVKY KGICTEDGGN GIKLIMEFLP 

       970        980        990       1000       1010       1020 
SGSLKEYLPK NKNKINLKQQ LKYAVQICKG MDYLGSRQYV HRDLAARNVL VESEHQVKIG 

      1030       1040       1050       1060       1070       1080 
DFGLTKAIET DKEYYTVKDD RDSPVFWYAP ECLMQSKFYI ASDVWSFGVT LHELLTYCDS 

      1090       1100       1110       1120       1130       1140 
DSSPMALFLK MIGPTHGQMT VTRLVNTLKE GKRLPCPPNC PDEVYQLMRK CWEFQPSNRT 

      1150 
SFQNLIEGFE ALLK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Receptor tyrosine kinases expressed in metastatic colon cancer."
Craven R.J., Xu L.H., Weiner T.M., Fridell Y.-W., Dent G.A., Srivastava S., Varnum B., Liu E.T., Cance W.G.
Int. J. Cancer 60:791-797(1995) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS41346.1.
PIRA39577.
RefSeqNP_002218.2. NM_002227.2.
XP_005270898.1. XM_005270841.1.
XP_006710687.1. XM_006710624.1.
UniGeneHs.207538.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP23458.
SMRP23458. Positions 56-1154.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109919. 71 interactions.
DIPDIP-133N.
IntActP23458. 20 interactions.
MINTMINT-145830.
STRING9606.ENSP00000343204.

Chemistry

BindingDBP23458.
ChEMBLCHEMBL2835.
GuidetoPHARMACOLOGY2047.

PTM databases

PhosphoSiteP23458.

Polymorphism databases

DMDM215274013.

Proteomic databases

MaxQBP23458.
PaxDbP23458.
PRIDEP23458.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000342505; ENSP00000343204; ENSG00000162434.
GeneID3716.
KEGGhsa:3716.
UCSCuc001dbu.1. human.

Organism-specific databases

CTD3716.
GeneCardsGC01M065247.
HGNCHGNC:6190. JAK1.
HPACAB013088.
MIM147795. gene.
neXtProtNX_P23458.
PharmGKBPA29988.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000049158.
HOVERGENHBG006195.
InParanoidP23458.
KOK11217.
OMAIMRDINK.
OrthoDBEOG7BW0HM.
PhylomeDBP23458.
TreeFamTF327041.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_6900. Immune System.
SignaLinkP23458.

Gene expression databases

BgeeP23458.
CleanExHS_JAK1.
GenevestigatorP23458.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR019749. 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]
PfamPF07714. Pkinase_Tyr. 2 hits.
[Graphical view]
PIRSFPIRSF000636. TyrPK_Jak. 1 hit.
PRINTSPR01823. JANUSKINASE.
PR01824. JANUSKINASE1.
PR00109. TYRKINASE.
SMARTSM00295. B41. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 2 hits.
[Graphical view]
SUPFAMSSF47031. SSF47031. 1 hit.
SSF55550. SSF55550. 1 hit.
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.
PS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSJAK1. human.
EvolutionaryTraceP23458.
GeneWikiJanus_kinase_1.
GenomeRNAi3716.
NextBio14563.
PROP23458.
SOURCESearch...

Entry information

Entry nameJAK1_HUMAN
AccessionPrimary (citable) accession number: P23458
Secondary accession number(s): Q59GQ2, Q9UD26
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM