P23458 (JAK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1154 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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.10 Ref.11
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.
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 component	Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat SH2 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	enzyme linked receptor protein signaling pathway Inferred from electronic annotation. Source: Compara interferon-gamma-mediated signaling pathway Traceable author statement. Source: Reactome intracellular protein kinase cascade Inferred from electronic annotation. Source: Compara intracellular signal transduction Traceable author statement PubMed 8232552. Source: ProtInc peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: Compara 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-mediated signaling pathway Traceable author statement. Source: Reactome
Cellular_component	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_function	ATP 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: EC protein tyrosine kinase activity Inferred from experiment. Source: Reactome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1154

1154

Tyrosine-protein kinase JAK1

PRO_0000088108

Regions

Domain

34 – 420

387

FERM

Domain

439 – 544

106

SH2

Domain

583 – 855

273

Protein kinase 1

Domain

875 – 1153

279

Protein kinase 2

Nucleotide binding

881 – 889

9

ATP By similarity

Sites

Active site

1003

1

Proton acceptor By similarity

Binding site

908

1

ATP By similarity

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.12

Modified residue

3

1

Phosphotyrosine Ref.12

Modified residue

228

1

Phosphoserine Ref.12

Modified residue

1034

1

Phosphotyrosine; by autocatalysis By similarity

Natural variations

Natural variant

973

1

N → K. Ref.15
Corresponds to variant rs34680086 [ dbSNP | Ensembl ].

VAR_041715

Experimental info

Sequence conflict

350

1

H → D in AAA36527. Ref.1

Sequence conflict

368

1

Y → F in AAA36527. Ref.1

Sequence conflict

898

1

Missing in AAA36527. Ref.1

Secondary structure

1

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1154

Helix Strand Turn

Details...

Helix

872 – 874

3

Beta strand

875 – 883

9

Beta strand

885 – 894

10

Beta strand

898 – 900

3

Beta strand

902 – 910

9

Helix

919 – 930

12

Beta strand

940 – 945

6

Beta strand

952 – 957

6

Helix

964 – 971

8

Turn

972 – 974

3

Helix

977 – 996

20

Helix

1006 – 1008

3

Beta strand

1009 – 1013

5

Beta strand

1016 – 1019

4

Beta strand

1034 – 1036

3

Helix

1045 – 1047

3

Helix

1050 – 1055

6

Beta strand

1057 – 1059

3

Helix

1060 – 1075

16

Turn

1076 – 1078

3

Helix

1080 – 1082

3

Helix

1084 – 1092

9

Helix

1097 – 1099

3

Helix

1100 – 1109

10

Helix

1122 – 1130

9

Helix

1136 – 1138

3

Helix

1142 – 1153

12

Sequences

	Sequence		Length	Mass (Da)
	P23458 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: A2C4BE27851ACABB	FASTA	1,154	133,277
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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.
[11]	"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.
[12]	"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, MASS SPECTROMETRY.
[13]	"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].
[14]	"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.
[15]	"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.
+	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.

IPI

IPI00784013.

PIR

A39577.

RefSeq

NP_002218.2. NM_002227.2.

UniGene

Hs.207538.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P23458.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-133N.

IntAct

P23458. 11 interactions.

MINT

MINT-145830.

STRING

9606.ENSP00000343204.

PTM databases

PhosphoSite

P23458.

Polymorphism databases

DMDM

215274013.

Proteomic databases

PaxDb

P23458.

PRIDE

P23458.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000342505; ENSP00000343204; ENSG00000162434.

GeneID

3716.

KEGG

hsa:3716.

UCSC

uc001dbu.1. human.

Organism-specific databases

CTD

3716.

GeneCards

GC01M065247.

HGNC

HGNC:6190. JAK1.

HPA

CAB013088.

MIM

147795. gene.

neXtProt

NX_P23458.

PharmGKB

PA29988.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000049158.

HOVERGEN

HBG006195.

InParanoid

P23458.

KO

K11217.

OMA

PICTEYA.

OrthoDB

EOG4PVNXT.

Enzyme and pathway databases

BRENDA

2.7.10.2. 2681.

Pathway_Interaction_DB

ifngpathway. IFN-gamma pathway.
il2_pi3kpathway. IL2 signaling events mediated by PI3K.
il2_stat5pathway. IL2 signaling events mediated by STAT5.
il2_1pathway. IL2-mediated signaling events.
il27pathway. IL27-mediated signaling events.
il4_2pathway. IL4-mediated signaling events.
il6_7pathway. IL6-mediated signaling events.
pdgfrapathway. PDGFR-alpha signaling pathway.

Reactome

REACT_6900. Immune System.

Gene expression databases

Bgee

P23458.

CleanEx

HS_JAK1.

Genevestigator

P23458.

GermOnline

ENSG00000162434. Homo sapiens.

Family and domain databases

Gene3D

3.30.505.10. 1 hit.

InterPro

IPR019749. Band_41_domain.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_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]

Pfam

PF07714. Pkinase_Tyr. 2 hits.
[Graphical view]

PIRSF

PIRSF000636. TyrPK_Jak. 1 hit.

PRINTS

PR01823. JANUSKINASE.
PR01824. JANUSKINASE1.
PR00109. TYRKINASE.

SMART

SM00295. B41. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 2 hits.
[Graphical view]

SUPFAM

SSF47031. FERM_3-hlx. 1 hit.
SSF56112. Kinase_like. 2 hits.

PROSITE

PS00660. FERM_1. False negative.
PS00661. FERM_2. False negative.
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]

ProtoNet

Search...

Other

BindingDB

P23458.

ChEMBL

CHEMBL2835.

ChiTaRS

JAK1. human.

EvolutionaryTrace

P23458.

GenomeRNAi

3716.

NextBio

14563.

SOURCE

Search...

Entry information

Entry name

JAK1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 145 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.