JAK1
entrez
3716
canonical
uniprot
P23458
canonical
ensembl
ENSG00000162434
resolver
ensp
ENSP00000343204
resolver
ensp
ENSP00000499884
resolver
ensp
ENSP00000499900
resolver
ensp
ENSP00000500296
resolver
ensp
ENSP00000500485
resolver
ensp
ENSP00000500745
resolver
ensp
ENSP00000500841
resolver
ensp
ENSP00000514240
resolver
ensp
ENSP00000514241
resolver
ensp
ENSP00000514243
resolver
ensp
ENSP00000514291
resolver
ensp
ENSP00000563499
resolver
ensp
ENSP00000563501
resolver
ensp
ENSP00000563504
resolver
ensp
ENSP00000641002
resolver
ensp
ENSP00000641003
resolver
ensp
ENSP00000641005
resolver
ensp
ENSP00000641006
resolver
enst
ENST00000342505
resolver
enst
ENST00000671929
resolver
enst
ENST00000671954
resolver
enst
ENST00000672179
resolver
enst
ENST00000672247
resolver
enst
ENST00000672434
resolver
enst
ENST00000672751
resolver
enst
ENST00000699259
resolver
enst
ENST00000699260
resolver
enst
ENST00000699262
resolver
enst
ENST00000699312
resolver
enst
ENST00000893440
resolver
enst
ENST00000893442
resolver
enst
ENST00000893445
resolver
enst
ENST00000970943
resolver
enst
ENST00000970944
resolver
enst
ENST00000970946
resolver
enst
ENST00000970947
resolver
genesymbol
JAK1
resolver
genesymbol_syn
JAK1A
resolver
genesymbol_syn
JAK1B
resolver
hgnc
HGNC:6190
resolver
uniprot
A0A8V8TPQ9
resolver
uniprot
Q59GQ2
resolver
uniprot
Q6P669
resolver
uniprot
Q9UD26
resolver
uniprot_entry
A0A8V8TPQ9_HUMAN
resolver
uniprot_entry
JAK1_HUMAN
resolver
uniprot_entry
Q6P669_HUMAN
resolver
uniprot_sec
Q59GQ2
resolver
uniprot_sec
Q9UD26
resolver
amino_acid_sequence
MQYLNIKEDCNAMAFCAKMRSSKKTEVNLEAPEPGVEVIFYLSDREPLRLGSGEYTAEELCIRAAQACRISPLCHNLFALYDENTKLWYAPNRTITVDDKMSLRLHYRMRFYFTNWHGTNDNEQSVWRHSPKKQKNGYEKKKIPDATPLLDASSLEYLFAQGQYDLVKCLAPIRDPKTEQDGHDIENECLGMAVLAISHYAMMKKMQLPELPKDISYKRYIPETLNKSIRQRNLLTRMRINNVFKDFLKEFNNKTICDSSVSTHDLKVKYLATLETLTKHYGAEIFETSMLLISSENEMNWFHSNDGGNVLYYEVMVTGNLGIQWRHKPNVVSVEKEKNKLKRKKLENKHKKDEEKNKIREEWNNFSYFPEITHIVIKESVVSINKQDNKKMELKLSSHEEALSFVSLVDGYFRLTADAHHYLCTDVAPPLIVHNIQNGCHGPICTEYAINKLRQEGSEEGMYVLRWSCTDFDNILMTVTCFEKSEQVQGAQKQFKNFQIEVQKGRYSLHGSDRSFPSLGDLMSHLKKQILRTDNISFMLKRCCQPKPREISNLLVATKKAQEWQPVYPMSQLSFDRILKKDLVQGEHLGRGTRTHIYSGTLMDYKDDEGTSEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSECGPFIKLSDPGIPITVLSRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRDINKLEEQNPDIVSEKKPATEVDPTHFEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSSPMALFLKMIGPTHGQMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK
uniprot
proteins
disease_involvement
DISEASE: Autoinflammation, immune dysregulation, and eosinophilia (AIIDE) [MIM:618999]: An autosomal dominant disorder characterized by immune dysregulation, severe atopic dermatitis, and chronic gastrointestinal inflammation. Additional features include asthma, food or environmental allergies, as well as poor overall growth with short stature. {ECO:0000269|PubMed:28111307, ECO:0000269|PubMed:32750333}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.10.2
uniprot
proteins
function
FUNCTION: Non-membrane spanning protein tyrosine kinase that phosphorylates signal-transducing subunits of cytokine receptor complexes like IL2RB, IL10RA, IFNAR2, IL6ST, LIFR, OSMR and IL31RA (PubMed:11909529, PubMed:12133952, PubMed:15194700, PubMed:16239216, PubMed:28111307, PubMed:32750333, PubMed:7615558, PubMed:8232552, PubMed:9188471). Functionally, is involved in the IFN-alpha/beta/gamma signal pathway (PubMed:16239216, PubMed:28111307, PubMed:32750333, PubMed:7615558, PubMed:8232552). Mechanistically, in response to interferon-binding to IFNAR1-IFNAR2 heterodimer, phosphorylates and activates its binding partner IFNAR2, creating docking sites for STAT proteins (PubMed:7759950). Directly phosphorylates STAT proteins but also activates STAT signaling through the transactivation of other JAK kinases associated with signaling receptors (PubMed:16239216, PubMed:32750333, PubMed:8232552). Involved in the MT-RNR2/humanin-mediated signaling pathway leading to STAT3 phosphorylation (PubMed:27384491). Binding of CNTF or the CLCF1/CLF heterodimer to CNTFR leads to IL6ST/gp130-LIFR dimerization followed by activation of JAK1 and JAK2 which in turns phosphorylate IL6ST/gp130 and LIFR (PubMed:11294841). The tyrosine phosphorylated signaling receptors serve in turn as docking proteins for STAT3 (PubMed:11294841). Involved in the oncostatin-M-mediated signaling pathway through both type I OSM receptor complex (heterodimers composed of LIFR and IL6ST) and type II OSM receptor complex (heterodimers composed of OSMR and IL6ST) (PubMed:9188471). Involved in the oncostatin-M-mediated signaling pathway through both type I OSM receptor complex (heterodimers composed of LIFR and IL6ST) and type II OSM receptor complex (heterodimers composed of OSMR and IL6ST) (PubMed:9188471). Involved in the Interleukin-31-mediated signaling pathway through the IL31 receptor complex (heterodimers composed of OSMR and IL31RA) (PubMed:15194700). {ECO:0000269|PubMed:11294841, ECO:0000269|PubMed:11909529, ECO:0000269|PubMed:12133952, ECO:0000269|PubMed:15194700, ECO:0000269|PubMed:16239216, ECO:0000269|PubMed:27384491, ECO:0000269|PubMed:28111307, ECO:0000269|PubMed:32750333, ECO:0000269|PubMed:7615558, ECO:0000269|PubMed:7657660, ECO:0000269|PubMed:8232552, ECO:0000269|PubMed:9188471}.
uniprot
proteins
mass_dalton
133277
uniprot
proteins
mutagenesis
MUTAGEN 658; /note="V->F: Constitutively active. Increased receptor signaling pathway via JAK-STAT."; /evidence="ECO:0000269|PubMed:16239216"; MUTAGEN 908; /note="K->A: Loss of protein tyrosine kinase activity."; /evidence="ECO:0000269|PubMed:32750333
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated (PubMed:7615558). Phosphorylated by TYK2 on tyrosine residues in response to type-I interferon signaling, leading to its activation (PubMed:8232552). Phosphorylated on tyrosine residues in response to interferon gamma signaling (PubMed:7615558). Dephosphorylation of Tyr-1034 and Tyr-1035 by PTPN2 negatively regulates cytokine-mediated signaling (PubMed:11909529). {ECO:0000269|PubMed:11909529, ECO:0000269|PubMed:7615558, ECO:0000305|PubMed:8232552}.; PTM: Ubiquitinated by RNF125; leading to its degradation by the proteasome. {ECO:0000269|PubMed:26027934}.
uniprot
proteins
protein_family
JAK subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
11294841
uniprot
proteins
pubmed
11909529
uniprot
proteins
pubmed
12133952
uniprot
proteins
pubmed
12200137
uniprot
proteins
pubmed
15194700
uniprot
proteins
pubmed
15277531
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16239216
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
1848670
uniprot
proteins
pubmed
19361440
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26027934
uniprot
proteins
pubmed
27384491
uniprot
proteins
pubmed
28111307
uniprot
proteins
pubmed
32750333
uniprot
proteins
pubmed
7615558
uniprot
proteins
pubmed
7657660
uniprot
proteins
pubmed
7759950
uniprot
proteins
pubmed
7896447
uniprot
proteins
pubmed
8232552
uniprot
proteins
pubmed
8247543
uniprot
proteins
pubmed
9188471
uniprot
proteins
sequence_length
1154
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein. Note=Wholly intracellular, possibly membrane associated.
uniprot
proteins