P52332 · JAK1_MOUSE
- ProteinTyrosine-protein kinase JAK1
- GeneJak1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1153 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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 as well as interleukin (IL)-10 receptor. Kinase partner for the type I interferon receptor IFNAR2. In response to interferon-binding to IFNAR1-IFNAR2 heterodimer, phosphorylates and activates its binding partner IFNAR2, creating docking sites for STAT proteins. Directly phosphorylates STAT proteins but also activates STAT signaling through the transactivation of other JAK kinases associated with signaling receptors.
Catalytic activity
- ATP + L-tyrosyl-[protein] = ADP + H+ + O-phospho-L-tyrosyl-[protein]
Cofactor
Note: Mn2+ was used in the in vitro kinase assay but Mg2+ is likely to be the in vivo cofactor.
Features
Showing features for binding site, active site.
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTyrosine-protein kinase JAK1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP52332
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endomembrane system ; Peripheral membrane protein
Note: Wholly intracellular, possibly membrane associated.
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000088109 | 1-1153 | Tyrosine-protein kinase JAK1 | |||
Sequence: MQYLNIKEDCNAMAFCAKMRSFKKTEVKQVVPEPGVEVTFYLLDREPLRLGSGEYTAEELCIRAAQECSISPLCHNLFALYDESTKLWYAPNRIITVDDKTSLRLHYRMRFYFTNWHGTNDNEQSVWRHSPKKQKNGYEKKRVPEATPLLDASSLEYLFAQGQYDLIKCLAPIRDPKTEQDGHDIENECLGMAVLAISHYAMMKKMQLPELPKDISYKRYIPETLNKSIRQRNLLTRMRINNVFKDFLKEFNNKTICDSSVHDLKVKYLATLETSTLTKHYGAEIFETSMLLISSENELSRCHSNDSGNVLYEVMVTGNLGIQWRQKPNVVPVEKEKNKLKRKKLEYNKHKKDDERNKLREEWNNFSYFPEITHIVIKESVVSINKQDNKNMELKLSSREEALSFVSLVDGYFRLTADAHHYLCTDVAPPLIVHNIQNGCHGPICTEYAINKLRQEGSEEGMYVLRWSCTDFDNILMTVTCFEKSEVLGGQKQFKNFQIEVQKGRYSLHGSMDHFPSLRDLMNHLKKQILRTDNISFVLKRCCQPKPREISNLLVATKKAQEWQPVYSMSQLSFDRILKKDIIQGEHLGRGTRTHIYSGTLLDYKDEEGIAEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDALTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSDIGPFIKLSDPGIPVSVLTRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRDINKLEEQNPDIVSEKQPTTEVDPTHFEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICMEDGGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAIQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDDRDSPVFWYAPECLIQCKFYIASDVWSFGVTLHELLTYCDSDFSPMALFLKMIGPTHGQMTVTRLVKTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTTFQNLIEGFEALLK | ||||||
Modified residue | 3 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 228 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1033 | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | ||||||
Modified residue | 1034 | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y |
Post-translational modification
Ubiquitinated by RNF125; leading to its degradation by the proteasome.
Autophosphorylated. Phosphorylated on tyrosine residues in response to interferon gamma signaling. Dephosphorylation of Tyr-1034 and Tyr-1034 by PTPN2 negatively regulates cytokine-mediated signaling.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with IL31RA. Interacts with IFNAR2. Interacts with IFNGR1. Interacts with JAKMIP1. Interacts with SHB. Interacts (via N-terminus) with IL2RB and IL10RA (via its cytoplasmic domain) (By similarity).
Interacts with FER (PubMed:12738762).
Interacts with FER (PubMed:12738762).
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 34-420 | FERM | ||||
Sequence: PGVEVTFYLLDREPLRLGSGEYTAEELCIRAAQECSISPLCHNLFALYDESTKLWYAPNRIITVDDKTSLRLHYRMRFYFTNWHGTNDNEQSVWRHSPKKQKNGYEKKRVPEATPLLDASSLEYLFAQGQYDLIKCLAPIRDPKTEQDGHDIENECLGMAVLAISHYAMMKKMQLPELPKDISYKRYIPETLNKSIRQRNLLTRMRINNVFKDFLKEFNNKTICDSSVHDLKVKYLATLETSTLTKHYGAEIFETSMLLISSENELSRCHSNDSGNVLYEVMVTGNLGIQWRQKPNVVPVEKEKNKLKRKKLEYNKHKKDDERNKLREEWNNFSYFPEITHIVIKESVVSINKQDNKNMELKLSSREEALSFVSLVDGYFRLTADAH | ||||||
Domain | 439-542 | SH2 | ||||
Sequence: GCHGPICTEYAINKLRQEGSEEGMYVLRWSCTDFDNILMTVTCFEKSEVLGGQKQFKNFQIEVQKGRYSLHGSMDHFPSLRDLMNHLKKQILRTDNISFVLKRC | ||||||
Domain | 582-854 | Protein kinase 1 | ||||
Sequence: IIQGEHLGRGTRTHIYSGTLLDYKDEEGIAEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDALTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSDIGPFIKLSDPGIPVSVLTRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRDINKLEEQNPDI | ||||||
Domain | 874-1152 | Protein kinase 2 | ||||
Sequence: LKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICMEDGGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAIQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDDRDSPVFWYAPECLIQCKFYIASDVWSFGVTLHELLTYCDSDFSPMALFLKMIGPTHGQMTVTRLVKTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTTFQNLIEGFEALL |
Domain
The FERM domain mediates interaction with JAKMIP1.
The protein kinase 1 domain is also called the pseudokinase domain and has a regulatory role through the transactivation of other JAK kinases associated with signaling receptors.
The protein kinase 2 domain is the catalytically active domain.
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,153
- Mass (Da)133,367
- Last updated1996-10-01 v1
- Checksum0B9816AEA5B3868B
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 999 | in Ref. 3 and 4 | ||||
Sequence: V → I | ||||||
Sequence conflict | 1068-1069 | in Ref. 3 and 4 | ||||
Sequence: VT → IP |
Keywords
- Technical term