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P23458

- JAK1_HUMAN

UniProt

P23458 - JAK1_HUMAN

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Protein

Tyrosine-protein kinase JAK1

Gene

JAK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 phosphatase binding Source: UniProtKB
  5. 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
Complete GO annotation...

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_1183. ERK2 activation.
REACT_1391. ERK1 activation.
REACT_1695. GPVI-mediated activation cascade.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
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. focal adhesion Source: UniProtKB
  5. membrane Source: UniProtKB-KW
  6. nucleus Source: BHF-UCL
Complete GO annotation...

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. 74 interactions.
DIPiDIP-133N.
IntActiP23458. 21 interactions.
MINTiMINT-145830.
STRINGi9606.ENSP00000343204.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118799.
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

        10         20         30         40         50
MQYLNIKEDC NAMAFCAKMR SSKKTEVNLE APEPGVEVIF YLSDREPLRL
60 70 80 90 100
GSGEYTAEEL CIRAAQACRI SPLCHNLFAL YDENTKLWYA PNRTITVDDK
110 120 130 140 150
MSLRLHYRMR FYFTNWHGTN DNEQSVWRHS PKKQKNGYEK KKIPDATPLL
160 170 180 190 200
DASSLEYLFA QGQYDLVKCL APIRDPKTEQ DGHDIENECL GMAVLAISHY
210 220 230 240 250
AMMKKMQLPE LPKDISYKRY IPETLNKSIR QRNLLTRMRI NNVFKDFLKE
260 270 280 290 300
FNNKTICDSS VSTHDLKVKY LATLETLTKH YGAEIFETSM LLISSENEMN
310 320 330 340 350
WFHSNDGGNV LYYEVMVTGN LGIQWRHKPN VVSVEKEKNK LKRKKLENKH
360 370 380 390 400
KKDEEKNKIR EEWNNFSYFP EITHIVIKES VVSINKQDNK KMELKLSSHE
410 420 430 440 450
EALSFVSLVD GYFRLTADAH HYLCTDVAPP LIVHNIQNGC HGPICTEYAI
460 470 480 490 500
NKLRQEGSEE GMYVLRWSCT DFDNILMTVT CFEKSEQVQG AQKQFKNFQI
510 520 530 540 550
EVQKGRYSLH GSDRSFPSLG DLMSHLKKQI LRTDNISFML KRCCQPKPRE
560 570 580 590 600
ISNLLVATKK AQEWQPVYPM SQLSFDRILK KDLVQGEHLG RGTRTHIYSG
610 620 630 640 650
TLMDYKDDEG TSEEKKIKVI LKVLDPSHRD ISLAFFEAAS MMRQVSHKHI
660 670 680 690 700
VYLYGVCVRD VENIMVEEFV EGGPLDLFMH RKSDVLTTPW KFKVAKQLAS
710 720 730 740 750
ALSYLEDKDL VHGNVCTKNL LLAREGIDSE CGPFIKLSDP GIPITVLSRQ
760 770 780 790 800
ECIERIPWIA PECVEDSKNL SVAADKWSFG TTLWEICYNG EIPLKDKTLI
810 820 830 840 850
EKERFYESRC RPVTPSCKEL ADLMTRCMNY DPNQRPFFRA IMRDINKLEE
860 870 880 890 900
QNPDIVSEKK PATEVDPTHF EKRFLKRIRD LGEGHFGKVE LCRYDPEGDN
910 920 930 940 950
TGEQVAVKSL KPESGGNHIA DLKKEIEILR NLYHENIVKY KGICTEDGGN
960 970 980 990 1000
GIKLIMEFLP SGSLKEYLPK NKNKINLKQQ LKYAVQICKG MDYLGSRQYV
1010 1020 1030 1040 1050
HRDLAARNVL VESEHQVKIG DFGLTKAIET DKEYYTVKDD RDSPVFWYAP
1060 1070 1080 1090 1100
ECLMQSKFYI ASDVWSFGVT LHELLTYCDS DSSPMALFLK MIGPTHGQMT
1110 1120 1130 1140 1150
VTRLVNTLKE GKRLPCPPNC PDEVYQLMRK CWEFQPSNRT SFQNLIEGFE

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

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 74 interactions.
DIPi DIP-133N.
IntActi P23458. 21 interactions.
MINTi MINT-145830.
STRINGi 9606.ENSP00000343204.

Chemistry

BindingDBi P23458.
ChEMBLi CHEMBL3038491.
DrugBanki DB08877. Ruxolitinib.
DB08895. Tofacitinib.
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.
GeneTreei ENSGT00760000118799.
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_1183. ERK2 activation.
REACT_1391. ERK1 activation.
REACT_1695. GPVI-mediated activation cascade.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 163 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