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JAK1_HUMAN
ID   JAK1_HUMAN              Reviewed;        1154 AA.
AC   P23458; Q59GQ2; Q9UD26;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   03-AUG-2022, entry version 229.
DE   RecName: Full=Tyrosine-protein kinase JAK1;
DE            EC=2.7.10.2 {ECO:0000269|PubMed:1848670, ECO:0000269|PubMed:7615558};
DE   AltName: Full=Janus kinase 1;
DE            Short=JAK-1;
GN   Name=JAK1; Synonyms=JAK1A, JAK1B;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RX   PubMed=1848670; DOI=10.1128/mcb.11.4.2057-2065.1991;
RA   Wilks A.F., Harpur A.G., Kurban R.R., Ralph S.J., Zuercher G.,
RA   Ziemiecki A.;
RT   "Two novel protein-tyrosine kinases, each with a second phosphotransferase-
RT   related catalytic domain, define a new class of protein kinase.";
RL   Mol. Cell. Biol. 11:2057-2065(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1005-1062.
RX   PubMed=8247543;
RA   Lee S.-T., Strunk K.M., Spritz R.A.;
RT   "A survey of protein tyrosine kinase mRNAs expressed in normal human
RT   melanocytes.";
RL   Oncogene 8:3403-3410(1993).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1008-1062, AND TISSUE SPECIFICITY.
RC   TISSUE=Colon tumor;
RX   PubMed=7896447; DOI=10.1002/ijc.2910600611;
RA   Craven R.J., Xu L.H., Weiner T.M., Fridell Y.-W., Dent G.A., Srivastava S.,
RA   Varnum B., Liu E.T., Cance W.G.;
RT   "Receptor tyrosine kinases expressed in metastatic colon cancer.";
RL   Int. J. Cancer 60:791-797(1995).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH IFNGR1, AND
RP   PHOSPHORYLATION.
RX   PubMed=7615558; DOI=10.1074/jbc.270.29.17528;
RA   Sakatsume M., Igarashi K., Winestock K.D., Garotta G., Larner A.C.,
RA   Finbloom D.S.;
RT   "The Jak kinases differentially associate with the alpha and beta
RT   (accessory factor) chains of the interferon gamma receptor to form a
RT   functional receptor unit capable of activating STAT transcription
RT   factors.";
RL   J. Biol. Chem. 270:17528-17534(1995).
RN   [9]
RP   INTERACTION WITH IFNAR2.
RX   PubMed=7759950; DOI=10.1002/jlb.57.5.712;
RA   Novick D., Cohen B., Tal N., Rubinstein M.;
RT   "Soluble and membrane-anchored forms of the human IFN-alpha/beta
RT   receptor.";
RL   J. Leukoc. Biol. 57:712-718(1995).
RN   [10]
RP   INTERACTION WITH SHB.
RX   PubMed=12200137; DOI=10.1016/s0006-291x(02)02016-8;
RA   Lindholm C.K.;
RT   "IL-2 receptor signaling through the Shb adapter protein in T and NK
RT   cells.";
RL   Biochem. Biophys. Res. Commun. 296:929-936(2002).
RN   [11]
RP   FUNCTION IN CYTOKINE SIGNALING, PHOSPHORYLATION AT TYR-1034 AND TYR-1035,
RP   AND DEPHOSPHORYLATION AT TYR-1034 AND TYR-1035 BY PTPN2.
RX   PubMed=11909529; DOI=10.1016/s0960-9822(02)00697-8;
RA   Simoncic P.D., Lee-Loy A., Barber D.L., Tremblay M.L., McGlade C.J.;
RT   "The T cell protein tyrosine phosphatase is a negative regulator of janus
RT   family kinases 1 and 3.";
RL   Curr. Biol. 12:446-453(2002).
RN   [12]
RP   FUNCTION, AND INTERACTION WITH IL2RB AND IL10RA.
RX   PubMed=12133952; DOI=10.4049/jimmunol.169.3.1302;
RA   Usacheva A., Kotenko S., Witte M.M., Colamonici O.R.;
RT   "Two distinct domains within the N-terminal region of Janus kinase 1
RT   interact with cytokine receptors.";
RL   J. Immunol. 169:1302-1308(2002).
RN   [13]
RP   INTERACTION WITH IL31RA.
RX   PubMed=15194700; DOI=10.1074/jbc.m401122200;
RA   Dreuw A., Radtke S., Pflanz S., Lippok B.E., Heinrich P.C., Hermanns H.M.;
RT   "Characterization of the signaling capacities of the novel gp130-like
RT   cytokine receptor.";
RL   J. Biol. Chem. 279:36112-36120(2004).
RN   [14]
RP   INTERACTION WITH JAKMIP1.
RX   PubMed=15277531; DOI=10.1074/jbc.m401915200;
RA   Steindler C., Li Z., Algarte M., Alcover A., Libri V., Ragimbeau J.,
RA   Pellegrini S.;
RT   "Jamip1 (marlin-1) defines a family of proteins interacting with Janus
RT   kinases and microtubules.";
RL   J. Biol. Chem. 279:43168-43177(2004).
RN   [15]
RP   FUNCTION, DOMAIN, AND MUTAGENESIS OF VAL-658.
RX   PubMed=16239216; DOI=10.1074/jbc.c500358200;
RA   Staerk J., Kallin A., Demoulin J.B., Vainchenker W., Constantinescu S.N.;
RT   "JAK1 and Tyk2 activation by the homologous polycythemia vera JAK2 V617F
RT   mutation: cross-talk with IGF1 receptor.";
RL   J. Biol. Chem. 280:41893-41899(2005).
RN   [16]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT TYR-3 AND SER-228, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [19]
RP   UBIQUITINATION.
RX   PubMed=26027934; DOI=10.1016/j.celrep.2015.04.049;
RA   Kim H., Frederick D.T., Levesque M.P., Cooper Z.A., Feng Y., Krepler C.,
RA   Brill L., Samuels Y., Hayward N.K., Perlina A., Piris A., Zhang T.,
RA   Halaban R., Herlyn M.M., Brown K.M., Wargo J.A., Dummer R., Flaherty K.T.,
RA   Ronai Z.A.;
RT   "Downregulation of the ubiquitin ligase RNF125 underlies resistance of
RT   melanoma cells to BRAF inhibitors via JAK1 deregulation.";
RL   Cell Rep. 11:1458-1473(2015).
RN   [20]
RP   INVOLVEMENT IN AIIDE, VARIANT AIIDE ASP-634, CHARACTERIZATION OF VARIANT
RP   AIIDE ASP-634, AND FUNCTION.
RX   PubMed=28111307; DOI=10.1016/j.jaci.2016.12.957;
RA   Del Bel K.L., Ragotte R.J., Saferali A., Lee S., Vercauteren S.M.,
RA   Mostafavi S.A., Schreiber R.A., Prendiville J.S., Phang M.S., Halparin J.,
RA   Au N., Dean J.M., Priatel J.J., Jewels E., Junker A.K., Rogers P.C.,
RA   Seear M., McKinnon M.L., Turvey S.E.;
RT   "JAK1 gain-of-function causes an autosomal dominant immune dysregulatory
RT   and hypereosinophilic syndrome.";
RL   J. Allergy Clin. Immunol. 139:e52016-e52020(2017).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 865-1154 IN COMPLEXES WITH
RP   SYNTHETIC INHIBITORS CMP6 AND CP-690,550.
RX   PubMed=19361440; DOI=10.1016/j.jmb.2009.01.041;
RA   Williams N.K., Bamert R.S., Patel O., Wang C., Walden P.M., Wilks A.F.,
RA   Fantino E., Rossjohn J., Lucet I.S.;
RT   "Dissecting specificity in the Janus kinases: the structures of JAK-
RT   specific inhibitors complexed to the JAK1 and JAK2 protein tyrosine kinase
RT   domains.";
RL   J. Mol. Biol. 387:219-232(2009).
RN   [22]
RP   VARIANT [LARGE SCALE ANALYSIS] LYS-973.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA   Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA   Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA   Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA   Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA   Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA   Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA   Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA   Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA   Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA   Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA   Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
RN   [23]
RP   VARIANT AIIDE ILE-703, CHARACTERIZATION OF VARIANT AIIDE ILE-703, FUNCTION,
RP   MUTAGENESIS OF LYS-908, AND ATP-BINDING.
RX   PubMed=32750333; DOI=10.1016/j.immuni.2020.07.006;
RA   Gruber C.N., Calis J.J.A., Buta S., Evrony G., Martin J.C., Uhl S.A.,
RA   Caron R., Jarchin L., Dunkin D., Phelps R., Webb B.D., Saland J.M.,
RA   Merad M., Orange J.S., Mace E.M., Rosenberg B.R., Gelb B.D., Bogunovic D.;
RT   "Complex Autoinflammatory Syndrome Unveils Fundamental Principles of JAK1
RT   Kinase Transcriptional and Biochemical Function.";
RL   Immunity 53:e11672-e11684(2020).
CC   -!- FUNCTION: Tyrosine kinase of the non-receptor type, involved in the
CC       IFN-alpha/beta/gamma signal pathway (PubMed:7615558, PubMed:28111307,
CC       PubMed:32750333, PubMed:16239216). Kinase partner for the interleukin
CC       (IL)-2 receptor (PubMed:11909529) as well as interleukin (IL)-10
CC       receptor (PubMed:12133952). Directly phosphorylates STAT but also
CC       activates STAT signaling through the transactivation of other JAK
CC       kinases associated with signaling receptors (PubMed:16239216,
CC       PubMed:32750333). {ECO:0000269|PubMed:11909529,
CC       ECO:0000269|PubMed:12133952, ECO:0000269|PubMed:16239216,
CC       ECO:0000269|PubMed:28111307, ECO:0000269|PubMed:32750333,
CC       ECO:0000269|PubMed:7615558}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
CC         ECO:0000269|PubMed:1848670, ECO:0000269|PubMed:7615558};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000305|PubMed:7615558};
CC       Note=Mn(2+) was used in the in vitro kinase assay but Mg(2+) is likely
CC       to be the in vivo cofactor. {ECO:0000305|PubMed:7615558};
CC   -!- SUBUNIT: Interacts with IL31RA (PubMed:15194700). Interacts with IFNAR2
CC       (PubMed:7759950). Interacts with IFNGR1 (PubMed:7615558). Interacts
CC       with JAKMIP1 (PubMed:15277531). Interacts with SHB (PubMed:12200137).
CC       Interacts (via N-terminus) with IL2RB and IL10RA (via its cytoplasmic
CC       domain) (PubMed:12133952). Interacts with FER (By similarity).
CC       {ECO:0000250|UniProtKB:P52332, ECO:0000269|PubMed:12133952,
CC       ECO:0000269|PubMed:12200137, ECO:0000269|PubMed:15194700,
CC       ECO:0000269|PubMed:15277531, ECO:0000269|PubMed:7615558,
CC       ECO:0000269|PubMed:7759950}.
CC   -!- INTERACTION:
CC       P23458; P04626: ERBB2; NbExp=2; IntAct=EBI-1383438, EBI-641062;
CC       P23458; P48551: IFNAR2; NbExp=3; IntAct=EBI-1383438, EBI-958408;
CC       P23458; P40189-1: IL6ST; NbExp=3; IntAct=EBI-1383438, EBI-15742214;
CC       P23458; O60674: JAK2; NbExp=4; IntAct=EBI-1383438, EBI-518647;
CC       P23458; P42224: STAT1; NbExp=6; IntAct=EBI-1383438, EBI-1057697;
CC       P23458; P40763: STAT3; NbExp=2; IntAct=EBI-1383438, EBI-518675;
CC   -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein.
CC       Note=Wholly intracellular, possibly membrane associated.
CC   -!- TISSUE SPECIFICITY: Expressed at higher levels in primary colon tumors
CC       than in normal colon tissue. The expression level in metastatic colon
CC       tumors is comparable to the expression level in normal colon tissue.
CC       {ECO:0000269|PubMed:7896447}.
CC   -!- DOMAIN: The protein kinase 1 domain is also called the pseudokinase
CC       domain and has a regulatory role through the transactivation of other
CC       JAK kinases associated with signaling receptors.
CC       {ECO:0000269|PubMed:16239216, ECO:0000269|PubMed:32750333}.
CC   -!- DOMAIN: The protein kinase 2 domain is the catalytically active domain.
CC       {ECO:0000269|PubMed:32750333}.
CC   -!- DOMAIN: The FERM domain mediates interaction with JAKMIP1.
CC   -!- PTM: Autophosphorylated (PubMed:7615558). Phosphorylated on tyrosine
CC       residues in response to interferon gamma signaling (PubMed:7615558).
CC       Dephosphorylation of Tyr-1034 and Tyr-1035 by PTPN2 negatively
CC       regulates cytokine-mediated signaling (PubMed:11909529).
CC       {ECO:0000269|PubMed:11909529, ECO:0000269|PubMed:7615558}.
CC   -!- PTM: Ubiquitinated by RNF125; leading to its degradation by the
CC       proteasome. {ECO:0000269|PubMed:26027934}.
CC   -!- DISEASE: Autoinflammation, immune dysregulation, and eosinophilia
CC       (AIIDE) [MIM:618999]: An autosomal dominant disorder characterized by
CC       immune dysregulation, severe atopic dermatitis, and chronic
CC       gastrointestinal inflammation. Additional features include asthma, food
CC       or environmental allergies, as well as poor overall growth with short
CC       stature. {ECO:0000269|PubMed:28111307, ECO:0000269|PubMed:32750333}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. JAK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA36527.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAA36527.1; Type=Frameshift; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/JAK1ID41031ch1p31.html";
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DR   EMBL; M64174; AAA36527.1; ALT_SEQ; mRNA.
DR   EMBL; AB209057; BAD92294.1; -; mRNA.
DR   EMBL; AC093427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471059; EAX06547.1; -; Genomic_DNA.
DR   EMBL; BC132729; AAI32730.1; -; mRNA.
DR   CCDS; CCDS41346.1; -.
DR   PIR; A39577; A39577.
DR   RefSeq; NP_001307852.1; NM_001320923.1.
DR   RefSeq; NP_001308781.1; NM_001321852.1.
DR   RefSeq; NP_001308782.1; NM_001321853.1.
DR   RefSeq; NP_001308783.1; NM_001321854.1.
DR   RefSeq; NP_001308784.1; NM_001321855.1.
DR   RefSeq; NP_001308785.1; NM_001321856.1.
DR   RefSeq; NP_002218.2; NM_002227.3.
DR   PDB; 3EYG; X-ray; 1.90 A; A=865-1154.
DR   PDB; 3EYH; X-ray; 2.00 A; A=865-1154.
DR   PDB; 4E4L; X-ray; 2.00 A; A/B/D/E=854-1154.
DR   PDB; 4E4N; X-ray; 1.90 A; A/B=854-1154.
DR   PDB; 4E5W; X-ray; 1.86 A; A/B=854-1154.
DR   PDB; 4EHZ; X-ray; 2.17 A; A/B/C/D=854-1154.
DR   PDB; 4EI4; X-ray; 2.22 A; A/B=854-1154.
DR   PDB; 4FK6; X-ray; 2.20 A; A/B=854-1154.
DR   PDB; 4GS0; X-ray; 1.80 A; C=1033-1036.
DR   PDB; 4I5C; X-ray; 2.10 A; A/B=854-1154.
DR   PDB; 4IVB; X-ray; 1.90 A; A/B=854-1154.
DR   PDB; 4IVC; X-ray; 2.35 A; A/B=854-1154.
DR   PDB; 4IVD; X-ray; 1.93 A; A/B=854-1154.
DR   PDB; 4K6Z; X-ray; 2.73 A; A=854-1154.
DR   PDB; 4K77; X-ray; 2.40 A; A/B=854-1154.
DR   PDB; 4L00; X-ray; 1.80 A; A/B=561-860.
DR   PDB; 4L01; X-ray; 1.90 A; A/B=561-860.
DR   PDB; 5E1E; X-ray; 2.30 A; A/B=865-1154.
DR   PDB; 5HX8; X-ray; 2.20 A; A/B=854-1154.
DR   PDB; 5IXD; X-ray; 2.85 A; A=35-559.
DR   PDB; 5IXI; X-ray; 2.57 A; A=35-559.
DR   PDB; 5KHW; X-ray; 2.47 A; A/B=841-1154.
DR   PDB; 5KHX; X-ray; 2.40 A; A=841-1154.
DR   PDB; 5L04; X-ray; 2.10 A; A=31-577.
DR   PDB; 5WO4; X-ray; 1.84 A; A/B=854-1154.
DR   PDB; 6AAH; X-ray; 1.83 A; A/B=865-1154.
DR   PDB; 6BBU; X-ray; 2.08 A; A=841-1154.
DR   PDB; 6C7Y; X-ray; 2.50 A; A=869-1153.
DR   PDB; 6DBN; X-ray; 2.48 A; A=841-1154.
DR   PDB; 6ELR; X-ray; 1.80 A; A/B=854-1154.
DR   PDB; 6GGH; X-ray; 1.70 A; A/B=863-1154.
DR   PDB; 6HZU; X-ray; 2.20 A; A/B=854-1154.
DR   PDB; 6N77; X-ray; 1.64 A; A/B=854-1154.
DR   PDB; 6N78; X-ray; 1.83 A; A=854-1154.
DR   PDB; 6N79; X-ray; 2.27 A; A=854-1154.
DR   PDB; 6N7A; X-ray; 1.33 A; A/B=854-1154.
DR   PDB; 6N7B; X-ray; 1.81 A; A=854-1154.
DR   PDB; 6N7C; X-ray; 1.69 A; A/B=854-1154.
DR   PDB; 6N7D; X-ray; 1.78 A; A=854-1154.
DR   PDB; 6RSB; X-ray; 1.80 A; A/B=854-1154.
DR   PDB; 6RSC; X-ray; 1.85 A; A/B=854-1154.
DR   PDB; 6RSD; X-ray; 1.76 A; A/B=854-1154.
DR   PDB; 6RSE; X-ray; 1.80 A; A/B=854-1154.
DR   PDB; 6RSH; X-ray; 1.71 A; A/B=854-1154.
DR   PDB; 6SM8; X-ray; 1.85 A; A/B=854-1154.
DR   PDB; 6SMB; X-ray; 2.04 A; A/B=854-1154.
DR   PDB; 6TPE; X-ray; 2.87 A; A/B=864-1154.
DR   PDB; 6TPF; X-ray; 2.31 A; A/B=864-1154.
DR   PDB; 6W8L; X-ray; 2.11 A; A=841-1154.
DR   PDBsum; 3EYG; -.
DR   PDBsum; 3EYH; -.
DR   PDBsum; 4E4L; -.
DR   PDBsum; 4E4N; -.
DR   PDBsum; 4E5W; -.
DR   PDBsum; 4EHZ; -.
DR   PDBsum; 4EI4; -.
DR   PDBsum; 4FK6; -.
DR   PDBsum; 4GS0; -.
DR   PDBsum; 4I5C; -.
DR   PDBsum; 4IVB; -.
DR   PDBsum; 4IVC; -.
DR   PDBsum; 4IVD; -.
DR   PDBsum; 4K6Z; -.
DR   PDBsum; 4K77; -.
DR   PDBsum; 4L00; -.
DR   PDBsum; 4L01; -.
DR   PDBsum; 5E1E; -.
DR   PDBsum; 5HX8; -.
DR   PDBsum; 5IXD; -.
DR   PDBsum; 5IXI; -.
DR   PDBsum; 5KHW; -.
DR   PDBsum; 5KHX; -.
DR   PDBsum; 5L04; -.
DR   PDBsum; 5WO4; -.
DR   PDBsum; 6AAH; -.
DR   PDBsum; 6BBU; -.
DR   PDBsum; 6C7Y; -.
DR   PDBsum; 6DBN; -.
DR   PDBsum; 6ELR; -.
DR   PDBsum; 6GGH; -.
DR   PDBsum; 6HZU; -.
DR   PDBsum; 6N77; -.
DR   PDBsum; 6N78; -.
DR   PDBsum; 6N79; -.
DR   PDBsum; 6N7A; -.
DR   PDBsum; 6N7B; -.
DR   PDBsum; 6N7C; -.
DR   PDBsum; 6N7D; -.
DR   PDBsum; 6RSB; -.
DR   PDBsum; 6RSC; -.
DR   PDBsum; 6RSD; -.
DR   PDBsum; 6RSE; -.
DR   PDBsum; 6RSH; -.
DR   PDBsum; 6SM8; -.
DR   PDBsum; 6SMB; -.
DR   PDBsum; 6TPE; -.
DR   PDBsum; 6TPF; -.
DR   PDBsum; 6W8L; -.
DR   AlphaFoldDB; P23458; -.
DR   SMR; P23458; -.
DR   BioGRID; 109919; 232.
DR   ComplexPortal; CPX-5995; Interferon alpha receptor-ligand complex, IFNA2 variant.
DR   ComplexPortal; CPX-5996; Interferon alpha receptor-ligand complex, IFNA1 variant.
DR   ComplexPortal; CPX-5997; Interferon alpha receptor-ligand complex, IFNA7 variant.
DR   ComplexPortal; CPX-5998; Interferon alpha receptor-ligand complex, IFNA4 variant.
DR   ComplexPortal; CPX-5999; Interferon alpha receptor-ligand complex, IFNA5 variant.
DR   ComplexPortal; CPX-6000; Interferon alpha receptor-ligand complex, IFNA6 variant.
DR   ComplexPortal; CPX-6001; Interferon alpha receptor-ligand complex, IFNA8 variant.
DR   ComplexPortal; CPX-6002; Interferon alpha receptor-ligand complex, IFNA10 variant.
DR   ComplexPortal; CPX-6003; Interferon alpha receptor-ligand complex, IFNA14 variant.
DR   ComplexPortal; CPX-6004; Interferon alpha receptor-ligand complex, IFNA16 variant.
DR   ComplexPortal; CPX-6005; Interferon alpha receptor-ligand complex, IFNA17 variant.
DR   ComplexPortal; CPX-6006; Interferon alpha receptor-ligand complex, IFNA21 variant.
DR   ComplexPortal; CPX-6007; Interferon beta receptor-ligand complex.
DR   ComplexPortal; CPX-6008; Interferon epsilon receptor-ligand complex.
DR   ComplexPortal; CPX-6009; Interferon kappa receptor-ligand complex.
DR   ComplexPortal; CPX-6010; Interferon omega receptor-ligand complex.
DR   ComplexPortal; CPX-6011; Interferon lambda receptor-ligand complex, IFNL1 variant.
DR   ComplexPortal; CPX-6012; Interferon lambda receptor-ligand complex, IFNL2 variant.
DR   ComplexPortal; CPX-6013; Interferon lambda receptor-ligand complex, IFNL3 variant.
DR   ComplexPortal; CPX-6014; Interferon lambda receptor-ligand complex, IFNL4 variant.
DR   ComplexPortal; CPX-6015; Interferon gamma receptor-ligand complex.
DR   CORUM; P23458; -.
DR   DIP; DIP-133N; -.
DR   IntAct; P23458; 84.
DR   MINT; P23458; -.
DR   STRING; 9606.ENSP00000343204; -.
DR   BindingDB; P23458; -.
DR   ChEMBL; CHEMBL2835; -.
DR   DrugBank; DB04716; 2-tert-butyl-9-fluoro-1,6-dihydrobenzo[h]imidazo[4,5-f]isoquinolin-7-one.
DR   DrugBank; DB11817; Baricitinib.
DR   DrugBank; DB12500; Fedratinib.
DR   DrugBank; DB14845; Filgotinib.
DR   DrugBank; DB12010; Fostamatinib.
DR   DrugBank; DB02375; Myricetin.
DR   DrugBank; DB15822; Pralsetinib.
DR   DrugBank; DB08877; Ruxolitinib.
DR   DrugBank; DB08895; Tofacitinib.
DR   DrugBank; DB15091; Upadacitinib.
DR   DrugCentral; P23458; -.
DR   GuidetoPHARMACOLOGY; 2047; -.
DR   CarbonylDB; P23458; -.
DR   GlyConnect; 1869; 2 N-Linked glycans (1 site).
DR   GlyGen; P23458; 1 site, 2 N-linked glycans (1 site).
DR   iPTMnet; P23458; -.
DR   PhosphoSitePlus; P23458; -.
DR   SwissPalm; P23458; -.
DR   BioMuta; JAK1; -.
DR   DMDM; 215274013; -.
DR   CPTAC; CPTAC-1251; -.
DR   EPD; P23458; -.
DR   jPOST; P23458; -.
DR   MassIVE; P23458; -.
DR   MaxQB; P23458; -.
DR   PaxDb; P23458; -.
DR   PeptideAtlas; P23458; -.
DR   PRIDE; P23458; -.
DR   ProteomicsDB; 54097; -.
DR   Antibodypedia; 3400; 632 antibodies from 43 providers.
DR   CPTC; P23458; 1 antibody.
DR   DNASU; 3716; -.
DR   Ensembl; ENST00000342505.5; ENSP00000343204.4; ENSG00000162434.13.
DR   Ensembl; ENST00000671929.1; ENSP00000500485.1; ENSG00000162434.13.
DR   Ensembl; ENST00000671954.1; ENSP00000500841.1; ENSG00000162434.13.
DR   Ensembl; ENST00000672179.1; ENSP00000500296.1; ENSG00000162434.13.
DR   Ensembl; ENST00000672247.1; ENSP00000499884.1; ENSG00000162434.13.
DR   Ensembl; ENST00000672434.1; ENSP00000499900.1; ENSG00000162434.13.
DR   GeneID; 3716; -.
DR   KEGG; hsa:3716; -.
DR   MANE-Select; ENST00000342505.5; ENSP00000343204.4; NM_002227.4; NP_002218.2.
DR   UCSC; uc001dbu.2; human.
DR   CTD; 3716; -.
DR   DisGeNET; 3716; -.
DR   GeneCards; JAK1; -.
DR   HGNC; HGNC:6190; JAK1.
DR   HPA; ENSG00000162434; Low tissue specificity.
DR   MalaCards; JAK1; -.
DR   MIM; 147795; gene.
DR   MIM; 618999; phenotype.
DR   neXtProt; NX_P23458; -.
DR   OpenTargets; ENSG00000162434; -.
DR   Orphanet; 574957; Autosomal recessive mendelian susceptibility to mycobacterial diseases due to partial JAK1 deficiency.
DR   PharmGKB; PA29988; -.
DR   VEuPathDB; HostDB:ENSG00000162434; -.
DR   eggNOG; KOG0197; Eukaryota.
DR   GeneTree; ENSGT00940000157092; -.
DR   HOGENOM; CLU_008155_1_0_1; -.
DR   InParanoid; P23458; -.
DR   OMA; AQECRIS; -.
DR   OrthoDB; 58906at2759; -.
DR   PhylomeDB; P23458; -.
DR   TreeFam; TF327041; -.
DR   BRENDA; 2.7.10.2; 2681.
DR   PathwayCommons; P23458; -.
DR   Reactome; R-HSA-1059683; Interleukin-6 signaling.
DR   Reactome; R-HSA-110056; MAPK3 (ERK1) activation.
DR   Reactome; R-HSA-112411; MAPK1 (ERK2) activation.
DR   Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR   Reactome; R-HSA-1266695; Interleukin-7 signaling.
DR   Reactome; R-HSA-449836; Other interleukin signaling.
DR   Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR   Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR   Reactome; R-HSA-6788467; IL-6-type cytokine receptor ligand interactions.
DR   Reactome; R-HSA-877300; Interferon gamma signaling.
DR   Reactome; R-HSA-877312; Regulation of IFNG signaling.
DR   Reactome; R-HSA-8854691; Interleukin-20 family signaling.
DR   Reactome; R-HSA-8983432; Interleukin-15 signaling.
DR   Reactome; R-HSA-8984722; Interleukin-35 Signalling.
DR   Reactome; R-HSA-8985947; Interleukin-9 signaling.
DR   Reactome; R-HSA-9020558; Interleukin-2 signaling.
DR   Reactome; R-HSA-9020591; Interleukin-12 signaling.
DR   Reactome; R-HSA-9020956; Interleukin-27 signaling.
DR   Reactome; R-HSA-9020958; Interleukin-21 signaling.
DR   Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR   Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
DR   Reactome; R-HSA-912694; Regulation of IFNA/IFNB signaling.
DR   Reactome; R-HSA-9674555; Signaling by CSF3 (G-CSF).
DR   Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR   Reactome; R-HSA-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR   Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR   SignaLink; P23458; -.
DR   SIGNOR; P23458; -.
DR   BioGRID-ORCS; 3716; 48 hits in 1124 CRISPR screens.
DR   ChiTaRS; JAK1; human.
DR   EvolutionaryTrace; P23458; -.
DR   GeneWiki; Janus_kinase_1; -.
DR   GenomeRNAi; 3716; -.
DR   Pharos; P23458; Tclin.
DR   PRO; PR:P23458; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P23458; protein.
DR   Bgee; ENSG00000162434; Expressed in type B pancreatic cell and 203 other tissues.
DR   ExpressionAtlas; P23458; baseline and differential.
DR   Genevisible; P23458; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; TAS:Reactome.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0031730; F:CCR5 chemokine receptor binding; IEA:Ensembl.
DR   GO; GO:0005126; F:cytokine receptor binding; IBA:GO_Central.
DR   GO; GO:0005131; F:growth hormone receptor binding; ISS:BHF-UCL.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; EXP:Reactome.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0098586; P:cellular response to virus; IC:ComplexPortal.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR   GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0038110; P:interleukin-2-mediated signaling pathway; IDA:UniProtKB.
DR   GO; GO:0070102; P:interleukin-6-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0034112; P:positive regulation of homotypic cell-cell adhesion; IMP:ARUK-UCL.
DR   GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IGI:BHF-UCL.
DR   GO; GO:0150105; P:protein localization to cell-cell junction; IMP:ARUK-UCL.
DR   GO; GO:0006468; P:protein phosphorylation; IMP:UniProtKB.
DR   GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IMP:UniProtKB.
DR   GO; GO:0046677; P:response to antibiotic; IDA:MGI.
DR   GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
DR   GO; GO:0038196; P:type III interferon signaling pathway; IC:ComplexPortal.
DR   GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IBA:GO_Central.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   Gene3D; 3.30.505.10; -; 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR041155; FERM_F1.
DR   InterPro; IPR041046; FERM_F2.
DR   InterPro; IPR041381; JAK1-3/TYK2_PHL_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR016251; Tyr_kinase_non-rcpt_Jak/Tyk2.
DR   InterPro; IPR020776; Tyr_kinase_non-rcpt_Jak1.
DR   Pfam; PF18379; FERM_F1; 1.
DR   Pfam; PF18377; FERM_F2; 1.
DR   Pfam; PF17887; Jak1_Phl; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR   PIRSF; PIRSF000636; TyrPK_Jak; 1.
DR   PRINTS; PR01823; JANUSKINASE.
DR   PRINTS; PR01824; JANUSKINASE1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00219; TyrKc; 2.
DR   SUPFAM; SSF47031; SSF47031; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   SUPFAM; SSF56112; SSF56112; 2.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Disease variant; Kinase; Magnesium;
KW   Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Repeat; SH2 domain; Transferase;
KW   Tyrosine-protein kinase; Ubl conjugation.
FT   CHAIN           1..1154
FT                   /note="Tyrosine-protein kinase JAK1"
FT                   /id="PRO_0000088108"
FT   DOMAIN          34..420
FT                   /note="FERM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT   DOMAIN          439..544
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          583..855
FT                   /note="Protein kinase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          875..1153
FT                   /note="Protein kinase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        1003
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         881..889
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         908
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000305|PubMed:32750333"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:19369195"
FT   MOD_RES         3
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:19369195"
FT   MOD_RES         228
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19369195"
FT   MOD_RES         1034
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:11909529"
FT   MOD_RES         1035
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:11909529"
FT   VARIANT         634
FT                   /note="A -> D (in AIIDE; constitutive gain of function
FT                   resulting in increased receptor signaling pathway via JAK-
FT                   STAT; no effect on protein abundance)"
FT                   /evidence="ECO:0000269|PubMed:28111307"
FT                   /id="VAR_084991"
FT   VARIANT         703
FT                   /note="S -> I (in AIIDE; increased activation of protein
FT                   kinase activity; constitutive gain of function through the
FT                   transactivation of associated JAK kinases; increased
FT                   receptor signaling pathway via JAK-STAT)"
FT                   /evidence="ECO:0000269|PubMed:32750333"
FT                   /id="VAR_084992"
FT   VARIANT         973
FT                   /note="N -> K (in dbSNP:rs34680086)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041715"
FT   MUTAGEN         658
FT                   /note="V->F: Constitutively active. Increased receptor
FT                   signaling pathway via JAK-STAT."
FT                   /evidence="ECO:0000269|PubMed:16239216"
FT   MUTAGEN         908
FT                   /note="K->A: Loss of protein tyrosine kinase activity."
FT                   /evidence="ECO:0000269|PubMed:32750333"
FT   CONFLICT        350
FT                   /note="H -> D (in Ref. 1; AAA36527)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        368
FT                   /note="Y -> F (in Ref. 1; AAA36527)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        898
FT                   /note="Missing (in Ref. 1; AAA36527)"
FT                   /evidence="ECO:0000305"
FT   STRAND          36..39
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          43..45
FT                   /evidence="ECO:0007829|PDB:5IXI"
FT   STRAND          48..50
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          52..56
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   HELIX           57..67
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   TURN            72..74
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   HELIX           75..77
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          78..82
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   TURN            83..86
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          94..97
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          103..109
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   TURN            114..117
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          121..123
FT                   /evidence="ECO:0007829|PDB:5IXI"
FT   STRAND          149..151
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   HELIX           152..167
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   HELIX           179..204
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   TURN            208..210
FT                   /evidence="ECO:0007829|PDB:5IXD"
FT   HELIX           217..220
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   HELIX           223..230
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   HELIX           234..252
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   HELIX           254..259
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   HELIX           263..277
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          278..280
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          284..289
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          291..293
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          299..304
FT                   /evidence="ECO:0007829|PDB:5IXI"
FT   STRAND          313..318
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   TURN            319..321
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          322..327
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          364..367
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   HELIX           369..371
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          372..378
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          381..386
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          391..395
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   HELIX           399..416
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   HELIX           425..427
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   HELIX           430..437
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   HELIX           446..456
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          463..467
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          472..482
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          493..503
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          506..509
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          516..518
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   HELIX           519..527
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          529..533
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          536..538
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   STRAND          555..557
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   HELIX           559..562
FT                   /evidence="ECO:0007829|PDB:5L04"
FT   HELIX           569..572
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   STRAND          575..578
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   HELIX           580..582
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   STRAND          583..592
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   STRAND          595..603
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   STRAND          616..624
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   HELIX           629..644
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   STRAND          653..659
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   STRAND          662..668
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   HELIX           675..682
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   TURN            683..685
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   HELIX           688..707
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   HELIX           717..719
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   STRAND          720..724
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   STRAND          727..731
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   STRAND          734..737
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   HELIX           744..746
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   HELIX           749..754
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   TURN            755..758
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   HELIX           761..765
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   HELIX           767..769
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   HELIX           774..787
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   TURN            788..790
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   TURN            793..796
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   HELIX           799..807
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   HELIX           818..827
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   HELIX           832..834
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   HELIX           838..848
FT                   /evidence="ECO:0007829|PDB:4L00"
FT   HELIX           872..874
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   STRAND          875..883
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   STRAND          885..894
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   STRAND          898..900
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   STRAND          902..910
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   TURN            915..917
FT                   /evidence="ECO:0007829|PDB:6RSE"
FT   HELIX           919..930
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   STRAND          940..944
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   STRAND          947..949
FT                   /evidence="ECO:0007829|PDB:6HZU"
FT   STRAND          953..957
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   HELIX           964..970
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   TURN            972..974
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   HELIX           977..996
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   STRAND          998..1000
FT                   /evidence="ECO:0007829|PDB:4K6Z"
FT   HELIX           1006..1008
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   STRAND          1009..1013
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   STRAND          1016..1019
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   STRAND          1033..1036
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   STRAND          1039..1041
FT                   /evidence="ECO:0007829|PDB:5KHX"
FT   HELIX           1045..1047
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   HELIX           1050..1055
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   STRAND          1057..1059
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   HELIX           1060..1075
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   TURN            1076..1078
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   HELIX           1080..1082
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   HELIX           1084..1092
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   TURN            1097..1099
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   HELIX           1100..1109
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   HELIX           1122..1129
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   HELIX           1130..1132
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   HELIX           1136..1138
FT                   /evidence="ECO:0007829|PDB:6N7A"
FT   HELIX           1142..1153
FT                   /evidence="ECO:0007829|PDB:6N7A"
SQ   SEQUENCE   1154 AA;  133277 MW;  A2C4BE27851ACABB CRC64;
     MQYLNIKEDC NAMAFCAKMR SSKKTEVNLE APEPGVEVIF YLSDREPLRL GSGEYTAEEL
     CIRAAQACRI SPLCHNLFAL YDENTKLWYA PNRTITVDDK MSLRLHYRMR FYFTNWHGTN
     DNEQSVWRHS PKKQKNGYEK KKIPDATPLL DASSLEYLFA QGQYDLVKCL APIRDPKTEQ
     DGHDIENECL GMAVLAISHY AMMKKMQLPE LPKDISYKRY IPETLNKSIR QRNLLTRMRI
     NNVFKDFLKE FNNKTICDSS VSTHDLKVKY LATLETLTKH YGAEIFETSM LLISSENEMN
     WFHSNDGGNV LYYEVMVTGN LGIQWRHKPN VVSVEKEKNK LKRKKLENKH KKDEEKNKIR
     EEWNNFSYFP EITHIVIKES VVSINKQDNK KMELKLSSHE EALSFVSLVD GYFRLTADAH
     HYLCTDVAPP LIVHNIQNGC HGPICTEYAI NKLRQEGSEE GMYVLRWSCT DFDNILMTVT
     CFEKSEQVQG AQKQFKNFQI EVQKGRYSLH GSDRSFPSLG DLMSHLKKQI LRTDNISFML
     KRCCQPKPRE ISNLLVATKK AQEWQPVYPM SQLSFDRILK KDLVQGEHLG RGTRTHIYSG
     TLMDYKDDEG TSEEKKIKVI LKVLDPSHRD ISLAFFEAAS MMRQVSHKHI VYLYGVCVRD
     VENIMVEEFV EGGPLDLFMH RKSDVLTTPW KFKVAKQLAS ALSYLEDKDL VHGNVCTKNL
     LLAREGIDSE CGPFIKLSDP GIPITVLSRQ ECIERIPWIA PECVEDSKNL SVAADKWSFG
     TTLWEICYNG EIPLKDKTLI EKERFYESRC RPVTPSCKEL ADLMTRCMNY DPNQRPFFRA
     IMRDINKLEE QNPDIVSEKK PATEVDPTHF EKRFLKRIRD LGEGHFGKVE LCRYDPEGDN
     TGEQVAVKSL KPESGGNHIA DLKKEIEILR NLYHENIVKY KGICTEDGGN GIKLIMEFLP
     SGSLKEYLPK NKNKINLKQQ LKYAVQICKG MDYLGSRQYV HRDLAARNVL VESEHQVKIG
     DFGLTKAIET DKEYYTVKDD RDSPVFWYAP ECLMQSKFYI ASDVWSFGVT LHELLTYCDS
     DSSPMALFLK MIGPTHGQMT VTRLVNTLKE GKRLPCPPNC PDEVYQLMRK CWEFQPSNRT
     SFQNLIEGFE ALLK
 
 
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