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
