CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005176
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tyrosine-protein kinase JAK1 
Protein Synonyms/Alias
 Janus kinase 1; JAK-1 
Gene Name
 JAK1 
Gene Synonyms/Alias
 JAK1A; JAK1B 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
86ALYDENTKLWYAPNRubiquitination[1]
100RTITVDDKMSLRLHYubiquitination[2, 3]
141QKNGYEKKKIPDATPubiquitination[2]
142KNGYEKKKIPDATPLubiquitination[2]
213MQLPELPKDISYKRYubiquitination[4, 5, 6, 7]
227YIPETLNKSIRQRNLubiquitination[2, 5, 6, 7, 8]
245MRINNVFKDFLKEFNubiquitination[2, 5, 6, 7]
249NVFKDFLKEFNNKTIubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12]
269STHDLKVKYLATLETubiquitination[5, 7]
493EQVQGAQKQFKNFQIubiquitination[2]
496QGAQKQFKNFQIEVQubiquitination[12]
504NFQIEVQKGRYSLHGubiquitination[2]
541DNISFMLKRCCQPKPubiquitination[2]
560NLLVATKKAQEWQPVubiquitination[2]
802KDKTLIEKERFYESRubiquitination[2]
859NPDIVSEKKPATEVDubiquitination[1]
860PDIVSEKKPATEVDPubiquitination[1]
924NHIADLKKEIEILRNubiquitination[1, 12]
1130EVYQLMRKCWEFQPSubiquitination[2]
Reference
 [1] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [8] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113]
 [9] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [10] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [11] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [12] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
Functional Description
 Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway. Kinase partner for the interleukin (IL)-2 receptor. 
Sequence Annotation
 DOMAIN 34 420 FERM.
 DOMAIN 439 544 SH2.
 DOMAIN 583 855 Protein kinase 1.
 DOMAIN 875 1153 Protein kinase 2.
 NP_BIND 881 889 ATP (By similarity).
 ACT_SITE 1003 1003 Proton acceptor (By similarity).
 BINDING 908 908 ATP (By similarity).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 3 3 Phosphotyrosine.
 MOD_RES 228 228 Phosphoserine.
 MOD_RES 1034 1034 Phosphotyrosine; by autocatalysis (By  
Keyword
 3D-structure; Acetylation; ATP-binding; Complete proteome; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH2 domain; Transferase; Tyrosine-protein kinase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1154 AA 
Protein Sequence
MQYLNIKEDC NAMAFCAKMR SSKKTEVNLE APEPGVEVIF YLSDREPLRL GSGEYTAEEL 60
CIRAAQACRI SPLCHNLFAL YDENTKLWYA PNRTITVDDK MSLRLHYRMR FYFTNWHGTN 120
DNEQSVWRHS PKKQKNGYEK KKIPDATPLL DASSLEYLFA QGQYDLVKCL APIRDPKTEQ 180
DGHDIENECL GMAVLAISHY AMMKKMQLPE LPKDISYKRY IPETLNKSIR QRNLLTRMRI 240
NNVFKDFLKE FNNKTICDSS VSTHDLKVKY LATLETLTKH YGAEIFETSM LLISSENEMN 300
WFHSNDGGNV LYYEVMVTGN LGIQWRHKPN VVSVEKEKNK LKRKKLENKH KKDEEKNKIR 360
EEWNNFSYFP EITHIVIKES VVSINKQDNK KMELKLSSHE EALSFVSLVD GYFRLTADAH 420
HYLCTDVAPP LIVHNIQNGC HGPICTEYAI NKLRQEGSEE GMYVLRWSCT DFDNILMTVT 480
CFEKSEQVQG AQKQFKNFQI EVQKGRYSLH GSDRSFPSLG DLMSHLKKQI LRTDNISFML 540
KRCCQPKPRE ISNLLVATKK AQEWQPVYPM SQLSFDRILK KDLVQGEHLG RGTRTHIYSG 600
TLMDYKDDEG TSEEKKIKVI LKVLDPSHRD ISLAFFEAAS MMRQVSHKHI VYLYGVCVRD 660
VENIMVEEFV EGGPLDLFMH RKSDVLTTPW KFKVAKQLAS ALSYLEDKDL VHGNVCTKNL 720
LLAREGIDSE CGPFIKLSDP GIPITVLSRQ ECIERIPWIA PECVEDSKNL SVAADKWSFG 780
TTLWEICYNG EIPLKDKTLI EKERFYESRC RPVTPSCKEL ADLMTRCMNY DPNQRPFFRA 840
IMRDINKLEE QNPDIVSEKK PATEVDPTHF EKRFLKRIRD LGEGHFGKVE LCRYDPEGDN 900
TGEQVAVKSL KPESGGNHIA DLKKEIEILR NLYHENIVKY KGICTEDGGN GIKLIMEFLP 960
SGSLKEYLPK NKNKINLKQQ LKYAVQICKG MDYLGSRQYV HRDLAARNVL VESEHQVKIG 1020
DFGLTKAIET DKEYYTVKDD RDSPVFWYAP ECLMQSKFYI ASDVWSFGVT LHELLTYCDS 1080
DSSPMALFLK MIGPTHGQMT VTRLVNTLKE GKRLPCPPNC PDEVYQLMRK CWEFQPSNRT 1140
SFQNLIEGFE ALLK 1154 
Gene Ontology
 GO:0005856; C:cytoskeleton; IEA:InterPro.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
 GO:0016020; C:membrane; IEA:UniProtKB-KW.
 GO:0005634; C:nucleus; IDA:BHF-UCL.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0005131; F:growth hormone receptor binding; ISS:BHF-UCL.
 GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:EC.
 GO:0004713; F:protein tyrosine kinase activity; EXP:Reactome.
 GO:0007167; P:enzyme linked receptor protein signaling pathway; IEA:Compara.
 GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
 GO:0007243; P:intracellular protein kinase cascade; IEA:Compara.
 GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
 GO:0018108; P:peptidyl-tyrosine phosphorylation; IEA:Compara.
 GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; TAS:Reactome.
 GO:0060338; P:regulation of type I interferon-mediated signaling pathway; TAS:Reactome.
 GO:0046677; P:response to antibiotic; IDA:MGI.
 GO:0060337; P:type I interferon-mediated signaling pathway; TAS:Reactome. 
Interpro
 IPR019749; Band_41_domain.
 IPR019748; FERM_central.
 IPR000299; FERM_domain.
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_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. 
Pfam
 PF07714; Pkinase_Tyr 
SMART
 SM00295; B41
 SM00252; SH2
 SM00219; TyrKc 
PROSITE
 PS00660; FERM_1
 PS00661; FERM_2
 PS50057; FERM_3
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00109; PROTEIN_KINASE_TYR
 PS50001; SH2 
PRINTS
 PR01823; JANUSKINASE.
 PR01824; JANUSKINASE1.
 PR00109; TYRKINASE.