CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-030601
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Jumonji, AT rich interactive domain 1B (RBP2-like), isoform CRA_a 
Protein Synonyms/Alias
 Lysine-specific demethylase 5B; cDNA FLJ16281 fis, clone NT2RI3003104, highly similar to Homo sapiens Jumonji, AT rich interactive domain 1B (RBP2-like) (JARID1B), mRNA 
Gene Name
 JARID1B 
Gene Synonyms/Alias
 KDM5B; hCG_2027322 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
7*MGFAPGKAVGSHIRubiquitination[1]
38DSLRCLQKPNLTTDTubiquitination[1]
48LTTDTKDKEYKPHDIubiquitination[1]
120KEMKSSIKQEPIERKubiquitination[1]
135DYIVENEKEKPKSRSubiquitination[1]
197KGDWRCPKCLAQECSubiquitination[1]
205CLAQECSKPQEAFGFubiquitination[1, 2, 3]
232GEMADAFKSDYFNMPubiquitination[1, 2]
250VPTELVEKEFWRLVSubiquitination[1, 2]
378QLENVMKKLAPELFVubiquitination[1]
477SHDEMICKMASKADVubiquitination[1, 2]
481MICKMASKADVLDVVubiquitination[1]
505AIMIEDEKALRETVRubiquitination[1]
513ALRETVRKLGVIDSEubiquitination[1, 4]
536DDERQCVKCKTTCFMubiquitination[1]
571LCSCPPYKYKLRYRYubiquitination[1]
591YPMMNALKLRAESYNubiquitination[1, 2, 4]
616EAKINKKKSLVSFKAubiquitination[1]
622KKSLVSFKALIEESEubiquitination[1]
631LIEESEMKKFPDNDLubiquitination[1]
632IEESEMKKFPDNDLLubiquitination[1]
651LVTQDAEKCASVAQQubiquitination[1]
663AQQLLNGKRQTRYRSubiquitination[1, 4]
674RYRSGGGKSQNQLTVacetylation[3]
674RYRSGGGKSQNQLTVubiquitination[1, 2, 3, 5]
798APYSAVEKAMARLQEubiquitination[1, 2, 5]
816VSEHWDDKAKSLLKAubiquitination[1]
818EHWDDKAKSLLKARPubiquitination[1]
822DKAKSLLKARPRHSLubiquitination[1]
837NSLATAVKEIEEIPAubiquitination[1]
853LPNGAALKDSVQRARubiquitination[1, 2, 5]
944DIGLLGLKRKQRKLKubiquitination[1, 2]
960PLPNGKKKSTKLESLubiquitination[1]
963NGKKKSTKLESLSDLubiquitination[1, 2]
978ERALTESKETASAMAubiquitination[1, 2, 3, 5]
1008LRLANEGKLLSPLQDubiquitination[1, 4, 5]
1025IKICLCQKAPAAPMIubiquitination[1, 2]
1068PHCRRSEKPPLEKILubiquitination[1]
1118LLSSGNLKFVQDRVGubiquitination[1, 2, 5, 6]
1145GQVSDTNKVSQPPGTubiquitination[2]
1234PVRPSSEKNDCCRGKubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] 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]
 [6] 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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1275 AA 
Protein Sequence
MGFAPGKAVG SHIRGHYERI LNPYNLFLSG DSLRCLQKPN LTTDTKDKEY KPHDIPQRQS 60
VQPSETCPPA RRAKRMRAEA MNIKIEPEET TEARTHNLRR RMGCPTPKCE NEKEMKSSIK 120
QEPIERKDYI VENEKEKPKS RSKKATNAVD LYVCLLCGSG NDEDRLLLCD GCDDSYHTFC 180
LIPPLHDVPK GDWRCPKCLA QECSKPQEAF GFEQAARDYT LRTFGEMADA FKSDYFNMPV 240
HMVPTELVEK EFWRLVSTIE EDVTVEYGAD IASKEFGSGF PVRDGKIKLS PEEEEYLDSG 300
WNLNNMPVME QSVLAHITAD ICGMKLPWLY VGMCFSSFCW HIEDHWSYSI NYLHWGEPKT 360
WYGVPGYAAE QLENVMKKLA PELFVSQPDL LHQLVTIMNP NTLMTHEVPV YRTNQCAGEF 420
VITFPRAYHS GFNQGFNFAE AVNFCTVDWL PLGRQCVEHY RLLHRYCVFS HDEMICKMAS 480
KADVLDVVVA STVQKDMAIM IEDEKALRET VRKLGVIDSE RMDFELLPDD ERQCVKCKTT 540
CFMSAISCSC KPGLLVCLHH VKELCSCPPY KYKLRYRYTL DDLYPMMNAL KLRAESYNEW 600
ALNVNEALEA KINKKKSLVS FKALIEESEM KKFPDNDLLR HLRLVTQDAE KCASVAQQLL 660
NGKRQTRYRS GGGKSQNQLT VNELRQFVTQ LYALPCVLSQ TPLLKDLLNR VEDFQQHSQK 720
LLSEETPSAA ELQDLLDVSF EFDVELPQLA EMRIRLEQAR WLEEVQQACL DPSSLTLDDM 780
RRLIDLGVGL APYSAVEKAM ARLQELLTVS EHWDDKAKSL LKARPRHSLN SLATAVKEIE 840
EIPAYLPNGA ALKDSVQRAR DWLQDVEGLQ AGGRVPVLDT LIELVTRGRS IPVHLNSLPR 900
LETLVAEVQA WKECAVNTFL TENSPYSLLE VLCPRCDIGL LGLKRKQRKL KEPLPNGKKK 960
STKLESLSDL ERALTESKET ASAMATLGEA RLREMEALQS LRLANEGKLL SPLQDVDIKI 1020
CLCQKAPAAP MIQCELCRDA FHTSCVAVPS ISQGLRIWLC PHCRRSEKPP LEKILPLLAS 1080
LQRIRVRLPE GDALRYMIER TVNWQHRAQQ LLSSGNLKFV QDRVGSGLLY SRWQASAGQV 1140
SDTNKVSQPP GTTSFSLPDD WDNRTSYLHS PFSTGRSCIP LHGVSPEVNE LLMEAQLLQV 1200
SLPEIQELYQ TLLAKPSPAQ QTDRSSPVRP SSEKNDCCRG KRDGINSLER KLKRRLEREG 1260
LSSERWERVK KMRTP 1275 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-KW.
 GO:0032453; F:histone demethylase activity (H3-K4 specific); IEA:Compara.
 GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0034720; P:histone H3-K4 demethylation; IEA:GOC. 
Interpro
 IPR003347; JmjC_dom.
 IPR013637; Lys_sp_deMease_like_dom.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR004198; Znf_C5HC2.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF02373; JmjC
 PF00628; PHD
 PF08429; PLU-1
 PF02928; zf-C5HC2 
SMART
 SM00558; JmjC
 SM00249; PHD 
PROSITE
 PS51184; JMJC
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS