CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022907
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lysine-specific demethylase 5B 
Protein Synonyms/Alias
 Cancer/testis antigen 31; CT31; Histone demethylase JARID1B; Jumonji/ARID domain-containing protein 1B; PLU-1; Retinoblastoma-binding protein 2 homolog 1; RBP2-H1 
Gene Name
 KDM5B 
Gene Synonyms/Alias
 JARID1B; PLU1; RBBP2H1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
80PFACDVDKLHFTPRIubiquitination[1]
100LEAQTRVKLNFLDQIubiquitination[1]
119ELQGSTLKIPHVERKubiquitination[1]
126KIPHVERKILDLFQLubiquitination[1]
148GGFAVVCKDRKWTKIubiquitination[1]
158KWTKIATKMGFAPGKubiquitination[1, 2]
165KMGFAPGKAVGSHIRubiquitination[1]
196DSLRCLQKPNLTTDTubiquitination[1]
206LTTDTKDKEYKPHDIubiquitination[1]
314KEMKSSIKQEPIERKubiquitination[1]
329DYIVENEKEKPKSRSubiquitination[1]
331IVENEKEKPKSRSKKubiquitination[1]
391KGDWRCPKCLAQECSubiquitination[1]
399CLAQECSKPQEAFGFubiquitination[1]
426GEMADAFKSDYFNMPubiquitination[1]
444VPTELVEKEFWRLVSubiquitination[1]
572QLENVMKKLAPELFVubiquitination[1]
671SHDEMICKMASKADVubiquitination[1]
675MICKMASKADVLDVVubiquitination[1]
699AIMIEDEKALRETVRubiquitination[1]
707ALRETVRKLGVIDSEubiquitination[1, 2]
730DDERQCVKCKTTCFMubiquitination[1]
765LCSCPPYKYKLRYRYubiquitination[1]
785YPMMNALKLRAESYNubiquitination[1, 2]
810EAKINKKKSLVSFKAubiquitination[1]
816KKSLVSFKALIEESEubiquitination[1]
825LIEESEMKKFPDNDLubiquitination[1]
826IEESEMKKFPDNDLLubiquitination[1]
845LVTQDAEKCASVAQQubiquitination[1]
857AQQLLNGKRQTRYRSubiquitination[1, 2]
868RYRSGGGKSQNQLTVubiquitination[1]
992APYSAVEKAMARLQEubiquitination[1]
1010VSEHWDDKAKSLLKAubiquitination[1]
1012EHWDDKAKSLLKARPubiquitination[1]
1016DKAKSLLKARPRHSLubiquitination[1]
1031NSLATAVKEIEEIPAubiquitination[1]
1047LPNGAALKDSVQRARubiquitination[1]
1138DIGLLGLKRKQRKLKubiquitination[1]
1154PLPNGKKKSTKLESLubiquitination[1]
1157NGKKKSTKLESLSDLubiquitination[1]
1172ERALTESKETASAMAubiquitination[1]
1202LRLANEGKLLSPLQDubiquitination[1, 2]
1219IKICLCQKAPAAPMIubiquitination[1]
1262PHCRRSEKPPLEKILubiquitination[1]
1312LLSSGNLKFVQDRVGubiquitination[1]
1428PVRPSSEKNDCCRGKubiquitination[1]
1486PKDMNNFKLERERSYubiquitination[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] 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] 
Functional Description
 Histone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9' or H3 'Lys-27'. Demethylates trimethylated, dimethylated and monomethylated H3 'Lys-4'. Acts as a transcriptional corepressor for FOXG1B and PAX9. Favors the proliferation of breast cancer cells by repressing tumor suppressor genes such as BRCA1 and HOXA5. In contrast, may act as a tumor suppressor for melanoma. 
Sequence Annotation
 DOMAIN 32 73 JmjN.
 DOMAIN 97 187 ARID.
 DOMAIN 453 619 JmjC.
 ZN_FING 309 359 PHD-type 1.
 ZN_FING 1176 1224 PHD-type 2.
 ZN_FING 1484 1538 PHD-type 3.
 METAL 499 499 Iron; catalytic (By similarity).
 METAL 502 502 Iron; catalytic (By similarity).
 METAL 587 587 Iron; catalytic (By similarity).  
Keyword
 Alternative splicing; Chromatin regulator; Complete proteome; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1544 AA 
Protein Sequence
MEAATTLHPG PRPALPLGGP GPLGEFLPPP ECPVFEPSWE EFADPFAFIH KIRPIAEQTG 60
ICKVRPPPDW QPPFACDVDK LHFTPRIQRL NELEAQTRVK LNFLDQIAKY WELQGSTLKI 120
PHVERKILDL FQLNKLVAEE GGFAVVCKDR KWTKIATKMG FAPGKAVGSH IRGHYERILN 180
PYNLFLSGDS LRCLQKPNLT TDTKDKEYKP HDIPQRQSVQ PSETCPPARR AKRMRAERQS 240
LAVLPRLECS GAILAHCNLR LLDSSNSSAS ASQAMNIKIE PEETTEARTH NLRRRMGCPT 300
PKCENEKEMK SSIKQEPIER KDYIVENEKE KPKSRSKKAT NAVDLYVCLL CGSGNDEDRL 360
LLCDGCDDSY HTFCLIPPLH DVPKGDWRCP KCLAQECSKP QEAFGFEQAA RDYTLRTFGE 420
MADAFKSDYF NMPVHMVPTE LVEKEFWRLV STIEEDVTVE YGADIASKEF GSGFPVRDGK 480
IKLSPEEEEY LDSGWNLNNM PVMEQSVLAH ITADICGMKL PWLYVGMCFS SFCWHIEDHW 540
SYSINYLHWG EPKTWYGVPG YAAEQLENVM KKLAPELFVS QPDLLHQLVT IMNPNTLMTH 600
EVPVYRTNQC AGEFVITFPR AYHSGFNQGF NFAEAVNFCT VDWLPLGRQC VEHYRLLHRY 660
CVFSHDEMIC KMASKADVLD VVVASTVQKD MAIMIEDEKA LRETVRKLGV IDSERMDFEL 720
LPDDERQCVK CKTTCFMSAI SCSCKPGLLV CLHHVKELCS CPPYKYKLRY RYTLDDLYPM 780
MNALKLRAES YNEWALNVNE ALEAKINKKK SLVSFKALIE ESEMKKFPDN DLLRHLRLVT 840
QDAEKCASVA QQLLNGKRQT RYRSGGGKSQ NQLTVNELRQ FVTQLYALPC VLSQTPLLKD 900
LLNRVEDFQQ HSQKLLSEET PSAAELQDLL DVSFEFDVEL PQLAEMRIRL EQARWLEEVQ 960
QACLDPSSLT LDDMRRLIDL GVGLAPYSAV EKAMARLQEL LTVSEHWDDK AKSLLKARPR 1020
HSLNSLATAV KEIEEIPAYL PNGAALKDSV QRARDWLQDV EGLQAGGRVP VLDTLIELVT 1080
RGRSIPVHLN SLPRLETLVA EVQAWKECAV NTFLTENSPY SLLEVLCPRC DIGLLGLKRK 1140
QRKLKEPLPN GKKKSTKLES LSDLERALTE SKETASAMAT LGEARLREME ALQSLRLANE 1200
GKLLSPLQDV DIKICLCQKA PAAPMIQCEL CRDAFHTSCV AVPSISQGLR IWLCPHCRRS 1260
EKPPLEKILP LLASLQRIRV RLPEGDALRY MIERTVNWQH RAQQLLSSGN LKFVQDRVGS 1320
GLLYSRWQAS AGQVSDTNKV SQPPGTTSFS LPDDWDNRTS YLHSPFSTGR SCIPLHGVSP 1380
EVNELLMEAQ LLQVSLPEIQ ELYQTLLAKP SPAQQTDRSS PVRPSSEKND CCRGKRDGIN 1440
SLERKLKRRL EREGLSSERW ERVKKMRTPK KKKIKLSHPK DMNNFKLERE RSYELVRSAE 1500
THSLPSDTSY SEQEDSEDED AICPAVSCLQ PEGDEVDWVQ CDGSCNQWFH QVCVGVSPEM 1560
AEKEDYICVR CTVKDAPSRK 1580 
Gene Ontology
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0003677; F:DNA binding; IDA:GDB.
 GO:0034648; F:histone demethylase activity (H3-dimethyl-K4 specific); IDA:UniProtKB.
 GO:0034647; F:histone demethylase activity (H3-trimethyl-K4 specific); IDA:UniProtKB.
 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:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
 GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:GDB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR001606; ARID/BRIGHT_DNA-bd.
 IPR003347; JmjC_dom.
 IPR013637; Lys_sp_deMease_like_dom.
 IPR003349; TF_JmjN.
 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
 PF01388; ARID
 PF02373; JmjC
 PF02375; JmjN
 PF00628; PHD
 PF08429; PLU-1
 PF02928; zf-C5HC2 
SMART
 SM00501; BRIGHT
 SM00558; JmjC
 SM00545; JmjN
 SM00249; PHD 
PROSITE
 PS51011; ARID
 PS51184; JMJC
 PS51183; JMJN
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS