CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022906
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]
109NFLDQIAKYWELQGSubiquitination[2]
119ELQGSTLKIPHVERKubiquitination[1]
126KIPHVERKILDLFQLubiquitination[1]
148GGFAVVCKDRKWTKIubiquitination[1]
158KWTKIATKMGFAPGKubiquitination[1, 3]
1136ERALTESKETASAMAubiquitination[4]
1276LLSSGNLKFVQDRVGubiquitination[5]
1450PKDMNNFKLERERSYubiquitination[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] 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]
 [3] 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]
 [4] 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]
 [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] 
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 AKRMRAEAMN 240
IKIEPEETTE ARTHNLRRRM GCPTPKCENE KEMKSSIKQE PIERKDYIVE NEKEKPKSRS 300
KKATNAVDLY VCLLCGSGND EDRLLLCDGC DDSYHTFCLI PPLHDVPKGD WRCPKCLAQE 360
CSKPQEAFGF EQAARDYTLR TFGEMADAFK SDYFNMPVHM VPTELVEKEF WRLVSTIEED 420
VTVEYGADIA SKEFGSGFPV RDGKIKLSPE EEEYLDSGWN LNNMPVMEQS VLAHITADIC 480
GMKLPWLYVG MCFSSFCWHI EDHWSYSINY LHWGEPKTWY GVPGYAAEQL ENVMKKLAPE 540
LFVSQPDLLH QLVTIMNPNT LMTHEVPVYR TNQCAGEFVI TFPRAYHSGF NQGFNFAEAV 600
NFCTVDWLPL GRQCVEHYRL LHRYCVFSHD EMICKMASKA DVLDVVVAST VQKDMAIMIE 660
DEKALRETVR KLGVIDSERM DFELLPDDER QCVKCKTTCF MSAISCSCKP GLLVCLHHVK 720
ELCSCPPYKY KLRYRYTLDD LYPMMNALKL RAESYNEWAL NVNEALEAKI NKKKSLVSFK 780
ALIEESEMKK FPDNDLLRHL RLVTQDAEKC ASVAQQLLNG KRQTRYRSGG GKSQNQLTVN 840
ELRQFVTQLY ALPCVLSQTP LLKDLLNRVE DFQQHSQKLL SEETPSAAEL QDLLDVSFEF 900
DVELPQLAEM RIRLEQARWL EEVQQACLDP SSLTLDDMRR LIDLGVGLAP YSAVEKAMAR 960
LQELLTVSEH WDDKAKSLLK ARPRHSLNSL ATAVKEIEEI PAYLPNGAAL KDSVQRARDW 1020
LQDVEGLQAG GRVPVLDTLI ELVTRGRSIP VHLNSLPRLE TLVAEVQAWK ECAVNTFLTE 1080
NSPYSLLEVL CPRCDIGLLG LKRKQRKLKE PLPNGKKKST KLESLSDLER ALTESKETAS 1140
AMATLGEARL REMEALQSLR LANEGKLLSP LQDVDIKICL CQKAPAAPMI QCELCRDAFH 1200
TSCVAVPSIS QGLRIWLCPH CRRSEKPPLE KILPLLASLQ RIRVRLPEGD ALRYMIERTV 1260
NWQHRAQQLL SSGNLKFVQD RVGSGLLYSR WQASAGQVSD TNKVSQPPGT TSFSLPDDWD 1320
NRTSYLHSPF STGRSCIPLH GVSPEVNELL MEAQLLQVSL PEIQELYQTL LAKPSPAQQT 1380
DRSSPVRPSS EKNDCCRGKR DGINSLERKL KRRLEREGLS SERWERVKKM RTPKKKKIKL 1440
SHPKDMNNFK LERERSYELV RSAETHSLPS DTSYSEQEDS EDEDAICPAV SCLQPEGDEV 1500
DWVQCDGSCN QWFHQVCVGV SPEMAEKEDY ICVRCTVKDA PSRK 1544 
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