CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-029674
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lysine-specific demethylase 5C 
Protein Synonyms/Alias
 Smcy homolog, X-linked (Mouse), isoform CRA_a 
Gene Name
 KDM5C 
Gene Synonyms/Alias
 SMCX; hCG_19161 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
40KIRPIAEKSGICKIRubiquitination[1]
45AEKSGICKIRPPADWubiquitination[1]
82LEAQTRVKLNYLDQIubiquitination[1]
91NYLDQIAKFWEIQGSubiquitination[1]
101EIQGSSLKIPNVERRubiquitination[1, 2, 3]
204RQSVQPSKFNSYGRRubiquitination[1]
234EKNPELKKLQIYGAGubiquitination[1]
306HSPEPCTKMTMRLRRubiquitination[1]
369KGVWRCPKCVMAECKubiquitination[1]
376KCVMAECKRPPEAFGubiquitination[1]
458GFPVSDSKRHLTPEEubiquitination[1, 4]
656KMAACPEKLDLNLAAubiquitination[1]
681QEERRLRKALLEKGIubiquitination[1, 3]
686LRKALLEKGITEAERubiquitination[3]
775SFDTWANKVRVALEVubiquitination[1]
934ARWLDEVKRTLAPSAubiquitination[1]
995LCLEARQKHPPATLEubiquitination[1]
1022LPNIQALKEALAKARubiquitination[1]
1091ASKTFLKKNSCYTLLubiquitination[1]
1113DAGSDSTKRSRWMEKubiquitination[1]
1120KRSRWMEKELGLYKSubiquitination[1, 2]
1441RTLLELEKAERHGSRubiquitination[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] 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]
 [3] 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]
 [4] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1559 AA 
Protein Sequence
MEPGSDDFLP PPECPVFEPS WAEFRDPLGY IAKIRPIAEK SGICKIRPPA DWQPPFAVEV 60
DNFRFTPRIQ RLNELEAQTR VKLNYLDQIA KFWEIQGSSL KIPNVERRIL DLYSLSKIVV 120
EEGGYEAICK DRRWARVAQR LNYPPGKNIG SLLRSHYERI VYPYEMYQSG ANLVCNTRPF 180
DNEEKDKEYK PHSIPLRQSV QPSKFNSYGR RAKRLQPDPE PTEEDIEKNP ELKKLQIYGA 240
GPKMMGLGLM AKDKTLRKKD KEGPECPPTV VVKEELGGDV KVESTSPKTF LESKEELSHS 300
PEPCTKMTMR LRRNHSNAQF IESYVCRMCS RGDEDDKLLL CDGCDDNYHI FCLLPPLPEI 360
PKGVWRCPKC VMAECKRPPE AFGFEQATRE YTLQSFGEMA DSFKADYFNM PVHMVPTELV 420
EKEFWRLVNS IEEDVTVEYG ADIHSKEFGS GFPVSDSKRH LTPEEEEYAT SGWNLNVMPV 480
LEQSVLCHIN ADISGMKVPW LYVGMVFSAF CWHIEDHWSY SINYLHWGEP KTWYGVPSLA 540
AEHLEEVMKK LTPELFDSQP DLLHQLVTLM NPNTLMSHGV PVVRTNQCAG EFVITFPRAY 600
HSGFNQGYNF AEAVNFCTAD WLPAGRQCIE HYRRLRRYCV FSHEELICKM AACPEKLDLN 660
LAAAVHKEMF IMVQEERRLR KALLEKGITE AEREAFELLP DDERQCIKCK TTCFLSALAC 720
YDCPDGLVCL SHINDLCKCS SSRQYLRYRY TLDELPAMLH KLKVRAESFD TWANKVRVAL 780
EVEDGRKRSL EELRALESEA RERRFPNSEL LQQLKNCLSE AEACVSRALG LVSGQEAGPH 840
RVAGLQMTLT ELRAFLDQMN NLPCAMHQIG DVKGVLEQVE AYQAEAREAL ASLPSSPGLL 900
QSLLERGRQL GVEVPEAQQL QRQVEQARWL DEVKRTLAPS ARRGTLAVMR GLLVAGASVA 960
PSPAVDKAQA ELQELLTIAE RWEEKAHLCL EARQKHPPAT LEAIIREAEN IPVHLPNIQA 1020
LKEALAKARA WIADVDEIQN GDHYPCLDDL EGLVAVGRDL PVGLEELRQL ELQVLTAHSW 1080
REKASKTFLK KNSCYTLLEV LCPCADAGSD STKRSRWMEK ELGLYKSDTE LLGLSAQDLR 1140
DPGSVIVAFK EGEQKEKEGI LQLRRTNSAK PSPLASSSTA SSTTSICVCG QVLAGAGALQ 1200
CDLCQDWFHG RCVSVPRLLS SPRPNPTSSP LLAWWEWDTK FLCPLCMRSR RPRLETILAL 1260
LVALQRLPVR LPEGEALQCL TERAISWQGR ARQALASEDV TALLGRLAEL RQRLQAEPRP 1320
EEPPNYPAAP ASDPLREGSG KDMPKVQGLL ENGDSVTSPE KVAPEEGSGK RDLELLSSLL 1380
PQLTGPVLEL PEATRAPLEE LMMEGDLLEV TLDENHSIWQ LLQAGQPPDL ERIRTLLELE 1440
KAERHGSRAR GRALERRRRR KVDRGGEGDD PAREELEPKR VRSSGPEAEE VQEEEELEEE 1500
TGGEGPPAPI PTTGSPSTQE NQNGLEPAEG TTSGPSAPFS TLTPRLHLPC PQQPPQQQL 1559 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:InterPro.
 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. 
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