CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007474
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lysine-specific demethylase 5C 
Protein Synonyms/Alias
 Histone demethylase JARID1C; Jumonji/ARID domain-containing protein 1C; Protein SmcX; Protein Xe169 
Gene Name
 Kdm5c 
Gene Synonyms/Alias
 Jarid1c; Kiaa0234; Smcx; Xe169 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
82LEAQTRVKLNYLDQIubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 Histone demethylase that specifically demethylates 'Lys- 4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Participates in transcriptional repression of neuronal genes by recruiting histone deacetylases and REST at neuron-restrictive silencer elements (By similarity). 
Sequence Annotation
 DOMAIN 14 55 JmjN.
 DOMAIN 79 169 ARID.
 DOMAIN 468 634 JmjC.
 ZN_FING 326 372 PHD-type 1.
 ZN_FING 1187 1248 PHD-type 2.
 METAL 514 514 Iron; catalytic (By similarity).
 METAL 517 517 Iron; catalytic (By similarity).
 METAL 602 602 Iron; catalytic (By similarity).
 MOD_RES 317 317 Phosphoserine (By similarity).
 MOD_RES 1353 1353 Phosphoserine (By similarity).  
Keyword
 Alternative splicing; Chromatin regulator; Complete proteome; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1554 AA 
Protein Sequence
MELGSDDFLP PPECPVFEPS WAEFRDPLGY IAKIRPIAEK SGICKIRPPA DWQPPFAVEV 60
DNFRFTPRIQ RLNELEAQTR VKLNYLDQIA KFWEIQGSSL KIPNVERRIL DLYSLSKIVV 120
EEGGYETICK DRRWARVAQR LNYPPGKNIG SLLRSHYERI VYPYEMYQSG ANLVQCNTRP 180
FDNEEKDKEY KPHSIPLRQS VQPSKFNSYG RRAKRLQPDP EPTEEDIEKN PELKKLQIYG 240
AGPKMMGLGL MAKDKTLRKK DKEGPECPPT VVVKEELGGD VKMESTSPKT FLEGKEELSH 300
SPEPCTKMTM RLRRNHSNAQ FIESYVCRMC SRGDEDDKLL LCDGCDDNYH IFCLLPPLPE 360
IPKGVWRCPK CVMAECKRPP EAFGFEQATR EYTLQSFGEM ADSFKADYFN MPVHMVPTEL 420
VEKEFWRLVN SIEEDVTVEY GADIHSKEFG SGFPVSDSKR HLTPEEEEYA TSGWNLNVMP 480
VLEQSVLCHI NADISGMKVP WLYVGMVFSA FCWHIEDHWS YSINYLHWGE PKTWYGVPSL 540
AAEHLEEVMK KLTPELFDSQ PDLLHQLVTL MNPNTLMSHG VPVVRTNQCA GEFVITFPRA 600
YHSGFNQGYN FAEAVNFCTA DWLPAGRQCI EHYRRLRRYC VFSHEELICK MAACPEKLDL 660
NLAAAVHKEM FIMVQEERRL RKALLEKGIT EAEREAFELL PDDERQCIKC KTTCFLSALA 720
CYDCPDGLVC LSHINDLCKC SSSRQYLRYR YTLDELPAML HKLKVRAESF DTWANKVRVA 780
LEVEDGRKRS LEELRALESE ARERRFPNSE LLQRLKNCLS EAEACVSRAL GLVSGQEAGP 840
DRVAGLQMTL AELRDFLGQM NNLPCAMHQI GDVKGILEQV EAYQTEAREA LVSQPSSPGL 900
LQSLLERGQQ LGVEVPEAQQ LQRQVEQARW LDEVKRTLAP SARRGTLAIM RGLLVAGASV 960
APSPAVDKAQ AELQELLTIA ERWEEKAHLC LEARQKHPPA TLEAIIHEAE NIPVHLPNIQ 1020
SLKEALAKAR AWIADVDEIQ NGDHYPCLDD LEGLVAVGRD LPVGLEELRQ LELQVLTAHS 1080
WREKASKTFL KKNSCYTLLE VLCPCADAGS DSTKRSRWME KELGLYKSDT ELLGLSAQDL 1140
RDPGSVIVAF KEGEQKEKEG ILQLRRTNSA KPSPLALLTT ASSTASICVC GQVPAGVGAL 1200
QCDLCQDWFH GRCVTVPRLL SSQRSSLPSS PLLAWWEWDT KFLCPLCMRS RRPRLETILA 1260
LLVALQRLPV RLPEGEALQC LTERAISWQG RARQVLASEE VTALLGRLAE LRQRLQAESK 1320
PEESLAYPSD GGEGTGNMPK VQGLLENGDS VTSPEKVATE EGSGKRDLEL LSSILPQLSG 1380
PVLELPEATR APLEELMMEG DLLEVTLDEN HSIWQLLQAG QPPDLKRVQT LLELEKAERH 1440
GSRTRGRALE RRRRRKVDRG GEPDDPAREE LEPKRVRSSG PEAEEVQEEE ELEEETGGEV 1500
PPVPFPNSGS PSIQEDQDGL EPVLEAGSDT SAPFSTLTSR LLMSCPQQPS LQQL 1554 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IEA:InterPro.
 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:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 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