Tag | Content |
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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 |
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82 | LEAQTRVKLNYLDQI | ubiquitination | [1] |
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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. |
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