CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012608
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable JmjC domain-containing histone demethylation protein 2C 
Protein Synonyms/Alias
 Jumonji domain-containing protein 1C; Thyroid receptor-interacting protein 8; TR-interacting protein 8; TRIP-8 
Gene Name
 JMJD1C 
Gene Synonyms/Alias
 JHDM2C; KIAA1380; TRIP8 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
552KHSIANAKFLETAKKacetylation[1]
659SPDSVKSKATYVNSQubiquitination[2]
2100SMGAPSSKSGRTMPNubiquitination[2, 3]
2183SSNWKLFKECWKQGQubiquitination[2]
2296EYCNPEGKFNLASHLubiquitination[2]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] 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]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
Functional Description
 Probable histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May be involved in hormone-dependent transcriptional activation, by participating in recruitment to androgen-receptor target genes (By similarity). 
Sequence Annotation
 DOMAIN 2274 2498 JmjC.
 ZN_FING 1846 1871 C6-type (Potential).
 MOTIF 2066 2070 LXXLL motif.
 METAL 2336 2336 Iron; catalytic (By similarity).
 METAL 2338 2338 Iron; catalytic (By similarity).
 METAL 2466 2466 Iron; catalytic (By similarity).
 MOD_RES 317 317 Phosphoserine.
 MOD_RES 373 373 Phosphoserine.
 MOD_RES 376 376 Phosphoserine.
 MOD_RES 617 617 Phosphoserine.
 MOD_RES 638 638 Phosphoserine.
 MOD_RES 641 641 Phosphoserine.
 MOD_RES 652 652 Phosphoserine.
 MOD_RES 1989 1989 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Chromatin regulator; Complete proteome; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2540 AA 
Protein Sequence
MAVETRAELV GKRFLCVAVG DEARSERWES GRGWRSWRAG VIRAVSHRDS RNPDLAVYVE 60
FDDLEWDKRE WVKVYEDFST FLVEYHLIWA KRNDPSQTQG SKSKQIQWPA LTFKPLVERN 120
IPSSVTAVEF LVDKQLDFLT EDSAFQPYQD DIDSLNPVLR DNPQLHEEVK VWVKEQKVQE 180
IFMQGPYSLN GYRVRVYRQD SATQWFTGII THHDLFTRTM IVMNDQVLEP QNVDPSMVQM 240
TFLDDVVHSL LKGENIGITS RRRSRANQNV NAVHSHYTRA QANSPRPAMN SQAAVPKQNT 300
HQQQQQRSIR PNKRKGSDSS IPDEEKMKEE KYDYISRGEN PKGKNKHLMN KRRKPEEDEK 360
KLNMKRLRTD NVSDFSESSD SENSNKRIID NSSEQKPENE LKNKNTSKIN GEEGKPHNNE 420
KAGEETLKNS QPPWDQIQED KKHEEAEKRK SVDTQLQEDM IIHSSEQSTV SDHNSNDLLP 480
QECNMDKTHT MELLPKEKFV SRPPTPKCVI DITNDTNLEK VAQENSSTFG LQTLQKMDPN 540
VSDSKHSIAN AKFLETAKKD SDQSWVSDVV KVDLTQSSVT NASSGNDHLN MEKEKYVSYI 600
SPLSAVSVME DKLHKRSPPP ETIKSKLNTS VDTHKIKSSP SPEVVKPKIT HSPDSVKSKA 660
TYVNSQATGE RRLANKIEHE LSRCSFHPIP TRSSTLETTK SPLIIDKNEH FTVYRDPALI 720
GSETGANHIS PFLSQHPFPL HSSSHRTCLN PGTHHPALTP APHLLAGSSS QTPLPTINTH 780
PLTSGPHHAV HHPHLLPTVL PGVPTASLLG GHPRLESAHA SSLSHLALAH QQQQQLLQHQ 840
SPHLLGQAHP SASYNQLGLY PIIWQYPNGT HAYSGLGLPS SKWVHPENAV NAEASLRRNS 900
PSPWLHQPTP VTSADGIGLL SHIPVRPSSA EPHRPLKITA HSSPPLTKTL VDHHKEELER 960
KAFMEPLRSV ASTSAKNDLD LNRSQTGKDC HLHRHFVDPV LNQLQRPPQE TGERLNKYKE 1020
EHRRILQESI DVAPFTTKIK GLEGERENYS RVASSSSSPK SHIIKQDMDV ERSVSDLYKM 1080
KHSVPQSLPQ SNYFTTLSNS VVNEPPRSYP SKEVSNIYGD KQSNALAAAA ANPQTLTSFI 1140
TSLSKPPPLI KHQPESEGLV GKIPEHLPHQ IASHSVTTFR NDCRSPTHLT VSSTNTLRSM 1200
PALHRAPVFH PPIHHSLERK EGSYSSLSPP TLTPVMPVNA GGKVQESQKP PTLIPEPKDS 1260
QANFKSSSEQ SLTEMWRPNN NLSKEKTEWH VEKSSGKLQA AMASVIVRPS SSTKTDSMPA 1320
MQLASKDRVS ERSSAGAHKT DCLKLAEAGE TGRIILPNVN SDSVHTKSEK NFQAVSQGSV 1380
PSSVMSAVNT MCNTKTDVIT SAADTTSVSS WGGSEVISSL SNTILASTSS ECVSSKSVSQ 1440
PVAQKQECKV STTAPVTLAS SKTGSVVQPS SGFSGTTDFI HLKKHKAALA AAQYKSSNAS 1500
ETEPNAIKNQ TLSASLPLDS TVICSTINKA NSVGNGQASQ TSQPNYHTKL KKAWLTRHSE 1560
EDKNTNKMEN SGNSVSEIIK PCSVNLIAST SSDIQNSVDS KIIVDKYVKD DKVNRRKAKR 1620
TYESGSESGD SDESESKSEQ RTKRQPKPTY KKKQNDLQKR KGEIEEDLKP NGVLSRSAKE 1680
RSKLKLQSNS NTGIPRSVLK DWRKVKKLKQ TGESFLQDDS CCEIGPNLQK CRECRLIRSK 1740
KGEEPAHSPV FCRFYYFRRL SFSKNGVVRI DGFSSPDQYD DEAMSLWTHE NFEDDELDIE 1800
TSKYILDIIG DKFCQLVTSE KTALSWVKKD AKIAWKRAVR GVREMCDACE ATLFNIHWVC 1860
QKCGFVVCLD CYKAKERKSS RDKELYAWMK CVKGQPHDHK HLMPTQIIPG SVLTDLLDAM 1920
HTLREKYGIK SHCHCTNKQN LQVGNFPTMN GVSQVLQNVL NHSNKISLCM PESQQQNTPP 1980
KSEKNGGSSP ESDVGTDNKL TPPESQSPLH WLADLAEQKA REEKKENKEL TLENQIKEER 2040
EQDNSESPNG RTSPLVSQNN EQGSTLRDLL TTTAGKLRVG STDAGIAFAP VYSMGAPSSK 2100
SGRTMPNILD DIIASVVENK IPPSKTSKIN VKPELKEEPE ESIISAVDEN NKLYSDIPHS 2160
WICEKHILWL KDYKNSSNWK LFKECWKQGQ PAVVSGVHKK MNISLWKAES ISLDFGDHQA 2220
DLLNCKDSII SNANVKEFWD GFEEVSKRQK NKSGETVVLK LKDWPSGEDF KTMMPARYED 2280
LLKSLPLPEY CNPEGKFNLA SHLPGFFVRP DLGPRLCSAY GVVAAKDHDI GTTNLHIEVS 2340
DVVNILVYVG IAKGNGILSK AGILKKFEEE DLDDILRKRL KDSSEIPGAL WHIYAGKDVD 2400
KIREFLQKIS KEQGLEVLPE HDPIRDQSWY VNKKLRQRLL EEYGVRTCTL IQFLGDAIVL 2460
PAGALHQVQN FHSCIQVTED FVSPEHLVES FHLTQELRLL KEEINYDDKL QVKNILYHAV 2520
KEMVRALKIH EDEVEDMEEN 2540 
Gene Ontology
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW.
 GO:0046966; F:thyroid hormone receptor binding; TAS:UniProtKB.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0006355; P:regulation of transcription, DNA-dependent; TAS:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR003347; JmjC_dom. 
Pfam
 PF02373; JmjC 
SMART
 SM00558; JmjC 
PROSITE
 PS51184; JMJC 
PRINTS