CPLM-021345

CPLM 1.0 - Compendium of Protein Lysine Modification

Tag

Content

CPLM ID

CPLM-021345

UniProt Accession

KDM4C_HUMAN; Q9H3R0; B4E1Y4; B7ZL46; F5H347; F5H7P0; O94877; Q2M3M0; Q5JUC9; Q5VYJ2; Q5VYJ3

Genbank Protein ID

AB037901; AB018323; AK304032; AK310439; AL354707; AL137020; AL161443; AL445592; AL513412; AL354707; AL137020; AL161443; AL513412; AL445592; AL445592; AL161443; AL513412; AL354707; AL137020; AL445592; AL137020; AL354707; AL513412; AL161443; AL161443; AL137020; AL354707; AL513412; AL445592; AL161443; AL513412; AL445592; AL354707; AL137020; AL161443; AL137020; AL513412; BC104859; BC104861; BC143571

Genbank Nucleotide ID

BAB16102.1; BAA34500.1; BAG64946.1; CAH73283.1; CAH73283.1; CAH73283.1; CAH73283.1; CAH73283.1; CAH73284.1; CAH73284.1; CAH73284.1; CAH73284.1; CAH73284.1; CAI16322.1; CAI16322.1; CAI16322.1; CAI16322.1; CAI16322.1; CAI16323.1; CAI16323.1; CAI16323.1; CAI16323.1; CAI16323.1; CAI39606.1; CAI39606.1; CAI39606.1; CAI39606.1; CAI39606.1; CAI39607.1; CAI39607.1; CAI39607.1; CAI39607.1; CAI39607.1; CAI39608.1; CAI39608.1; CAI39608.1; AAI04860.1; AAI04862.1; AAI43572.1

Protein Name

Lysine-specific demethylase 4C

Protein Synonyms/Alias

Gene amplified in squamous cell carcinoma 1 protein; GASC-1 protein; JmjC domain-containing histone demethylation protein 3C; Jumonji domain-containing protein 2C

Gene Name

KDM4C

Gene Synonyms/Alias

GASC1; JHDM3C; JMJD2C; KIAA0780

Created Date

July 27, 2013

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Lysine Modification

Position	Peptide	Type	References
31	EEFREFNKYLAYMES	ubiquitination	[1]
97	QKKAMTVKEFRQLAN	ubiquitination	[1]
254	ISPSVLKKYGIPFDK	ubiquitination	[1]
303	VRWIDYGKVAKLCTC	ubiquitination	[1]
338	YQLWKQGKDIYTIDH	ubiquitination	[1]
809	PLQRLKLKCIFCRHR	ubiquitination	[1]
933	IVSRDCLKLGPPAEG	ubiquitination	[1]
951	QVKWPDGKLYGAKYF	ubiquitination	[1]
992	TLDEELPKRVKARFS	ubiquitination	[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]

Functional Description

Histone demethylase that specifically demethylates 'Lys- 9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate.

Sequence Annotation

DOMAIN 16 58 JmjN.
DOMAIN 144 310 JmjC.
DOMAIN 877 934 Tudor 1.
DOMAIN 935 991 Tudor 2.
ZN_FING 689 747 PHD-type 1.
ZN_FING 809 865 PHD-type 2.
METAL 190 190 Iron; catalytic.
METAL 192 192 Iron; catalytic.
METAL 236 236 Zinc.
METAL 242 242 Zinc.
METAL 278 278 Iron; catalytic.
METAL 308 308 Zinc.
METAL 310 310 Zinc.
BINDING 134 134 Alpha-ketoglutarate (By similarity).
BINDING 200 200 Alpha-ketoglutarate (By similarity).
BINDING 208 208 Alpha-ketoglutarate (By similarity).

Keyword

3D-structure; Alternative splicing; Chromatin regulator; Complete proteome; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.

Sequence Source

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

Protein Length

1056 AA

Protein Sequence

MEVAEVESPL NPSCKIMTFR PSMEEFREFN KYLAYMESKG AHRAGLAKVI PPKEWKPRQC 60
YDDIDNLLIP APIQQMVTGQ SGLFTQYNIQ KKAMTVKEFR QLANSGKYCT PRYLDYEDLE 120
RKYWKNLTFV APIYGADING SIYDEGVDEW NIARLNTVLD VVEEECGISI EGVNTPYLYF 180
GMWKTTFAWH TEDMDLYSIN YLHFGEPKSW YAIPPEHGKR LERLAQGFFP SSSQGCDAFL 240
RHKMTLISPS VLKKYGIPFD KITQEAGEFM ITFPYGYHAG FNHGFNCAES TNFATVRWID 300
YGKVAKLCTC RKDMVKISMD IFVRKFQPDR YQLWKQGKDI YTIDHTKPTP ASTPEVKAWL 360
QRRRKVRKAS RSFQCARSTS KRPKADEEEE VSDEVDGAEV PNPDSVTDDL KVSEKSEAAV 420
KLRNTEASSE EESSASRMQV EQNLSDHIKL SGNSCLSTSV TEDIKTEDDK AYAYRSVPSI 480
SSEADDSIPL SSGYEKPEKS DPSELSWPKS PESCSSVAES NGVLTEGEES DVESHGNGLE 540
PGEIPAVPSG ERNSFKVPSI AEGENKTSKS WRHPLSRPPA RSPMTLVKQQ APSDEELPEV 600
LSIEEEVEET ESWAKPLIHL WQTKSPNFAA EQEYNATVAR MKPHCAICTL LMPYHKPDSS 660
NEENDARWET KLDEVVTSEG KTKPLIPEMC FIYSEENIEY SPPNAFLEED GTSLLISCAK 720
CCVRVHASCY GIPSHEICDG WLCARCKRNA WTAECCLCNL RGGALKQTKN NKWAHVMCAV 780
AVPEVRFTNV PERTQIDVGR IPLQRLKLKC IFCRHRVKRV SGACIQCSYG RCPASFHVTC 840
AHAAGVLMEP DDWPYVVNIT CFRHKVNPNV KSKACEKVIS VGQTVITKHR NTRYYSCRVM 900
AVTSQTFYEV MFDDGSFSRD TFPEDIVSRD CLKLGPPAEG EVVQVKWPDG KLYGAKYFGS 960
NIAHMYQVEF EDGSQIAMKR EDIYTLDEEL PKRVKARFST ASDMRFEDTF YGADIIQGER 1020
KRQRVLSSRF KNEYVADPVY RTFLKSSFQK KCQKRQ 1056

Gene Ontology

GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO:0032454; F:histone demethylase activity (H3-K9 specific); IDA:UniProtKB.
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:0008284; P:positive regulation of cell proliferation; IMP:BHF-UCL.
GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.

Interpro

IPR003347; JmjC_dom.
IPR003349; TF_JmjN.
IPR002999; Tudor.
IPR001965; Znf_PHD.

Pfam

PF02373; JmjC
PF02375; JmjN

SMART

SM00558; JmjC
SM00545; JmjN
SM00249; PHD
SM00333; TUDOR

PROSITE

PS51184; JMJC
PS51183; JMJN
PS50304; TUDOR
PS01359; ZF_PHD_1
PS50016; ZF_PHD_2

PRINTS