| Tag | Content |
|---|
| CPLM ID | CPLM-014878 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Lysine-specific demethylase 4D |
Protein Synonyms/Alias | JmjC domain-containing histone demethylation protein 3D; Jumonji domain-containing protein 2D |
Gene Name | KDM4D |
Gene Synonyms/Alias | JHDM3D; JMJD2D |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 362 | SQELSTQKEVQLPRR | 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' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Demethylates both di- and trimethylated H3 'Lys- 9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. |
Sequence Annotation | DOMAIN 18 60 JmjN.
DOMAIN 146 312 JmjC.
METAL 192 192 Iron; catalytic (By similarity).
METAL 194 194 Iron; catalytic (By similarity).
METAL 238 238 Zinc (By similarity).
METAL 244 244 Zinc (By similarity).
METAL 280 280 Iron; catalytic (By similarity).
METAL 310 310 Zinc (By similarity).
METAL 312 312 Zinc (By similarity).
BINDING 136 136 Alpha-ketoglutarate (By similarity).
BINDING 202 202 Alpha-ketoglutarate (By similarity).
BINDING 210 210 Alpha-ketoglutarate (By similarity).
MOD_RES 26 26 PolyADP-ribosyl glutamic acid.
MOD_RES 27 27 PolyADP-ribosyl glutamic acid. |
Keyword | 3D-structure; ADP-ribosylation; Chromatin regulator; Complete proteome; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; Polymorphism; Reference proteome; Transcription; Transcription regulation; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 523 AA |
Protein Sequence | METMKSKANC AQNPNCNIMI FHPTKEEFND FDKYIAYMES QGAHRAGLAK IIPPKEWKAR 60
ETYDNISEIL IATPLQQVAS GRAGVFTQYH KKKKAMTVGE YRHLANSKKY QTPPHQNFED 120
LERKYWKNRI YNSPIYGADI SGSLFDENTK QWNLGHLGTI QDLLEKECGV VIEGVNTPYL 180
YFGMWKTTFA WHTEDMDLYS INYLHLGEPK TWYVVPPEHG QRLERLAREL FPGSSRGCGA 240
FLRHKVALIS PTVLKENGIP FNRITQEAGE FMVTFPYGYH AGFNHGFNCA EAINFATPRW 300
IDYGKMASQC SCGEARVTFS MDAFVRILQP ERYDLWKRGQ DRAVVDHMEP RVPASQELST 360
QKEVQLPRRA ALGLRQLPSH WARHSPWPMA ARSGTRCHTL VCSSLPRRSA VSGTATQPRA 420
AAVHSSKKPS STPSSTPGPS AQIIHPSNGR RGRGRPPQKL RAQELTLQTP AKRPLLAGTT 480
CTASGPEPEP LPEDGALMDK PVPLSPGLQH PVKASGCSWA PVP 523 |
Gene Ontology | GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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:0016568; P:chromatin modification; IEA:UniProtKB-KW. GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |