| Tag | Content |
|---|
| CPLM ID | CPLM-001504 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Lysine-specific demethylase 4B |
Protein Synonyms/Alias | JmjC domain-containing histone demethylation protein 3B; Jumonji domain-containing protein 2B |
Gene Name | KDM4B |
Gene Synonyms/Alias | JHDM3B; JMJD2B; KIAA0876 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 602 | QAPSTFSKLKMEIKK | acetylation | [1] | | 1056 | AFSGEEAKAAKRPRV | ubiquitination | [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] Systematic and quantitative assessment of the ubiquitin-modified proteome. Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP. Mol Cell. 2011 Oct 21;44(2):325-40. [ PMID: 21906983] |
Functional Description | Histone demethylase that specifically demethylates 'Lys- 9' of histone H3, thereby playing a role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Only able to demethylate trimethylated H3 'Lys-9', with a weaker activity than KDM4A, KDM4C and KDM4D. Demethylation of Lys residue generates formaldehyde and succinate. |
Sequence Annotation | DOMAIN 15 57 JmjN.
DOMAIN 146 309 JmjC.
DOMAIN 917 974 Tudor 1.
DOMAIN 975 1031 Tudor 2.
ZN_FING 731 789 PHD-type 1.
ZN_FING 851 907 PHD-type 2.
METAL 189 189 Iron; catalytic (By similarity).
METAL 191 191 Iron; catalytic (By similarity).
METAL 235 235 Zinc (By similarity).
METAL 241 241 Zinc (By similarity).
METAL 277 277 Iron; catalytic (By similarity).
METAL 307 307 Zinc (By similarity).
METAL 309 309 Zinc (By similarity).
BINDING 133 133 Alpha-ketoglutarate (By similarity).
BINDING 199 199 Alpha-ketoglutarate (By similarity).
BINDING 207 207 Alpha-ketoglutarate (By similarity).
MOD_RES 305 305 Phosphothreonine (By similarity).
MOD_RES 566 566 Phosphoserine.
MOD_RES 602 602 N6-acetyllysine.
MOD_RES 1065 1065 Phosphothreonine. |
Keyword | Acetylation; Alternative splicing; Chromatin regulator; Complete proteome; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1096 AA |
Protein Sequence | MGSEDHGAQN PSCKIMTFRP TMEEFKDFNK YVAYIESQGA HRAGLAKIIP PKEWKPRQTY 60
DDIDDVVIPA PIQQVVTGQS GLFTQYNIQK KAMTVGEYRR LANSEKYCTP RHQDFDDLER 120
KYWKNLTFVS PIYGADISGS LYDDDVAQWN IGSLRTILDM VERECGTIIE GVNTPYLYFG 180
MWKTTFAWHT EDMDLYSINY LHFGEPKSWY AIPPEHGKRL ERLAIGFFPG SSQGCDAFLR 240
HKMTLISPII LKKYGIPFSR ITQEAGEFMI TFPYGYHAGF NHGFNCAEST NFATLRWIDY 300
GKVATQCTCR KDMVKISMDV FVRILQPERY ELWKQGKDLT VLDHTRPTAL TSPELSSWSA 360
SRASLKAKLL RRSHRKRSQP KKPKPEDPKF PGEGTAGAAL LEEAGGSVKE EAGPEVDPEE 420
EEEEPQPLPH GREAEGAEED GRGKLRPTKA KSERKKKSFG LLPPQLPPPP AHFPSEEALW 480
LPSPLEPPVL GPGPAAMEES PLPAPLNVVP PEVPSEELEA KPRPIIPMLY VVPRPGKAAF 540
NQEHVSCQQA FEHFAQKGPT WKEPVSPMEL TGPEDGAASS GAGRMETKAR AGEGQAPSTF 600
SKLKMEIKKS RRHPLGRPPT RSPLSVVKQE ASSDEEASPF SGEEDVSDPD ALRPLLSLQW 660
KNRAASFQAE RKFNAAAART EPYCAICTLF YPYCQALQTE KEAPIASLGK GCPATLPSKS 720
RQKTRPLIPE MCFTSGGENT EPLPANSYIG DDGTSPLIAC GKCCLQVHAS CYGIRPELVN 780
EGWTCSRCAA HAWTAECCLC NLRGGALQMT TDRRWIHVIC AIAVPEARFL NVIERHPVDI 840
SAIPEQRWKL KCVYCRKRMK KVSGACIQCS YEHCSTSFHV TCAHAAGVLM EPDDWPYVVS 900
ITCLKHKSGG HAVQLLRAVS LGQVVITKNR NGLYYRCRVI GAASQTCYEV NFDDGSYSDN 960
LYPESITSRD CVQLGPPSEG ELVELRWTDG NLYKAKFISS VTSHIYQVEF EDGSQLTVKR 1020
GDIFTLEEEL PKRVRSRLSL STGAPQEPAF SGEEAKAAKR PRVGTPLATE DSGRSQDYVA 1080
FVESLLQVQG RPGAPF 1096 |
Gene Ontology | GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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: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 | |