CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023670
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lysine-specific demethylase 2A 
Protein Synonyms/Alias
 CXXC-type zinc finger protein 8; F-box and leucine-rich repeat protein 11; F-box protein FBL7; F-box protein Lilina; F-box/LRR-repeat protein 11; JmjC domain-containing histone demethylation protein 1A; [Histone-H3]-lysine-36 demethylase 1A 
Gene Name
 KDM2A 
Gene Synonyms/Alias
 CXXC8; FBL7; FBXL11; JHDM1A; KIAA1004 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
79LRDPLIFKNSDGLGIubiquitination[1]
409LDYDGLGKTCRSLPSacetylation[2]
518VPIVQWPKRDKLKFPubiquitination[3, 4]
932CDKRLWTKIDLSRCKubiquitination[1]
951QALSGIIKRQPVSLDubiquitination[2]
1015LRWAVGIKDPQIRDLubiquitination[1]
1029LLTPPADKPGQDNRSubiquitination[1, 5]
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]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] 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- 36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys- 36'. May also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Required to maintain the heterochromatic state. Associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. Required to sustain centromeric integrity and genomic stability, particularly during mitosis. 
Sequence Annotation
 DOMAIN 148 316 JmjC.
 DOMAIN 889 936 F-box.
 REPEAT 961 982 LRR 1.
 REPEAT 984 1010 LRR 2.
 REPEAT 1048 1073 LRR 3.
 REPEAT 1074 1103 LRR 4.
 REPEAT 1104 1128 LRR 5.
 REPEAT 1129 1156 LRR 6.
 ZN_FING 564 610 CXXC-type.
 ZN_FING 617 678 PHD-type.
 METAL 212 212 Iron; catalytic (Probable).
 METAL 214 214 Iron; catalytic (By similarity).
 METAL 284 284 Iron; catalytic (By similarity).
 BINDING 209 209 Substrate (By similarity).
 BINDING 229 229 Substrate (By similarity).
 MOD_RES 28 28 Phosphoserine.
 MOD_RES 390 390 Phosphoserine.
 MOD_RES 394 394 Phosphoserine.
 MOD_RES 550 550 Phosphothreonine.
 MOD_RES 558 558 Phosphoserine.
 MOD_RES 632 632 Phosphothreonine.
 MOD_RES 692 692 Phosphoserine.
 MOD_RES 713 713 Phosphothreonine.
 MOD_RES 731 731 Phosphoserine.
 MOD_RES 832 832 Phosphoserine.
 MOD_RES 869 869 Phosphoserine.
 MOD_RES 883 883 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Chromatin regulator; Complete proteome; Dioxygenase; DNA-binding; Iron; Leucine-rich repeat; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1162 AA 
Protein Sequence
MEPEEERIRY SQRLRGTMRR RYEDDGISDD EIEGKRTFDL EEKLHTNKYN ANFVTFMEGK 60
DFNVEYIQRG GLRDPLIFKN SDGLGIKMPD PDFTVNDVKM CVGSRRMVDV MDVNTQKGIE 120
MTMAQWTRYY ETPEEEREKL YNVISLEFSH TRLENMVQRP STVDFIDWVD NMWPRHLKES 180
QTESTNAILE MQYPKVQKYC LMSVRGCYTD FHVDFGGTSV WYHIHQGGKV FWLIPPTAHN 240
LELYENWLLS GKQGDIFLGD RVSDCQRIEL KQGYTFVIPS GWIHAVYTPT DTLVFGGNFL 300
HSFNIPMQLK IYNIEDRTRV PNKFRYPFYY EMCWYVLERY VYCITNRSHL TKEFQKESLS 360
MDLELNGLES GNGDEEAVDR EPRRLSSRRS VLTSPVANGV NLDYDGLGKT CRSLPSLKKT 420
LAGDSSSDCS RGSHNGQVWD PQCAPRKDRQ VHLTHFELEG LRCLVDKLES LPLHKKCVPT 480
GIEDEDALIA DVKILLEELA NSDPKLALTG VPIVQWPKRD KLKFPTRPKV RVPTIPITKP 540
HTMKPAPRLT PVRPAAASPI VSGARRRRVR CRKCKACVQG ECGVCHYCRD MKKFGGPGRM 600
KQSCVLRQCL APRLPHSVTC SLCGEVDQNE ETQDFEKKLM ECCICNEIVH PGCLQMDGEG 660
LLNEELPNCW ECPKCYQEDS SEKAQKRKME ESDEEAVQAK VLRPLRSCDE PLTPPPHSPT 720
SMLQLIHDPV SPRGMVTRSS PGAGPSDHHS ASRDERFKRR QLLRLQATER TMVREKENNP 780
SGKKELSEVE KAKIRGSYLT VTLQRPTKEL HGTSIVPKLQ AITASSANLR HSPRVLVQHC 840
PARTPQRGDE EGLGGEEEEE EEEEEEDDSA EEGGAARLNG RGSWAQDGDE SWMQREVWMS 900
VFRYLSRREL CECMRVCKTW YKWCCDKRLW TKIDLSRCKA IVPQALSGII KRQPVSLDLS 960
WTNISKKQLT WLVNRLPGLK DLLLAGCSWS AVSALSTSSC PLLRTLDLRW AVGIKDPQIR 1020
DLLTPPADKP GQDNRSKLRN MTDFRLAGLD ITDATLRLII RHMPLLSRLD LSHCSHLTDQ 1080
SSNLLTAVGS STRYSLTELN MAGCNKLTDQ TLIYLRRIAN VTLIDLRGCK QITRKACEHF 1140
ISDLSINSLY CLSDEKLIQK IS 1162 
Gene Ontology
 GO:0000790; C:nuclear chromatin; IEA:Compara.
 GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
 GO:0051864; F:histone demethylase activity (H3-K36 specific); IEA:EC.
 GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW.
 GO:0045322; F:unmethylated CpG binding; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0070544; P:histone H3-K36 demethylation; IMP:MGI.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR001810; F-box_dom_cyclin-like.
 IPR003347; JmjC_dom.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR002857; Znf_CXXC.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00646; F-box
 PF02373; JmjC
 PF02008; zf-CXXC 
SMART
 SM00256; FBOX
 SM00558; JmjC
 SM00249; PHD 
PROSITE
 PS50181; FBOX
 PS51184; JMJC
 PS51058; ZF_CXXC
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS