CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015193
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RNA demethylase ALKBH5 
Protein Synonyms/Alias
 Alkylated DNA repair protein alkB homolog 5; Alpha-ketoglutarate-dependent dioxygenase alkB homolog 5 
Gene Name
 ALKBH5 
Gene Synonyms/Alias
 ABH5; OFOXD1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
57PYPVSGAKRKYQEDSubiquitination[1]
102FSQDECAKIEARIDEubiquitination[2]
116EVVSRAEKGLYNEHTubiquitination[1, 2]
132DRAPLRNKYFFGEGYacetylation[2, 3, 4]
132DRAPLRNKYFFGEGYubiquitination[1]
147TYGAQLQKRGPGQERubiquitination[1, 5, 6]
235FGCKFQFKPIRVSEPacetylation[2, 3, 4, 7]
235FGCKFQFKPIRVSEPubiquitination[1]
295DAPRLETKSLSSSVLubiquitination[1]
321NNRDPALKPKRSHRKacetylation[2, 4]
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] 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]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [5] 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]
 [6] 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]
 [7] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773
Functional Description
 Dioxygenase that demethylates RNA by oxidative demethylation: specifically demethylates N(6)-methyladenosine (m(6)A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. Requires molecular oxygen, alpha- ketoglutarate and iron. Demethylation of m(6)A mRNA affects mRNA processing and export and is required for spermatogenesis. 
Sequence Annotation
 METAL 204 204 Iron; catalytic (Probable).
 METAL 206 206 Iron; catalytic (By similarity).
 METAL 266 266 Iron; catalytic (Probable).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 64 64 Phosphoserine.
 MOD_RES 69 69 Phosphoserine.
 MOD_RES 71 71 Phosphotyrosine.
 MOD_RES 132 132 N6-acetyllysine.
 MOD_RES 361 361 Phosphoserine.
 MOD_RES 371 371 Phosphoserine (By similarity).
 MOD_RES 374 374 Phosphoserine.
 MOD_RES 384 384 Phosphoserine (By similarity).  
Keyword
 Acetylation; Alternative splicing; Coiled coil; Complete proteome; Differentiation; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Spermatogenesis. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 394 AA 
Protein Sequence
MAAASGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP YPVSGAKRKY 60
QEDSDPERSD YEEQQLQKEE EARKVKSGIR QMRLFSQDEC AKIEARIDEV VSRAEKGLYN 120
EHTVDRAPLR NKYFFGEGYT YGAQLQKRGP GQERLYPPGD VDEIPEWVHQ LVIQKLVEHR 180
VIPEGFVNSA VINDYQPGGC IVSHVDPIHI FERPIVSVSF FSDSALCFGC KFQFKPIRVS 240
EPVLSLPVRR GSVTVLSGYA ADEITHCIRP QDIKERRAVI ILRKTRLDAP RLETKSLSSS 300
VLPPSYASDR LSGNNRDPAL KPKRSHRKAD PDAAHRPRIL EMDKEENRRS VLLPTHRRRG 360
SFSSENYWRK SYESSEDCSE AAGSPARKVK MRRH 394 
Gene Ontology
 GO:0016607; C:nuclear speck; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0035515; F:oxidative RNA demethylase activity; IDA:UniProtKB.
 GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; 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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0006406; P:mRNA export from nucleus; IMP:UniProtKB.
 GO:0006397; P:mRNA processing; IMP:UniProtKB.
 GO:0035553; P:oxidative single-stranded RNA demethylation; IDA:UniProtKB.
 GO:0001666; P:response to hypoxia; IDA:UniProtKB.
 GO:0007283; P:spermatogenesis; ISS:UniProtKB. 
Interpro
 IPR027450; AlkB-like. 
Pfam
 PF13532; 2OG-FeII_Oxy_2 
SMART
  
PROSITE
  
PRINTS