CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023725
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein MTO1 homolog, mitochondrial 
Protein Synonyms/Alias
  
Gene Name
 MTO1 
Gene Synonyms/Alias
 CGI-02 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
227GLAQTLEKLGFVVGRubiquitination[1, 2, 3]
245GTPPRIAKESINFSIubiquitination[2, 4, 5]
275TNETVWIKPEDQLPCubiquitination[1]
297RVDEIVLKNLHLNSHubiquitination[1, 2, 4, 5, 6]
306LHLNSHVKETTRGPRubiquitination[2, 5]
321YCPSIESKVLRFPNRubiquitination[2, 5]
460ASLRVSRKPPFVVSRubiquitination[2, 5]
555FLSSKWKKLIPEASIubiquitination[6]
577VRALDVLKYEEVDMDubiquitination[1]
588VDMDSLAKAVPEPLKubiquitination[1]
625FHQLQEIKGVQQDEAubiquitination[1]
637DEALQLPKDLDYLTIubiquitination[1, 2, 3, 5]
701SAMNESSKTDQYLCDubiquitination[4]
Reference
 [1] 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]
 [2] 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]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] 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]
 [6] 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
Functional Description
 Involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs. 
Sequence Annotation
 NP_BIND 43 48 FAD (By similarity).  
Keyword
 Alternative splicing; Cardiomyopathy; Complete proteome; Disease mutation; FAD; Flavoprotein; Mitochondrion; Reference proteome; Transit peptide; tRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 717 AA 
Protein Sequence
MFYFRGCGRW VAVSFTKQQF PLARLSSDSA APRTPHFDVI VIGGGHAGTE AATAAARCGS 60
RTLLLTHRVD TIGQMSCNPS FGGIGKGHLM REVDALDGLC SRICDQSGVH YKVLNRRKGP 120
AVWGLRAQID RKLYKQNMQK EILNTPLLTV QEGAVEDLIL TEPEPEHTGK CRVSGVVLVD 180
GSTVYAESVI LTTGTFLRGM IVIGLETHPA GRLGDQPSIG LAQTLEKLGF VVGRLKTGTP 240
PRIAKESINF SILNKHIPDN PSIPFSFTNE TVWIKPEDQL PCYLTHTNPR VDEIVLKNLH 300
LNSHVKETTR GPRYCPSIES KVLRFPNRLH QVWLEPEGMD SDLIYPQGLS MTLPAELQEK 360
MITCIRGLEK AKVIQPDGVL LLLPRMECNG AISAHHNLPL PGYGVQYDYL DPRQITPSLE 420
THLVQRLFFA GQINGTTGYE EAAAQGVIAG INASLRVSRK PPFVVSRTEG YIGVLIDDLT 480
TLGTSEPYRM FTSRVEFRLS LRPDNADSRL TLRGYKDAGC VSQQRYERAC WMKSSLEEGI 540
SVLKSIEFLS SKWKKLIPEA SISTSRSLPV RALDVLKYEE VDMDSLAKAV PEPLKKYTKC 600
RELAERLKIE ATYESVLFHQ LQEIKGVQQD EALQLPKDLD YLTIRDVSLS HEVREKLHFS 660
RPQTIGAASR IPGVTPAAII NLLRFVKTTQ RRQSAMNESS KTDQYLCDAD RLQEREL 717 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0070899; P:mitochondrial tRNA wobble uridine modification; IEA:Compara.
 GO:0055114; P:oxidation-reduction process; IEA:InterPro. 
Interpro
 IPR013027; FAD_pyr_nucl-diS_OxRdtase.
 IPR026904; GidA-assoc_3.
 IPR002218; GIDA-rel.
 IPR020595; GIDA-rel_CS. 
Pfam
 PF01134; GIDA
 PF13932; GIDA_assoc_3 
SMART
  
PROSITE
 PS01280; GIDA_1
 PS01281; GIDA_2 
PRINTS
 PR00368; FADPNR.