CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001277
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial 
Protein Synonyms/Alias
 Glu-AdT subunit B; Cytochrome c oxidase assembly factor PET112 homolog 
Gene Name
 PET112 
Gene Synonyms/Alias
 PET112L; HSPC199 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
181KQSQVIPKTVRIKQIacetylation[1]
186IPKTVRIKQIQLEQDubiquitination[2, 3]
280LGVRTEVKNLNSIRFubiquitination[2]
290NSIRFLAKAIDYEIQubiquitination[3]
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] 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] 
Functional Description
 Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). 
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Direct protein sequencing; Ligase; Mitochondrion; Nucleotide-binding; Polymorphism; Protein biosynthesis; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 557 AA 
Protein Sequence
MAAPMLRWGC RGRRWAFARV DGGSCHRRGA PTGSTSNQIR GESSVAQQPL HTAQKTRKGE 60
HKWAAVVGLE IHAQISSNSK LFSGSQVRFS APPNSLVSFF DASLPGTLPV LNRRCVEAAV 120
MTGLALNCHI NKKSLFDRKH YFYADLPAGY QITQQRLPIA VNGSLIYGVC AGKKQSQVIP 180
KTVRIKQIQL EQDSGKSLHD NLRSQTLIDL NRAGVGLLEV VLEPDMSCGE EAATAVRELQ 240
LILQALGTSQ ANMAEGQLRV DANISVHHPG EPLGVRTEVK NLNSIRFLAK AIDYEIQRQI 300
NELENGGEIL NETRSFHHKL GCTMSMRDKE GKQDYRFMPE PNLPPLVLYD ATSLPAGADP 360
QQVINIDQIR ETLPELPSVT REKLVQQYGM LLEHSFTLLN EVGLLEFFQN VIKETRAEPK 420
KVTSWVLNTF LGYLKQQNLA VSESPVTPSA LAELLDLLDS RTISSSAAKQ VFEELWKREG 480
KTPGQIVSEK QLELMQDQGA LEQLCHSVME AHPQVVMDVK NRNPRAINKL IGLVRKATQS 540
RADPVMIKEI LEKKLSL 557 
Gene Ontology
 GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IDA:UniProtKB.
 GO:0005739; C:mitochondrion; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IDA:UniProtKB.
 GO:0008135; F:translation factor activity, nucleic acid binding; TAS:ProtInc.
 GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IDA:UniProtKB.
 GO:0032543; P:mitochondrial translation; IMP:UniProtKB. 
Interpro
 IPR004413; Apn/Gln-ADT_bsu.
 IPR017959; Asn/Gln-tRNA_amidoTrfase_suB/E.
 IPR006075; Asn/Gln-tRNA_Trfase_suB/E_cat.
 IPR018027; Asn/Gln_amidotransferase.
 IPR003789; Asn/Gln_tRNA_amidoTrfrase-rel.
 IPR017958; Gln-tRNA_amidoTrfase_suB_CS. 
Pfam
 PF02934; GatB_N
 PF02637; GatB_Yqey 
SMART
 SM00845; GatB_Yqey 
PROSITE
 PS01234; GATB 
PRINTS