CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013688
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alanine--tRNA ligase, mitochondrial 
Protein Synonyms/Alias
 Alanyl-tRNA synthetase; AlaRS 
Gene Name
 AARS2 
Gene Synonyms/Alias
 AARSL; KIAA1270 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
83NAGMNQFKPIFLGTVubiquitination[1]
280LVAVLQGKHSTYDTDubiquitination[2]
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] 
Functional Description
 Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain (By similarity). 
Sequence Annotation
 METAL 632 632 Zinc (Potential).
 METAL 636 636 Zinc (Potential).
 METAL 749 749 Zinc (Potential).
 METAL 753 753 Zinc (Potential).  
Keyword
 Aminoacyl-tRNA synthetase; ATP-binding; Cardiomyopathy; Complete proteome; Disease mutation; Ligase; Metal-binding; Mitochondrion; Nucleotide-binding; Polymorphism; Protein biosynthesis; Reference proteome; RNA-binding; Transit peptide; tRNA-binding; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 985 AA 
Protein Sequence
MAASVAAAAR RLRRAIRRSP AWRGLSHRPL SSEPPAAKAS AVRAAFLNFF RDRHGHRLVP 60
SASVRPRGDP SLLFVNAGMN QFKPIFLGTV DPRSEMAGFR RVANSQKCVR AGGHHNDLED 120
VGRDLSHHTF FEMLGNWAFG GEYFKEEACN MAWELLTQVY GIPEERLWIS YFDGDPKAGL 180
DPDLETRDIW LSLGVPASRV LSFGPQENFW EMGDTGPCGP CTEIHYDLAG GVGAPQLVEL 240
WNLVFMQHNR EADGSLQPLP QRHVDTGMGL ERLVAVLQGK HSTYDTDLFS PLLNAIQQGC 300
RAPPYLGRVG VADEGRTDTA YRVVADHIRT LSVCISDGIF PGMSGPPLVL RRILRRAVRF 360
SMEILKAPPG FLGSLVPVVV ETLGDAYPEL QRNSAQIANL VSEDEAAFLA SLERGRRIID 420
RTLRTLGPSD MFPAEVAWSL SLCGDLGLPL DMVELMLEEK GVQLDSAGLE RLAQEEAQHR 480
ARQAEPVQKQ GLWLDVHALG ELQRQGVPPT DDSPKYNYSL RPSGSYEFGT CEAQVLQLYT 540
EDGTAVASVG KGQRCGLLLD RTNFYAEQGG QASDRGYLVR AGQEDVLFPV ARAQVCGGFI 600
LHEAVAPECL RLGDQVQLHV DEAWRLGCMA KHTATHLLNW ALRQTLGPGT EQQGSHLNPE 660
QLRLDVTTQT PLTPEQLRAV ENTVQEAVGQ DEAVYMEEVP LALTAQVPGL RSLDEVYPDP 720
VRVVSVGVPV AHALDPASQA ALQTSVELCC GTHLLRTGAV GDLVIIGDRQ LSKGTTRLLA 780
VTGEQAQQAR ELGQSLAQEV KAATERLSLG SRDVAEALRL SKDIGRLIEA VETAVMPQWQ 840
RRELLATVKM LQRRANTAIR KLQMGQAAKK TQELLERHSK GPLIVDTVSA ESLSVLVKVV 900
RQLCEQAPST SVLLLSPQPM GKVLCACQVA QGAMPTFTAE AWALAVCSHM GGKAWGSRVV 960
AQGTGSTTDL EAALSIAQTY ALSQL 985 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:UniProtKB.
 GO:0004813; F:alanine-tRNA ligase activity; IMP:BHF-UCL.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
 GO:0070143; P:mitochondrial alanyl-tRNA aminoacylation; IMP:BHF-UCL.
 GO:0033108; P:mitochondrial respiratory chain complex assembly; IMP:BHF-UCL. 
Interpro
 IPR002318; Ala-tRNA-lgiase_IIc.
 IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
 IPR018165; Ala-tRNA-synth_IIc_core.
 IPR018164; Ala-tRNA-synth_IIc_N.
 IPR023033; Ala_tRNA_ligase_euk/bac.
 IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
 IPR012947; tRNA_SAD. 
Pfam
 PF01411; tRNA-synt_2c
 PF07973; tRNA_SAD 
SMART
 SM00863; tRNA_SAD 
PROSITE
 PS50860; AA_TRNA_LIGASE_II_ALA 
PRINTS
 PR00980; TRNASYNTHALA.