Tag | Content |
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CPLM ID | CPLM-029597 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Arginyl-tRNA synthetase 2, mitochondrial |
Protein Synonyms/Alias | Arginyl-tRNA synthetase-like (Predicted); Protein Rars2 |
Gene Name | Rars2 |
Gene Synonyms/Alias | Rarsl_predicted; rCG_55034 |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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139 | SSPNIAKKFHVGHLR | acetylation | [1] | 557 | GARLHLFKAVRSVLA | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | |
Sequence Annotation | |
Keyword | Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 578 AA |
Protein Sequence | MACGFRRSIA CQLSRVLALP PESLIKSISA VPVSKKEEVA DFQLSVDSLL ENNSHKSQLD 60 TQDQAQRLAE KLKCDTVVTA ISAGPRTLNF KINRALLTKA VLQQVTEDGS KYGLKSELFS 120 DLPQKRIVVE FSSPNIAKKF HVGHLRSTII GNFIANLKEA LGHQVTRINY IGDWGMQFGL 180 LGTGFQLFGY EEKLQANPLQ HLFDVYVQVN KEATDDKNVT KLAHEFFHRL ELGDTQALAL 240 WQRFRDLSIE EYTQIYKRLG IYFDEYSGES FYREKSQDVL KLLDSKGLLQ KTAKGNVVVD 300 VSETGDLSSV CTVMRSDGTS LYATRDLAAA IHRKDKYNFD TMIYVADKGQ KRHFQQVFQM 360 LKIMGHEWAE RCQHVPFGIV KGMKTRRGEV TFLEDVLNEV QSRMLQNMAS IKTTKKMENP 420 RETAEKVGLA ALIIQDFRGL LLSDYQFSWD RVFQSRGDTG VFLQYTHARL CSLEETFGCG 480 YLNDFNVACL QEPQSVSILQ HLLRFDEVLY TASQDLQPKH IVSYLLTLSH LAAVAHKTLQ 540 VKDSPPEVAG ARLHLFKAVR SVLANGMKLL GITPVCKM 578 |
Gene Ontology | GO:0005739; C:mitochondrion; IEA:Compara. GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |