CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-039619
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Arginyl-tRNA--protein transferase 1 
Protein Synonyms/Alias
 Arginyltransferase 1; R-transferase 1; Arginine-tRNA--protein transferase 1 
Gene Name
 ATE1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
8MASVVEYKGLRAGYHubiquitination[1]
Reference
 [1] 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] 
Functional Description
 Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Does not arginylate cysteine residues (By similarity). 
Sequence Annotation
  
Keyword
 Acyltransferase; Complete proteome; Reference proteome; Transferase; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 511 AA 
Protein Sequence
MASVVEYKGL RAGYHCGYCD SKEGKASCGM WAHSMTVQDY QDLIDRGWRR SGKYVYKPVM 60
NQTCCPQYTI RCRPLQFQPS KSHKKVLKKM LKFLAKGEVP KGSCEDEPMD STMDDAVAGD 120
FALINKLDIQ CDLKTLSDDI KESLESEGKN SKKEEPQELL QSQDFVGEKL GSGEPSHSVK 180
VHTVPKPGKG ADLSKPPCRK AKEIRKERKR LKLMQQNPAG ELEGFQAQGH PPSLFPPKAK 240
SNQPKSLEDL IFESLPENAS HKLEVRLVPV SFEDPEFKSS FSQSFSLYVK YQVAIHQDPP 300
DECGKTEFTR FLCSSPLEAE TPPNGPDCGY GSFHQQYWLD GKIIAVGVID ILPNCVSSVY 360
LYYDPDYSFL SLGVYSALRE IAFTRQLHEK TSQLSYYYMG FYIHSCPKMK YKGQYRPSDL 420
LCPETYVWVP IEQCLPSLEN SKYCRFNQDP EAVDEDRSTE PDRLQVFHKR AIMPYGVYKK 480
QQKDPSEEAA VLQYASLVGQ KCSERMLLFR N 511 
Gene Ontology
 GO:0004057; F:arginyltransferase activity; IEA:EC.
 GO:0016598; P:protein arginylation; IEA:InterPro. 
Interpro
 IPR016181; Acyl_CoA_acyltransferase.
 IPR017137; Arg-tRNA-P_Trfase_1_euk.
 IPR007472; Arg-tRNA-P_Trfase_C.
 IPR007471; Arg_tRNA_PTrfase_N. 
Pfam
 PF04377; ATE_C
 PF04376; ATE_N 
SMART
  
PROSITE
  
PRINTS