CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000251
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Eukaryotic translation initiation factor 1A, Y-chromosomal 
Protein Synonyms/Alias
 eIF-1A Y isoform; Eukaryotic translation initiation factor 4C; eIF-4C 
Gene Name
 EIF1AY 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
23KNENESEKRELVFKEubiquitination[1]
40QEYAQVIKMLGNGRLubiquitination[2]
56ALCFDGVKRLCHIRGubiquitination[2, 3]
67HIRGKLRKKVWINTSubiquitination[2]
68IRGKLRKKVWINTSDubiquitination[2]
88LRDYQDNKADVILKYacetylation[4]
88LRDYQDNKADVILKYubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9]
94NKADVILKYNADEARubiquitination[1, 2, 7]
104ADEARSLKAYGELPEubiquitination[1, 2, 7]
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] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [4] 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]
 [5] Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.
 Meierhofer D, Wang X, Huang L, Kaiser P.
 J Proteome Res. 2008 Oct;7(10):4566-76. [PMID: 18781797]
 [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]
 [7] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [9] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
Functional Description
 Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits (By similarity). 
Sequence Annotation
 DOMAIN 22 96 S1-like.
 CROSSLNK 88 88 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Complete proteome; Initiation factor; Isopeptide bond; Protein biosynthesis; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 144 AA 
Protein Sequence
MPKNKGKGGK NRRRGKNENE SEKRELVFKE DGQEYAQVIK MLGNGRLEAL CFDGVKRLCH 60
IRGKLRKKVW INTSDIILVG LRDYQDNKAD VILKYNADEA RSLKAYGELP EHAKINETDT 120
FGPGDDDEIQ FDDIGDDDED IDDI 144 
Gene Ontology
 GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW. 
Interpro
 IPR012340; NA-bd_OB-fold.
 IPR006196; RNA-binding_domain_S1_IF1.
 IPR001253; TIF_eIF-1A.
 IPR018104; TIF_eIF-1A_CS. 
Pfam
 PF01176; eIF-1a 
SMART
 SM00652; eIF1a 
PROSITE
 PS01262; IF1A
 PS50832; S1_IF1_TYPE 
PRINTS