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Showing Protein Eukaryotic translation initiation factor 2 subunit 1 (HMDBP02276)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP02276
Secondary Accession Numbers
  • 7761
Name Eukaryotic translation initiation factor 2 subunit 1
Synonyms
  1. Eukaryotic translation initiation factor 2 subunit alpha
  2. eIF-2-alpha
  3. eIF-2A
  4. eIF-2alpha
Gene Name EIF2S1
Protein Type Unknown
Biological Properties
General Function Translation, ribosomal structure and biogenesis
Specific Function Functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B
Pathways Not Available
Reactions Not Available
GO Classification
Component
macromolecular complex
protein complex
eukaryotic translation initiation factor 2 complex
Function
binding
translation initiation factor activity
nucleic acid binding
translation factor activity, nucleic acid binding
rna binding
Process
macromolecule biosynthetic process
cellular macromolecule biosynthetic process
translation
metabolic process
biosynthetic process
Cellular Location
  1. Cytoplasmic
Gene Properties
Chromosome Location Chromosome:1
Locus 14q23.3
SNPs EIF2S1
Gene Sequence 
>948 bp
ATGCCGGGTCTAAGTTGTAGATTTTATCAACACAAATTTCCTGAGGTGGAAGATGTAGTG
ATGGTGAATGTCAGATCCATTGCTGAAATGGGGGCTTATGTCAGCTTGCTGGAATACAAC
AACATTGAAGGCATGATTCTTCTTAGTGAATTATCCAGAAGGCGTATCCGTTCTATCAAC
AAACTCATCCGAATTGGCAGGAATGAGTGTGTGGTTGTCATTAGGGTGGACAAAGAAAAA
GGATATATTGATTTGTCAAAAAGAAGAGTTTCTCCAGAGGAAGCAATCAAATGTGAAGAC
AAATTCACAAAATCCAAAACTGTTTATAGCATTCTTCGTCATGTTGCTGAGGTGTTAGAA
TACACCAAGGATGAGCAGCTGGAAAGCCTATTCCAGAGGACTGCCTGGGTCTTTGATGAC
AAGTACAAGAGACCTGGATATGGTGCCTATGATGCATTTAAGCATGCAGTCTCAGACCCA
TCTATTTTGGATAGTTTAGATTTGAATGAAGATGAACGGGAAGTACTCATTAATAATATT
AATAGGCGCTTGACCCCACAGGCTGTCAAAATTCGAGCAGATATTGAAGTGGCTTGTTAT
GGTTATGAAGGCATTGATGCTGTAAAAGAAGCCCTAAGAGCAGGTTTGAATTGTTCTACA
GAAAACATGCCCATTAAGATTAATCTAATAGCTCCTCCTCGGTATGTAATGACTACGACA
ACCCTGGAGAGAACAGAAGGCCTTTCTGTCCTCAGTCAAGCTATGGCTGTTATCAAAGAG
AAGATTGAGGAAAAGAGGGGTGTGTTCAATGTTCAAATGGAGCCCAAAGTGGTCACAGAT
ACAGATGAGACTGAACTTGCGAGGCAGATGGAGAGGCTTGAAAGAGAAAATGCCGAAGTG
GATGGAGATGATGATGCAGAAGAAATGGAAGCCAAAGCTGAAGATTAA
Protein Properties
Number of Residues 315
Molecular Weight 36111.8
Theoretical pI 4.73
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>Eukaryotic translation initiation factor 2 subunit 1
MPGLSCRFYQHKFPEVEDVVMVNVRSIAEMGAYVSLLEYNNIEGMILLSELSRRRIRSIN
KLIRIGRNECVVVIRVDKEKGYIDLSKRRVSPEEAIKCEDKFTKSKTVYSILRHVAEVLE
YTKDEQLESLFQRTAWVFDDKYKRPGYGAYDAFKHAVSDPSILDSLDLNEDEREVLINNI
NRRLTPQAVKIRADIEVACYGYEGIDAVKEALRAGLNCSTENMPIKINLIAPPRYVMTTT
TLERTEGLSVLSQAMAVIKEKIEEKRGVFNVQMEPKVVTDTDETELARQMERLERENAEV
DGDDDAEEMEAKAED
GenBank ID Protein 12803385
UniProtKB/Swiss-Prot ID P05198
UniProtKB/Swiss-Prot Entry Name IF2A_HUMAN
PDB IDs
GenBank Gene ID BC002513
GeneCard ID EIF2S1
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  4. Ernst H, Duncan RF, Hershey JW: Cloning and sequencing of complementary DNAs encoding the alpha-subunit of translational initiation factor eIF-2. Characterization of the protein and its messenger RNA. J Biol Chem. 1987 Jan 25;262(3):1206-12. [PubMed:2948954 ]
  5. Langland JO, Jacobs BL: Inhibition of PKR by vaccinia virus: role of the N- and C-terminal domains of E3L. Virology. 2004 Jul 1;324(2):419-29. [PubMed:15207627 ]
  6. Montero H, Rojas M, Arias CF, Lopez S: Rotavirus infection induces the phosphorylation of eIF2alpha but prevents the formation of stress granules. J Virol. 2008 Feb;82(3):1496-504. Epub 2007 Nov 21. [PubMed:18032499 ]
  7. Nonato MC, Widom J, Clardy J: Crystal structure of the N-terminal segment of human eukaryotic translation initiation factor 2alpha. J Biol Chem. 2002 May 10;277(19):17057-61. Epub 2002 Feb 21. [PubMed:11859078 ]
  8. Ito T, Marintchev A, Wagner G: Solution structure of human initiation factor eIF2alpha reveals homology to the elongation factor eEF1B. Structure. 2004 Sep;12(9):1693-704. [PubMed:15341733 ]