Tag | Content |
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CPLM ID | CPLM-010496 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Eukaryotic translation initiation factor 2 subunit 3 |
Protein Synonyms/Alias | Eukaryotic translation initiation factor 2 subunit gamma; eIF-2-gamma; PP42 |
Gene Name | Eif2s3 |
Gene Synonyms/Alias | Eif2g |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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303 | VRPGIVSKDSEGKLM | acetylation | [1] | 421 | GGRVSAVKADLGKIV | acetylation | [1] | 449 | ALSRRVEKHWRLIGW | 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 | eIF-2 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. |
Sequence Annotation | NP_BIND 48 55 GTP (By similarity). NP_BIND 134 138 GTP (By similarity). NP_BIND 190 193 GTP (By similarity). MOD_RES 2 2 N-acetylalanine (By similarity). MOD_RES 22 22 Phosphothreonine (By similarity). |
Keyword | Acetylation; Complete proteome; Direct protein sequencing; GTP-binding; Initiation factor; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 472 AA |
Protein Sequence | MAGGEAGVTL GQPHLSRQDL ATLDVTKLTP LSHEVISRQA TINIGTIGHV AHGKSTVVKA 60 ISGVHTVRFK NELERNITIK LGYANAKIYK LDDPSCPRPE CYRSCGSSTP DEFPTDIPGT 120 KGNFKLVRHV SFVDCPGHDI LMATMLNGAA VMDAALLLIA GNESCPQPQT SEHLAAIEIM 180 KLKHILILQN KIDLVKESQA KEQYEQILAF VQGTVAEGAP IIPISAQLKY NIEVVCEYIV 240 KKIPVPPRDF TSEPRLIVIR SFDVNKPGCE VDDLKGGVAG GSILKGVLKV GQEIEVRPGI 300 VSKDSEGKLM CKPIFSKIVS LFAEHNDLQY AAPGGLIGVG TKIDPTLCRA DRMVGQVLGA 360 VGALPEIFTE LEISYFLLRR LLGVRTEGDK KAAKVQKLSK NEVLMVNIGS LSTGGRVSAV 420 KADLGKIVLT NPVCTEVGEK IALSRRVEKH WRLIGWGQIR RGVTIKPTVD DD 472 |
Gene Ontology | GO:0005525; F:GTP binding; IEA:UniProtKB-KW. GO:0003924; F:GTPase activity; IEA:InterPro. GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW. GO:0006184; P:GTP catabolic process; IEA:GOC. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |