UniProt Accession

 ERF3A_HUMAN; P15170; J3KQG6; Q96GF2 

Genbank Protein ID

 X17644; U95742; AC007216; BC009503 

Genbank Nucleotide ID

 CAA35635.1; AAB67250.1; AAH09503.2 

Protein Name

 Eukaryotic peptide chain release factor GTP-binding subunit ERF3A 

Protein Synonyms/Alias

 Eukaryotic peptide chain release factor subunit 3a; eRF3a; G1 to S phase transition protein 1 homolog 

Gene Name

 GSPT1 

Gene Synonyms/Alias

 ERF3A 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
108	VDKRTLEKYEREAKE	acetylation	[1]
196	EFETGFEKGGQTREH	acetylation	[1]
196	EFETGFEKGGQTREH	ubiquitination	[2]
240	RYEECKEKLVPFLKK	ubiquitination	[2]
254	KVGFNPKKDIHFMPC	ubiquitination	[2]
309	IRLPIVDKYKDMGTV	ubiquitination	[3, 4]
448	KTRPRFVKQDQVCIA	ubiquitination	[5]
490	GKTIAIGKVLKLVPE	acetylation	[1]
490	GKTIAIGKVLKLVPE	ubiquitination	[4]
493	IAIGKVLKLVPEKD*	acetylation	[1]

Reference

 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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] 

Functional Description

 Involved in translation termination in response to the termination codons UAA, UAG and UGA. Stimulates the activity of ERF1. Involved in regulation of mammalian cell growth. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. 

Sequence Annotation

 NP_BIND 81 88 GTP (By similarity).
 NP_BIND 158 162 GTP (By similarity).
 NP_BIND 220 223 GTP (By similarity).  

Keyword

 3D-structure; Alternative splicing; Complete proteome; GTP-binding; Nonsense-mediated mRNA decay; Nucleotide-binding; Protein biosynthesis; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 499 AA 

Protein Sequence

Gene Ontology

 GO:0005622; C:intracellular; NAS:UniProtKB.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; TAS:UniProtKB.
 GO:0003747; F:translation release factor activity; IMP:UniProtKB.
 GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:UniProtKB.
 GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:UniProtKB.
 GO:0006479; P:protein methylation; IDA:MGI. 

Interpro

 IPR000795; EF_GTP-bd_dom.
 IPR027417; P-loop_NTPase.
 IPR009001; Transl_elong_EF1A/Init_IF2_C.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR004160; Transl_elong_EFTu/EF1A_C.
 IPR009000; Transl_elong_init/rib_B-barrel. 

Pfam

 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2
 PF03143; GTP_EFTU_D3 

SMART

  

PROSITE

 PS00301; EFACTOR_GTP 

PRINTS

 PR00315; ELONGATNFCT.