P41091 (IF2G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Eukaryotic translation initiation factor 2 subunit 3

Alternative name(s):
Eukaryotic translation initiation factor 2 subunit gamma X
Short name=eIF-2-gamma X
Short name=eIF-2gX

Gene names

Name:	EIF2S3
Synonyms:	EIF2G

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	472 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Heterotrimer composed of an alpha, a beta and a gamma chain.
Sequence similarities	Belongs to the GTP-binding elongation factor family. EIF2G subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Coding sequence diversity	Polymorphism
Ligand	GTP-binding Nucleotide-binding
Molecular function	Initiation factor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Traceable author statement Ref.1. Source: ProtInc translation initiation factor activity Inferred from direct assay PubMed 10900014PubMed 16289705. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF2S1	P05198	4	EBI-1054228,EBI-1056162
EIF2S2	P20042	3	EBI-1054228,EBI-711977

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5 Ref.6
	Chain	2 – 472	471	Eukaryotic translation initiation factor 2 subunit 3		PRO_0000137438
Regions
	Nucleotide binding	48 – 55	8	GTP By similarity
	Nucleotide binding	134 – 138	5	GTP By similarity
	Nucleotide binding	190 – 193	4	GTP By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine; partial Ref.6
	Modified residue	22	1	Phosphothreonine By similarity
Natural variations
	Natural variant	125	1	K → R. Corresponds to variant rs16997659 [ dbSNP | Ensembl ].		VAR_002352

Sequences

	Sequence		Length	Mass (Da)
	P41091 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 7A292A6AAF6DF983	FASTA	472	51,109
	10 20 30 40 50 60 MAGGEAGVTL GQPHLSRQDL TTLDVTKLTP LSHEVISRQA TINIGTIGHV AHGKSTVVKA 70 80 90 100 110 120 ISGVHTVRFK NELERNITIK LGYANAKIYK LDDPSCPRPE CYRSCGSSTP DEFPTDIPGT 130 140 150 160 170 180 KGNFKLVRHV SFVDCPGHDI LMATMLNGAA VMDAALLLIA GNESCPQPQT SEHLAAIEIM 190 200 210 220 230 240 KLKHILILQN KIDLVKESQA KEQYEQILAF VQGTVAEGAP IIPISAQLKY NIEVVCEYIV 250 260 270 280 290 300 KKIPVPPRDF TSEPRLIVIR SFDVNKPGCE VDDLKGGVAG GSILKGVLKV GQEIEVRPGI 310 320 330 340 350 360 VSKDSEGKLM CKPIFSKIVS LFAEHNDLQY AAPGGLIGVG TKIDPTLCRA DRMVGQVLGA 370 380 390 400 410 420 VGALPEIFTE LEISYFLLRR LLGVRTEGDK KAAKVQKLSK NEVLMVNIGS LSTGGRVSAV 430 440 450 460 470 KADLGKIVLT NPVCTEVGEK IALSRRVEKH WRLIGWGQIR RGVTIKPTVD DD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Translation initiation factor eIF-2. Cloning and expression of the human cDNA encoding the gamma-subunit." Gaspar N.J., Kinzy T.G., Scherer B.J., Huembelin M., Hershey J.W.B., Merrick W.C. J. Biol. Chem. 269:3415-3422(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Leukemia.
[2]	"Human protein factory for converting the transcriptome into an in vitro-expressed proteome." Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N. Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph.
[5]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-17. Tissue: Platelet.
[6]	Bienvenut W.V., Boldt K., von Kriegsheim A., Kolch W., Heiserich L., Gottlieb E., Vousden K.H., Lukashchuk N., Lilla S., Lempens A. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-54; 60-75; 182-191; 242-255; 276-285; 290-303; 318-342; 401-416; 453-460 AND 462-472, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Colon carcinoma, Hepatoma, Lung carcinoma and Ovarian carcinoma.
[7]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L19161 mRNA. Translation: AAA19696.1. AB451230 mRNA. Translation: BAG70044.1. AB451353 mRNA. Translation: BAG70167.1. CH471074 Genomic DNA. Translation: EAW99010.1. BC019906 mRNA. Translation: AAH19906.1.
IPI	IPI00297982.
PIR	A53048.
RefSeq	NP_001406.1. NM_001415.3.
UniGene	Hs.539684.
3D structure databases
ProteinModelPortal	P41091.
ModBase	Search...
Protein-protein interaction databases
IntAct	P41091. 9 interactions.
STRING	9606.ENSP00000253039.
PTM databases
PhosphoSite	P41091.
Polymorphism databases
DMDM	729816.
Proteomic databases
PaxDb	P41091.
PeptideAtlas	P41091.
PRIDE	P41091.
Protocols and materials databases
DNASU	1968.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000253039; ENSP00000253039; ENSG00000130741.
GeneID	1968.
KEGG	hsa:1968.
UCSC	uc004dbc.3. human.
Organism-specific databases
CTD	1968.
GeneCards	GC0XP024072.
HGNC	HGNC:3267. EIF2S3.
HPA	CAB012471.
MIM	300161. gene.
neXtProt	NX_P41091.
PharmGKB	PA27697.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5257.
HOVERGEN	HBG006123.
InParanoid	P41091.
KO	K03242.
OMA	IAANEPC.
OrthoDB	EOG4KWJSN.
PhylomeDB	P41091.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins. REACT_1762. 3' -UTR-mediated translational regulation. REACT_71. Gene Expression.
Gene expression databases
Bgee	P41091.
CleanEx	HS_EIF2S3.
Genevestigator	P41091.
GermOnline	ENSG00000130741. Homo sapiens.
Family and domain databases
InterPro	IPR000795. EF_GTP-bd_dom. IPR015256. TIF2_gsu_C. IPR009001. Transl_elong_EF1A/Init_IF2_C. IPR004161. Transl_elong_EFTu/EF1A_2. IPR009000. Transl_elong_init/rib_B-barrel. [Graphical view]
Pfam	PF09173. eIF2_C. 1 hit. PF00009. GTP_EFTU. 1 hit. PF03144. GTP_EFTU_D2. 1 hit. [Graphical view]
PRINTS	PR00315. ELONGATNFCT.
SUPFAM	SSF50465. Elong_init_C. 1 hit. SSF50447. Translat_factor. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	EIF2S3. human.
GenomeRNAi	1968.
NextBio	7979.
SOURCE	Search...

Entry information

Entry name

IF2G_HUMAN

Accession

Primary (citable) accession number: P41091
Secondary accession number(s): B5BTZ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 125 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.