P20042 (IF2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Eukaryotic translation initiation factor 2 subunit 2

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

Gene names

Name:	EIF2S2
Synonyms:	EIF2B

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	333 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. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 By similarity.
Sequence similarities	Belongs to the eIF-2-beta/eIF-5 family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Coding sequence diversity	Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Initiation factor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytosol Traceable author statement. Source: Reactome eukaryotic translation initiation factor 2 complex Traceable author statement Ref.1. Source: ProtInc
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW translation initiation factor activity Inferred from direct assay PubMed 16289705. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF2S1	P05198	5	EBI-711977,EBI-1056162
EIF2S3	P41091	3	EBI-711977,EBI-1054228

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.10
	Chain	2 – 333	332	Eukaryotic translation initiation factor 2 subunit 2		PRO_0000137406
Regions
	Zinc finger	281 – 305	25	C4-type Potential
	Compositional bias	14 – 21	8	Poly-Lys
	Compositional bias	79 – 87	9	Poly-Lys
	Compositional bias	124 – 129	6	Poly-Lys
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.10
	Modified residue	2	1	Phosphoserine Ref.4 Ref.8 Ref.10
	Modified residue	13	1	Phosphoserine By similarity
	Modified residue	67	1	Phosphoserine Ref.8 Ref.10
	Modified residue	105	1	Phosphoserine Ref.6 Ref.10
	Modified residue	111	1	Phosphothreonine Ref.6 Ref.10
	Modified residue	158	1	Phosphoserine Ref.8
	Modified residue	218	1	Phosphoserine By similarity
	Modified residue	265	1	N6-acetyllysine Ref.7
	Modified residue	293	1	N6-acetyllysine Ref.7
Natural variations
	Natural variant	177	1	E → D. Ref.3 Corresponds to variant rs17856024 [ dbSNP | Ensembl ].		VAR_048909
Experimental info
	Sequence conflict	295	1	T → I in AAA52383. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P20042 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 3E9FD4B48AA61A51	FASTA	333	38,388
	10 20 30 40 50 60 MSGDEMIFDP TMSKKKKKKK KPFMLDEEGD TQTEETQPSE TKEVEPEPTE DKDLEADEED 70 80 90 100 110 120 TRKKDASDDL DDLNFFNQKK KKKKTKKIFD IDEAEEGVKD LKIESDVQEP TEPEDDLDIM 130 140 150 160 170 180 LGNKKKKKKN VKFPDEDEIL EKDEALEDED NKKDDGISFS NQTGPAWAGS ERDYTYEELL 190 200 210 220 230 240 NRVFNIMREK NPDMVAGEKR KFVMKPPQVV RVGTKKTSFV NFTDICKLLH RQPKHLLAFL 250 260 270 280 290 300 LAELGTSGSI DGNNQLVIKG RFQQKQIENV LRRYIKEYVT CHTCRSPDTI LQKDTRLYFL 310 320 330 QCETCHSRCS VASIKTGFQA VTGKRAQLRA KAN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of the beta subunit of translational initiation factor eIF-2." Pathak V.K., Nielsen P.J., Trachsel H., Hershey J.W.B. Cell 54:633-639(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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], VARIANT ASP-177. Tissue: Lung and Placenta.
[4]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[6]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105 AND THR-111, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[7]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-265 AND LYS-293, MASS SPECTROMETRY.
[8]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-67 AND SER-158, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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].
[10]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-67; SER-105 AND THR-111, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M29536 mRNA. Translation: AAA52383.1. AL031668 Genomic DNA. Translation: CAB43741.1. BC000461 mRNA. Translation: AAH00461.1. BC000934 mRNA. Translation: AAH00934.1.
IPI	IPI00021728.
PIR	A31226.
RefSeq	NP_003899.2. NM_003908.3.
UniGene	Hs.429180.
3D structure databases
ProteinModelPortal	P20042.
ModBase	Search...
Protein-protein interaction databases
IntAct	P20042. 20 interactions.
MINT	MINT-5004121.
STRING	9606.ENSP00000364119.
PTM databases
PhosphoSite	P20042.
Polymorphism databases
DMDM	12644154.
Proteomic databases
PRIDE	P20042.
Protocols and materials databases
DNASU	8894.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000374980; ENSP00000364119; ENSG00000125977.
GeneID	8894.
KEGG	hsa:8894.
UCSC	uc002xaf.3. human.
Organism-specific databases
CTD	8894.
GeneCards	GC20M032676.
HGNC	HGNC:3266. EIF2S2.
HPA	CAB034415.
MIM	603908. gene.
neXtProt	NX_P20042.
PharmGKB	PA27696.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HOG000107198.
HOVERGEN	HBG000927.
InParanoid	P20042.
KO	K03238.
OMA	QMIFDPT.
OrthoDB	EOG42Z4QJ.
PhylomeDB	P20042.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins. REACT_1762. 3' -UTR-mediated translational regulation. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	P20042.
Bgee	P20042.
CleanEx	HS_EIF2S2.
Genevestigator	P20042.
GermOnline	ENSG00000125977. Homo sapiens.
Family and domain databases
Gene3D	3.30.30.50. 1 hit.
InterPro	IPR002735. Transl_init_fac_IF2/IF5. IPR016189. Transl_init_fac_IF2/IF5_N. IPR016190. Transl_init_fac_IF2/IF5_Zn-bd. [Graphical view]
Pfam	PF01873. eIF-5_eIF-2B. 1 hit. [Graphical view]
SMART	SM00653. eIF2B_5. 1 hit. [Graphical view]
SUPFAM	SSF100966. Transl_init_fac_IF2/IF5_N. 1 hit. SSF75689. Transl_init_fac_IF2/IF5_Zn-bd. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	EIF2S2. human.
GenomeRNAi	8894.
NextBio	33403.
SOURCE	Search...

Entry information

Entry name

IF2B_HUMAN

Accession

Primary (citable) accession number: P20042
Secondary accession number(s): Q9BVU0, Q9UJE4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 142 of the entry and version 2 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.