P41375 (IF2B_DROME) 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:	eIF-2beta
Synonyms:	eIF2b
ORF Names:	CG4153

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	312 AA.
Sequence status	Complete.
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 preinitiation complex mediates ribosomal recognition of a start codon during the scanning process of the leader region.
Subunit structure	Heterotrimer composed of an alpha, a beta and a gamma chain.
Sequence similarities	Belongs to the eIF-2-beta/eIF-5 family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Initiation factor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	mitotic spindle elongation Inferred from mutant phenotype. Source: FlyBase
Cellular component	microtubule associated complex Inferred from direct assay. Source: FlyBase
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW translation initiation factor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 312	312	Eukaryotic translation initiation factor 2 subunit 2		PRO_0000137409
Regions
	Zinc finger	260 – 284	25	C4-type Potential
	Compositional bias	13 – 19	7	Poly-Lys
	Compositional bias	63 – 70	8	Poly-Lys
	Compositional bias	93 – 99	7	Poly-Glu
	Compositional bias	110 – 118	9	Poly-Lys
Amino acid modifications
	Modified residue	44	1	Phosphoserine Ref.5
	Modified residue	133	1	Phosphoserine Ref.6
	Modified residue	145	1	Phosphothreonine Ref.6
Experimental info
	Sequence conflict	60	1	S → G in AAL48875. Ref.4
	Sequence conflict	64	1	K → E in AAL48875. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P41375 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 163B98C43A35A764	FASTA	312	35,218
	10 20 30 40 50 60 MDAEDGFDPT LLKKKKKKKT TFDLDAALGL EDDTKKEDPQ DEASAEGGAA AEEDNLDLES 70 80 90 100 110 120 FGKKKKKKKK PFNMDEIEAA IPSFGGDDVA ASEEPEEEEI NLDMDFSMAK KKKKSKKKEL 130 140 150 160 170 180 DELFADQADD DKSEDKENDE DNSSTWFGSD RDYTYDELLK RVFEIILDKN PDMAAGRKPK 190 200 210 220 230 240 FVMRPPQVLR VGTKKTSFAN FMDIAKTLHR LPKHLLDFLL AELGTSGSMD GNQQLIIKGR 250 260 270 280 290 300 FQPKQIENVL RRYIKEYVTC HTCRSPETIL QKDTRLFFLQ CESCGSRCSV ASIKSGFQAV 310 TGKRAAIRAK TT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of the Drosophila melanogaster gene encoding translation-initiation factor eIF-2 beta." Ye X., Cavener D.R. Gene 142:271-274(1994) [PubMed: 8194763] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Oregon-R. Tissue: Embryo and Pupae.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells." Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A. Mol. Biosyst. 3:275-286(2007) [PubMed: 17372656] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, MASS SPECTROMETRY.
[6]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND THR-145, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L19197 mRNA. Translation: AAA28504.1. AE014296 Genomic DNA. Translation: AAF49902.1. AY071253 mRNA. Translation: AAL48875.1.
RefSeq	NP_524043.1. NM_079319.3.
3D structure databases
ProteinModelPortal	P41375.
SMR	P41375. Positions 153-291.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-21095N.
IntAct	P41375. 1 interaction.
MINT	MINT-878612.
STRING	P41375.
Proteomic databases
PRIDE	P41375.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0075968; FBpp0075700; FBgn0004926.
GeneID	39433.
KEGG	dme:Dmel_CG4153.
NMPDR	fig|7227.3.peg.9557.
Organism-specific databases
CTD	39433.
FlyBase	FBgn0004926. eIF-2beta.
Phylogenomic databases
eggNOG	inNOG04932.
GeneTree	EMGT00050000014283.
InParanoid	P41375.
OMA	MAGGRKP.
OrthoDB	EOG4H44KT.
PhylomeDB	P41375.
Gene expression databases
Bgee	P41375.
GermOnline	CG4153. Drosophila melanogaster.
Family and domain databases
InterPro	IPR002735. Transl_init_fac_IF2/IF5. IPR016189. Transl_init_fac_IF2/IF5_N. IPR016190. Transl_init_fac_IF2/IF5_Zn-bd. [Graphical view]
Gene3D	G3DSA:3.30.30.50. G3DSA:3.30.30.50. 1 hit.
KO	K03238.
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
NextBio	813610.

Entry information

Entry name

IF2B_DROME

Accession

Primary (citable) accession number: P41375
Secondary accession number(s): Q8SYX9, Q9VTZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project