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Q99LD9 (EI2BB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Translation initiation factor eIF-2B subunit beta
Alternative name(s):
eIF-2B GDP-GTP exchange factor subunit beta
Gene names
Name:Eif2b2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length351 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP By similarity.

Subunit structure

Complex of five different subunits; alpha, beta, gamma, delta and epsilon By similarity.

Sequence similarities

Belongs to the eIF-2B alpha/beta/delta subunits family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Molecular functionInitiation factor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

central nervous system development

Inferred from sequence or structural similarity. Source: UniProtKB

myelination

Inferred from sequence or structural similarity. Source: UniProtKB

oligodendrocyte development

Inferred from sequence or structural similarity. Source: UniProtKB

ovarian follicle development

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of GTPase activity

Inferred from Biological aspect of Ancestor. Source: GOC

regulation of translational initiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

translational initiation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

eukaryotic translation initiation factor 2B complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

GTP binding

Inferred from sequence or structural similarity. Source: UniProtKB

guanyl-nucleotide exchange factor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

translation initiation factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 351351Translation initiation factor eIF-2B subunit beta
PRO_0000156062

Sequences

Sequence LengthMass (Da)Tools
Q99LD9 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 56FF1B8A96845853

FASTA35138,898
        10         20         30         40         50         60 
MPGAAAKGSE LSERIEGFVE TLKRGGGQRS SEDMARETLG LLRRLITDHH WNNAGDLMDL 

        70         80         90        100        110        120 
IRREGRRMTA AQPSETTVGN MVRRVLKIIR EEYGRLHGRS DESDQQESLH KLLTSGGLSE 

       130        140        150        160        170        180 
DFSFHFAPLK ANIIEAINEL LVELEGTMEN IAAQALEHIH SNEVIMTIGY SRTVEAFLKE 

       190        200        210        220        230        240 
AARKRKFHVI VAECAPFCQG HEMAVNLSKE GIETTVMTDA AIFAVMSRVN KVIIGTKTIL 

       250        260        270        280        290        300 
ANGSLRAVAG THTLALAAKH HSTPLIVCAP MFKLSPQFPS EEDSFHKFVA PEEVLPFTEG 

       310        320        330        340        350 
DILEKVSVHC PVFDYVPPDL ITLFISNIGG NAPSYIYRLM SELYHPDDHV L 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Spinal cord.
[2]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK049731 mRNA. Translation: BAC33897.1.
BC003326 mRNA. Translation: AAH03326.1.
CCDSCCDS26053.1.
RefSeqNP_663420.1. NM_145445.3.
UniGeneMm.29041.

3D structure databases

ProteinModelPortalQ99LD9.
SMRQ99LD9. Positions 73-344.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ99LD9. 1 interaction.
MINTMINT-4094186.

PTM databases

PhosphoSiteQ99LD9.

Proteomic databases

MaxQBQ99LD9.
PaxDbQ99LD9.
PRIDEQ99LD9.

Protocols and materials databases

DNASU217715.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000004910; ENSMUSP00000004910; ENSMUSG00000004788.
GeneID217715.
KEGGmmu:217715.
UCSCuc007ogr.1. mouse.

Organism-specific databases

CTD8892.
MGIMGI:2145118. Eif2b2.

Phylogenomic databases

eggNOGCOG1184.
GeneTreeENSGT00550000074908.
HOGENOMHOG000208487.
HOVERGENHBG051458.
InParanoidQ99LD9.
KOK03754.
OMARIITDHR.
OrthoDBEOG7N0C4T.
PhylomeDBQ99LD9.
TreeFamTF101506.

Gene expression databases

ArrayExpressQ99LD9.
BgeeQ99LD9.
GenevestigatorQ99LD9.

Family and domain databases

InterProIPR000649. IF-2B-related.
[Graphical view]
PfamPF01008. IF-2B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF2B2. mouse.
NextBio375988.
PROQ99LD9.
SOURCESearch...

Entry information

Entry nameEI2BB_MOUSE
AccessionPrimary (citable) accession number: Q99LD9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot