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Protein

Translation initiation factor eIF-2B subunit beta

Gene

Eif2b2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. GTP binding Source: UniProtKB
  3. guanyl-nucleotide exchange factor activity Source: GO_Central
  4. translation initiation factor activity Source: UniProtKB-KW

GO - Biological processi

  1. cellular response to stimulus Source: UniProtKB
  2. central nervous system development Source: UniProtKB
  3. myelination Source: UniProtKB
  4. oligodendrocyte development Source: UniProtKB
  5. ovarian follicle development Source: UniProtKB
  6. positive regulation of GTPase activity Source: MGI
  7. regulation of translational initiation Source: GO_Central
  8. translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiREACT_343149. Recycling of eIF2:GDP.

Names & Taxonomyi

Protein namesi
Recommended name:
Translation initiation factor eIF-2B subunit beta
Alternative name(s):
eIF-2B GDP-GTP exchange factor subunit beta
Gene namesi
Name:Eif2b2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:2145118. Eif2b2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. eukaryotic translation initiation factor 2B complex Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 351351Translation initiation factor eIF-2B subunit betaPRO_0000156062Add
BLAST

Proteomic databases

MaxQBiQ99LD9.
PaxDbiQ99LD9.
PRIDEiQ99LD9.

PTM databases

PhosphoSiteiQ99LD9.

Expressioni

Gene expression databases

BgeeiQ99LD9.
ExpressionAtlasiQ99LD9. baseline and differential.
GenevestigatoriQ99LD9.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ99LD9. 1 interaction.
MINTiMINT-4094186.

Structurei

3D structure databases

ProteinModelPortaliQ99LD9.
SMRiQ99LD9. Positions 73-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1184.
GeneTreeiENSGT00550000074908.
HOGENOMiHOG000208487.
HOVERGENiHBG051458.
InParanoidiQ99LD9.
KOiK03754.
OMAiRIITDHR.
OrthoDBiEOG7N0C4T.
PhylomeDBiQ99LD9.
TreeFamiTF101506.

Family and domain databases

InterProiIPR000649. IF-2B-related.
[Graphical view]
PfamiPF01008. IF-2B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99LD9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGAAAKGSE LSERIEGFVE TLKRGGGQRS SEDMARETLG LLRRLITDHH
60 70 80 90 100
WNNAGDLMDL IRREGRRMTA AQPSETTVGN MVRRVLKIIR EEYGRLHGRS
110 120 130 140 150
DESDQQESLH KLLTSGGLSE DFSFHFAPLK ANIIEAINEL LVELEGTMEN
160 170 180 190 200
IAAQALEHIH SNEVIMTIGY SRTVEAFLKE AARKRKFHVI VAECAPFCQG
210 220 230 240 250
HEMAVNLSKE GIETTVMTDA AIFAVMSRVN KVIIGTKTIL ANGSLRAVAG
260 270 280 290 300
THTLALAAKH HSTPLIVCAP MFKLSPQFPS EEDSFHKFVA PEEVLPFTEG
310 320 330 340 350
DILEKVSVHC PVFDYVPPDL ITLFISNIGG NAPSYIYRLM SELYHPDDHV

L
Length:351
Mass (Da):38,898
Last modified:June 1, 2001 - v1
Checksum:i56FF1B8A96845853
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK049731 mRNA. Translation: BAC33897.1.
BC003326 mRNA. Translation: AAH03326.1.
CCDSiCCDS26053.1.
RefSeqiNP_663420.1. NM_145445.3.
UniGeneiMm.29041.

Genome annotation databases

EnsembliENSMUST00000004910; ENSMUSP00000004910; ENSMUSG00000004788.
GeneIDi217715.
KEGGimmu:217715.
UCSCiuc007ogr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK049731 mRNA. Translation: BAC33897.1.
BC003326 mRNA. Translation: AAH03326.1.
CCDSiCCDS26053.1.
RefSeqiNP_663420.1. NM_145445.3.
UniGeneiMm.29041.

3D structure databases

ProteinModelPortaliQ99LD9.
SMRiQ99LD9. Positions 73-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99LD9. 1 interaction.
MINTiMINT-4094186.

PTM databases

PhosphoSiteiQ99LD9.

Proteomic databases

MaxQBiQ99LD9.
PaxDbiQ99LD9.
PRIDEiQ99LD9.

Protocols and materials databases

DNASUi217715.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000004910; ENSMUSP00000004910; ENSMUSG00000004788.
GeneIDi217715.
KEGGimmu:217715.
UCSCiuc007ogr.1. mouse.

Organism-specific databases

CTDi8892.
MGIiMGI:2145118. Eif2b2.

Phylogenomic databases

eggNOGiCOG1184.
GeneTreeiENSGT00550000074908.
HOGENOMiHOG000208487.
HOVERGENiHBG051458.
InParanoidiQ99LD9.
KOiK03754.
OMAiRIITDHR.
OrthoDBiEOG7N0C4T.
PhylomeDBiQ99LD9.
TreeFamiTF101506.

Enzyme and pathway databases

ReactomeiREACT_343149. Recycling of eIF2:GDP.

Miscellaneous databases

ChiTaRSiEif2b2. mouse.
NextBioi375988.
PROiQ99LD9.
SOURCEiSearch...

Gene expression databases

BgeeiQ99LD9.
ExpressionAtlasiQ99LD9. baseline and differential.
GenevestigatoriQ99LD9.

Family and domain databases

InterProiIPR000649. IF-2B-related.
[Graphical view]
PfamiPF01008. IF-2B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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(2004) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiEI2BB_MOUSE
AccessioniPrimary (citable) accession number: Q99LD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2001
Last modified: April 1, 2015
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.