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Protein
Submitted name:

Eukaryotic translation initiation factor 2B, subunit 2 beta, 39kDa

Gene

EIF2B2

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Initiation factorImported

Keywords - Biological processi

Protein biosynthesis

Names & Taxonomyi

Protein namesi
Submitted name:
Eukaryotic translation initiation factor 2B, subunit 2 beta, 39kDaImported
Submitted name:
Full-length cDNA clone CS0DI071YM04 of Placenta of Homo sapiens (human)Imported
Gene namesi
Name:EIF2B2Imported
ORF Names:hCG_22350Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27689.

Expressioni

Gene expression databases

ExpressionAtlasiQ53XC2. baseline and differential.
GenevisibleiQ53XC2. HS.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
C9orf72Q96LT73EBI-10288660,EBI-2961725
EIF2B4Q9UI104EBI-10288660,EBI-2340132
MRFAP1L1Q96HT83EBI-10288660,EBI-748896

Protein-protein interaction databases

IntActiQ53XC2. 3 interactions.
STRINGi9606.ENSP00000266126.

Structurei

3D structure databases

ProteinModelPortaliQ53XC2.
SMRiQ53XC2. Positions 56-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOVERGENiHBG051458.
KOiK03754.
OMAiFVSPHEV.
PhylomeDBiQ53XC2.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q53XC2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGSAAKGSE LSERIESFVE TLKRGGGPRS SEEMARETLG LLRQIITDHR
60 70 80 90 100
WSNAGELMEL IRREGRRMTA AQPSETTVGN MVRRVLKIIR EEYGRLHGRS
110 120 130 140 150
DESDQQESLH KLLTSGGLNE DFSFHYAQLQ SNIIEAINEL LVELEGTMEN
160 170 180 190 200
IAAQALEHIH SNEVIMTIGF SRTVEAFLKE AARKRKFHVI VAECAPFCQG
210 220 230 240 250
HEMAVNLSKA GIETTVMTDA AIFAVMSRVN KVIIGTKTIL ANGALRAVTG
260 270 280 290 300
THTLALAAKH HSTPLIVCAP MFKLSPQFPN EEDSFHKFVA PEEVLPFTEG
310 320 330 340 350
DILEKVSVHC PVFDYVPPEL ITLFISNIGG NAPSYIYRLM SELYHPDDHV

L
Length:351
Mass (Da):38,990
Last modified:May 24, 2005 - v1
Checksum:iC29FE477143F545A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX161473 mRNA. Translation: CAD61929.1.
CH471061 Genomic DNA. Translation: EAW81210.1.
RefSeqiNP_055054.1. NM_014239.3.
UniGeneiHs.409137.

Genome annotation databases

GeneIDi8892.
KEGGihsa:8892.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX161473 mRNA. Translation: CAD61929.1.
CH471061 Genomic DNA. Translation: EAW81210.1.
RefSeqiNP_055054.1. NM_014239.3.
UniGeneiHs.409137.

3D structure databases

ProteinModelPortaliQ53XC2.
SMRiQ53XC2. Positions 56-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ53XC2. 3 interactions.
STRINGi9606.ENSP00000266126.

Protocols and materials databases

DNASUi8892.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi8892.
KEGGihsa:8892.

Organism-specific databases

CTDi8892.
PharmGKBiPA27689.

Phylogenomic databases

HOVERGENiHBG051458.
KOiK03754.
OMAiFVSPHEV.
PhylomeDBiQ53XC2.

Miscellaneous databases

ChiTaRSiEIF2B2. human.
GenomeRNAii8892.
NextBioi33395.

Gene expression databases

ExpressionAtlasiQ53XC2. baseline and differential.
GenevisibleiQ53XC2. HS.

Family and domain databases

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

Publicationsi

  1. "The sequence of the human genome."
    Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.
    , Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.
    Science 291:1304-1351(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: PlacentaImported.
  3. Genoscope
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: PlacentaImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiQ53XC2_HUMAN
AccessioniPrimary (citable) accession number: Q53XC2
Entry historyi
Integrated into UniProtKB/TrEMBL: May 24, 2005
Last sequence update: May 24, 2005
Last modified: July 22, 2015
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
DisclaimerAny 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.

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.