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O60841 (IF2P_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 5B

Short name=eIF-5B
Alternative name(s):
Translation initiation factor IF-2
Gene names
Name:EIF5B
Synonyms:IF2, KIAA0741
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1220 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Function in general translation initiation by promoting the binding of the formylmethionine-tRNA to ribosomes. Seems to function along with eIF-2 By similarity.

Subunit structure

Interacts with ANXA5 in a calcium and phospholipid-dependent manner By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the IF-2 family.

Sequence caution

The sequence BAA34461.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandGTP-binding
Nucleotide-binding
   Molecular functionInitiation factor
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from electronic annotation. Source: GOC

regulation of translational initiation

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from electronic annotation. Source: InterPro

translation initiation factor activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EIF1AYO146022EBI-928530,EBI-286439
ETS1P149212EBI-928530,EBI-913209

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12201220Eukaryotic translation initiation factor 5B
PRO_0000137294

Regions

Nucleotide binding638 – 6458GTP By similarity
Compositional bias39 – 5012Poly-Lys
Compositional bias94 – 996Poly-Lys
Compositional bias138 – 1425Poly-Asp
Compositional bias313 – 32210Poly-Lys
Compositional bias353 – 3564Poly-Glu
Compositional bias361 – 3644Poly-Glu
Compositional bias491 – 4966Poly-Glu
Compositional bias529 – 56739Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue1071Phosphoserine Ref.8 Ref.13 Ref.14 Ref.18
Modified residue1131Phosphoserine Ref.8 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18
Modified residue1341Phosphotyrosine Ref.13 Ref.16 Ref.18
Modified residue1351Phosphoserine Ref.13 Ref.16 Ref.17 Ref.18
Modified residue1371Phosphoserine Ref.13 Ref.16 Ref.17 Ref.18
Modified residue1641Phosphoserine Ref.8 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18
Modified residue1711Phosphoserine Ref.18
Modified residue1821Phosphoserine Ref.13 Ref.16 Ref.17
Modified residue1831Phosphoserine Ref.13 Ref.16
Modified residue1861Phosphoserine Ref.13 Ref.16 Ref.17
Modified residue1901Phosphoserine Ref.5 Ref.13 Ref.16 Ref.17
Modified residue2141Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11 Ref.16 Ref.17 Ref.18
Modified residue3011Phosphothreonine Ref.13 Ref.17
Modified residue4981Phosphothreonine Ref.18
Modified residue5471Phosphoserine Ref.13
Modified residue5601Phosphoserine Ref.13
Modified residue5881Phosphoserine Ref.13 Ref.17
Modified residue5891Phosphoserine Ref.17
Modified residue5911Phosphoserine Ref.17
Modified residue5951Phosphoserine Ref.13 Ref.17

Natural variations

Natural variant3371S → G.
Corresponds to variant rs10642 [ dbSNP | Ensembl ].
VAR_055954
Natural variant3601R → G.
Corresponds to variant rs3205296 [ dbSNP | Ensembl ].
VAR_055955
Natural variant5221K → T. Ref.1 Ref.2 Ref.19
Corresponds to variant rs7558074 [ dbSNP | Ensembl ].
VAR_060587

Experimental info

Mutagenesis6401V → G: Loss of activity in vivo. Retains full activity in vitro. Ref.2
Mutagenesis7061H → E: Loss of activity; both in vivo and in vitro. Ref.2
Mutagenesis7061H → Q: Loss of activity in vivo. Partial activity in vitro. Ref.2
Mutagenesis7591D → N: Loss of activity; both in vivo and in vitro. Ref.2
Sequence conflict641E → G in BAA34461. Ref.3
Sequence conflict921T → I in CAB44357. Ref.1
Sequence conflict1801I → M in AAD16006. Ref.2
Sequence conflict2561K → R in AAD16006. Ref.2
Sequence conflict5491E → V in AAD16006. Ref.2
Sequence conflict6691G → W in AAD16006. Ref.2
Sequence conflict8941E → K in CAB44357. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O60841 [UniParc].

Last modified November 24, 2009. Version 4.
Checksum: 454C29FB90AA768E

FASTA1,220138,827
        10         20         30         40         50         60 
MGKKQKNKSE DSTKDDIDLD ALAAEIEGAG AAKEQEPQKS KGKKKKEKKK QDFDEDDILK 

        70         80         90        100        110        120 
ELEELSLEAQ GIKADRETVA VKPTENNEEE FTSKDKKKKG QKGKKQSFDD NDSEELEDKD 

       130        140        150        160        170        180 
SKSKKTAKPK VEMYSGSDDD DDFNKLPKKA KGKAQKSNKK WDGSEEDEDN SKKIKERSRI 

       190        200        210        220        230        240 
NSSGESGDES DEFLQSRKGQ KKNQKNKPGP NIESGNEDDD ASFKIKTVAQ KKAEKKERER 

       250        260        270        280        290        300 
KKRDEEKAKL RKLKEKEELE TGKKDQSKQK ESQRKFEEET VKSKVTVDTG VIPASEEKAE 

       310        320        330        340        350        360 
TPTAAEDDNE GDKKKKDKKK KKGEKEEKEK EKKKGPSKAT VKAMQEALAK LKEEEERQKR 

       370        380        390        400        410        420 
EEEERIKRLE ELEAKRKEEE RLEQEKRERK KQKEKERKER LKKEGKLLTK SQREARARAE 

       430        440        450        460        470        480 
ATLKLLQAQG VEVPSKDSLP KKRPIYEDKK RKKIPQQLES KEVSESMELC AAVEVMEQGV 

       490        500        510        520        530        540 
PEKEETPPPV EPEEEEDTED AGLDDWEAMA SDEETEKVEG NKVHIEVKEN PEEEEEEEEE 

       550        560        570        580        590        600 
EEEDEESEEE EEEEGESEGS EGDEEDEKVS DEKDSGKTLD KKPSKEMSSD SEYDSDDDRT 

       610        620        630        640        650        660 
KEERAYDKAK RRIEKRRLEH SKNVNTEKLR APIICVLGHV DTGKTKILDK LRHTHVQDGE 

       670        680        690        700        710        720 
AGGITQQIGA TNVPLEAINE QTKMIKNFDR ENVRIPGMLI IDTPGHESFS NLRNRGSSLC 

       730        740        750        760        770        780 
DIAILVVDIM HGLEPQTIES INLLKSKKCP FIVALNKIDR LYDWKKSPDS DVAATLKKQK 

       790        800        810        820        830        840 
KNTKDEFEER AKAIIVEFAQ QGLNAALFYE NKDPRTFVSL VPTSAHTGDG MGSLIYLLVE 

       850        860        870        880        890        900 
LTQTMLSKRL AHCEELRAQV MEVKALPGMG TTIDVILING RLKEGDTIIV PGVEGPIVTQ 

       910        920        930        940        950        960 
IRGLLLPPPM KELRVKNQYE KHKEVEAAQG VKILGKDLEK TLAGLPLLVA YKEDEIPVLK 

       970        980        990       1000       1010       1020 
DELIHELKQT LNAIKLEEKG VYVQASTLGS LEALLEFLKT SEVPYAGINI GPVHKKDVMK 

      1030       1040       1050       1060       1070       1080 
ASVMLEHDPQ YAVILAFDVR IERDAQEMAD SLGVRIFSAE IIYHLFDAFT KYRQDYKKQK 

      1090       1100       1110       1120       1130       1140 
QEEFKHIAVF PCKIKILPQY IFNSRDPIVM GVTVEAGQVK QGTPMCVPSK NFVDIGIVTS 

      1150       1160       1170       1180       1190       1200 
IEINHKQVDV AKKGQEVCVK IEPIPGESPK MFGRHFEATD ILVSKISRQS IDALKDWFRD 

      1210       1220 
EMQKSDWQLI VELKKVFEII 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of hIF2, a human homologue of bacterial translation initiation factor 2 and its interaction with HIV-1 matrix."
Wilson S.A., Sieiro-Vazquez C., Edwards N.J., Iourin O., Byles E.D., Kotsopoulou E., Adamson C.S., Kingsman S.M., Kingsman A.J., Martin-Rendon E.
Biochem. J. 342:97-103(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-522.
Tissue: Cervix carcinoma.
[2]"Universal conservation in translation initiation revealed by human and archaeal homologs of bacterial translation initiation factor IF2."
Lee J.H., Choi S.K., Roll-Mecak A., Burley S.K., Dever T.E.
Proc. Natl. Acad. Sci. U.S.A. 96:4342-4347(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF VAL-640; HIS-706 AND ASP-759, CHARACTERIZATION, VARIANT THR-522.
Tissue: Testis.
[3]"Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Bienvenut W.V., Waridel P., Quadroni M.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 9-33; 77-94; 106-122; 180-197; 206-224; 285-298; 425-436; 629-644; 653-683; 695-713; 749-757; 766-777; 882-902; 1000-1015; 1044-1055; 1096-1120 AND 1175-1185, PHOSPHORYLATION AT SER-190, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-1220.
Tissue: Testis.
[7]"Characterization of 16 novel human genes showing high similarity to yeast sequences."
Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N., Zimbello R., Lanfranchi G., Valle G.
Yeast 18:69-80(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 833-1220.
[8]"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-107; SER-113; SER-164 AND SER-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Prostate cancer.
[10]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[12]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[13]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-113; TYR-134; SER-135; SER-137; SER-164; SER-182; SER-183; SER-186; SER-190; THR-301; SER-547; SER-560; SER-588 AND SER-595, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-113 AND SER-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[15]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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-113; TYR-134; SER-135; SER-137; SER-164; SER-182; SER-183; SER-186; SER-190 AND SER-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"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-113; SER-135; SER-137; SER-164; SER-182; SER-186; SER-190; SER-214; THR-301; SER-588; SER-589; SER-591 AND SER-595, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-113; TYR-134; SER-135; SER-137; SER-164; SER-171; SER-214 AND THR-498, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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: VARIANT [LARGE SCALE ANALYSIS] THR-522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ006776 mRNA. Translation: CAB44357.1.
AF078035 mRNA. Translation: AAD16006.1.
AC018690 Genomic DNA. Translation: AAY24313.1.
AC079447 Genomic DNA. Translation: AAX93258.1.
AB018284 mRNA. Translation: BAA34461.2. Different initiation.
AL133563 mRNA. Translation: CAB63717.1.
AJ006412 mRNA. Translation: CAA07018.1.
PIRT43483.
RefSeqNP_056988.3. NM_015904.3.
UniGeneHs.158688.

3D structure databases

ProteinModelPortalO60841.
SMRO60841. Positions 600-1215.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115024. 19 interactions.
IntActO60841. 14 interactions.
MINTMINT-3000520.
STRING9606.ENSP00000289371.

PTM databases

PhosphoSiteO60841.

Proteomic databases

PaxDbO60841.
PRIDEO60841.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000289371; ENSP00000289371; ENSG00000158417.
GeneID9669.
KEGGhsa:9669.
UCSCuc002tab.3. human.

Organism-specific databases

CTD9669.
GeneCardsGC02P099953.
H-InvDBHIX0002308.
HGNCHGNC:30793. EIF5B.
HPAHPA034648.
HPA040095.
MIM606086. gene.
neXtProtNX_O60841.
PharmGKBPA134864457.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0532.
HOGENOMHOG000105770.
HOVERGENHBG019036.
InParanoidO60841.
KOK03243.
OMAMMKLGQM.
OrthoDBEOG7034GC.
TreeFamTF101535.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressO60841.
BgeeO60841.
CleanExHS_EIF5B.
GenevestigatorO60841.

Family and domain databases

Gene3D3.40.50.10050. 1 hit.
InterProIPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR023115. TIF_IF2_dom3.
IPR009000. Transl_B-barrel.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view]
PfamPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF11987. IF-2. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SUPFAMSSF50447. SSF50447. 1 hit.
SSF52156. SSF52156. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
ProtoNetSearch...

Other

ChiTaRSEIF5B. human.
GeneWikiEIF5B.
GenomeRNAi9669.
NextBio36307.
PMAP-CutDBO60841.
PROO60841.
SOURCESearch...

Entry information

Entry nameIF2P_HUMAN
AccessionPrimary (citable) accession number: O60841
Secondary accession number(s): O95805 expand/collapse secondary AC list , Q53RV7, Q53SI8, Q9UF81, Q9UMN7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 24, 2009
Last modified: March 19, 2014
This is version 136 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Translation initiation factors

List of translation initiation factor entries

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM