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P55010 (IF5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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:
Eukaryotic translation initiation factor 5

Short name=eIF-5
Gene names
Name:EIF5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]).

Sequence similarities

Belongs to the eIF-2-beta/eIF-5 family.

Contains 1 W2 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 431431Eukaryotic translation initiation factor 5
PRO_0000212516

Regions

Domain233 – 392160W2
Nucleotide binding27 – 348GTP Potential
Compositional bias196 – 2027Asp/Glu-rich (highly acidic)
Compositional bias384 – 40219Asp/Glu-rich (highly acidic)
Compositional bias423 – 4297Asp-rich (acidic)

Amino acid modifications

Modified residue101Phosphoserine Ref.8 Ref.11
Modified residue2291Phosphoserine Ref.8
Modified residue3891Phosphoserine Ref.8 Ref.10 Ref.11 Ref.13
Modified residue3901Phosphoserine Ref.8 Ref.10 Ref.11 Ref.13
Modified residue4191Phosphoserine Ref.8 Ref.11

Natural variations

Natural variant4181K → M in a breast cancer sample; somatic mutation. Ref.15
VAR_036467

Experimental info

Sequence conflict601E → G in CAB45711. Ref.2
Sequence conflict2031W → S in AAC50572. Ref.1
Sequence conflict2951K → E in CAB45711. Ref.2
Sequence conflict3111Q → K in AAH32866. Ref.6

Secondary structure

.............................................................. 431
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P55010 [UniParc].

Last modified January 10, 2003. Version 2.
Checksum: C6CCC3A255F9B9BC

FASTA43149,223
        10         20         30         40         50         60 
MSVNVNRSVS DQFYRYKMPR LIAKVEGKGN GIKTVIVNMV DVAKALNRPP TYPTKYFGCE 

        70         80         90        100        110        120 
LGAQTQFDVK NDRYIVNGSH EANKLQDMLD GFIKKFVLCP ECENPETDLH VNPKKQTIGN 

       130        140        150        160        170        180 
SCKACGYRGM LDTHHKLCTF ILKNPPENSD SGTGKKEKEK KNRKGKDKEN GSVSSSETPP 

       190        200        210        220        230        240 
PPPPPNEINP PPHTMEEEED DDWGEDTTEE AQRRRMDEIS DHAKVLTLSD DLERTIEERV 

       250        260        270        280        290        300 
NILFDFVKKK KEEGVIDSSD KEIVAEAERL DVKAMGPLVL TEVLFNEKIR EQIKKYRRHF 

       310        320        330        340        350        360 
LRFCHNNKKA QRYLLHGLEC VVAMHQAQLI SKIPHILKEM YDADLLEEEV IISWSEKASK 

       370        380        390        400        410        420 
KYVSKELAKE IRVKAEPFIK WLKEAEEESS GGEEEDEDEN IEVVYSKAAS VPKVETVKSD 

       430 
NKDDDIDIDA I 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of multiple mRNAs that encode mammalian translation initiation factor 5 (eIF-5)."
Si K., Das K., Maitra U.
J. Biol. Chem. 271:16934-16938(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"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].
Tissue: Testis.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
Tissue: Brain and Uterus.
[7]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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-10; SER-229; SER-389; SER-390 AND SER-419, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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].
[10]"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-389 AND SER-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"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-10; SER-389; SER-390 AND SER-419, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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-389 AND SER-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Solution structure of the EIF-5_EIF-2B domain from human eukaryotic translation initiation factor 5."
RIKEN structural genomics initiative (RSGI)
Submitted (JAN-2008) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-150.
[15]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-418.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U49436 mRNA. Translation: AAC50572.1.
AL080102 mRNA. Translation: CAB45711.1.
AK026933 mRNA. Translation: BAB15593.1.
BX537367 mRNA. Translation: CAD97610.1.
CH471061 Genomic DNA. Translation: EAW81809.1.
BC007728 mRNA. Translation: AAH07728.1.
BC032866 mRNA. Translation: AAH32866.1.
CCDSCCDS9980.1.
PIRT12450.
RefSeqNP_001960.2. NM_001969.4.
NP_892116.2. NM_183004.4.
UniGeneHs.433702.
Hs.741278.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E9HNMR-A1-150[»]
2G2KNMR-A2-170[»]
2IU1X-ray1.80A232-431[»]
ProteinModelPortalP55010.
SMRP55010. Positions 3-150, 232-407.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108298. 39 interactions.
IntActP55010. 5 interactions.
MINTMINT-5004352.
STRING9606.ENSP00000216554.

PTM databases

PhosphoSiteP55010.

Polymorphism databases

DMDM27735202.

Proteomic databases

MaxQBP55010.
PaxDbP55010.
PeptideAtlasP55010.
PRIDEP55010.

Protocols and materials databases

DNASU1983.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216554; ENSP00000216554; ENSG00000100664.
ENST00000392715; ENSP00000376477; ENSG00000100664.
ENST00000558506; ENSP00000453743; ENSG00000100664.
GeneID1983.
KEGGhsa:1983.
UCSCuc001ymq.4. human.

Organism-specific databases

CTD1983.
GeneCardsGC14P103800.
HGNCHGNC:3299. EIF5.
HPACAB004226.
HPA000867.
MIM601710. gene.
neXtProtNX_P55010.
PharmGKBPA27725.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1601.
HOGENOMHOG000214327.
HOVERGENHBG006132.
InParanoidP55010.
KOK03262.
OMAMHQAQLL.
OrthoDBEOG7FV3QF.
PhylomeDBP55010.
TreeFamTF101533.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP55010.
BgeeP55010.
CleanExHS_EIF5.
GenevestigatorP55010.

Family and domain databases

Gene3D1.25.40.180. 1 hit.
3.30.30.50. 1 hit.
InterProIPR016024. ARM-type_fold.
IPR016021. MIF4-like_typ_1/2/3.
IPR002735. Transl_init_fac_IF2/IF5.
IPR016189. Transl_init_fac_IF2/IF5_N.
IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
IPR003307. W2_domain.
[Graphical view]
PfamPF01873. eIF-5_eIF-2B. 1 hit.
PF02020. W2. 1 hit.
[Graphical view]
SMARTSM00653. eIF2B_5. 1 hit.
SM00515. eIF5C. 1 hit.
[Graphical view]
SUPFAMSSF100966. SSF100966. 1 hit.
SSF48371. SSF48371. 1 hit.
SSF75689. SSF75689. 1 hit.
PROSITEPS51363. W2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSeIF5. human.
EvolutionaryTraceP55010.
GeneWikiEIF5.
GenomeRNAi1983.
NextBio8031.
PROP55010.
SOURCESearch...

Entry information

Entry nameIF5_HUMAN
AccessionPrimary (citable) accession number: P55010
Secondary accession number(s): Q53XB3, Q9H5N2, Q9UG48
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 10, 2003
Last modified: July 9, 2014
This is version 141 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 14

Human chromosome 14: entries, gene names and cross-references to MIM