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Q9GZV4 (IF5A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 5A-2

Short name=eIF-5A-2
Short name=eIF-5A2
Alternative name(s):
Eukaryotic initiation factor 5A isoform 2
Gene names
Name:EIF5A2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length153 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Functions as a regulator of apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation By similarity. Ref.7

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Nucleusnuclear pore complex By similarity. Note: Hypusine modification promotes the nuclear export and cytoplasmic localization and there was a dynamic shift in the localization from predominantly cytoplasmic to primarily nuclear under apoptotic inducing conditions By similarity.

Tissue specificity

Expressed in ovarian and colorectal cancer cell lines (at protein level). Highly expressed in testis. Overexpressed in some cancer cells. Ref.2 Ref.8

Post-translational modification

eIF-5A seems to be the only eukaryotic protein to have a hypusine residue which is a post-translational modification of a lysine by the addition of a butylamino group (from spermidine).

Sequence similarities

Belongs to the eIF-5A family.

Ontologies

Keywords
   Biological processmRNA transport
Protein biosynthesis
Protein transport
Translocation
Transport
   Cellular componentCytoplasm
Endoplasmic reticulum
Membrane
Nuclear pore complex
Nucleus
   Coding sequence diversityPolymorphism
   LigandRNA-binding
   Molecular functionElongation factor
   PTMAcetylation
Hypusine
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein metabolic process

Traceable author statement. Source: Reactome

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-lysine modification to peptidyl-hypusine

Traceable author statement. Source: Reactome

polyamine homeostasis

Non-traceable author statement Ref.2. Source: UniProtKB

positive regulation of cell proliferation

Inferred from genetic interaction Ref.7. Source: UniProtKB

positive regulation of translational elongation

Inferred from electronic annotation. Source: InterPro

positive regulation of translational termination

Inferred from electronic annotation. Source: InterPro

post-translational protein modification

Traceable author statement. Source: Reactome

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

spermatogenesis

Non-traceable author statement Ref.2. Source: UniProtKB

translational frameshifting

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear pore

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction Ref.7. Source: UniProtKB

ribosome binding

Inferred from electronic annotation. Source: InterPro

translation elongation factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 153152Eukaryotic translation initiation factor 5A-2
PRO_0000229764

Amino acid modifications

Modified residue21N-acetylalanine Ref.9
Modified residue501Hypusine

Natural variations

Natural variant421E → D. Ref.10
VAR_027943

Sequences

Sequence LengthMass (Da)Tools
Q9GZV4 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 632BFE7F6DB073BD

FASTA15316,793
        10         20         30         40         50         60 
MADEIDFTTG DAGASSTYPM QCSALRKNGF VVLKGRPCKI VEMSTSKTGK HGHAKVHLVG 

        70         80         90        100        110        120 
IDIFTGKKYE DICPSTHNMD VPNIKRNDYQ LICIQDGYLS LLTETGEVRE DLKLPEGELG 

       130        140        150 
KEIEGKYNAG EDVQVSVMCA MSEEYAVAIK PCK 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of a novel candidate oncogene within a frequently amplified region at 3q26 in ovarian cancer."
Guan X.-Y.Y., Sham J.S.T., Tang T.C.-M., Fang Y., Huo K.-K., Yang J.-M.
Cancer Res. 61:3806-3809(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovarian carcinoma.
[2]"Human eIF5A2 on chromosome 3q25-q27 is a phylogenetically conserved vertebrate variant of eukaryotic translation initiation factor 5A with tissue-specific expression."
Jenkins Z.A., Haag P.G., Johansson H.E.
Genomics 71:101-109(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
[3]"Expression of eIF5A genes in human cancer cells."
Clement P.M.J., Jenkins Z.A., Park M.H., Johansson H.E.
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"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].
Tissue: Brain.
[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 (SEP-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.
[7]"Identification and characterization of eukaryotic initiation factor 5A-2."
Clement P.M.J., Henderson C.A., Jenkins Z.A., Smit-McBride Z., Wolff E.C., Hershey J.W., Park M.H., Johansson H.E.
Eur. J. Biochem. 270:4254-4263(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, HYPUSINE AT LYS-50.
[8]"Differential expression of eIF5A-1 and eIF5A-2 in human cancer cells."
Clement P.M.J., Johansson H.E., Wolff E.C., Park M.H.
FEBS J. 273:1102-1114(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[9]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"Screening the SPO11 and EIF5A2 genes in a population of infertile men."
Christensen G.L., Ivanov I.P., Atkins J.F., Mielnik A., Schlegel P.N., Carrell D.T.
Fertil. Steril. 84:758-760(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ASP-42.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF262027 mRNA. Translation: AAF98810.1.
AF293387, AF293386 Genomic DNA. Translation: AAG23176.1.
AY205258 mRNA. Translation: AAO18676.1.
AY205259 mRNA. Translation: AAO18677.1.
AY205260 mRNA. Translation: AAO18678.1.
AY205261 mRNA. Translation: AAO18679.1.
AK311962 mRNA. Translation: BAG34902.1.
CH471052 Genomic DNA. Translation: EAW78501.1.
BC036072 mRNA. Translation: AAH36072.1.
CCDSCCDS3214.1.
RefSeqNP_065123.1. NM_020390.5.
UniGeneHs.164144.

3D structure databases

ProteinModelPortalQ9GZV4.
SMRQ9GZV4. Positions 15-150.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121162. 10 interactions.
IntActQ9GZV4. 8 interactions.
MINTMINT-1453868.
STRING9606.ENSP00000295822.

PTM databases

PhosphoSiteQ9GZV4.

Polymorphism databases

DMDM74762725.

Proteomic databases

MaxQBQ9GZV4.
PaxDbQ9GZV4.
PRIDEQ9GZV4.

Protocols and materials databases

DNASU56648.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295822; ENSP00000295822; ENSG00000163577.
GeneID56648.
KEGGhsa:56648.
UCSCuc003fhd.3. human.

Organism-specific databases

CTD56648.
GeneCardsGC03M170607.
HGNCHGNC:3301. EIF5A2.
HPAHPA029090.
MIM605782. gene.
neXtProtNX_Q9GZV4.
PharmGKBPA27727.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0231.
HOGENOMHOG000106270.
HOVERGENHBG001104.
InParanoidQ9GZV4.
KOK03263.
OMACAMSEEC.
OrthoDBEOG7KSXB7.
PhylomeDBQ9GZV4.
TreeFamTF101534.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ9GZV4.
BgeeQ9GZV4.
CleanExHS_EIF5A2.
GenevestigatorQ9GZV4.

Family and domain databases

Gene3D2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
InterProIPR012340. NA-bd_OB-fold.
IPR014722. Rib_L2_dom2.
IPR019769. Trans_elong_IF5A_hypusine_site.
IPR001884. Transl_elong_IF5A.
IPR020189. Transl_elong_IF5A_C.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERPTHR11673. PTHR11673. 1 hit.
PfamPF01287. eIF-5a. 1 hit.
[Graphical view]
PIRSFPIRSF003025. eIF5A. 1 hit.
SUPFAMSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsTIGR00037. eIF_5A. 1 hit.
PROSITEPS00302. IF5A_HYPUSINE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF5A2. human.
GeneWikiEIF5A2.
GenomeRNAi56648.
NextBio62085.
PROQ9GZV4.
SOURCESearch...

Entry information

Entry nameIF5A2_HUMAN
AccessionPrimary (citable) accession number: Q9GZV4
Secondary accession number(s): B2R4V5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 120 of the entry and version 3 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 3

Human chromosome 3: entries, gene names and cross-references to MIM