IF5A2_HUMAN
ID IF5A2_HUMAN Reviewed; 153 AA.
AC Q9GZV4; B2R4V5;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Eukaryotic translation initiation factor 5A-2;
DE Short=eIF-5A-2;
DE Short=eIF-5A2;
DE AltName: Full=Eukaryotic initiation factor 5A isoform 2;
GN Name=EIF5A2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovarian carcinoma;
RX PubMed=11325856;
RA Guan X.-Y.Y., Sham J.S.T., Tang T.C.-M., Fang Y., Huo K.-K., Yang J.-M.;
RT "Isolation of a novel candidate oncogene within a frequently amplified
RT region at 3q26 in ovarian cancer.";
RL Cancer Res. 61:3806-3809(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11161802; DOI=10.1006/geno.2000.6418;
RA Jenkins Z.A., Haag P.G., Johansson H.E.;
RT "Human eIF5A2 on chromosome 3q25-q27 is a phylogenetically conserved
RT vertebrate variant of eukaryotic translation initiation factor 5A with
RT tissue-specific expression.";
RL Genomics 71:101-109(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Clement P.M.J., Jenkins Z.A., Park M.H., Johansson H.E.;
RT "Expression of eIF5A genes in human cancer cells.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, AND HYPUSINE AT LYS-50.
RX PubMed=14622290; DOI=10.1046/j.1432-1033.2003.03806.x;
RA Clement P.M.J., Henderson C.A., Jenkins Z.A., Smit-McBride Z., Wolff E.C.,
RA Hershey J.W., Park M.H., Johansson H.E.;
RT "Identification and characterization of eukaryotic initiation factor 5A-
RT 2.";
RL Eur. J. Biochem. 270:4254-4263(2003).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=16519677; DOI=10.1111/j.1742-4658.2006.05135.x;
RA Clement P.M.J., Johansson H.E., Wolff E.C., Park M.H.;
RT "Differential expression of eIF5A-1 and eIF5A-2 in human cancer cells.";
RL FEBS J. 273:1102-1114(2006).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP VARIANT ASP-42.
RX PubMed=16169419; DOI=10.1016/j.fertnstert.2005.03.053;
RA Christensen G.L., Ivanov I.P., Atkins J.F., Mielnik A., Schlegel P.N.,
RA Carrell D.T.;
RT "Screening the SPO11 and EIF5A2 genes in a population of infertile men.";
RL Fertil. Steril. 84:758-760(2005).
CC -!- FUNCTION: mRNA-binding protein involved in translation elongation. Has
CC an important function at the level of mRNA turnover, probably acting
CC downstream of decapping. Critical for the efficient synthesis of
CC peptide bonds between consecutive proline residues. Can resolve
CC ribosomal stalling caused by consecutive prolines during translation
CC (By similarity). Involved in actin dynamics and cell cycle progression,
CC mRNA decay and probably in a pathway involved in stress response and
CC maintenance of cell wall integrity. Functions as a regulator of
CC apoptosis. Mediates effects of polyamines on neuronal process extension
CC and survival. May play an important role in brain development and
CC function, and in skeletal muscle stem cell differentiation (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63241,
CC ECO:0000269|PubMed:14622290}.
CC -!- INTERACTION:
CC Q9GZV4; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-748028, EBI-396137;
CC Q9GZV4; P49366: DHPS; NbExp=7; IntAct=EBI-748028, EBI-741925;
CC Q9GZV4; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-748028, EBI-740897;
CC Q9GZV4; Q04864: REL; NbExp=3; IntAct=EBI-748028, EBI-307352;
CC Q9GZV4; Q04864-2: REL; NbExp=3; IntAct=EBI-748028, EBI-10829018;
CC Q9GZV4; O00560: SDCBP; NbExp=6; IntAct=EBI-748028, EBI-727004;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear
CC pore complex {ECO:0000250}. Note=Hypusine modification promotes the
CC nuclear export and cytoplasmic localization and there was a dynamic
CC shift in the localization from predominantly cytoplasmic to primarily
CC nuclear under apoptotic inducing conditions. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in ovarian and colorectal cancer cell
CC lines (at protein level). Highly expressed in testis. Overexpressed in
CC some cancer cells. {ECO:0000269|PubMed:11161802,
CC ECO:0000269|PubMed:16519677}.
CC -!- PTM: Lys-50 undergoes hypusination, a unique post-translational
CC modification that consists in the addition of a butylamino group from
CC spermidine to lysine side chain and leads to the formation of a
CC hypusine residue. eIF-5As are the only known proteins to undergo this
CC modification, which is essential for their function.
CC {ECO:0000269|PubMed:14622290}.
CC -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
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DR EMBL; AF262027; AAF98810.1; -; mRNA.
DR EMBL; AF293387; AAG23176.1; -; Genomic_DNA.
DR EMBL; AF293386; AAG23176.1; JOINED; Genomic_DNA.
DR EMBL; AY205258; AAO18676.1; -; mRNA.
DR EMBL; AY205259; AAO18677.1; -; mRNA.
DR EMBL; AY205260; AAO18678.1; -; mRNA.
DR EMBL; AY205261; AAO18679.1; -; mRNA.
DR EMBL; AK311962; BAG34902.1; -; mRNA.
DR EMBL; CH471052; EAW78501.1; -; Genomic_DNA.
DR EMBL; BC036072; AAH36072.1; -; mRNA.
DR CCDS; CCDS3214.1; -.
DR RefSeq; NP_065123.1; NM_020390.5.
DR AlphaFoldDB; Q9GZV4; -.
DR SMR; Q9GZV4; -.
DR BioGRID; 121162; 47.
DR IntAct; Q9GZV4; 18.
DR MINT; Q9GZV4; -.
DR STRING; 9606.ENSP00000295822; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q9GZV4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9GZV4; -.
DR PhosphoSitePlus; Q9GZV4; -.
DR SwissPalm; Q9GZV4; -.
DR BioMuta; EIF5A2; -.
DR DMDM; 74762725; -.
DR EPD; Q9GZV4; -.
DR jPOST; Q9GZV4; -.
DR MassIVE; Q9GZV4; -.
DR MaxQB; Q9GZV4; -.
DR PaxDb; Q9GZV4; -.
DR PeptideAtlas; Q9GZV4; -.
DR PRIDE; Q9GZV4; -.
DR ProteomicsDB; 80156; -.
DR Antibodypedia; 33716; 390 antibodies from 30 providers.
DR DNASU; 56648; -.
DR Ensembl; ENST00000295822.7; ENSP00000295822.2; ENSG00000163577.8.
DR GeneID; 56648; -.
DR KEGG; hsa:56648; -.
DR MANE-Select; ENST00000295822.7; ENSP00000295822.2; NM_020390.6; NP_065123.1.
DR UCSC; uc003fhd.4; human.
DR CTD; 56648; -.
DR DisGeNET; 56648; -.
DR GeneCards; EIF5A2; -.
DR HGNC; HGNC:3301; EIF5A2.
DR HPA; ENSG00000163577; Tissue enhanced (testis).
DR MIM; 605782; gene.
DR neXtProt; NX_Q9GZV4; -.
DR OpenTargets; ENSG00000163577; -.
DR PharmGKB; PA27727; -.
DR VEuPathDB; HostDB:ENSG00000163577; -.
DR eggNOG; KOG3271; Eukaryota.
DR GeneTree; ENSGT00390000003738; -.
DR HOGENOM; CLU_102600_0_0_1; -.
DR InParanoid; Q9GZV4; -.
DR OMA; VTYPQQC; -.
DR OrthoDB; 1370513at2759; -.
DR PhylomeDB; Q9GZV4; -.
DR TreeFam; TF101534; -.
DR PathwayCommons; Q9GZV4; -.
DR Reactome; R-HSA-204626; Hypusine synthesis from eIF5A-lysine.
DR SignaLink; Q9GZV4; -.
DR BioGRID-ORCS; 56648; 9 hits in 1076 CRISPR screens.
DR ChiTaRS; EIF5A2; human.
DR GeneWiki; EIF5A2; -.
DR GenomeRNAi; 56648; -.
DR Pharos; Q9GZV4; Tbio.
DR PRO; PR:Q9GZV4; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9GZV4; protein.
DR Bgee; ENSG00000163577; Expressed in endothelial cell and 141 other tissues.
DR ExpressionAtlas; Q9GZV4; baseline and differential.
DR Genevisible; Q9GZV4; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0010509; P:polyamine homeostasis; NAS:UniProtKB.
DR GO; GO:0045901; P:positive regulation of translational elongation; IBA:GO_Central.
DR GO; GO:0045905; P:positive regulation of translational termination; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; NAS:UniProtKB.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR001884; IF5A-like.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR019769; Trans_elong_IF5A_hypusine_site.
DR InterPro; IPR020189; Transl_elong_IF5A_C.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11673; PTHR11673; 1.
DR Pfam; PF01287; eIF-5a; 1.
DR PIRSF; PIRSF003025; eIF5A; 1.
DR SMART; SM01376; eIF-5a; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00037; eIF_5A; 1.
DR PROSITE; PS00302; IF5A_HYPUSINE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Elongation factor; Endoplasmic reticulum; Hypusine;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus;
KW Protein biosynthesis; Protein transport; Reference proteome; RNA-binding;
KW Translocation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..153
FT /note="Eukaryotic translation initiation factor 5A-2"
FT /id="PRO_0000229764"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 50
FT /note="Hypusine"
FT /evidence="ECO:0000269|PubMed:14622290"
FT VARIANT 42
FT /note="E -> D (in dbSNP:rs776545602)"
FT /evidence="ECO:0000269|PubMed:16169419"
FT /id="VAR_027943"
SQ SEQUENCE 153 AA; 16793 MW; 632BFE7F6DB073BD CRC64;
MADEIDFTTG DAGASSTYPM QCSALRKNGF VVLKGRPCKI VEMSTSKTGK HGHAKVHLVG
IDIFTGKKYE DICPSTHNMD VPNIKRNDYQ LICIQDGYLS LLTETGEVRE DLKLPEGELG
KEIEGKYNAG EDVQVSVMCA MSEEYAVAIK PCK
