ID IF5_HUMAN Reviewed; 431 AA. AC P55010; Q53XB3; Q9H5N2; Q9UG48; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2003, sequence version 2. DT 04-NOV-2026, entry version 225. DE RecName: Full=Eukaryotic translation initiation factor 5; DE Short=eIF-5; GN Name=EIF5; 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]. RX PubMed=8663286; DOI=10.1074/jbc.271.28.16934; RA Si K., Das K., Maitra U.; RT "Characterization of multiple mRNAs that encode mammalian translation RT initiation factor 5 (eIF-5)."; RL J. Biol. Chem. 271:16934-16938(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Uterus; 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 MUTAGENESIS OF ARG-15. RX PubMed=11166181; DOI=10.1016/s0960-9822(00)00025-7; RA Paulin F.E., Campbell L.E., O'Brien K., Loughlin J., Proud C.G.; RT "Eukaryotic translation initiation factor 5 (eIF5) acts as a classical RT GTPase-activator protein."; RL Curr. Biol. 11:55-59(2001). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-229; SER-389; SER-390 RP AND SER-419, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-390, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-389; SER-390 AND RP SER-419, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP INTERACTION WITH EIF2S2. RX PubMed=21745818; DOI=10.1093/nar/gkr339; RA Singh C.R., Watanabe R., Zhou D., Jennings M.D., Fukao A., Lee B., RA Ikeda Y., Chiorini J.A., Campbell S.G., Ashe M.P., Fujiwara T., Wek R.C., RA Pavitt G.D., Asano K.; RT "Mechanisms of translational regulation by a human eIF5-mimic protein."; RL Nucleic Acids Res. 39:8314-8328(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-390, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [16] RP SUBUNIT, INTERACTION WITH EIF1 AND EIF2S2, AND MUTAGENESIS OF HIS-305; RP ASN-306; GLU-347 AND GLU-348. RX PubMed=22813744; DOI=10.1016/j.celrep.2012.04.007; RA Luna R.E., Arthanari H., Hiraishi H., Nanda J., Martin-Marcos P., RA Markus M.A., Akabayov B., Milbradt A.G., Luna L.E., Seo H.C., Hyberts S.G., RA Fahmy A., Reibarkh M., Miles D., Hagner P.R., O'Day E.M., Yi T., RA Marintchev A., Hinnebusch A.G., Lorsch J.R., Asano K., Wagner G.; RT "The C-terminal domain of eukaryotic initiation factor 5 promotes start RT codon recognition by its dynamic interplay with eIF1 and eIF2beta."; RL Cell Rep. 1:689-702(2012). RN [17] RP FUNCTION, SUBUNIT, AND INTERACTION WITH EIF1A. RX PubMed=24319994; DOI=10.1021/bi4009775; RA Luna R.E., Arthanari H., Hiraishi H., Akabayov B., Tang L., Cox C., RA Markus M.A., Luna L.E., Ikeda Y., Watanabe R., Bedoya E., Yu C., RA Alikhan S., Wagner G., Asano K.; RT "The interaction between eukaryotic initiation factor 1A and eIF5 retains RT eIF1 within scanning preinitiation complexes."; RL Biochemistry 52:9510-9518(2013). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; THR-227; SER-229; RP SER-389; SER-390; SER-410 AND SER-419, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [20] RP INTERACTION WITH FMR1. RX PubMed=24658146; DOI=10.1371/journal.pone.0091465; RA Taha M.S., Nouri K., Milroy L.G., Moll J.M., Herrmann C., Brunsveld L., RA Piekorz R.P., Ahmadian M.R.; RT "Subcellular fractionation and localization studies reveal a direct RT interaction of the fragile X mental retardation protein (FMRP) with RT nucleolin."; RL PLoS ONE 9:E91465-E91465(2014). RN [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-413 AND LYS-418, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [22] RP INTERACTION WITH EIF5B. RX PubMed=30211544; DOI=10.1021/acs.biochem.8b00839; RA Lin K.Y., Nag N., Pestova T.V., Marintchev A.; RT "Human eIF5 and eIF1A compete for binding to eIF5B."; RL Biochemistry 57:5910-5920(2018). RN [23] RP STRUCTURE BY NMR OF 1-150. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the EIF-5_EIF-2B domain from human eukaryotic RT translation initiation factor 5."; RL Submitted (JAN-2008) to the PDB data bank. RN [24] RP VARIANT [LARGE SCALE ANALYSIS] MET-418. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Component of the 43S pre-initiation complex (43S PIC), which CC binds to the mRNA cap-proximal region, scans mRNA 5'-untranslated CC region, and locates the initiation codon (PubMed:11166181, CC PubMed:22813744, PubMed:24319994). In this complex, acts as a GTPase- CC activating protein, by promoting GTP hydrolysis by eIF2G (EIF2S3) CC (PubMed:11166181). During scanning, interacts with both EIF1 (via its CC C-terminal domain (CTD)) and EIF1A (via its NTD) (PubMed:22813744). CC This interaction with EIF1A contributes to the maintenance of EIF1 CC within the open 43S PIC (PubMed:24319994). When start codon is CC recognized, EIF5, via its NTD, induces eIF2G (EIF2S3) to hydrolyze the CC GTP (PubMed:11166181). Start codon recognition also induces a CC conformational change of the PIC to a closed state (PubMed:22813744). CC This change increases the affinity of EIF5-CTD for EIF2-beta (EIF2S2), CC which allows the release, by an indirect mechanism, of EIF1 from the CC PIC (PubMed:22813744). Finally, EIF5 stabilizes the PIC in its closed CC conformation (PubMed:22813744). {ECO:0000269|PubMed:11166181, CC ECO:0000269|PubMed:22813744, ECO:0000269|PubMed:24319994}. CC -!- SUBUNIT: Component of the 43S pre-initiation complex (43S PIC), which CC is composed of the 40S ribosomal subunit, EIF1, eIF1A (EIF1AX), eIF3 CC complex, EIF5 and eIF2-GTP-initiator tRNA complex (eIF2 ternary CC complex). Interacts with eIF1A (EIF1AX) during scanning CC (PubMed:24319994). Interacts through its C-terminal domain (CTD) with CC EIF1 or with eIF2-beta (EIF2S2) (mutually exclusive) through a common CC binding site (PubMed:21745818, PubMed:22813744). Interacts through its CC C-terminal domain (CTD) with the CTD of EIF5B (PubMed:30211544). CC Interacts with FMR1 isoform 6; this interaction occurs in a RNA- CC dependent manner (PubMed:24658146). {ECO:0000269|PubMed:21745818, CC ECO:0000269|PubMed:22813744, ECO:0000269|PubMed:24319994, CC ECO:0000269|PubMed:24658146}. CC -!- INTERACTION: CC P55010; Q9UNI6: DUSP12; NbExp=6; IntAct=EBI-286450, EBI-715161; CC P55010; P42858: HTT; NbExp=3; IntAct=EBI-286450, EBI-466029; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U49436; AAC50572.1; -; mRNA. DR EMBL; AL080102; CAB45711.1; -; mRNA. DR EMBL; AK026933; BAB15593.1; -; mRNA. DR EMBL; BX537367; CAD97610.1; -; mRNA. DR EMBL; CH471061; EAW81809.1; -; Genomic_DNA. DR EMBL; BC007728; AAH07728.1; -; mRNA. DR EMBL; BC032866; AAH32866.1; -; mRNA. DR CCDS; CCDS9980.1; -. DR PIR; T12450; T12450. DR RefSeq; NP_001960.2; NM_001969.5. DR RefSeq; NP_892116.2; NM_183004.5. DR PDB; 2E9H; NMR; -; A=1-150. DR PDB; 2G2K; NMR; -; A=2-170. DR PDB; 2IU1; X-ray; 1.80 A; A=232-431. DR PDB; 8OZ0; EM; 3.50 A; H=1-431. DR PDB; 8PJ2; EM; 3.40 A; z=1-430. DR PDB; 8PJ3; EM; 3.70 A; z=1-430. DR BMRB; P55010; -. DR SMR; P55010; -. DR BioGRID; 108298; 238. DR IntAct; P55010; 118. DR STRING; 9606.ENSP00000216554; -. DR NDEx; IQUERY-CP-EIF5; 4 NDEx IQuery Curated Pathways. DR GlyCosmos; P55010; 2 sites, 2 glycans. DR GlyGen; P55010; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR iPTMnet; P55010; -. DR PhosphoSitePlus; P55010; -. DR SwissPalm; P55010; -. DR MetOSite; P55010; -. DR BioMuta; EIF5; -. DR DMDM; 27735202; -. DR CPTAC; CPTAC-357; -. DR CPTAC; CPTAC-358; -. DR PaxDb; 9606-ENSP00000216554; -. DR PeptideAtlas; P55010; -. DR ProteomicsDB; 56756; -. DR Pumba; P55010; -. DR TopDownProteomics; P55010; -. DR jPOST; P55010; -. DR MassIVE; P55010; -. DR DNASU; 1983; -. DR Ensembl; ENST00000216554.8; ENSP00000216554.3; ENSG00000100664.11. DR Ensembl; ENST00000392715.6; ENSP00000376477.2; ENSG00000100664.11. DR Ensembl; ENST00000558506.1; ENSP00000453743.1; ENSG00000100664.11. DR GeneID; 1983; -. DR KEGG; hsa:1983; -. DR MANE-Select; ENST00000216554.8; ENSP00000216554.3; NM_001969.5; NP_001960.2. DR UCSC; uc001ymq.5; human. DR CTD; 1983; -. DR DisGeNET; 1983; -. DR VEuPathDB; HostDB:ENSG00000100664; -. DR GeneCards; EIF5; -. DR HGNC; HGNC:3299; EIF5. DR AGR; HGNC:3299; -. DR HPA; ENSG00000100664; Low tissue specificity. DR MIM; 601710; gene. DR OpenTargets; ENSG00000100664; -. DR ClinPGx; PA27725; -. DR eggNOG; KOG2767; Eukaryota. DR GeneTree; ENSGT00390000016478; -. DR HOGENOM; CLU_026663_1_0_1; -. DR InParanoid; P55010; -. DR OMA; AACGYQG; -. DR OrthoDB; 10250831at2759; -. DR PhylomeDB; P55010; -. DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition. DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit. DR SignaLink; P55010; -. DR SIGNOR; P55010; -. DR ChiTaRS; EIF5; human. DR EvolutionaryTrace; P55010; -. DR Agora; ENSG00000100664; -. DR GeneWiki; EIF5; -. DR GenomeRNAi; 1983; -. DR PRO; PR:P55010; -. DR Bgee; ENSG00000100664; Expressed in postcentral gyrus and 220 other cell types or tissues. DR ExpressionAtlas; P55010; baseline and differential. DR CDD; cd11561; W2_eIF5; 1. DR FunFam; 2.20.25.350:FF:000002; Eukaryotic translation initiation factor 5; 1. DR FunFam; 3.30.30.170:FF:000002; Eukaryotic translation initiation factor 5; 1. DR FunFam; 1.25.40.180:FF:000018; eukaryotic translation initiation factor 5; 1. DR Gene3D; 1.25.40.180; -; 1. DR Gene3D; 2.20.25.350; -; 1. DR Gene3D; 3.30.30.170; -; 1. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR045196; IF2/IF5. DR InterPro; IPR002735; Transl_init_fac_IF2/IF5_dom. DR InterPro; IPR016189; Transl_init_fac_IF2/IF5_N. DR InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd. DR InterPro; IPR003307; W2_domain. DR PANTHER; PTHR23001; EUKARYOTIC TRANSLATION INITIATION FACTOR; 1. DR PANTHER; PTHR23001:SF7; EUKARYOTIC TRANSLATION INITIATION FACTOR 5; 1. DR Pfam; PF01873; eIF-5_eIF-2B; 1. DR Pfam; PF02020; W2; 1. DR SMART; SM00653; eIF2B_5; 1. DR SMART; SM00515; eIF5C; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF100966; Translation initiation factor 2 beta, aIF2beta, N-terminal domain; 1. DR SUPFAM; SSF75689; Zinc-binding domain of translation initiation factor 2 beta; 1. DR PROSITE; PS51363; W2; 1. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0071074; F:eukaryotic initiation factor eIF2 binding; IBA:GO_Central. DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central. DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central. DR GO; GO:0006446; P:regulation of translational initiation; IDA:CACAO. DR GO; GO:0042255; P:ribosome assembly; IDA:UniProtKB. DR Proteomes; UP000005640; Chromosome 14. DR PathwayCommons; P55010; -. DR Pharos; P55010; Tbio. DR Antibodypedia; 47; 321 antibodies from 37 providers. DR RNAct; P55010; protein. DR BioGRID-ORCS; 1983; 783 hits in 1123 CRISPR screens. DR AlphaFoldDB; P55010; -. DR EMDB; EMD-17297; -. DR EMDB; EMD-17697; -. DR EMDB; EMD-17698; -. DR CD-CODE; DEE660B4; Stress granule. DR FunCoup; P55010; 3102. DR PAN-GO; P55010; 5 GO annotations based on evolutionary models. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; GTP-binding; GTPase activation; Initiation factor; KW Isopeptide bond; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; KW Proteomics identification; Reference proteome; Ubl conjugation. FT CHAIN 1..431 FT /note="Eukaryotic translation initiation factor 5" FT /id="PRO_0000212516" FT DOMAIN 233..392 FT /note="W2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695" FT REGION 143..216 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 153..170 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 178..193 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 196..209 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 27..34 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255" FT SITE 15 FT /note="Arginine finger" FT /evidence="ECO:0000269|PubMed:11166181" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 227 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 229 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 389 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 390 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 410 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 419 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT CROSSLNK 413 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 418 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 418 FT /note="K -> M (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036467" FT MUTAGEN 15 FT /note="R->M: Loss of ability to promote hydrolysis of GTP." FT /evidence="ECO:0000269|PubMed:11166181" FT MUTAGEN 305..306 FT /note="HN->DD: Disruption of binding to eIF1 and EIF2-beta FT (EIF2S2); when associated with 347-K-K-348." FT /evidence="ECO:0000269|PubMed:22813744" FT MUTAGEN 347..348 FT /note="EE->KK: Disruption of binding to eIF1 and EIF2-beta FT (EIF2S2); when associated with 305-D-D-306." FT /evidence="ECO:0000269|PubMed:22813744" FT CONFLICT 60 FT /note="E -> G (in Ref. 2; CAB45711)" FT /evidence="ECO:0000305" FT CONFLICT 203 FT /note="W -> S (in Ref. 1; AAC50572)" FT /evidence="ECO:0000305" FT CONFLICT 295 FT /note="K -> E (in Ref. 2; CAB45711)" FT /evidence="ECO:0000305" FT CONFLICT 311 FT /note="Q -> K (in Ref. 6; AAH32866)" FT /evidence="ECO:0000305" FT STRAND 2..6 FT /evidence="ECO:0007829|PDB:8PJ2" FT STRAND 17..19 FT /evidence="ECO:0007829|PDB:8PJ2" FT STRAND 23..25 FT /evidence="ECO:0007829|PDB:2E9H" FT STRAND 29..31 FT /evidence="ECO:0007829|PDB:8PJ2" FT STRAND 33..37 FT /evidence="ECO:0007829|PDB:8PJ2" FT HELIX 39..46 FT /evidence="ECO:0007829|PDB:8PJ2" FT HELIX 51..61 FT /evidence="ECO:0007829|PDB:8PJ2" FT STRAND 65..68 FT /evidence="ECO:0007829|PDB:8PJ2" FT TURN 69..72 FT /evidence="ECO:0007829|PDB:8PJ2" FT STRAND 73..78 FT /evidence="ECO:0007829|PDB:8PJ2" FT HELIX 82..92 FT /evidence="ECO:0007829|PDB:8PJ2" FT HELIX 93..97 FT /evidence="ECO:0007829|PDB:8PJ2" FT TURN 100..102 FT /evidence="ECO:0007829|PDB:8PJ2" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:2G2K" FT STRAND 108..112 FT /evidence="ECO:0007829|PDB:8PJ2" FT TURN 113..116 FT /evidence="ECO:0007829|PDB:8PJ2" FT STRAND 117..121 FT /evidence="ECO:0007829|PDB:8PJ2" FT STRAND 123..125 FT /evidence="ECO:0007829|PDB:8PJ2" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:8PJ2" FT STRAND 133..136 FT /evidence="ECO:0007829|PDB:2G2K" FT HELIX 137..143 FT /evidence="ECO:0007829|PDB:8PJ2" FT HELIX 145..148 FT /evidence="ECO:0007829|PDB:2E9H" FT HELIX 236..253 FT /evidence="ECO:0007829|PDB:2IU1" FT HELIX 256..258 FT /evidence="ECO:0007829|PDB:2IU1" FT HELIX 260..269 FT /evidence="ECO:0007829|PDB:2IU1" FT HELIX 273..275 FT /evidence="ECO:0007829|PDB:2IU1" FT HELIX 276..284 FT /evidence="ECO:0007829|PDB:2IU1" FT HELIX 289..295 FT /evidence="ECO:0007829|PDB:2IU1" FT HELIX 297..304 FT /evidence="ECO:0007829|PDB:2IU1" FT HELIX 308..324 FT /evidence="ECO:0007829|PDB:2IU1" FT HELIX 326..329 FT /evidence="ECO:0007829|PDB:2IU1" FT HELIX 330..332 FT /evidence="ECO:0007829|PDB:2IU1" FT HELIX 333..342 FT /evidence="ECO:0007829|PDB:2IU1" FT HELIX 348..356 FT /evidence="ECO:0007829|PDB:2IU1" FT STRAND 361..363 FT /evidence="ECO:0007829|PDB:2IU1" FT HELIX 365..383 FT /evidence="ECO:0007829|PDB:2IU1" FT HELIX 400..408 FT /evidence="ECO:0007829|PDB:2IU1" SQ SEQUENCE 431 AA; 49223 MW; C6CCC3A255F9B9BC CRC64; MSVNVNRSVS DQFYRYKMPR LIAKVEGKGN GIKTVIVNMV DVAKALNRPP TYPTKYFGCE LGAQTQFDVK NDRYIVNGSH EANKLQDMLD GFIKKFVLCP ECENPETDLH VNPKKQTIGN SCKACGYRGM LDTHHKLCTF ILKNPPENSD SGTGKKEKEK KNRKGKDKEN GSVSSSETPP PPPPPNEINP PPHTMEEEED DDWGEDTTEE AQRRRMDEIS DHAKVLTLSD DLERTIEERV NILFDFVKKK KEEGVIDSSD KEIVAEAERL DVKAMGPLVL TEVLFNEKIR EQIKKYRRHF LRFCHNNKKA QRYLLHGLEC VVAMHQAQLI SKIPHILKEM YDADLLEEEV IISWSEKASK KYVSKELAKE IRVKAEPFIK WLKEAEEESS GGEEEDEDEN IEVVYSKAAS VPKVETVKSD NKDDDIDIDA I //