ID Q6IBU0_HUMAN Unreviewed; 431 AA. AC Q6IBU0; DT 10-MAY-2005, integrated into UniProtKB/TrEMBL. DT 10-MAY-2005, sequence version 1. DT 27-MAR-2024, entry version 83. DE RecName: Full=Eukaryotic translation initiation factor 5 {ECO:0000256|ARBA:ARBA00018059}; GN Name=EIF5 {ECO:0000313|EMBL:CAG32993.1}; 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 {ECO:0000313|EMBL:CAG32993.1}; RN [1] {ECO:0000313|EMBL:CAG32993.1} RP NUCLEOTIDE SEQUENCE. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. CC {ECO:0000256|ARBA:ARBA00010397}. 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; CR456712; CAG32993.1; -; mRNA. DR AlphaFoldDB; Q6IBU0; -. DR PeptideAtlas; Q6IBU0; -. DR ChiTaRS; EIF5; human. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW. DR CDD; cd11561; W2_eIF5; 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. PE 2: Evidence at transcript level; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134}; KW Initiation factor {ECO:0000256|ARBA:ARBA00022540}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}. FT DOMAIN 233..392 FT /note="W2" FT /evidence="ECO:0000259|PROSITE:PS51363" FT REGION 143..216 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 150..171 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 176..191 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 431 AA; 49152 MW; EB7B841431C0D9BC CRC64; MSVNVNRSVS DQFYRYKMPR LIAKVEGKGN GIKTVIVNMV DVAKALNRPP TYPTKYFGCG LGAQTQFDVK NDRYIVNGSH EANKLQDMLD GFIKKFVLCP ECENPETDLH VNPKKQTIGN SCKACGYRGM LDTHHKLCTF ILKNPPENSD SGTGKKEKEK KNRKGKDKEN GSVSSSETPP PPPPPNEINP PPHTMEEEED DDWGEDTTEE AQRRRMDEIS DHAKVLTLSD DLERTIEERV NILFDFVKKK KEEGVIDSSD KEIVAEAERL DVKAMGPLVL TEVLFNEKIR EQIKEYRRHF LRFCHNNKKA QRYLLHGLEC VVAMHQAQLI SKIPHILKEM YDADLLEEEV IISWSEKASK KYVSKELAKE IRVKAEPFIK WLKEAEEESS GGEEEDEDEN IEVVYSKAAS VPKVETVKSD NKDDDIDIDA I //