EIF1_HUMAN
ID EIF1_HUMAN Reviewed; 113 AA.
AC P41567; Q9UNQ9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Eukaryotic translation initiation factor 1;
DE Short=eIF1;
DE AltName: Full=A121;
DE AltName: Full=Protein translation factor SUI1 homolog;
DE AltName: Full=Sui1iso1;
GN Name=EIF1; Synonyms=SUI1;
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=7904817; DOI=10.1006/bbrc.1994.1040;
RA Fields C.A., Adams M.D.;
RT "Expressed sequence tags identify a human isolog of the suil translation
RT initiation factor.";
RL Biochem. Biophys. Res. Commun. 198:288-291(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Singh S.K., Murray S.F., Chin L.S.;
RT "Okadaic acid-responsive genes in malignant glioma cells identified by mRNA
RT differential display.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10347211; DOI=10.1074/jbc.274.23.16487;
RA Sheikh M.S., Fernandez-Salas E., Yu M., Hussain A., Dinman J.D.,
RA Peltz S.W., Huang Y., Fornace A.J. Jr.;
RT "Cloning and characterization of a human genotoxic and endoplasmic
RT reticulum stress-inducible cDNA that encodes translation initiation factor
RT 1 (eIF1(A121/SUI1)).";
RL J. Biol. Chem. 274:16487-16493(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Lung;
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 [5]
RP INTERACTION WITH RENT2.
RX PubMed=11073994; DOI=10.1128/mcb.20.23.8944-8957.2000;
RA Mendell J.T., Medghalchi S.M., Lake R.G., Noensie E.N., Dietz H.C.;
RT "Novel Upf2p orthologues suggest a functional link between translation
RT initiation and nonsense surveillance complexes.";
RL Mol. Cell. Biol. 20:8944-8957(2000).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-9, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-9, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [10]
RP STRUCTURE BY NMR.
RX PubMed=10228174; DOI=10.1093/emboj/18.9.2631;
RA Fletcher C.M., Pestova T.V., Hellen C.U., Wagner G.;
RT "Structure and interactions of the translation initiation factor eIF1.";
RL EMBO J. 18:2631-2637(1999).
CC -!- FUNCTION: Necessary for scanning and involved in initiation site
CC selection. Promotes the assembly of 48S ribosomal complexes at the
CC authentic initiation codon of a conventional capped mRNA.
CC -!- SUBUNIT: Interacts with RENT2. {ECO:0000269|PubMed:11073994}.
CC -!- INTERACTION:
CC P41567; Q14152: EIF3A; NbExp=2; IntAct=EBI-726200, EBI-366617;
CC P41567; Q99613: EIF3C; NbExp=2; IntAct=EBI-726200, EBI-353741;
CC -!- SIMILARITY: Belongs to the SUI1 family. {ECO:0000305}.
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DR EMBL; L26247; AAA60602.1; -; mRNA.
DR EMBL; AF083441; AAD52028.1; -; mRNA.
DR EMBL; AF100737; AAD19900.1; -; mRNA.
DR EMBL; BC005118; AAH05118.1; -; mRNA.
DR EMBL; BC008710; AAH08710.1; -; mRNA.
DR CCDS; CCDS11403.1; -.
DR PIR; JC2042; JC2042.
DR RefSeq; NP_005792.1; NM_005801.3.
DR PDB; 2IF1; NMR; -; A=1-113.
DR PDB; 4KZX; X-ray; 7.81 A; l=1-113.
DR PDB; 4KZY; X-ray; 7.01 A; l=1-113.
DR PDB; 6YBW; EM; 3.10 A; p=1-113.
DR PDB; 6ZMW; EM; 3.70 A; p=1-113.
DR PDB; 6ZP4; EM; 2.90 A; Z=1-113.
DR PDB; 6ZVJ; EM; 3.80 A; N=23-113.
DR PDB; 7A09; EM; 3.50 A; Z=1-113.
DR PDBsum; 2IF1; -.
DR PDBsum; 4KZX; -.
DR PDBsum; 4KZY; -.
DR PDBsum; 6YBW; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 7A09; -.
DR AlphaFoldDB; P41567; -.
DR BMRB; P41567; -.
DR SMR; P41567; -.
DR BioGRID; 115504; 25.
DR DIP; DIP-50783N; -.
DR IntAct; P41567; 10.
DR MINT; P41567; -.
DR STRING; 9606.ENSP00000419449; -.
DR GlyGen; P41567; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P41567; -.
DR PhosphoSitePlus; P41567; -.
DR BioMuta; EIF1; -.
DR EPD; P41567; -.
DR jPOST; P41567; -.
DR MassIVE; P41567; -.
DR PaxDb; P41567; -.
DR PeptideAtlas; P41567; -.
DR PRIDE; P41567; -.
DR ProteomicsDB; 55464; -.
DR TopDownProteomics; P41567; -.
DR Antibodypedia; 28894; 215 antibodies from 29 providers.
DR DNASU; 10209; -.
DR Ensembl; ENST00000469257.2; ENSP00000419449.1; ENSG00000173812.11.
DR GeneID; 10209; -.
DR KEGG; hsa:10209; -.
DR MANE-Select; ENST00000469257.2; ENSP00000419449.1; NM_005801.4; NP_005792.1.
DR CTD; 10209; -.
DR DisGeNET; 10209; -.
DR GeneCards; EIF1; -.
DR HGNC; HGNC:3249; EIF1.
DR HPA; ENSG00000173812; Low tissue specificity.
DR neXtProt; NX_P41567; -.
DR OpenTargets; ENSG00000173812; -.
DR PharmGKB; PA27683; -.
DR VEuPathDB; HostDB:ENSG00000173812; -.
DR eggNOG; KOG1770; Eukaryota.
DR GeneTree; ENSGT00390000015789; -.
DR HOGENOM; CLU_082805_3_0_1; -.
DR InParanoid; P41567; -.
DR OMA; VENHIHI; -.
DR OrthoDB; 1493146at2759; -.
DR PhylomeDB; P41567; -.
DR TreeFam; TF314417; -.
DR PathwayCommons; P41567; -.
DR SignaLink; P41567; -.
DR BioGRID-ORCS; 10209; 701 hits in 1084 CRISPR screens.
DR ChiTaRS; EIF1; human.
DR EvolutionaryTrace; P41567; -.
DR GeneWiki; EIF1; -.
DR GenomeRNAi; 10209; -.
DR Pharos; P41567; Tbio.
DR PRO; PR:P41567; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P41567; protein.
DR Bgee; ENSG00000173812; Expressed in sperm and 205 other tissues.
DR ExpressionAtlas; P41567; baseline and differential.
DR Genevisible; P41567; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008135; F:translation factor activity, RNA binding; TAS:ProtInc.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0006446; P:regulation of translational initiation; IDA:CACAO.
DR CDD; cd11566; eIF1_SUI1; 1.
DR DisProt; DP00910; -.
DR InterPro; IPR001950; SUI1.
DR InterPro; IPR036877; SUI1_dom_sf.
DR InterPro; IPR005874; SUI1_euk.
DR Pfam; PF01253; SUI1; 1.
DR PIRSF; PIRSF004499; SUI1_euk; 1.
DR SUPFAM; SSF55159; SSF55159; 1.
DR TIGRFAMs; TIGR01160; SUI1_MOF2; 1.
DR PROSITE; PS50296; SUI1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT CHAIN 2..113
FT /note="Eukaryotic translation initiation factor 1"
FT /id="PRO_0000130554"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 59
FT /note="L -> P (in dbSNP:rs3390)"
FT /id="VAR_052505"
FT VARIANT 90
FT /note="R -> G (in dbSNP:rs3387)"
FT /id="VAR_052506"
FT CONFLICT 31
FT /note="I -> V (in Ref. 3; AAD19900)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="A -> P (in Ref. 3; AAD19900)"
FT /evidence="ECO:0000305"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:6YBW"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:6YBW"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:6YBW"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:6YBW"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:6YBW"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:6YBW"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:6YBW"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:6YBW"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:6YBW"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:6YBW"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:6YBW"
SQ SEQUENCE 113 AA; 12732 MW; A7BC7F9B53FFEB2C CRC64;
MSAIQNLHSF DPFADASKGD DLLPAGTEDY IHIRIQQRNG RKTLTTVQGI ADDYDKKKLV
KAFKKKFACN GTVIEHPEYG EVIQLQGDQR KNICQFLVEI GLAKDDQLKV HGF
