YIH1_YEAST
ID YIH1_YEAST Reviewed; 258 AA.
AC P25637; D6VR64;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Protein IMPACT homolog;
GN Name=YIH1; OrderedLocusNames=YCR059C; ORFNames=YCR59C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP SIMILARITY.
RX PubMed=8313894; DOI=10.1002/j.1460-2075.1994.tb06287.x;
RA Koonin E.V., Bork P., Sander C.;
RT "Yeast chromosome III: new gene functions.";
RL EMBO J. 13:493-503(1994).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH GCN1 AND ACT1.
RX PubMed=15126500; DOI=10.1074/jbc.m404009200;
RA Sattlegger E., Swanson M.J., Ashcraft E.A., Jennings J.L., Fekete R.A.,
RA Link A.J., Hinnebusch A.G.;
RT "YIH1 is an actin-binding protein that inhibits protein kinase GCN2 and
RT impairs general amino acid control when overexpressed.";
RL J. Biol. Chem. 279:29952-29962(2004).
RN [8]
RP FUNCTION.
RX PubMed=15937339; DOI=10.1074/jbc.m408571200;
RA Pereira C.M., Sattlegger E., Jiang H.-Y., Longo B.M., Jaqueta C.B.,
RA Hinnebusch A.G., Wek R.C., Mello L.E.A.M., Castilho B.A.;
RT "IMPACT, a protein preferentially expressed in the mouse brain, binds GCN1
RT and inhibits GCN2 activation.";
RL J. Biol. Chem. 280:28316-28323(2005).
RN [9]
RP INTERACTION WITH ACT1 AND GCN1, AND MUTAGENESIS OF GLU-87; ASP-90; ASP-102
RP AND GLU-106.
RX PubMed=21239490; DOI=10.1074/jbc.m110.171587;
RA Sattlegger E., Barbosa J.A., Moraes M.C., Martins R.M., Hinnebusch A.G.,
RA Castilho B.A.;
RT "Gcn1 and actin binding to Yih1: implications for activation of the eIF2
RT kinase GCN2.";
RL J. Biol. Chem. 286:10341-10355(2011).
RN [10]
RP INTERACTION WITH RPL39, AND ASSOCIATION WITH RIBOSOMES.
RX PubMed=22404850; DOI=10.1111/j.1742-4658.2012.08553.x;
RA Waller T., Lee S.J., Sattlegger E.;
RT "Evidence that Yih1 resides in a complex with ribosomes.";
RL FEBS J. 279:1761-1776(2012).
RN [11]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-187, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [12]
RP FUNCTION.
RX PubMed=24333428; DOI=10.1016/j.bbrc.2013.12.021;
RA Cambiaghi T.D., Pereira C.M., Shanmugam R., Bolech M., Wek R.C.,
RA Sattlegger E., Castilho B.A.;
RT "Evolutionarily conserved IMPACT impairs various stress responses that
RT require GCN1 for activating the eIF2 kinase GCN2.";
RL Biochem. Biophys. Res. Commun. 443:592-597(2014).
CC -!- FUNCTION: Translational regulator that ensures constant high levels of
CC translation under amino acid starvation. Plays a role as a negative
CC regulator of the GCN2 kinase activity; impairs GCN1-mediated GCN2
CC activation, and hence GCN2-mediated eIF-2-alpha phosphorylation in
CC amino acid-starved cells and subsequent down-regulation of protein
CC synthesis (PubMed:15126500, PubMed:15937339, PubMed:24333428). In
CC normal conditions, it resides in a actin complex and has no activity
CC (PubMed:15126500). {ECO:0000269|PubMed:15126500,
CC ECO:0000269|PubMed:15937339, ECO:0000269|PubMed:24333428}.
CC -!- SUBUNIT: Interacts (via N-terminus) with GCN1 (via C-terminus); this
CC interaction reduces the GCN1-GCN20 complex formation and prevents the
CC interaction of GCN1 with GCN2 protein kinase and GCN2 activation in
CC amino acid-starved cells (PubMed:15126500, PubMed:21239490). Interacts
CC (via C-terminus) with ACT1; this interaction occurs in a GCN1-
CC independent manner (PubMed:15126500, PubMed:21239490). Interacts with
CC RPL39; this interaction occurs in a GCN1-independent manner
CC (PubMed:22404850). Associates (via middle region) with ribosomes; this
CC association occurs in a GCN1-independent manner and persists under
CC amino acid starvation conditions (PubMed:22404850).
CC {ECO:0000269|PubMed:15126500, ECO:0000269|PubMed:21239490,
CC ECO:0000269|PubMed:22404850}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3030 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the IMPACT family. {ECO:0000305}.
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DR EMBL; X59720; CAA42287.1; -; Genomic_DNA.
DR EMBL; AY693113; AAT93132.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07533.1; -; Genomic_DNA.
DR PIR; S19473; S19473.
DR RefSeq; NP_009985.1; NM_001178770.1.
DR PDB; 6BQI; Other; -; A=1-258.
DR PDB; 6U1L; NMR; -; A=1-258.
DR PDB; 6U1O; NMR; -; A=1-258.
DR PDBsum; 6BQI; -.
DR PDBsum; 6U1L; -.
DR PDBsum; 6U1O; -.
DR AlphaFoldDB; P25637; -.
DR SMR; P25637; -.
DR BioGRID; 31036; 94.
DR DIP; DIP-1846N; -.
DR IntAct; P25637; 5.
DR MINT; P25637; -.
DR STRING; 4932.YCR059C; -.
DR iPTMnet; P25637; -.
DR MaxQB; P25637; -.
DR PaxDb; P25637; -.
DR PRIDE; P25637; -.
DR EnsemblFungi; YCR059C_mRNA; YCR059C; YCR059C.
DR GeneID; 850423; -.
DR KEGG; sce:YCR059C; -.
DR SGD; S000000655; YIH1.
DR VEuPathDB; FungiDB:YCR059C; -.
DR eggNOG; KOG3299; Eukaryota.
DR GeneTree; ENSGT00390000017571; -.
DR HOGENOM; CLU_045276_1_0_1; -.
DR InParanoid; P25637; -.
DR OMA; WNVMVVV; -.
DR BioCyc; YEAST:G3O-29364-MON; -.
DR PRO; PR:P25637; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25637; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0003785; F:actin monomer binding; IDA:SGD.
DR GO; GO:1905538; F:polysome binding; IDA:SGD.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IMP:SGD.
DR GO; GO:0043022; F:ribosome binding; IDA:SGD.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IDA:UniProtKB.
DR GO; GO:0140469; P:GCN2-mediated signaling; IMP:UniProtKB.
DR GO; GO:0033673; P:negative regulation of kinase activity; IMP:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IDA:UniProtKB.
DR GO; GO:0006446; P:regulation of translational initiation; IBA:GO_Central.
DR Gene3D; 3.10.110.10; -; 1.
DR Gene3D; 3.30.230.30; -; 1.
DR InterPro; IPR023582; Impact.
DR InterPro; IPR001498; Impact_N.
DR InterPro; IPR036956; Impact_N_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR006575; RWD-domain.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR020569; UPF0029_Impact_CS.
DR PANTHER; PTHR16301; PTHR16301; 1.
DR Pfam; PF05773; RWD; 1.
DR Pfam; PF01205; UPF0029; 1.
DR SMART; SM00591; RWD; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50908; RWD; 1.
DR PROSITE; PS00910; UPF0029; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cytoplasm; Isopeptide bond; Nucleus;
KW Reference proteome; Repressor; Stress response; Translation regulation;
KW Ubl conjugation.
FT CHAIN 1..258
FT /note="Protein IMPACT homolog"
FT /id="PRO_0000207657"
FT DOMAIN 10..114
FT /note="RWD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT CROSSLNK 187
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 87
FT /note="E->A: Slightly increases interaction with GCN1 and
FT ACT1 and does not prevent inhibition of GCN2 activity in
FT amino acid-starved cells; when associated with A-90."
FT MUTAGEN 90
FT /note="D->A: Slightly increases interaction with GCN1 and
FT ACT1 and does not prevent inhibition of GCN2 activity in
FT amino acid-starved cells; when associated with A-87."
FT MUTAGEN 102
FT /note="D->A: Decreases interaction with GCN1, but not with
FT ACT1, and prevents inhibition of GCN2 activity in amino
FT acid-starved cells; when associated with A-106."
FT MUTAGEN 106
FT /note="E->A: Decreases interaction with GCN1, but not with
FT ACT1, and prevents inhibition of GCN2 activity in amino
FT acid-starved cells; when associated with A-102."
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:6U1L"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:6U1L"
FT STRAND 23..36
FT /evidence="ECO:0007829|PDB:6U1L"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:6U1L"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:6U1L"
FT TURN 51..56
FT /evidence="ECO:0007829|PDB:6U1L"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:6U1L"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:6U1L"
FT HELIX 78..89
FT /evidence="ECO:0007829|PDB:6U1L"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:6U1L"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:6U1L"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:6U1L"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:6U1L"
FT STRAND 144..154
FT /evidence="ECO:0007829|PDB:6U1L"
FT HELIX 158..169
FT /evidence="ECO:0007829|PDB:6U1L"
FT TURN 172..176
FT /evidence="ECO:0007829|PDB:6U1L"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:6U1L"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:6U1O"
FT HELIX 204..216
FT /evidence="ECO:0007829|PDB:6U1L"
FT STRAND 221..230
FT /evidence="ECO:0007829|PDB:6U1L"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:6U1L"
FT HELIX 237..253
FT /evidence="ECO:0007829|PDB:6U1L"
SQ SEQUENCE 258 AA; 29017 MW; EC7AC7C747B53A48 CRC64;
MDDDHEQLVE ELEAVEAIYP DLLSKKQEDG SIIVVKVPQH EYMTLQISFP THYPSEEAPN
VIEVGVCTSL AKRDLYDTKY LQHLFQEVMD SVFHRGSVCL FDFLTELDGV LYVEPEEETE
PVQQSDIPTD PFEGWTASDP ITDRGSTFMA FAAHVTSEEQ AFAMLDLLKT DSKMRKANHV
MSAWRIKQDG SAATYQDSDD DGETAAGSRM LHLITIMDVW NVIVVVARWF GGAHIGPDRF
KHINSTAREA VVRAGFDS
