GIR2_YEAST
ID GIR2_YEAST Reviewed; 265 AA.
AC Q03768; D6VSD4;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein GIR2;
DE AltName: Full=DRG family-regulatory protein 2;
DE AltName: Full=Genetically interacts with ribosomal genes protein 2;
GN Name=GIR2; Synonyms=DFRP2; OrderedLocusNames=YDR152W; ORFNames=YD8358.08;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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 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 [5]
RP IDENTIFICATION.
RX PubMed=15676025; DOI=10.1111/j.1365-2443.2005.00825.x;
RA Ishikawa K., Azuma S., Ikawa S., Semba K., Inoue J.;
RT "Identification of DRG family regulatory proteins (DFRPs): specific
RT regulation of DRG1 and DRG2.";
RL Genes Cells 10:139-150(2005).
RN [6]
RP FUNCTION, INTERACTION WITH GCN1 AND RBG1, AND ASSOCIATION WITH RIBOSOMES.
RX PubMed=19448108; DOI=10.1128/ec.00356-08;
RA Wout P.K., Sattlegger E., Sullivan S.M., Maddock J.R.;
RT "Saccharomyces cerevisiae Rbg1 protein and its binding partner Gir2
RT interact on polyribosomes with Gcn1.";
RL Eukaryot. Cell 8:1061-1071(2009).
CC -!- FUNCTION: Acts as a negative regulator of the GCN2 kinase activity by
CC disrupting the GCN1-GCN2 interaction in amino acid-starved cells
CC (PubMed:19448108). {ECO:0000269|PubMed:19448108}.
CC -!- SUBUNIT: Interacts with GCN1; this interaction prevents the interaction
CC of GCN1 with GCN2 protein kinase and GCN2 activation in amino acid-
CC starved cells (PubMed:19448108). Interacts with RBG1 (PubMed:19448108).
CC Associates with ribosomes; the association occurs in a GCN1-dependent
CC manner (PubMed:19448108). {ECO:0000269|PubMed:19448108}.
CC -!- INTERACTION:
CC Q03768; P53295: RBG2; NbExp=5; IntAct=EBI-7618, EBI-23421;
CC -!- MISCELLANEOUS: Present with 10300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RWDD1/GIR2 family. {ECO:0000305}.
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DR EMBL; Z50046; CAA90374.1; -; Genomic_DNA.
DR EMBL; AY557681; AAS56007.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11994.1; -; Genomic_DNA.
DR PIR; S57978; S57978.
DR RefSeq; NP_010436.3; NM_001180459.3.
DR AlphaFoldDB; Q03768; -.
DR SMR; Q03768; -.
DR BioGRID; 32205; 58.
DR DIP; DIP-1751N; -.
DR IntAct; Q03768; 10.
DR MINT; Q03768; -.
DR STRING; 4932.YDR152W; -.
DR iPTMnet; Q03768; -.
DR MaxQB; Q03768; -.
DR PaxDb; Q03768; -.
DR PRIDE; Q03768; -.
DR EnsemblFungi; YDR152W_mRNA; YDR152W; YDR152W.
DR GeneID; 851730; -.
DR KEGG; sce:YDR152W; -.
DR SGD; S000002559; GIR2.
DR VEuPathDB; FungiDB:YDR152W; -.
DR eggNOG; KOG4018; Eukaryota.
DR GeneTree; ENSGT00390000009168; -.
DR HOGENOM; CLU_084528_0_0_1; -.
DR InParanoid; Q03768; -.
DR OMA; IYCGELE; -.
DR BioCyc; YEAST:G3O-29746-MON; -.
DR PRO; PR:Q03768; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03768; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005844; C:polysome; IDA:SGD.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IDA:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; IGI:SGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IDA:UniProtKB.
DR GO; GO:1903833; P:positive regulation of cellular response to amino acid starvation; IMP:SGD.
DR DisProt; DP00163; -.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR040213; GIR2-like.
DR InterPro; IPR006575; RWD-domain.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR12292; PTHR12292; 1.
DR Pfam; PF05773; RWD; 1.
DR SMART; SM00591; RWD; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50908; RWD; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Repressor; Stress response.
FT CHAIN 1..265
FT /note="Protein GIR2"
FT /id="PRO_0000087495"
FT DOMAIN 9..159
FT /note="RWD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
SQ SEQUENCE 265 AA; 31031 MW; CE09A067388638ED CRC64;
MDYKEEQKQE LEVLESIYPD ELRIINDEYP KIKFEVAIKL ELDTGDSTSV LTKEHTIIAE
FKLPENYPDE PCLISLEAQE VALNDNEEDN EEDEDEVEYD DHGNKVLKKF ENLPDLISFK
GYLPELTVQL ESQIETDMLL GMQMCFALIS SIKERCEQWY SEQLNKLEKQ YELEAQEREK
KEQAKFHGTK VTRESYLEWR SKFRQELKLD ERDQVRRMKA HHGKLTGKQM FEQGVVGTGD
EYMEEDDASV DDVAKGLAKT EIANQ
