NGR1_YEAST
ID NGR1_YEAST Reviewed; 672 AA.
AC P32831; D6VQK8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Negative growth regulatory protein NGR1;
DE AltName: Full=RNA-binding protein RBP1;
GN Name=NGR1; Synonyms=RBP1; OrderedLocusNames=YBR212W; ORFNames=YBR1459;
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 [GENOMIC DNA].
RX PubMed=8325883; DOI=10.1016/s0021-9258(18)82440-1;
RA Lee F.-J.S., Moss J.;
RT "An RNA-binding protein gene (RBP1) of Saccharomyces cerevisiae encodes a
RT putative glucose-repressible protein containing two RNA recognition
RT motifs.";
RL J. Biol. Chem. 268:15080-15087(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, ACETYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS] (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May be an RNA-binding protein involved in control of an RNA
CC processing pathway that influences the regulation of cell growth in
CC early log phase. Can bind to RNA and single-stranded DNA but not
CC double-stranded DNA.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=P32831-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P32831-2; Sequence=VSP_058122;
CC -!- MISCELLANEOUS: Present with 1540 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z14097; CAA78478.1; -; Genomic_DNA.
DR EMBL; Z36081; CAA85176.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07328.1; -; Genomic_DNA.
DR PIR; S46086; S46086.
DR RefSeq; NP_009771.3; NM_001178560.3. [P32831-1]
DR AlphaFoldDB; P32831; -.
DR BioGRID; 32909; 197.
DR DIP; DIP-5160N; -.
DR IntAct; P32831; 4.
DR MINT; P32831; -.
DR STRING; 4932.YBR212W; -.
DR iPTMnet; P32831; -.
DR MaxQB; P32831; -.
DR PaxDb; P32831; -.
DR PRIDE; P32831; -.
DR EnsemblFungi; YBR212W_mRNA; YBR212W; YBR212W. [P32831-1]
DR GeneID; 852513; -.
DR KEGG; sce:YBR212W; -.
DR SGD; S000000416; NGR1.
DR VEuPathDB; FungiDB:YBR212W; -.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_016304_5_0_1; -.
DR InParanoid; P32831; -.
DR OMA; EMNGIWC; -.
DR BioCyc; YEAST:G3O-29149-MON; -.
DR PRO; PR:P32831; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P32831; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:SGD.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:SGD.
DR GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding.
FT CHAIN 1..672
FT /note="Negative growth regulatory protein NGR1"
FT /id="PRO_0000081660"
FT DOMAIN 36..159
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 192..271
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 360..432
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:19779198"
FT VAR_SEQ 1
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_058122"
FT CONFLICT 322
FT /note="P -> S (in Ref. 1; CAA78478)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="T -> N (in Ref. 1; CAA78478)"
FT /evidence="ECO:0000305"
FT CONFLICT 585
FT /note="P -> S (in Ref. 1; CAA78478)"
FT /evidence="ECO:0000305"
FT INIT_MET P32831-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES P32831-2:2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 672 AA; 75024 MW; 12F64EC4C5716750 CRC64;
MMSNVANASQ RQENPYIIPL PPSSTVETST EPPRTLWMGD LDPSFDEATI EEIWSKLDKK
VIVKLIRAKK NLLIPCSSTS SSNNNTSEEN AENQQSASNS TDQLDNSQMI NINGISFIDP
STTQLHHAGY CFVEFETQKD AKFALSLNAT PLPNFYSPTT NSQTNPTFKR TFRLNWASGA
TLQSSIPSTP EFSLFVGDLS PTATEADLLS LFQTRFKSVK TVRVMTDPLT GSSRCFGFVR
FGDEDERRRA LIEMSGKWFQ GRALRVAYAT PRNNMMLQLQ EQQQQQQQLQ QQHQQLDQED
NNGPLLIKTA NNLIQNNSNM LPLNALHNAP PMHLNEGGIS NMRVNDSLPS NTYNTDPTNT
TVFVGGLVPK TTEFQLRSLF KPFGPILNVR IPNGKNCGFV KFEKRIDAEA SIQGLQGFIV
GGSPIRLSWG RPSSSNAKTN STIMGASQYM SSNGLRAPSA ASSVDNSKQI LEQYAEDKRR
LFLHQQQQQQ QQQQQDGNFS MEQMAHNNYY NYNNYDYHRN KNGSHSDLVN LQRSNVPYMQ
EDGALYPHQY SSPSYSLHPT GNQFSNATNN LPQFGNAMSI SMQLPNGNSN KTASSMNTNP
NTNMIMNSNM NMNMNVNPVP YGMGNGANMY DVSRMMTPPL NIAPNSNNSK SSIMNKHPNR
NNVPPIHPSL LH
