PXR1_YEAST
ID PXR1_YEAST Reviewed; 271 AA.
AC P53335; D6VV57; Q8TG89;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Protein PXR1;
DE AltName: Full=G-patch nucleolar protein;
DE AltName: Full=PinX1-related protein 1;
GN Name=PXR1; Synonyms=GNO1; OrderedLocusNames=YGR280C;
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 [MRNA].
RX PubMed=11701125; DOI=10.1016/s0092-8674(01)00538-4;
RA Zhou X.Z., Lu K.P.;
RT "The Pin2/TRF1-interacting protein PinX1 is a potent telomerase
RT inhibitor.";
RL Cell 107:347-359(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9090054;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<251::aid-yea63>3.0.co;2-r;
RA Volckaert G., Voet M., Robben J.;
RT "Sequence analysis of a near-subtelomeric 35.4 kb DNA segment on the right
RT arm of chromosome VII from Saccharomyces cerevisiae carrying the MAL1 locus
RT reveals 15 complete open reading frames, including ZUO1, BGL2 and BIO2
RT genes and an ABC transporter gene.";
RL Yeast 13:251-259(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12107183; DOI=10.1074/jbc.m205526200;
RA Guglielmi B., Werner M.;
RT "The yeast homolog of human PinX1 is involved in rRNA and small nucleolar
RT RNA maturation, not in telomere elongation inhibition.";
RL J. Biol. Chem. 277:35712-35719(2002).
RN [7]
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 [8]
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 [9]
RP FUNCTION, AND INTERACTION WITH EST2.
RX PubMed=14977919; DOI=10.1101/gad.1171804;
RA Lin J., Blackburn E.H.;
RT "Nucleolar protein PinX1p regulates telomerase by sequestering its protein
RT catalytic subunit in an inactive complex lacking telomerase RNA.";
RL Genes Dev. 18:387-396(2004).
RN [10]
RP FUNCTION.
RX PubMed=16544271; DOI=10.1002/yea.1353;
RA Wade C.H., Umbarger M.A., McAlear M.A.;
RT "The budding yeast rRNA and ribosome biosynthesis (RRB) regulon contains
RT over 200 genes.";
RL Yeast 23:293-306(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Involved in rRNA-processing at A0, A1 and A2 sites through
CC its action in U18 and U24 snoRNA 3'-end final trimming. Negative
CC regulator of telomerase through competition for binding to EST2 with
CC TLC1. {ECO:0000269|PubMed:12107183, ECO:0000269|PubMed:14977919,
CC ECO:0000269|PubMed:16544271}.
CC -!- SUBUNIT: Interacts with EST2. {ECO:0000269|PubMed:14977919}.
CC -!- INTERACTION:
CC P53335; P15790: CKA1; NbExp=2; IntAct=EBI-23652, EBI-9533;
CC P53335; P53131: PRP43; NbExp=6; IntAct=EBI-23652, EBI-505;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12107183,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3850 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PINX1 family. {ECO:0000305}.
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DR EMBL; AF432905; AAM18461.1; -; mRNA.
DR EMBL; Z73065; CAA97311.1; -; Genomic_DNA.
DR EMBL; AY558384; AAS56710.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08368.1; -; Genomic_DNA.
DR PIR; S64615; S64615.
DR RefSeq; NP_011796.1; NM_001181409.1.
DR AlphaFoldDB; P53335; -.
DR BioGRID; 33530; 63.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR DIP; DIP-4308N; -.
DR IntAct; P53335; 23.
DR MINT; P53335; -.
DR STRING; 4932.YGR280C; -.
DR iPTMnet; P53335; -.
DR MaxQB; P53335; -.
DR PaxDb; P53335; -.
DR PRIDE; P53335; -.
DR EnsemblFungi; YGR280C_mRNA; YGR280C; YGR280C.
DR GeneID; 853197; -.
DR KEGG; sce:YGR280C; -.
DR SGD; S000003512; PXR1.
DR VEuPathDB; FungiDB:YGR280C; -.
DR eggNOG; KOG2809; Eukaryota.
DR HOGENOM; CLU_052839_0_0_1; -.
DR InParanoid; P53335; -.
DR OMA; WDQSSEA; -.
DR BioCyc; YEAST:G3O-30943-MON; -.
DR PRO; PR:P53335; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53335; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR GO; GO:0008047; F:enzyme activator activity; IMP:SGD.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0010521; F:telomerase inhibitor activity; IMP:SGD.
DR GO; GO:0000494; P:box C/D RNA 3'-end processing; IMP:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:SGD.
DR GO; GO:0090069; P:regulation of ribosome biogenesis; IBA:GO_Central.
DR InterPro; IPR000467; G_patch_dom.
DR Pfam; PF01585; G-patch; 1.
DR SMART; SM00443; G_patch; 1.
DR PROSITE; PS50174; G_PATCH; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis;
KW rRNA processing.
FT CHAIN 1..271
FT /note="Protein PXR1"
FT /id="PRO_0000202871"
FT DOMAIN 25..72
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT REGION 147..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..206
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 148
FT /note="N -> H (in Ref. 1; AAM18461)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="K -> N (in Ref. 1; AAM18461)"
FT /evidence="ECO:0000305"
FT CONFLICT 165..167
FT /note="DDK -> ADQ (in Ref. 1; AAM18461)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="D -> A (in Ref. 1; AAM18461)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 271 AA; 31312 MW; D5AB6EB2C129922D CRC64;
MGLAATRTKQ RFGLDPRNTA WSNDTSRFGH QFLEKFGWKP GMGLGLSPMN SNTSHIKVSI
KDDNVGLGAK LKRKDKKDEF DNGECAGLDV FQRILGRLNG KESKISEELD TQRKQKIIDG
KWGIHFVKGE VLASTWDPKT HKLRNYSNAK KRKREGDDSE DEDDDDKEDK DSDKKKHKKH
KKHKKDKKKD KKDKKEHKKH KKEEKRLKKE KRAEKTKETK KTSKLKSSES ASNIPDAVNT
RLSVRSKWIK QKRAALMDSK ALNEIFMITN D
