PIH1_YEAST
ID PIH1_YEAST Reviewed; 344 AA.
AC P38768; D3DKY1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein interacting with Hsp90 1;
DE AltName: Full=Nucleolar protein 17;
GN Name=PIH1; Synonyms=NOP17; OrderedLocusNames=YHR034C;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 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 [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 INTERACTION WITH HSP90, IDENTIFICATION IN THE R2PT COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15766533; DOI=10.1016/j.cell.2004.12.024;
RA Zhao R., Davey M.G., Hsu Y.-C., Kaplanek P., Tong A., Parsons A.B.,
RA Krogan N.J., Cagney G., Mai D., Greenblatt J.F., Boone C., Emili A.,
RA Houry W.A.;
RT "Navigating the chaperone network: an integrative map of physical and
RT genetic interactions mediated by the hsp90 chaperone.";
RL Cell 120:715-727(2005).
RN [6]
RP INTERACTION WITH NOP53.
RX PubMed=16128814; DOI=10.1111/j.1742-4658.2005.04861.x;
RA Granato D.C., Gonzales F.A., Luz J.S., Cassiola F., Machado-Santelli G.M.,
RA Oliveira C.C.;
RT "Nop53p, an essential nucleolar protein that interacts with Nop17p and
RT Nip7p, is required for pre-rRNA processing in Saccharomyces cerevisiae.";
RL FEBS J. 272:4450-4463(2005).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RRP43 AND NOP58.
RX PubMed=15670595; DOI=10.1016/j.jmb.2004.11.071;
RA Gonzales F.A., Zanchin N.I., Luz J.S., Oliveira C.C.;
RT "Characterization of Saccharomyces cerevisiae Nop17p, a novel Nop58p-
RT interacting protein that is involved in pre-rRNA processing.";
RL J. Mol. Biol. 346:437-455(2005).
CC -!- FUNCTION: Involved in pre-rRNA processing and required for the NOP58-
CC snoRNA interaction. {ECO:0000269|PubMed:15670595}.
CC -!- SUBUNIT: Component of the R2TP complex composed at least of RVB1, RVB2,
CC TAH1 and PIH1. Interacts also with HSP90, RRP43, NOP53 and NOP58.
CC {ECO:0000269|PubMed:15670595, ECO:0000269|PubMed:15766533,
CC ECO:0000269|PubMed:16128814}.
CC -!- INTERACTION:
CC P38768; P02829: HSP82; NbExp=4; IntAct=EBI-24499, EBI-8659;
CC P38768; Q12498: PRM4; NbExp=3; IntAct=EBI-24499, EBI-32462;
CC P38768; P25359: RRP43; NbExp=2; IntAct=EBI-24499, EBI-1773;
CC P38768; Q03940: RVB1; NbExp=10; IntAct=EBI-24499, EBI-30712;
CC P38768; Q12464: RVB2; NbExp=7; IntAct=EBI-24499, EBI-31814;
CC P38768; P25638: TAH1; NbExp=17; IntAct=EBI-24499, EBI-21956;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- MISCELLANEOUS: Present with 2610 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PIH1 family. {ECO:0000305}.
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DR EMBL; U00062; AAB68914.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06725.1; -; Genomic_DNA.
DR PIR; S46745; S46745.
DR RefSeq; NP_011899.1; NM_001179164.1.
DR PDB; 2MNJ; NMR; -; B=257-344.
DR PDB; 4CGU; X-ray; 2.11 A; B=187-344.
DR PDB; 4CHH; X-ray; 2.03 A; A/B=1-185.
DR PDBsum; 2MNJ; -.
DR PDBsum; 4CGU; -.
DR PDBsum; 4CHH; -.
DR AlphaFoldDB; P38768; -.
DR BMRB; P38768; -.
DR SMR; P38768; -.
DR BioGRID; 36465; 261.
DR ComplexPortal; CPX-1814; R2TP co-chaperone complex.
DR DIP; DIP-807N; -.
DR IntAct; P38768; 17.
DR MINT; P38768; -.
DR STRING; 4932.YHR034C; -.
DR MaxQB; P38768; -.
DR PaxDb; P38768; -.
DR PRIDE; P38768; -.
DR EnsemblFungi; YHR034C_mRNA; YHR034C; YHR034C.
DR GeneID; 856429; -.
DR KEGG; sce:YHR034C; -.
DR SGD; S000001076; PIH1.
DR VEuPathDB; FungiDB:YHR034C; -.
DR eggNOG; KOG4356; Eukaryota.
DR HOGENOM; CLU_072113_0_0_1; -.
DR InParanoid; P38768; -.
DR OMA; EWCLESC; -.
DR BioCyc; YEAST:G3O-31094-MON; -.
DR PRO; PR:P38768; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38768; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0097255; C:R2TP complex; IDA:SGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0000492; P:box C/D snoRNP assembly; IMP:SGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IMP:SGD.
DR GO; GO:0050821; P:protein stabilization; IC:ComplexPortal.
DR GO; GO:0008361; P:regulation of cell size; HMP:SGD.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR IDEAL; IID50209; -.
DR InterPro; IPR041441; Pih1_CS_Ascomycota.
DR InterPro; IPR012981; PIH1_N.
DR Pfam; PF08190; PIH1; 1.
DR Pfam; PF18482; Pih1_fungal_CS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome.
FT CHAIN 1..344
FT /note="Protein interacting with Hsp90 1"
FT /id="PRO_0000058440"
FT REGION 195..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:4CHH"
FT STRAND 35..47
FT /evidence="ECO:0007829|PDB:4CHH"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:4CHH"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:4CHH"
FT HELIX 78..86
FT /evidence="ECO:0007829|PDB:4CHH"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:4CHH"
FT STRAND 109..118
FT /evidence="ECO:0007829|PDB:4CHH"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:4CHH"
FT HELIX 129..147
FT /evidence="ECO:0007829|PDB:4CHH"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:4CHH"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4CHH"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:4CHH"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:4CHH"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:4CHH"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:4CHH"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:4CHH"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:2MNJ"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:4CGU"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:4CGU"
FT STRAND 280..287
FT /evidence="ECO:0007829|PDB:4CGU"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:2MNJ"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:4CGU"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:4CGU"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:4CGU"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:4CGU"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:4CGU"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:4CGU"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:4CGU"
FT TURN 335..338
FT /evidence="ECO:0007829|PDB:4CGU"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:4CGU"
SQ SEQUENCE 344 AA; 39519 MW; 02C06D0A113B1B3B CRC64;
MADFLLRPIK QRHRNEDKYV SVDAADGSVS KIEPIADFVI KTKLLSANGP EKLQDGRKVF
INVCHSPLVP KPEVDFNARI VFPLIIQNEW EIPIITSCYR MDHDKKGQEC YVWDCCINSD
CSRWICDDIQ LREILVEWCL ESCEIRDSVV LCRDRIAFPK MKKKGAELPA LEVLNDELHQ
DYKAKMHKII EEEAGDPMSI LRGRNDDGDD NNDPDDGTLP PLFPIENKIS GAKIEEIDKN
EIAHRNLKQA PAPAPAPHEQ QEDVPEYEVK MKRFKGAAYK LRILIENKAP NSKPDRFSPS
YNFAENILYI NGKLSIPLPR DIVVNAADIK IFHIRKERTL YIYI
