IFH1_YEAST
ID IFH1_YEAST Reviewed; 1085 AA.
AC P39520; D6VYM3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Protein IFH1;
DE AltName: Full=Ribosomal RNA-processing protein 3;
GN Name=IFH1; Synonyms=RRP3; OrderedLocusNames=YLR223C; ORFNames=L8083.9;
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].
RC STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX PubMed=7785326; DOI=10.1002/yea.320110308;
RA Cherel I., Thuriaux P.;
RT "The IFH1 gene product interacts with a fork head protein in Saccharomyces
RT cerevisiae.";
RL Yeast 11:261-270(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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-208, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1041, 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).
CC -!- FUNCTION: Controls the pre-rRNA processing machinery in conjunction
CC with FHL1. Could convert FHL1 from a repressor to an activator.
CC -!- INTERACTION:
CC P39520; P53254: UTP22; NbExp=6; IntAct=EBI-9054, EBI-1878;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 1430 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the IFH1 family. {ECO:0000305}.
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DR EMBL; Z29488; CAA82624.1; -; Genomic_DNA.
DR EMBL; U19027; AAB67412.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09539.1; -; Genomic_DNA.
DR PIR; S55352; S55352.
DR RefSeq; NP_013324.1; NM_001182110.1.
DR AlphaFoldDB; P39520; -.
DR SMR; P39520; -.
DR BioGRID; 31490; 54.
DR ComplexPortal; CPX-774; CURI complex variant 1.
DR ComplexPortal; CPX-775; CURI complex variant 2.
DR ComplexPortal; CPX-776; CURI complex variant 3.
DR DIP; DIP-905N; -.
DR IntAct; P39520; 13.
DR MINT; P39520; -.
DR STRING; 4932.YLR223C; -.
DR iPTMnet; P39520; -.
DR MaxQB; P39520; -.
DR PaxDb; P39520; -.
DR PRIDE; P39520; -.
DR EnsemblFungi; YLR223C_mRNA; YLR223C; YLR223C.
DR GeneID; 850920; -.
DR KEGG; sce:YLR223C; -.
DR SGD; S000004213; IFH1.
DR VEuPathDB; FungiDB:YLR223C; -.
DR eggNOG; ENOG502QQB6; Eukaryota.
DR GeneTree; ENSGT00940000176808; -.
DR HOGENOM; CLU_009986_0_0_1; -.
DR InParanoid; P39520; -.
DR OMA; KLGTWET; -.
DR BioCyc; YEAST:G3O-32337-MON; -.
DR PRO; PR:P39520; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P39520; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0032545; C:CURI complex; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:SGD.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:ComplexPortal.
DR GO; GO:0060963; P:positive regulation of ribosomal protein gene transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0060962; P:regulation of ribosomal protein gene transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR InterPro; IPR018837; TF_CRF1/IFH1.
DR PANTHER; PTHR28057; PTHR28057; 1.
DR Pfam; PF10380; CRF1; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1085
FT /note="Protein IFH1"
FT /id="PRO_0000084164"
FT REGION 1..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..161
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..622
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1085 AA; 122492 MW; BE1C7DEF06213FE0 CRC64;
MAGKKSPRKS TINHSTHSGK LPANIKRLIK KGESDTKSRQ SPPTLSTTRP RRFSLIYSSE
SSLSDVSDSD KNKSTNPHKI KRKAKNISNN SQGKKSKLIQ RQIDNDDEGT ESSDYQAVTD
GEESENEEEE SEEEEEDDDE DDDDDDDDGS DSDSDSETSS DDENIDFVKL TAQRKKRAMK
ALSAMNTNSN TLYSSRENSN KNKSVKLSPK KENEEEQKEE KEKEKEEQQK QQESNKKEVN
GSGTTTTQQA LSFKFKKEDD GISFGNGNEG YNEDIGEEVL DLKNKENNGN EEDKLDSKVM
LGNNDELRFP NISESDESEY DIDQDAYFDV INNEDSHGEI GTDLETGEDD LPILEEEEQN
IVSELQNDDE LSFDGSIHEE GSDPVEDAEN KFLQNEYNQE NGYDEEDDEE DEIMSDFDMP
FYEDPKFANL YYYGDGSEPK LSLSTSLPLM LNDEKLSKLK KKEAKKREQE ERKQRRKLYK
KTQKPSTRTT SNVDNDEYIF NVFFQSDDEN SGHKSKKGRH KSGKSHIEHK NKGSNLIKSN
DDLEPSTHST VLNSGKYDSS DDEYDNILLD VAHMPSDDEC SESETSHDAD TDEELRALDS
DSLDIGTELD DDYEDDDDDS SVTNVFIDID DLDPDSFYFH YDSDGSSSLI SSNSDKENSD
GSKDCKHDLL ETVVYVDDES TDEDDNLPPP SSRSKNIGSK AKEIVSSNVV GLRPPKLGTW
ETDNKPFSII DGLSTKSLYA LIQEHQQLRE QHQRAQTPDV KREGSSNGNN GDELTLNELL
NMSELEDDSP SHTDDMENNY NDAINSKSTN GHAADWYEVP KVPLSAFRNK GINAYEEDEY
MIPANSNRKV PIGYIGNERT RKKIDKMKEL QRKKTEKKRQ LKKKKKLLKI RKQRQKAIKE
QETMNLQLGI NGHEIIGNNN SHSDINTGTD FTTNENTPMN ELPSHAPEDA SLIPHNSDLA
VDSNTRKNST KSVGLDEIHE ILGKDENDLL SVGDINGYDA QEGHVIEDTD ADILASLTAP
VQFDNTLSHE NSNSMWRRRQ SMVEAAAENL RFTKNGLFSE SALADIEGIM GNDVNHSFEF
NDVLQ
