ID   FHL1_YEAST              Reviewed;         936 AA.
AC   P39521; D6W4A2;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   08-NOV-2023, entry version 201.
DE   RecName: Full=Pre-rRNA-processing protein FHL1;
GN   Name=FHL1; OrderedLocusNames=YPR104C; ORFNames=P8283.15;
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=8164651; DOI=10.1128/mcb.14.5.2905-2913.1994;
RA   Hermann-Ledenmat S., Werner M., Sentenac A., Thuriaux P.;
RT   "Suppression of yeast RNA polymerase III mutations by FHL1, a gene coding
RT   for a fork head protein involved in rRNA processing.";
RL   Mol. Cell. Biol. 14:2905-2913(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(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-44, 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-44, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228; THR-230; THR-247 AND
RP   SER-264, AND 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: Controls the pre-rRNA processing machinery in conjunction
CC       with IFH1. Presumably acts as a transcriptional regulator of genes
CC       specifically involved in that process. IFH1 convert FHL1 from a
CC       repressor to an activator.
CC   -!- INTERACTION:
CC       P39521; P38930: CKB2; NbExp=2; IntAct=EBI-6897, EBI-9578;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 639 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; Z28348; CAA82202.1; -; Genomic_DNA.
DR   EMBL; U32445; AAB68074.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11518.1; -; Genomic_DNA.
DR   PIR; S43738; S43738.
DR   RefSeq; NP_015429.1; NM_001184201.1.
DR   AlphaFoldDB; P39521; -.
DR   SMR; P39521; -.
DR   BioGRID; 36270; 212.
DR   DIP; DIP-3821N; -.
DR   IntAct; P39521; 11.
DR   MINT; P39521; -.
DR   STRING; 4932.YPR104C; -.
DR   CarbonylDB; P39521; -.
DR   iPTMnet; P39521; -.
DR   MaxQB; P39521; -.
DR   PaxDb; 4932-YPR104C; -.
DR   PeptideAtlas; P39521; -.
DR   EnsemblFungi; YPR104C_mRNA; YPR104C; YPR104C.
DR   GeneID; 856219; -.
DR   KEGG; sce:YPR104C; -.
DR   AGR; SGD:S000006308; -.
DR   SGD; S000006308; FHL1.
DR   VEuPathDB; FungiDB:YPR104C; -.
DR   eggNOG; KOG2294; Eukaryota.
DR   HOGENOM; CLU_003924_0_0_1; -.
DR   InParanoid; P39521; -.
DR   OMA; IAVQRPM; -.
DR   OrthoDB; 5385885at2759; -.
DR   BioCyc; YEAST:G3O-34244-MONOMER; -.
DR   BioGRID-ORCS; 856219; 11 hits in 13 CRISPR screens.
DR   PRO; PR:P39521; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; P39521; Protein.
DR   GO; GO:0000785; C:chromatin; IDA:SGD.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR   GO; GO:0001223; F:transcription coactivator binding; IPI:SGD.
DR   GO; GO:0001222; F:transcription corepressor binding; IPI:SGD.
DR   GO; GO:0010688; P:negative regulation of ribosomal protein gene transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0060963; P:positive regulation of ribosomal protein gene transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   CDD; cd00059; FH_FOX; 1.
DR   CDD; cd22701; FHA_FKH1-like; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR045178; Fhl1/FHA1.
DR   InterPro; IPR001766; Fork_head_dom.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   InterPro; IPR018122; TF_fork_head_CS_1.
DR   InterPro; IPR030456; TF_fork_head_CS_2.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR21712:SF29; PRE-RRNA-PROCESSING PROTEIN FHL1; 1.
DR   PANTHER; PTHR21712; UNCHARACTERIZED; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF00250; Forkhead; 1.
DR   PRINTS; PR00053; FORKHEAD.
DR   SMART; SM00339; FH; 1.
DR   SMART; SM00240; FHA; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS00657; FORK_HEAD_1; 1.
DR   PROSITE; PS00658; FORK_HEAD_2; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..936
FT                   /note="Pre-rRNA-processing protein FHL1"
FT                   /id="PRO_0000091901"
FT   DOMAIN          300..357
FT                   /note="FHA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT   DNA_BIND        460..552
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT   REGION          1..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          718..936
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..420
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..442
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        738..796
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        811..857
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        861..922
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         44
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15665377,
FT                   ECO:0007744|PubMed:17330950"
FT   MOD_RES         228
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         230
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         247
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         264
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   936 AA;  103502 MW;  2FC02DFC0DFFF503 CRC64;
     MDGEMAIIES SNHVGTSSPT TETQFTIDSS ALKDQETKES ITNSPTSEVP IETKLPKSSD
     IVTEEKHPQN TTTDIENEVE NPVTDDNGNL KLELPDNLDN ADFSKLLEFD AKNDEALFNS
     NELLSHTMDP VNNIDLTHDH SREVSSKEDI NIEPVNPDED EREKTQDNTA AVKTEGIRNS
     EDTSIQKDEP TADAIYTDVH KLSVNKDTET LPTLVDEKNN MLHMRNNSIT PIMFQQHELV
     GQPPQNTVTE NNSTDAETTQ RKLSEPIDAS LPLPNEQPTI FAYARLDFQS FTFYVQTLHA
     IIGRRSENDF SHKVDVNLGP SKSISRRHAQ IFYNFGTGRF ELSIIGKNGA FVDDIFVEKG
     NTVPLRNKTK IQIGQIPFQF ILPEQERNDD SKSPENADIA ESEINTRNLK KNEPKSKKKI
     TTGAKPKKAQ TKPAVKKEKK PPKIPKKVYT LEEIPVEYRT KPTVSYSAML TTCIRKYSTA
     KGMSLSEIYA GIRELFPYYK YCPDGWQSSV RHNLSLNKSF RKVSKEGKGW LWGLDEEYIA
     ERERQKKKQS EIAVAKAQAA QLKLEQQQHK LQQVPQRGKK DIVSQRSNVN ARKQNISQTL
     AANRAASNRK NTASDNQRTM KYLQEQLVIL TRDRKGLSKQ VIAAILTQAL AMTINQVTQA
     AKNKGITGNP LTALMDKNPQ HLNLILAAAV NAATAKVTKG EVKQLVNPET TAAAALAAKA
     QHSKPIRQPI VQTPHVPDRP PSQLSASASS HPNNYLHDKQ PGSFDPSSLS RFFQPRQNAR
     ATSSVAATSV PAAASQNVDA QPKPKPAQDN DLESESGTSS SSSSSSESGS ESDSGSDDGS
     ASGSGDNSST SSESESESDS GSEVDEKNNK NEKIDSESIK NNESKDDIPS KDENSSNDNR
     EISKTDEEGH DSKRRKVSED INEGITEVNV SLEEKL
//