FHL1_YEAST
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 03-AUG-2022, entry version 195.
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; 211.
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; P39521; -.
DR PRIDE; P39521; -.
DR EnsemblFungi; YPR104C_mRNA; YPR104C; YPR104C.
DR GeneID; 856219; -.
DR KEGG; sce:YPR104C; -.
DR SGD; S000006308; FHL1.
DR VEuPathDB; FungiDB:YPR104C; -.
DR eggNOG; KOG2294; Eukaryota.
DR HOGENOM; CLU_003924_0_0_1; -.
DR InParanoid; P39521; -.
DR OMA; GQPASME; -.
DR BioCyc; YEAST:G3O-34244-MON; -.
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 transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd00059; FH; 1.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 1.10.10.10; -; 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; PTHR21712; 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; SSF46785; SSF46785; 1.
DR SUPFAM; SSF49879; SSF49879; 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
