HCM1_YEAST
ID HCM1_YEAST Reviewed; 564 AA.
AC P25364; D6VR68;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Forkhead transcription factor HCM1;
DE AltName: Full=High-copy suppressor of calmodulin protein 1;
GN Name=HCM1; OrderedLocusNames=YCR065W; ORFNames=YCR65W, YCR902;
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].
RX PubMed=8441413; DOI=10.1128/mcb.13.3.1779-1787.1993;
RA Zhu G., Muller E.G.D., Amacher S.L., Northrop J.L., Davis T.N.;
RT "A dosage-dependent suppressor of a temperature-sensitive calmodulin mutant
RT encodes a protein related to the fork head family of DNA-binding
RT proteins.";
RL Mol. Cell. Biol. 13:1779-1787(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1561837; DOI=10.1002/yea.320080209;
RA Benit P., Chanet R., Fabre F., Faye G., Fukuhara H., Sor F.;
RT "Sequence of the sup61-RAD18 region on chromosome III of Saccharomyces
RT cerevisiae.";
RL Yeast 8:147-153(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [4]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASN-155; HIS-159; SER-162
RP AND LEU-163, AND RECOGNITION OF DNA-BINDING SITE.
RX PubMed=9920414; DOI=10.1016/s0167-4889(98)00135-9;
RA Zhu G., Davis T.N.;
RT "The fork head transcription factor Hcm1p participates in the regulation of
RT SPC110, which encodes the calmodulin-binding protein in the yeast spindle
RT pole body.";
RL Biochim. Biophys. Acta 1448:236-244(1998).
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 PHOSPHORYLATION BY CDK1.
RX PubMed=14574415; DOI=10.1038/nature02062;
RA Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA Shokat K.M., Morgan D.O.;
RT "Targets of the cyclin-dependent kinase Cdk1.";
RL Nature 425:859-864(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-342 AND SER-496, AND
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Transcription factor regulating the cell cycle specific
CC transcription of a spindle pole body (SPB) calmodulin binding protein
CC SPC110. Required for full induction of SPC110 transcription in late G1.
CC Binds to DNA consensus sequence 5'-[AT]AA[TC]AAACAA[AT]-3'. Dosage
CC dependent suppressor of calmodulin mutants which have specific defects
CC in SPB assembly. {ECO:0000269|PubMed:9920414}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- PTM: Phosphorylated by CDK1. {ECO:0000269|PubMed:14574415}.
CC -!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; L08252; AAA34665.1; -; Genomic_DNA.
DR EMBL; X59720; CAA42280.2; -; Genomic_DNA.
DR EMBL; BK006937; DAA07537.1; -; Genomic_DNA.
DR PIR; S22262; S22262.
DR RefSeq; NP_009991.2; NM_001178776.1.
DR AlphaFoldDB; P25364; -.
DR SMR; P25364; -.
DR BioGRID; 31041; 299.
DR DIP; DIP-4993N; -.
DR IntAct; P25364; 6.
DR MINT; P25364; -.
DR STRING; 4932.YCR065W; -.
DR iPTMnet; P25364; -.
DR MaxQB; P25364; -.
DR PaxDb; P25364; -.
DR PRIDE; P25364; -.
DR EnsemblFungi; YCR065W_mRNA; YCR065W; YCR065W.
DR GeneID; 850429; -.
DR KEGG; sce:YCR065W; -.
DR SGD; S000000661; HCM1.
DR VEuPathDB; FungiDB:YCR065W; -.
DR eggNOG; KOG2294; Eukaryota.
DR HOGENOM; CLU_020432_0_0_1; -.
DR InParanoid; P25364; -.
DR OMA; DVYSVWK; -.
DR BioCyc; YEAST:G3O-29368-MON; -.
DR Reactome; R-SCE-3232118; SUMOylation of transcription factors.
DR Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
DR PRO; PR:P25364; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25364; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0051300; P:spindle pole body organization; IGI:SGD.
DR CDD; cd00059; FH; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR001766; Fork_head_dom.
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 Pfam; PF00250; Forkhead; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF46785; SSF46785; 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 Cytoplasm; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..564
FT /note="Forkhead transcription factor HCM1"
FT /id="PRO_0000091902"
FT DNA_BIND 108..199
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 33..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..239
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 342
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 155
FT /note="N->A: No recognition of DNA-binding site and no
FT suppression of calmodulin mutants; when associated with A-
FT 159; A-162 and A-163."
FT /evidence="ECO:0000269|PubMed:9920414"
FT MUTAGEN 159
FT /note="H->A: No recognition of DNA-binding site and no
FT suppression of calmodulin mutants; when associated with A-
FT 155; A-162 and A-163."
FT /evidence="ECO:0000269|PubMed:9920414"
FT MUTAGEN 162
FT /note="S->A: No recognition of DNA-binding site and no
FT suppression of calmodulin mutants; when associated with A-
FT 155; A-159 and A-163."
FT /evidence="ECO:0000269|PubMed:9920414"
FT MUTAGEN 163
FT /note="L->A: No recognition of DNA-binding site and no
FT suppression of calmodulin mutants; when associated with A-
FT 155; A-159 and A-162."
FT /evidence="ECO:0000269|PubMed:9920414"
FT CONFLICT 129..130
FT /note="KL -> NV (in Ref. 1; AAA34665)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 564 AA; 63647 MW; 0BF083C2617C0DCD CRC64;
MMNEDISIID GHNSFLTEKS TVLLTQAKRT LEDEKEMITP PSSTVRKTMK EVNKRPSHPL
SPDHSSPIAP SKAKRQRSDT CARSNGNLTL EEILQSLERR RINGELAKKP PYSYATLICL
AILQSQEGKL TLSQIYHWIH VHFPYYKQKD ASWQNSIRHN LSLNDAFIKT EKSCDGKGHF
WEVRPGAETK FFKGENRGYE FVKDSLQDIG KYFEIDSTLD ELEQVESGEG NDDLPDEEER
EEAGKFPSIE IQLNSSPILR VSQLHHIPQL KTDNSVLNPH ENLESMRNMI ENDVNNIDSL
EPPYVMKKYH TSLGLPSLVN AKDHFQAGVK NNNITQANRF NTLPITSAKS PQNFRKYFTS
FNSNFEDLSP LRSNVGAGSL LDPLPYSPLK LYDQKNLALM SKPQSQQSYS NSQLPPPPSS
HGSDLLKTPK MRHSDGLEKT PSRLISTPKD GNSILRKWQT PSHLFEDLYC SPLFRAIETP
IRYITTPGGT LETQISPRKS SAPDVLTSAT NSKFASSGLF GVDVYSVWKR ATEKISDGNN
TTDSNQKHHP YHNHPSNDSG NEKN
