HMS1_YEAST
ID HMS1_YEAST Reviewed; 434 AA.
AC Q12398; D6W297;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable transcription factor HMS1;
DE AltName: Full=High-copy MEP suppressor protein 1;
GN Name=HMS1; OrderedLocusNames=YOR032C; ORFNames=OR26.22;
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=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
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 FUNCTION.
RX PubMed=9832522; DOI=10.1093/genetics/150.4.1443;
RA Lorenz M.C., Heitman J.;
RT "Regulators of pseudohyphal differentiation in Saccharomyces cerevisiae
RT identified through multicopy suppressor analysis in ammonium permease
RT mutant strains.";
RL Genetics 150:1443-1457(1998).
RN [4]
RP FUNCTION, INTERACTION WITH PCL1, AND PHOSPHORYLATION BY PCL1-PHO85.
RX PubMed=15082539; DOI=10.1534/genetics.166.3.1177;
RA Keniry M.E., Kemp H.A., Rivers D.M., Sprague G.F. Jr.;
RT "The identification of Pcl1-interacting proteins that genetically interact
RT with Cla4 may indicate a link between G1 progression and mitotic exit.";
RL Genetics 166:1177-1186(2004).
CC -!- FUNCTION: Involved in exit from mitosis and pseudohyphal
CC differentiation. {ECO:0000269|PubMed:15082539,
CC ECO:0000269|PubMed:9832522}.
CC -!- SUBUNIT: Interacts with the G1/S-specific cyclin PCL1.
CC {ECO:0000269|PubMed:15082539}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- PTM: Phosphorylated by the cyclin-CDK complex PCL1-PHO85.
CC {ECO:0000269|PubMed:15082539}.
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DR EMBL; X87331; CAA60748.1; -; Genomic_DNA.
DR EMBL; Z74940; CAA99222.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10813.1; -; Genomic_DNA.
DR PIR; S62168; S62168.
DR RefSeq; NP_014675.1; NM_001183451.1.
DR AlphaFoldDB; Q12398; -.
DR SMR; Q12398; -.
DR BioGRID; 34434; 76.
DR DIP; DIP-5658N; -.
DR IntAct; Q12398; 6.
DR STRING; 4932.YOR032C; -.
DR PaxDb; Q12398; -.
DR PRIDE; Q12398; -.
DR EnsemblFungi; YOR032C_mRNA; YOR032C; YOR032C.
DR GeneID; 854197; -.
DR KEGG; sce:YOR032C; -.
DR SGD; S000005558; HMS1.
DR VEuPathDB; FungiDB:YOR032C; -.
DR eggNOG; KOG2588; Eukaryota.
DR GeneTree; ENSGT00940000168984; -.
DR HOGENOM; CLU_050098_0_0_1; -.
DR InParanoid; Q12398; -.
DR OMA; YSATDQY; -.
DR BioCyc; YEAST:G3O-33578-MON; -.
DR PRO; PR:Q12398; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12398; protein.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:SGD.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0007124; P:pseudohyphal growth; IGI:SGD.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..434
FT /note="Probable transcription factor HMS1"
FT /id="PRO_0000224147"
FT DOMAIN 266..341
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 365..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 434 AA; 48871 MW; 6D8E7176569B07A0 CRC64;
MPNFQKPFSG SSDGNSVMND LGNKVAIKVF DCRSAQDGSE EQNVNVTTNQ MYLMFQSNNY
NVPPPNYNTE DLGSQGPPTH AYYAPFQHPI HLQPPVPPVY KNNTYSATDQ YSDSSFPNTS
GHTPVIDSNY YNDALASIPT TTTGSTTMTT DNGNTIDSEE YIDNMEVFSS EENENIDNVK
QTDLKSEKDS SLLSAASIVK KEQLSGFENF LPLSKTESPL VTADEIKSSL NLENIDNADS
MSFKLKTSPI RKHFHVKPKR ITRVRTGRVS HNIIEKKYRS NINDKIEQLR RTVPTLRVAY
KKCNDLPITS RDLADLDGLE PATKLNKASI LTKSIEYICH LERKCLQLSL ANQHLSNDTR
DSFVHLTEPS QPLSDNSSSE QVQKQTRSCQ RQRQRQPRQQ QPLHNIQYNI PHQNGLMSGT
NNSHDMDFNN AGDF
