P25364 (HCM1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Forkhead transcription factor HCM1

Alternative name(s):
High-copy suppressor of calmodulin protein 1

Gene names

Name:	HCM1
Ordered Locus Names:	YCR065W
ORF Names:	YCR65W, YCR902

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	564 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcription factor regulating the cell cycle specific transcription of a spindle pole body (SPB) calmodulin binding protein SPC110. Required for full induction of SPC110 transcription in late G1. Binds to DNA consensus sequence 5'-[AT]AA[TC]AAACAA[AT]-3'. Dosage dependent suppressor of calmodulin mutants which have specific defects in SPB assembly. Ref.6
Subcellular location	Cytoplasm. Nucleus Ref.6 Ref.7.
Post-translational modification	Phosphorylated by CDK1. Ref.9
Miscellaneous	Present with 358 molecules/cell in log phase SD medium.
Sequence similarities	Contains 1 fork-head DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to oxidative stress Inferred from mutant phenotype PubMed 20847055. Source: SGD mitochondrion organization Inferred from mutant phenotype PubMed 20847055. Source: SGD positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.1. Source: SGD positive regulation of transcription involved in S-phase of mitotic cell cycle Inferred from mutant phenotype PubMed 16912276. Source: SGD regulation of sequence-specific DNA binding transcription factor activity Inferred from Biological aspect of Ancestor. Source: RefGenome spindle pole body organization Inferred from genetic interaction Ref.6. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 20847055. Source: SGD nuclear chromatin Inferred from direct assay PubMed 12464632. Source: SGD transcription factor complex Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Inferred from Biological aspect of Ancestor. Source: RefGenome double-stranded DNA binding Inferred from Biological aspect of Ancestor. Source: RefGenome sequence-specific DNA binding Inferred from direct assay PubMed 19111667. Source: SGD transcription factor binding Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 564	564	Forkhead transcription factor HCM1		PRO_0000091902
Regions
	DNA binding	108 – 199	92	Fork-head Ref.6
Amino acid modifications
	Modified residue	39	1	Phosphothreonine Ref.10
	Modified residue	312	1	Phosphoserine Ref.10
	Modified residue	342	1	Phosphothreonine Ref.10
	Modified residue	387	1	Phosphoserine Ref.10
	Modified residue	496	1	Phosphoserine Ref.10
	Modified residue	501	1	Phosphoserine Ref.10
Experimental info
	Mutagenesis	155	1	N → A: No recognition of DNA-binding site and no suppression of calmodulin mutants; when associated with A-159; A-162 and A-163. Ref.6
	Mutagenesis	159	1	H → A: No recognition of DNA-binding site and no suppression of calmodulin mutants; when associated with A-155; A-162 and A-163. Ref.6
	Mutagenesis	162	1	S → A: No recognition of DNA-binding site and no suppression of calmodulin mutants; when associated with A-155; A-159 and A-163. Ref.6
	Mutagenesis	163	1	L → A: No recognition of DNA-binding site and no suppression of calmodulin mutants; when associated with A-155; A-159 and A-162. Ref.6
	Sequence conflict	129 – 130	2	KL → NV in AAA34665. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P25364 [UniParc]. Last modified October 5, 2010. Version 3. Checksum: 0BF083C2617C0DCD	FASTA	564	63,647
	10 20 30 40 50 60 MMNEDISIID GHNSFLTEKS TVLLTQAKRT LEDEKEMITP PSSTVRKTMK EVNKRPSHPL 70 80 90 100 110 120 SPDHSSPIAP SKAKRQRSDT CARSNGNLTL EEILQSLERR RINGELAKKP PYSYATLICL 130 140 150 160 170 180 AILQSQEGKL TLSQIYHWIH VHFPYYKQKD ASWQNSIRHN LSLNDAFIKT EKSCDGKGHF 190 200 210 220 230 240 WEVRPGAETK FFKGENRGYE FVKDSLQDIG KYFEIDSTLD ELEQVESGEG NDDLPDEEER 250 260 270 280 290 300 EEAGKFPSIE IQLNSSPILR VSQLHHIPQL KTDNSVLNPH ENLESMRNMI ENDVNNIDSL 310 320 330 340 350 360 EPPYVMKKYH TSLGLPSLVN AKDHFQAGVK NNNITQANRF NTLPITSAKS PQNFRKYFTS 370 380 390 400 410 420 FNSNFEDLSP LRSNVGAGSL LDPLPYSPLK LYDQKNLALM SKPQSQQSYS NSQLPPPPSS 430 440 450 460 470 480 HGSDLLKTPK MRHSDGLEKT PSRLISTPKD GNSILRKWQT PSHLFEDLYC SPLFRAIETP 490 500 510 520 530 540 IRYITTPGGT LETQISPRKS SAPDVLTSAT NSKFASSGLF GVDVYSVWKR ATEKISDGNN 550 560 TTDSNQKHHP YHNHPSNDSG NEKN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A dosage-dependent suppressor of a temperature-sensitive calmodulin mutant encodes a protein related to the fork head family of DNA-binding proteins." Zhu G., Muller E.G.D., Amacher S.L., Northrop J.L., Davis T.N. Mol. Cell. Biol. 13:1779-1787(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence of the sup61-RAD18 region on chromosome III of Saccharomyces cerevisiae." Benit P., Chanet R., Fabre F., Faye G., Fukuhara H., Sor F. Yeast 8:147-153(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The complete DNA sequence of yeast chromosome III." Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G. Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Valles G., Volckaerts G. Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO C-TERMINUS.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"The fork head transcription factor Hcm1p participates in the regulation of SPC110, which encodes the calmodulin-binding protein in the yeast spindle pole body." Zhu G., Davis T.N. Biochim. Biophys. Acta 1448:236-244(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASN-155; HIS-159; SER-162 AND LEU-163, RECOGNITION OF DNA-BINDING SITE.
[7]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"Targets of the cyclin-dependent kinase Cdk1." Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K., Shokat K.M., Morgan D.O. Nature 425:859-864(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY CDK1.
[10]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-39; SER-312; THR-342; SER-387; SER-496 AND SER-501, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L08252 Genomic DNA. Translation: AAA34665.1. X59720 Genomic DNA. Translation: CAA42280.2. BK006937 Genomic DNA. Translation: DAA07537.1.
PIR	S22262.
RefSeq	NP_009991.2. NM_001178776.1.
3D structure databases
ProteinModelPortal	P25364.
SMR	P25364. Positions 109-191.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4993N.
IntAct	P25364. 5 interactions.
MINT	MINT-531907.
STRING	4932.YCR065W.
Proteomic databases
PaxDb	P25364.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YCR065W; YCR065W; YCR065W.
GeneID	850429.
KEGG	sce:YCR065W.
Organism-specific databases
SGD	S000000661. HCM1.
Phylogenomic databases
eggNOG	COG5025.
GeneTree	ENSGT00700000104094.
HOGENOM	HOG000142335.
KO	K09413.
OMA	CLAILQS.
OrthoDB	EOG4XKZH6.
Gene expression databases
Genevestigator	P25364.
GermOnline	YCR065W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.10.10.10. 1 hit.
InterPro	IPR001766. TF_fork_head. IPR018122. TF_fork_head_CS. IPR011991. WHTH_DNA-bd_dom. [Graphical view]
Pfam	PF00250. Fork_head. 1 hit. [Graphical view]
PRINTS	PR00053. FORKHEAD.
SMART	SM00339. FH. 1 hit. [Graphical view]
PROSITE	PS00657. FORK_HEAD_1. 1 hit. PS00658. FORK_HEAD_2. 1 hit. PS50039. FORK_HEAD_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	966009.

Entry information

Entry name

HCM1_YEAST

Accession

Primary (citable) accession number: P25364
Secondary accession number(s): D6VR68

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	October 5, 2010
Last modified:	May 1, 2013
This is version 120 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program