Reviewed, UniProtKB/Swiss-Prot P06774 (HAP2_YEAST)

Names and origin

Protein names

Recommended name:
    Transcriptional activator HAP2

Gene names

Name:	HAP2
Ordered Locus Names:	YGL237C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	265 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Acts a component of the CCAT-binding factor, which is a transcriptional activator and binds to the upstream activation site (UAS2) of the CYC1 gene and other genes involved in mitochondrial electron transport and activates their expression. Recognizes the sequence 5'-CCAAT-3'. HAP2 has primarily a structural role in the HAP complexes I and II.
Subunit structure	Component of the CCAT-binding factor (CBF or HAP complex II), which consists of one copy each of HAP2, HAP3, HAP4 and HAP5. The assembly of the HAP2-HAP3-HAP5 heteromer (HAP complex I) occurs in a one-step pathway and its binding to DNA is a prerequisite for the association of HAP4.
Subcellular location	Nucleus.
Sequence similarities	Belongs to the NFYA/HAP2 subunit family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	regulation of carbohydrate metabolic process Traceable author statement. Source: SGD transcription Traceable author statement. Source: SGD
Cellular component	CCAAT-binding factor complex Traceable author statement. Source: SGD
Molecular function	protein binding Inferred from physical interaction. Source: IntAct transcription activator activity Traceable author statement. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P48235	1	EBI-8152,EBI-23358
ATG17	Q06410	1	EBI-8152,EBI-30856
HAP3	P13434	1	EBI-8152,EBI-8157
HAP5	Q02516	1	EBI-8152,EBI-8165
STD1	Q02794	1	EBI-8152,EBI-18344

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 265	265	Transcriptional activator HAP2
Regions
	DNA binding	194 – 214	21	NFYA/HAP2-type
	Region	23 – 180	158	Interaction with the HAP2-HAP3-HAP5 heteromer
	Motif	162 – 178	17	Subunit association domain (SAD)
	Compositional bias	120 – 133	14	Poly-Gln
Amino acid modifications
	Modified residue	33	1	Phosphoserine
	Modified residue	35	1	Phosphoserine
Experimental info
	Mutagenesis	199	1	R → L: Favors CCACC binding over CCAAT

Sequences

	Sequence		Length	Mass (Da)
	P06774-1 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: 282D8AC2BD6A4CB3	FASTA	265	29,867
	10 20 30 40 50 60 MSADETDAKF HPLETDLQSD TAAATSTAAA SRSPSLQEKP IEMPLDMGKA PSPRGEDQRV 70 80 90 100 110 120 TNEEDLFLFN RLRASQNRVM DSLEPQQQSQ YTSSSVSTME PSADFTSFSA VTTLPPPPHQ 130 140 150 160 170 180 QQQQQQQQQQ QQQLVVQAQY TQNQPNLQSD VLGTAIAEQP FYVNAKQYYR ILKRRYARAK 190 200 210 220 230 240 LEEKLRISRE RKPYLHESRH KHAMRRPRGE GGRFLTAAEI KAMKSKKSGA SDDPDDSHED 250 260 KKITTKIIQE QPHATSTAAA ADKKT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and nuclear localization of the Saccharomyces cerevisiae HAP2 protein, a transcriptional activator." Pinkham J.L., Olesen J.T., Guarente L.P. Mol. Cell. Biol. 7:578-585(1987) [PubMed: 3547076] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"Mutations in yeast HAP2/HAP3 define a hybrid CCAAT box binding domain." Xing Y., Fikes J.D., Guarente L. EMBO J. 12:4647-4655(1993) [PubMed: 8223474] [Abstract] Cited for: MUTAGENESIS.
[4]	"A multiprotein complex that interacts with RNA polymerase II elongator." Li Y., Takagi Y., Jiang Y., Tokunaga M., Erdjument-Bromage H., Tempst P., Kornberg R.D. J. Biol. Chem. 276:29628-29631(2001) [PubMed: 11390369] [Abstract] Cited for: IDENTIFICATION IN THE CCAT-BINDING FACTOR.
[5]	"Identification, mutational analysis, and coactivator requirements of two distinct transcriptional activation domains of the Saccharomyces cerevisiae Hap4 protein." Stebbins J.L., Triezenberg S.J. Eukaryot. Cell 3:339-347(2004) [PubMed: 15075264] [Abstract] Cited for: FUNCTION.
[6]	"Assembly of the Hap2p/Hap3p/Hap4p/Hap5p-DNA complex in Saccharomyces cerevisiae." McNabb D.S., Pinto I. Eukaryot. Cell 4:1829-1839(2005) [PubMed: 16278450] [Abstract] Cited for: ASSOCIATION WITH THE HAP2-HAP3-HAP5 HETEROMER, ASSEMBLY OF THE CCAT-BINDING FACTOR.
[7]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-35, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M15243 Genomic DNA. Translation: AAA34663.1. Z72759 Genomic DNA. Translation: CAA96955.1.
PIR	A26771.
RefSeq	NP_011277.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:1361N.
IntAct	P06774.
Genome annotation databases
Ensembl	YGL237C. Saccharomyces cerevisiae. [Contig view]
GeneID	852614.
GenomeReviews	Gene locus YGL237C in contig Y13135_GR.
KEGG	sce:YGL237C.
NMPDR	fig|4932.3.peg.2380.
Organism-specific databases
CYGD	YGL237c.
SGD	S000003206. HAP2.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P06774.
Gene expression databases
GermOnline	YGL237C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001289. TF_CBFB. [Graphical view]
PANTHER	PTHR12632. TF_CBFB. 1 hit.
Pfam	PF02045. CBFB_NFYA. 1 hit. [Graphical view]
PRINTS	PR00616. CCAATSUBUNTB.
ProDom	PD003860. TF_CBFB. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00521. CBF. 1 hit. [Graphical view]
PROSITE	PS00686. NFYA_HAP2_1. 1 hit. PS51152. NFYA_HAP2_2. 1 hit. [Graphical view]
BLOCKS	Search...
Other Resources
LinkHub	P06774.
ProtoNet	Search...

Entry information

Entry name

HAP2_YEAST

Accession

Primary (citable) accession number: P06774

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	September 2, 2008
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)