Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q02516 (HAP5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcriptional activator HAP5
Gene names
Name:HAP5
Ordered Locus Names:YOR358W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length242 AA.
Sequence statusComplete.
Protein existenceEvidence 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'. HAP5 is essential for DNA-binding activity. It may be the linchpin that binds to the subunit association domains (SAD) of HAP2 and HAP3 to bring these proteins together.

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.

Miscellaneous

Present with 450 molecules/cell in log phase SD medium. Ref.7

Sequence similarities

Belongs to the NFYC/HAP5 subunit family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HAP2P067749EBI-8165,EBI-8152
HAP3P134345EBI-8165,EBI-8157

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 242242Transcriptional activator HAP5
PRO_0000218260

Amino acid modifications

Modified residue71Phosphoserine Ref.9

Sequences

Sequence LengthMass (Da)Tools
Q02516 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 4104058BF48A4319

FASTA24227,676
        10         20         30         40         50         60 
MTDRNFSPQQ GQGPQESLPE GPQPSTMIQR EEMNMPRQYS EQQQLQENEG EGENTRLPVS 

        70         80         90        100        110        120 
EEEFRMVQEL QAIQAGHDQA NLPPSGRGSL EGEDNGNSDG ADGEMDEDDE EYDVFRNVGQ 

       130        140        150        160        170        180 
GLVGHYKEIM IRYWQELINE IESTNEPGSE HQDDFKSHSL PFARIRKVMK TDEDVKMISA 

       190        200        210        220        230        240 
EAPIIFAKAC EIFITELTMR AWCVAERNKR RTLQKADIAE ALQKSDMFDF LIDVVPRRPL 


PQ 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of yeast HAP5: a novel subunit of a heterotrimeric complex required for CCAAT binding."
McNabb D.S., Xing Y., Guarente L.
Genes Dev. 9:47-58(1995) [PubMed: 7828851] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-242.
Strain: ATCC 204508 / S288c.
[2]McNabb D.S.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed: 9169874] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"The Saccharomyces cerevisiae Hap5p homolog from fission yeast reveals two conserved domains that are essential for assembly of heterotetrameric CCAAT-binding factor."
McNabb D.S., Tseng K.A.-S., Guarente L.
Mol. Cell. Biol. 17:7008-7018(1997) [PubMed: 9372932] [Abstract]
Cited for: IDENTIFICATION IN THE CCAT-BINDING FACTOR.
[6]"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.
[7]"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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"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: ASSEMBLY OF THE CCAT-BINDING FACTOR.
[9]"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-7, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U19932 Genomic DNA. Translation: AAC49610.1.
Z75266 Genomic DNA. Translation: CAA99687.1.
BK006948 Genomic DNA. Translation: DAA11119.1.
PIRS67270.
RefSeqNP_015003.1. NM_001183778.1.

3D structure databases

ProteinModelPortalQ02516.
SMRQ02516. Positions 160-237.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1363N.
IntActQ02516. 10 interactions.
MINTMINT-406466.
STRINGQ02516.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR358W; YOR358W; YOR358W.
GeneID854540.
KEGGsce:YOR358W.
NMPDRfig|4932.3.peg.6122.

Organism-specific databases

CYGDYOR358w.
SGDS000005885. HAP5.

Phylogenomic databases

eggNOGfuNOG09244.
GeneTreeEFGT00050000004185.
OrthoDBEOG4BS0W7.

Gene expression databases

ArrayExpressQ02516.
GenevestigatorQ02516.
GermOnlineYOR358W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
[Graphical view]
Gene3DG3DSA:1.10.20.10. Histone-fold. 1 hit.
PfamPF00125. Histone. 1 hit.
[Graphical view]
SUPFAMSSF47113. Histone-fold. 1 hit.
ProtoNetSearch...

Other

NextBio976943.

Entry information

Entry nameHAP5_YEAST
AccessionPrimary (citable) accession number: Q02516
Secondary accession number(s): D6W353, Q08827
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: December 14, 2011
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families