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Q08649 (ESA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Histone acetyltransferase ESA1

EC=2.3.1.48
Gene names
Name:ESA1
Ordered Locus Names:YOR244W
ORF Names:O5257
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, histone H2B to form H2BK16ac, histone H2A to form H2AK4ac and H2AK7ac, and histone variant H2A.Z to form H2A.ZK14ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression. Recruitment to promoters depends on H3K4me. Ref.6 Ref.7 Ref.8 Ref.9 Ref.13 Ref.16 Ref.17 Ref.18 Ref.21

Catalytic activity

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Subunit structure

Component of the NuA4 histone acetyltransferase complex composed of at least ACT1, ARP4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, SWC4, TRA1, VID21, YAF9 and YNG2. The complex interacts with histones H4 (HHF1 and HHF2), H3 (HHT1 and HHT2) and H2A (HTA1 and HTA2). Ref.5 Ref.9 Ref.18 Ref.19

Domain

The ESA1-RPD3 motif is common to ESA1 and RPD3 and is required for ESA1 histone acetyl-transferase (HAT) activity and RPD3 histone deacetylase (HDAC) activity. Ref.12 Ref.22

Post-translational modification

Autoacetylation at Lys-262 is required for proper function. Ref.7 Ref.10 Ref.11 Ref.14 Ref.24 Ref.25

Miscellaneous

Present with 1170 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the MYST (SAS/MOZ) family.

Contains 1 chromo domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Molecular functionActivator
Chromatin regulator
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from direct assay PubMed 16135807. Source: SGD

DNA-templated transcription, elongation

Inferred from direct assay Ref.20. Source: SGD

chromatin silencing at rDNA

Inferred from mutant phenotype PubMed 16436512. Source: SGD

histone H4 acetylation

Inferred from direct assay Ref.12. Source: GOC

histone acetylation

Inferred from direct assay Ref.7Ref.5. Source: SGD

peptidyl-lysine acetylation

Inferred from mutant phenotype PubMed 23050233. Source: SGD

positive regulation of macroautophagy

Inferred from mutant phenotype PubMed 22539722. Source: SGD

positive regulation of transcription elongation from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 19822662. Source: SGD

regulation of cell cycle

Inferred from mutant phenotype Ref.7. Source: SGD

regulation of transcription by chromatin organization

Inferred from mutant phenotype PubMed 11867538. Source: SGD

regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 11036083. Source: SGD

   Cellular_componentNuA4 histone acetyltransferase complex

Inferred from direct assay Ref.9. Source: SGD

Piccolo NuA4 histone acetyltransferase complex

Inferred from direct assay PubMed 12782659. Source: SGD

nuclear chromatin

Inferred from direct assay Ref.9. Source: SGD

   Molecular_functionH4 histone acetyltransferase activity

Inferred from direct assay Ref.12. Source: SGD

histone acetyltransferase activity

Inferred from direct assay PubMed 17274630. Source: SGD

peptide N-acetyltransferase activity

Inferred from mutant phenotype PubMed 23050233. Source: SGD

protein binding

Inferred from physical interaction Ref.5Ref.9PubMed 11036083PubMed 11805826PubMed 14690591Ref.18Ref.19PubMed 15485911PubMed 16429126PubMed 20489023PubMed 21179020PubMed 21183953Ref.25. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445Histone acetyltransferase ESA1
PRO_0000051562

Regions

Domain33 – 8654Chromo
Region312 – 3187Acetyl-CoA binding By similarity
Motif245 – 26622ESA1-RPD3 motif

Sites

Active site2621 Ref.25
Active site3041Nucleophile By similarity
Binding site3071Acetyl-CoA
Binding site3421Acetyl-CoA

Amino acid modifications

Modified residue171Phosphoserine Ref.23
Modified residue2621N6-acetyllysine; by autocatalysis Ref.25

Experimental info

Mutagenesis2471W → A: Reduces strongly HAT activity. Ref.12
Mutagenesis2501N → A: Reduces strongly HAT activity. Ref.12
Mutagenesis2511L → A: Reduces strongly HAT activity. Ref.12
Mutagenesis2521C → A: Reduces strongly HAT activity. Ref.12
Mutagenesis2531L → A: Reduces strongly HAT activity. Ref.12
Mutagenesis2541L → A: Reduces strongly HAT activity. Ref.12
Mutagenesis2561K → A: Reduces strongly HAT activity. Ref.12
Mutagenesis2591L → A: Reduces strongly HAT activity. Ref.12
Mutagenesis2601D → A: Reduces strongly HAT activity. Ref.12
Mutagenesis2621K → A: Reduces strongly HAT activity. Ref.12
Mutagenesis3041C → S: Loss of function; abolishes the formation of acetyl intermediate.
Mutagenesis3151G → E: Loss of function. Ref.4
Mutagenesis3381E → Q: Loss of function; abolishes transfer of acetyl to C-304.

Secondary structure

.................................................................... 445
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q08649 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 9E970F744D0B9E18

FASTA44552,613
        10         20         30         40         50         60 
MSHDGKEEPG IAKKINSVDD IIIKCQCWVQ KNDEERLAEI LSINTRKAPP KFYVHYVNYN 

        70         80         90        100        110        120 
KRLDEWITTD RINLDKEVLY PKLKATDEDN KKQKKKKATN TSETPQDSLQ DGVDGFSREN 

       130        140        150        160        170        180 
TDVMDLDNLN VQGIKDENIS HEDEIKKLRT SGSMTQNPHE VARVRNLNRI IMGKYEIEPW 

       190        200        210        220        230        240 
YFSPYPIELT DEDFIYIDDF TLQYFGSKKQ YERYRKKCTL RHPPGNEIYR DDYVSFFEID 

       250        260        270        280        290        300 
GRKQRTWCRN LCLLSKLFLD HKTLYYDVDP FLFYCMTRRD ELGHHLVGYF SKEKESADGY 

       310        320        330        340        350        360 
NVACILTLPQ YQRMGYGKLL IEFSYELSKK ENKVGSPEKP LSDLGLLSYR AYWSDTLITL 

       370        380        390        400        410        420 
LVEHQKEITI DEISSMTSMT TTDILHTAKT LNILRYYKGQ HIIFLNEDIL DRYNRLKAKK 

       430        440 
RRTIDPNRLI WKPPVFTASQ LRFAW 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of a 26.9 kb fragment from chromosome XV of the yeast Saccharomyces cerevisiae."
Boyer J., Michaux G., Fairhead C., Gaillon L., Dujon B.
Yeast 12:1575-1586(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"ESA1 is a histone acetyltransferase that is essential for growth in yeast."
Smith E.R., Eisen A., Gu W., Sattah M., Pannuti A., Zhou J., Cook R.G., Lucchesi J.C., Allis C.D.
Proc. Natl. Acad. Sci. U.S.A. 95:3561-3565(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF GLY-315.
[5]"NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p."
Allard S., Utley R.T., Savard J., Clarke A.S., Grant P.A., Brandl C.J., Pillus L., Workman J.L., Cote J.
EMBO J. 18:5108-5119(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A NUA4 COMPLEX WITH TRA1.
[6]"Activation domain-specific and general transcription stimulation by native histone acetyltransferase complexes."
Ikeda K., Steger D.J., Eberharter A., Workman J.L.
Mol. Cell. Biol. 19:855-863(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE NUA4 COMPLEX.
[7]"Esa1p is an essential histone acetyltransferase required for cell cycle progression."
Clarke A.S., Lowell J.E., Jacobson S.J., Pillus L.
Mol. Cell. Biol. 19:2515-2526(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ACETYLATION OF HISTONES H2A; H3 AND H4.
[8]"Distribution of acetylated histones resulting from Gal4-VP16 recruitment of SAGA and NuA4 complexes."
Vignali M., Steger D.J., Neely K.E., Workman J.L.
EMBO J. 19:2629-2640(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE NUA4 COMPLEX.
[9]"Multiple links between the NuA4 histone acetyltransferase complex and epigenetic control of transcription."
Galarneau L., Nourani A., Boudreault A.A., Zhang Y., Heliot L., Allard S., Savard J., Lane W.S., Stillman D.J., Cote J.
Mol. Cell 5:927-937(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, FUNCTION OF THE NUA4 COMPLEX, SUBCELLULAR LOCATION, INTERACTION WITH HISTONES H2A; H3 AND H4.
[10]"Global histone acetylation and deacetylation in yeast."
Vogelauer M., Wu J., Suka N., Grunstein M.
Nature 408:495-498(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION OF HISTONES H2A AND H4.
[11]"Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin."
Suka N., Suka Y., Carmen A.A., Wu J., Grunstein M.
Mol. Cell 8:473-479(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION OF HISTONES H2A; H2B AND H4.
[12]"A conserved motif common to the histone acetyltransferase Esa1 and the histone deacetylase Rpd3."
Adachi N., Kimura A., Horikoshi M.
J. Biol. Chem. 277:35688-35695(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN, MUTAGENESIS OF TRP-247; ASN-250; LEU-251; CYS-252; LEU-253; LEU-254; LYS-256; LEU-259; ASP-260 AND LYS-262.
[13]"Acetylation of histone H4 by Esa1 is required for DNA double-strand break repair."
Bird A.W., Yu D.Y., Pray-Grant M.G., Qiu Q., Harmon K.E., Megee P.C., Grant P.A., Smith M.M., Christman M.F.
Nature 419:411-415(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine 16 and spreading of heterochromatin."
Suka N., Luo K., Grunstein M.
Nat. Genet. 32:378-383(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION OF HISTONE H4.
[15]"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].
[16]"Recruitment of the NuA4 complex poises the PHO5 promoter for chromatin remodeling and activation."
Nourani A., Utley R.T., Allard S., Cote J.
EMBO J. 23:2597-2607(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE NUA4 COMPLEX.
[17]"Global position and recruitment of HATs and HDACs in the yeast genome."
Robert F., Pokholok D.K., Hannett N.M., Rinaldi N.J., Chandy M., Rolfe A., Workman J.L., Gifford D.K., Young R.A.
Mol. Cell 16:199-209(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin."
Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W., Jennings J.L., Link A.J., Madhani H.D., Rine J.
PLoS Biol. 2:587-599(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[19]"Regulation of chromosome stability by the histone H2A variant Htz1, the Swr1 chromatin remodeling complex, and the histone acetyltransferase NuA4."
Krogan N.J., Baetz K., Keogh M.-C., Datta N., Sawa C., Kwok T.C.Y., Thompson N.J., Davey M.G., Pootoolal J., Hughes T.R., Emili A., Buratowski S., Hieter P., Greenblatt J.F.
Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[20]"Dynamic lysine methylation on histone H3 defines the regulatory phase of gene transcription."
Morillon A., Karabetsou N., Nair A., Mellor J.
Mol. Cell 18:723-734(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REGULATION BY HISTONE H3 METHYLATION.
[21]"Localized histone acetylation and deacetylation triggered by the homologous recombination pathway of double-strand DNA repair."
Tamburini B.A., Tyler J.K.
Mol. Cell. Biol. 25:4903-4913(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"The Saccharomyces cerevisiae Piccolo NuA4 histone acetyltransferase complex requires the Enhancer of Polycomb A domain and chromodomain to acetylate nucleosomes."
Selleck W., Fortin I., Sermwittayawong D., Cote J., Tan S.
Mol. Cell. Biol. 25:5535-5542(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN.
[23]"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 SER-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Acetylation of H2AZ Lys 14 is associated with genome-wide gene activity in yeast."
Millar C.B., Xu F., Zhang K., Grunstein M.
Genes Dev. 20:711-722(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION OF HISTONE H2A VARIANT HTZ1.
[25]"MYST protein acetyltransferase activity requires active site lysine autoacetylation."
Yuan H., Rossetto D., Mellert H., Dang W., Srinivasan M., Johnson J., Hodawadekar S., Ding E.C., Speicher K., Abshiru N., Perry R., Wu J., Yang C., Zheng Y.G., Speicher D.W., Thibault P., Verreault A., Johnson F.B. expand/collapse author list , Berger S.L., Sternglanz R., McMahon S.B., Cote J., Marmorstein R.
EMBO J. 31:58-70(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 160-435, ACTIVE SITE, ACETYLATION AT LYS-262.
[26]"Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases."
Yan Y., Barlev N.A., Haley R.H., Berger S.L., Marmorstein R.
Mol. Cell 6:1195-1205(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH COENZYME A.
[27]"The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate."
Yan Y., Harper S., Speicher D.W., Marmorstein R.
Nat. Struct. Biol. 9:862-869(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 162-435 OF MUTANTS GLN-338 AND CYS-304 IN COMPLEX WITH COENZYME A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z75152 Genomic DNA. Translation: CAA99465.1.
BK006948 Genomic DNA. Translation: DAA11012.1.
PIRS67137.
RefSeqNP_014887.3. NM_001183663.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FY7X-ray2.00A160-435[»]
1MJ9X-ray2.50A160-435[»]
1MJAX-ray2.26A160-435[»]
1MJBX-ray2.50A160-435[»]
2RNZNMR-A17-89[»]
2RO0NMR-A1-89[»]
3TO6X-ray2.10A160-435[»]
3TO7X-ray1.90A160-435[»]
3TO9X-ray2.00A160-435[»]
ProteinModelPortalQ08649.
SMRQ08649. Positions 1-89, 160-435.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34635. 632 interactions.
DIPDIP-4115N.
IntActQ08649. 37 interactions.
MINTMINT-511080.
STRING4932.YOR244W.

Proteomic databases

MaxQBQ08649.
PaxDbQ08649.
PeptideAtlasQ08649.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR244W; YOR244W; YOR244W.
GeneID854418.
KEGGsce:YOR244W.

Organism-specific databases

CYGDYOR244w.
SGDS000005770. ESA1.

Phylogenomic databases

eggNOGCOG5027.
GeneTreeENSGT00550000074503.
HOGENOMHOG000182457.
KOK11304.
OMASQLRFAW.
OrthoDBEOG7RFTRR.

Enzyme and pathway databases

BioCycYEAST:G3O-33738-MONOMER.

Gene expression databases

GenevestigatorQ08649.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view]
PfamPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ08649.
NextBio976622.
PROQ08649.

Entry information

Entry nameESA1_YEAST
AccessionPrimary (citable) accession number: Q08649
Secondary accession number(s): D6W2U6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references