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P19097 (FAS2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 146. 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
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:
Fatty acid synthase subunit alpha
EC=2.3.1.86

Including the following 3 domains:

  1. Acyl carrier
  2. 3-oxoacyl-[acyl-carrier-protein] reductase
    EC=1.1.1.100
    Alternative name(s):
    Beta-ketoacyl reductase
  3. 3-oxoacyl-[acyl-carrier-protein] synthase
    EC=2.3.1.41
    Alternative name(s):
    Beta-ketoacyl synthase
Gene names
Name:FAS2
Ordered Locus Names:YPL231W
ORF Names:P1409
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length1887 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex.

Catalytic activity

Acetyl-CoA + n malonyl-CoA + 2n NADH + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO2 + 2n NAD+ + 2n NADP+.

Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.

Enzyme regulation

Inhibited by cerulenin by covalent binding to active site of the ketoacyl synthase (KS) region. Ref.13

Subunit structure

[Alpha6beta6] hexamers of two multifunctional subunits (alpha and beta). Ref.11 Ref.12

Post-translational modification

4'-phosphopantetheine is transferred from CoA to a specific serine of the Acyl carrier domain by the C-terminal PPT domain. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.

Miscellaneous

Present with 17000 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the fungal fatty acid synthetase subunit alpha family.

Contains 1 acyl carrier domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FAS1P071493EBI-6806,EBI-6795

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18871887Fatty acid synthase subunit alpha
PRO_0000180287

Regions

Domain140 – 301162Acyl carrier
Region675 – 874200Beta-ketoacyl reductase
Region1149 – 1363215Beta-ketoacyl synthase
Region1772 – 17743Acetyl-CoA binding
Region1817 – 183317Acetyl-CoA binding
Region1841 – 18444Acetyl-CoA binding
Region1871 – 18733Acetyl-CoA binding

Sites

Active site13051For beta-ketoacyl synthase activity
Metal binding17721Magnesium
Metal binding17731Magnesium; via carbonyl oxygen
Metal binding17741Magnesium
Metal binding18721Magnesium
Metal binding18731Magnesium; via carbonyl oxygen
Binding site17981Acetyl-CoA
Binding site18081Acetyl-CoA

Amino acid modifications

Modified residue501Phosphoserine Ref.7 Ref.10
Modified residue1801O-(pantetheine 4'-phosphoryl)serine
Modified residue5231Phosphoserine Ref.10
Modified residue5641Phosphoserine Ref.10
Modified residue5671Phosphothreonine Ref.9
Modified residue9581Phosphoserine Ref.8 Ref.10
Modified residue14401Phosphoserine Ref.8 Ref.10

Experimental info

Mutagenesis12501G → S: Cerulenin-resistance. Ref.5
Mutagenesis17691V → D: Does not affect oligomerization; when associated with S-1771 and L-1773 or S-1771; L-1773; S-1879 and E-1881. Ref.14
Mutagenesis17701G → D: Loss of transferase activity. Ref.14
Mutagenesis17711V → S: Does not affect oligomerization but lacks transferase activity; when associated with D-1769 and L-1773 or D-1769; L-1773; S-1879 and E-1881. Ref.14
Mutagenesis17721D → S: Loss of transferase activity; when associated with S-1774. Ref.14
Mutagenesis17731V → L: Does not affect oligomerization but lacks transferase activity; when associated with D-1769 and S-1771 or D-1769; S-1771; S-1879 and E-1881. Ref.14
Mutagenesis17741E → S: Loss of transferase activity; when associated with S-1772. Ref.14
Mutagenesis18411R → A: Loss off transferase activity. Ref.14
Mutagenesis18791V → S: Does not affect oligomerization but lacks transferase activity; when associated with D-1769; S-1771; L-1773 and E-1881. Ref.14
Mutagenesis18811V → E: Does not affect oligomerization but lacks transferase activity; when associated with D-1769; S-1771; L-1773 and S-1879. Ref.14
Sequence conflict3101G → GTTGTGG in AAA34601. Ref.1
Sequence conflict5941T → I in AAA34601. Ref.1
Sequence conflict941 – 101979AKLRK…LERVI → CLNCVKSWLKLLKLERQFPS KLLWSIRLSMAIALMLHMLK SKFNQELTFNWTSQNRNHTN RLNKLLPLSLRVCWIWKELF in AAA34601. Ref.1
Sequence conflict1036 – 10416RWEMEA → KMGNGS in AAA34601. Ref.1
Sequence conflict14081A → S in AAA34601. Ref.1
Sequence conflict16711N → T in AAA34601. Ref.1

Secondary structure

1 ................................................................................................................................................................................................................................................................................. 1887
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19097 [UniParc].

Last modified May 15, 2002. Version 2.
Checksum: 08B872734CF3AEEA

FASTA1,887206,947
        10         20         30         40         50         60 
MKPEVEQELA HILLTELLAY QFASPVRWIE TQDVFLKDFN TERVVEIGPS PTLAGMAQRT 

        70         80         90        100        110        120 
LKNKYESYDA ALSLHREILC YSKDAKEIYY TPDPSELAAK EEPAKEEAPA PTPAASAPAP 

       130        140        150        160        170        180 
AAAAPAPVAA AAPAAAAAEI ADEPVKASLL LHVLVAHKLK KSLDSIPMSK TIKDLVGGKS 

       190        200        210        220        230        240 
TVQNEILGDL GKEFGTTPEK PEETPLEELA ETFQDTFSGA LGKQSSSLLS RLISSKMPGG 

       250        260        270        280        290        300 
FTITVARKYL QTRWGLPSGR QDGVLLVALS NEPAARLGSE ADAKAFLDSM AQKYASIVGV 

       310        320        330        340        350        360 
DLSSAASASG AAGAGAAAGA AMIDAGALEE ITKDHKVLAR QQLQVLARYL KMDLDNGERK 

       370        380        390        400        410        420 
FLKEKDTVAE LQAQLDYLNA ELGEFFVNGV ATSFSRKKAR TFDSSWNWAK QSLLSLYFEI 

       430        440        450        460        470        480 
IHGVLKNVDR EVVSEAINIM NRSNDALIKF MEYHISNTDE TKGENYQLVK TLGEQLIENC 

       490        500        510        520        530        540 
KQVLDVDPVY KDVAKPTGPK TAIDKNGNIT YSEEPREKVR KLSQYVQEMA LGGPITKESQ 

       550        560        570        580        590        600 
PTIEEDLTRV YKAISAQADK QDISSSTRVE FEKLYSDLMK FLESSKEIDP SQTTQLAGMD 

       610        620        630        640        650        660 
VEDALDKDST KEVASLPNKS TISKTVSSTI PRETIPFLHL RKKTPAGDWK YDRQLSSLFL 

       670        680        690        700        710        720 
DGLEKAAFNG VTFKDKYVLI TGAGKGSIGA EVLQGLLQGG AKVVVTTSRF SKQVTDYYQS 

       730        740        750        760        770        780 
IYAKYGAKGS TLIVVPFNQG SKQDVEALIE FIYDTEKNGG LGWDLDAIIP FAAIPEQGIE 

       790        800        810        820        830        840 
LEHIDSKSEF AHRIMLTNIL RMMGCVKKQK SARGIETRPA QVILPMSPNH GTFGGDGMYS 

       850        860        870        880        890        900 
ESKLSLETLF NRWHSESWAN QLTVCGAIIG WTRGTGLMSA NNIIAEGIEK MGVRTFSQKE 

       910        920        930        940        950        960 
MAFNLLGLLT PEVVELCQKS PVMADLNGGL QFVPELKEFT AKLRKELVET SEVRKAVSIE 

       970        980        990       1000       1010       1020 
TALEHKVVNG NSADAAYAQV EIQPRANIQL DFPELKPYKQ VKQIAPAELE GLLDLERVIV 

      1030       1040       1050       1060       1070       1080 
VTGFAEVGPW GSARTRWEME AFGEFSLEGC VEMAWIMGFI SYHNGNLKGR PYTGWVDSKT 

      1090       1100       1110       1120       1130       1140 
KEPVDDKDVK AKYETSILEH SGIRLIEPEL FNGYNPEKKE MIQEVIVEED LEPFEASKET 

      1150       1160       1170       1180       1190       1200 
AEQFKHQHGD KVDIFEIPET GEYSVKLLKG ATLYIPKALR FDRLVAGQIP TGWNAKTYGI 

      1210       1220       1230       1240       1250       1260 
SDDIISQVDP ITLFVLVSVV EAFIASGITD PYEMYKYVHV SEVGNCSGSG MGGVSALRGM 

      1270       1280       1290       1300       1310       1320 
FKDRFKDEPV QNDILQESFI NTMSAWVNML LISSSGPIKT PVGACATSVE SVDIGVETIL 

      1330       1340       1350       1360       1370       1380 
SGKARICIVG GYDDFQEEGS FEFGNMKATS NTLEEFEHGR TPAEMSRPAT TTRNGFMEAQ 

      1390       1400       1410       1420       1430       1440 
GAGIQIIMQA DLALKMGVPI YGIVAMAATA TDKIGRSVPA PGKGILTTAR EHHSSVKYAS 

      1450       1460       1470       1480       1490       1500 
PNLNMKYRKR QLVTREAQIK DWVENELEAL KLEAEEIPSE DQNEFLLERT REIHNEAESQ 

      1510       1520       1530       1540       1550       1560 
LRAAQQQWGN DFYKRDPRIA PLRGALATYG LTIDDLGVAS FHGTSTKAND KNESATINEM 

      1570       1580       1590       1600       1610       1620 
MKHLGRSEGN PVIGVFQKFL TGHPKGAAGA WMMNGALQIL NSGIIPGNRN ADNVDKILEQ 

      1630       1640       1650       1660       1670       1680 
FEYVLYPSKT LKTDGVRAVS ITSFGFGQKG GQAIVVHPDY LYGAITEDRY NEYVAKVSAR 

      1690       1700       1710       1720       1730       1740 
EKSAYKFFHN GMIYNKLFVS KEHAPYTDEL EEDVYLDPLA RVSKDKKSGS LTFNSKNIQS 

      1750       1760       1770       1780       1790       1800 
KDSYINANTI ETAKMIENMT KEKVSNGGVG VDVELITSIN VENDTFIERN FTPQEIEYCS 

      1810       1820       1830       1840       1850       1860 
AQPSVQSSFA GTWSAKEAVF KSLGVKSLGG GAALKDIEIV RVNKNAPAVE LHGNAKKAAE 

      1870       1880 
EAGVTDVKVS ISHDDLQAVA VAVSTKK

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of the multifunctional alpha subunit protein of yeast fatty acid synthase derived from FAS2 gene sequence."
Mohamed A.H., Chirala S.S., Mody N.H., Huang W.Y., Wakil S.J.
J. Biol. Chem. 263:12315-12325(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Schueller H.-J.
Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 26786 / X2180-1A.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Cerulenin-resistant mutants of Saccharomyces cerevisiae with an altered fatty acid synthase gene."
Inokoshi J., Tomoda H., Hashimoto H., Watanabe A., Takeshima H., Omura S.
Mol. Gen. Genet. 244:90-96(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-1250.
Strain: ATCC 204508 / S288c.
[6]"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].
[7]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, MASS SPECTROMETRY.
Strain: YAL6B.
[8]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-958 AND SER-1440, MASS SPECTROMETRY.
Strain: ADR376.
[9]"Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-567, MASS SPECTROMETRY.
Strain: ATCC 76625 / YPH499.
[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 SER-50; SER-523; SER-564; SER-958 AND SER-1440, MASS SPECTROMETRY.
[11]"The crystal structure of yeast fatty acid synthase, a cellular machine with eight active sites working together."
Lomakin I.B., Xiong Y., Steitz T.A.
Cell 129:319-332(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 671-1744 IN COMPLEX WITH FAS1, SUBUNIT.
[12]"Structural basis for substrate delivery by acyl carrier protein in the yeast fatty acid synthase."
Leibundgut M., Jenni S., Frick C., Ban N.
Science 316:288-290(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH FAS1, SUBUNIT, MODIFICATION AT SER-180.
[13]"Inhibition of the fungal fatty acid synthase type I multienzyme complex."
Johansson P., Wiltschi B., Kumari P., Kessler B., Vonrhein C., Vonck J., Oesterhelt D., Grininger M.
Proc. Natl. Acad. Sci. U.S.A. 105:12803-12808(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) IN COMPLEX WITH FAS1 AND THE INHIBITOR CERULENIN, ENZYME REGULATION.
[14]"Multimeric options for the auto-activation of the Saccharomyces cerevisiae FAS type I megasynthase."
Johansson P., Mulinacci B., Koestler C., Vollrath R., Oesterhelt D., Grininger M.
Structure 17:1063-1074(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1766-1887 IN COMPLEX WITH FAS1 AND ACETYL-COA, MUTAGENESIS OF VAL-1769; GLY-1770; VAL-1771; ASP-1772; VAL-1773; GLU-1774; ARG-1841; VAL-1879 AND VAL-1881, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J03936 Genomic DNA. Translation: AAA34601.1.
X76890 Genomic DNA. Translation: CAA54218.1.
X94561 Genomic DNA. Translation: CAA64256.1.
Z73586 Genomic DNA. Translation: CAA97947.1.
Z73587 Genomic DNA. Translation: CAA97948.1.
BK006949 Genomic DNA. Translation: DAA11205.1.
PIRS61703.
RefSeqNP_015093.1. NM_001184045.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PFFX-ray4.00A/D/G671-1744[»]
2UV8X-ray3.10A/B/C1-1887[»]
2VKZX-ray4.00A/B/C1-1887[»]
2WASX-ray1.90A/B/C/D/E/F1766-1887[»]
2WATX-ray2.20A/B/C/D/E/F1766-1887[»]
3HMJX-ray4.00A/B/C1-1887[»]
ProteinModelPortalP19097.
SMRP19097. Positions 1766-1886.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-960N.
IntActP19097. 14 interactions.
MINTMINT-659193.
STRING4932.YPL231W.

Proteomic databases

PaxDbP19097.
PeptideAtlasP19097.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL231W; YPL231W; YPL231W.
GeneID855845.
KEGGsce:YPL231W.

Organism-specific databases

CYGDYPL231w.
SGDS000006152. FAS2.

Phylogenomic databases

eggNOGCOG4982.
HOGENOMHOG000177974.
KOK00667.
OMAFINTMSA.
OrthoDBEOG4VHPFG.

Enzyme and pathway databases

BioCycMetaCyc:YPL231W-MONOMER.
SABIO-RKP19097.

Gene expression databases

GenevestigatorP19097.
GermOnlineYPL231W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D3.40.366.10. 1 hit.
3.40.47.10. 3 hits.
3.40.50.720. 1 hit.
3.90.470.20. 1 hit.
InterProIPR008278. 4-PPantetheinyl_Trfase_SF.
IPR001227. Ac_transferase_dom.
IPR002582. ACPS.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR026025. FAS_alpha_yeast.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016040. NAD(P)-bd_dom.
IPR004568. PPantethiene-prot_Trfase_dom.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamPF01648. ACPS. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
PIRSFPIRSF000454. FAS_yeast_alpha. 1 hit.
ProDomPD004282. PPantethiene-prot_Trfase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF56214. 4-PPT_transf. 1 hit.
SSF52151. Acyl_Trfase/lysoPlipase. 1 hit.
SSF53901. Thiolase-like. 2 hits.
TIGRFAMsTIGR00556. pantethn_trn. 1 hit.
PROSITEPS50075. ACP_DOMAIN. False negative.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP19097.
NextBio980431.

Entry information

Entry nameFAS2_YEAST
AccessionPrimary (citable) accession number: P19097
Secondary accession number(s): D6W3D9, Q12533
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 15, 2002
Last modified: April 3, 2013
This is version 146 of the entry and version 2 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

Yeast chromosome XVI

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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