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P19880 (YAP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 149. 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:
AP-1-like transcription factor YAP1
Alternative name(s):
Phenanthroline resistance protein PAR1
Pleiotropic drug resistance protein PDR4
Gene names
Name:YAP1
Synonyms:PAR1, PDR4, SNQ3
Ordered Locus Names:YML007W
ORF Names:YM9571.12
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length650 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription activator involved in oxidative stress response and redox homeostasis. Regulates the transcription of genes encoding antioxidant enzymes and components of the cellular thiol-reducing pathways, including the thioredoxin system (TRX2, TRR1), the glutaredoxin system (GSH1, GLR1), superoxide dismutase (SOD1, SOD2), glutathione peroxidase (GPX2), and thiol-specific peroxidases (TSA1, AHP1). The induction of some of these genes requires the cooperative action of both, YAP1 and SKN7. YAP1 preferentially binds to promoters with the core binding site 5'-TTA[CG]TAA-3'. Activity of YAP1 is controlled through oxidation of specific cysteine residues resulting in the alteration of its subcellular location. Oxidative stress (as well as carbon stress, but not increased temperature, acidic pH, or ionic stress) induces nuclear accumulation and as a result YAP1 transcriptional activity. Nuclear export is restored when disulfide bonds are reduced by thioredoxin (TRX2), whose expression is controlled by YAP1, providing a mechanism for negative autoregulation. When overexpressed, YAP1 confers pleiotropic drug-resistance and increases cellular tolerance to cadmium, iron chelators and zinc. Ref.8 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25

Subunit structure

Homodimer By similarity. YAP1 interacts independent of oxidation state in the cytoplasm with the karyopherin PSE1/KAP121 (and less strongly with KAP123). The reduced form of YAP1 interacts in the nucleus with the nuclear export protein CRM1, and in the cytoplasm with YBP1 and the peroxiredoxin HYR1/GPX3/ORP1. Interacts with RBG1. Ref.13 Ref.19 Ref.25

Subcellular location

Nucleus. Cytoplasm. Note: Oxidized YAP1 is found predominantly in the nucleus, while reduced YAP1 is continuously exported to the cytoplasm by CRM1. Nuclear import requires the karyopherin PSE1/KAP121 and is independent on YAP1 oxidation state. Ref.20 Ref.26

Induction

YAP1 expression is at least partially regulated at the level of translation. A small upstream open reading frame (uORF) retains the 40S ribosomal subunit. By leaky scanning it then proceeds and reinitiates at the functional YAP1 ORF.

Domain

YAP1 contains two cysteine rich domains (CRD), referred to as the N- and C-terminal CRD's, n-CRD (Cys-303, Cys-310 and Cys-315) and c-CRD (Cys-598, Cys-620 and Cys-629), respectively. Cys-315 is not conserved in orthologs in other yeast species. A nuclear export signal is embedded in the c-CRD, with which the nuclear export protein CRM1 interacts only in the absence of disulfide bonds within the c-CRD or between the c-CRD and the n-CRD.

Post-translational modification

Depending on the oxidative stress inducing agent, YAP1 can undergo two distinct conformational changes, both involving disulfide bond formation, and both masking the nuclear export signal, thus abolishing nuclear export by CRM1. The disulfide stress-inducing agent diamide leads to the formation of one of three possible disulfide bonds in the c-CRD. Whereas, peroxide stress induces the formation of a disulfide bond between Cys-303 and Cys-598 (and the possibly stabilizing bond between Cys-310 and Cys-629) which is dependent on the hydroperoxide sensing peroxiredoxin HYR1/GPX3/ORP1 and YBP1.

Miscellaneous

One of 8 closely related fungi-specific YAP proteins (YAP1 to YAP8), which all seem to be transcription activators of the environmental stress response and metabolism control pathways and to have similar but not identical DNA binding specificities.

Present with 1600 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the bZIP family. YAP subfamily.

Contains 1 bZIP (basic-leucine zipper) domain.

Sequence caution

The sequence CAA37827.1 differs from that shown. Reason: Frameshift at positions 291 and 306.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CNB1P252962EBI-31265,EBI-3968
YBP1P383154EBI-31265,EBI-20985

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 650650AP-1-like transcription factor YAP1
PRO_0000076521

Regions

Domain64 – 12764bZIP
Region67 – 9024Basic motif By similarity
Region92 – 12029Leucine-zipper By similarity
Region220 – 378159Transcription activation 1 (PubMed:8182076)
Region430 – 537108Transcription activation 2 (PubMed:8182076)
Motif5 – 1612Nuclear localization signal
Motif50 – 5910Nuclear localization signal
Motif614 – 6218Nuclear export signal
Compositional bias411 – 4144Poly-Asn
Compositional bias517 – 5215Poly-Asp

Amino acid modifications

Modified residue91Phosphoserine Ref.32
Modified residue141Phosphoserine Ref.9 Ref.10 Ref.32
Modified residue171Phosphoserine Ref.32
Modified residue1651Phosphothreonine Ref.32
Modified residue2041Phosphoserine Ref.32
Modified residue3721Phosphoserine Ref.12
Modified residue5281Phosphoserine Ref.10 Ref.12 Ref.32
Disulfide bond303 ↔ 598In nuclear retained form; alternate Ref.23 Ref.24
Disulfide bond310 ↔ 629In nuclear retained form; alternate Ref.23 Ref.24
Disulfide bond598 ↔ 629In nuclear retained form; alternate Ref.23 Ref.24
Disulfide bond598 ↔ 620In nuclear retained form; alternate Ref.23 Ref.24
Disulfide bond598Interchain (with C-36 in HYR1); transient; alternate Ref.23 Ref.24
Disulfide bond620 ↔ 629In nuclear retained form; alternate Ref.23 Ref.24

Experimental info

Mutagenesis781Q → A: Dominant negative transcription activator. Ref.8
Mutagenesis6201C → T: Constitutive nuclear location and transcription activation. Ref.26
Sequence conflict3161P → S in CAA43195. Ref.4
Sequence conflict5861D → E in CAA41536. Ref.1
Sequence conflict6481H → D in CAA37827. Ref.2

Secondary structure

.............. 650
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19880 [UniParc].

Last modified October 1, 1993. Version 2.
Checksum: 192F20FA71027688

FASTA65072,533
        10         20         30         40         50         60 
MSVSTAKRSL DVVSPGSLAE FEGSKSRHDE IENEHRRTGT RDGEDSEQPK KKGSKTSKKQ 

        70         80         90        100        110        120 
DLDPETKQKR TAQNRAAQRA FRERKERKMK ELEKKVQSLE SIQQQNEVEA TFLRDQLITL 

       130        140        150        160        170        180 
VNELKKYRPE TRNDSKVLEY LARRDPNLHF SKNNVNHSNS EPIDTPNDDI QENVKQKMNF 

       190        200        210        220        230        240 
TFQYPLDNDN DNDNSKNVGK QLPSPNDPSH SAPMPINQTQ KKLSDATDSS SATLDSLSNS 

       250        260        270        280        290        300 
NDVLNNTPNS STSMDWLDNV IYTNRFVSGD DGSNSKTKNL DSNMFSNDFN FENQFDEQVS 

       310        320        330        340        350        360 
EFCSKMNQVC GTRQCPIPKK PISALDKEVF ASSSILSSNS PALTNTWESH SNITDNTPAN 

       370        380        390        400        410        420 
VIATDATKYE NSFSGFGRLG FDMSANHYVV NDNSTGSTDS TGSTGNKNKK NNNNSDDVLP 

       430        440        450        460        470        480 
FISESPFDMN QVTNFFSPGS TGIGNNAASN TNPSLLQSSK EDIPFINANL AFPDDNSTNI 

       490        500        510        520        530        540 
QLQPFSESQS QNKFDYDMFF RDSSKEGNNL FGEFLEDDDD DKKAANMSDD ESSLIKNQLI 

       550        560        570        580        590        600 
NEEPELPKQY LQSVPGNESE ISQKNGSSLQ NADKINNGND NDNDNDVVPS KEGSLLRCSE 

       610        620        630        640        650 
IWDRITTHPK YSDIDVDGLC SELMAKAKCS ERGVVINAED VQLALNKHMN 

« Hide

References

« Hide 'large scale' references
[1]"Yeast YAP1 encodes a novel form of the jun family of transcriptional activator proteins."
Moye-Rowley W.S., Harshman K.D., Parker C.S.
Genes Dev. 3:283-292(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Characterization of PDR4, a Saccharomyces cerevisiae gene that confers pleiotropic drug resistance in high-copy number: identity with YAP1, encoding a transcriptional activator."
Hussain M., Lenard J.
Gene 101:149-152(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The SNQ3 gene of Saccharomyces cerevisiae confers hyper-resistance to several functionally unrelated chemicals."
Hertle K., Haase E., Brendel M.
Curr. Genet. 19:429-433(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Identification and characterization of a Saccharomyces cerevisiae gene (PAR1) conferring resistance to iron chelators."
Schnell N., Entian K.-D.
Eur. J. Biochem. 200:487-493(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[7]"The PAR1 (YAP1/SNQ3) gene of Saccharomyces cerevisiae, a c-jun homologue, is involved in oxygen metabolism."
Schnell N., Krems B., Entian K.-D.
Curr. Genet. 21:269-273(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[8]"Transcriptional activation mediated by the yeast AP-1 protein is required for normal cadmium tolerance."
Wemmie J.A., Wu A.L., Harshman K.D., Parker C.S., Moye-Rowley W.S.
J. Biol. Chem. 269:14690-14697(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLN-78.
[9]"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-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: YAL6B.
[10]"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-14 AND SER-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[11]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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-372 AND SER-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Saccharomyces cerevisiae Rbg1 protein and its binding partner Gir2 interact on polyribosomes with Gcn1."
Wout P.K., Sattlegger E., Sullivan S.M., Maddock J.R.
Eukaryot. Cell 8:1061-1071(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RBG1.
[14]"Yap, a novel family of eight bZIP proteins in Saccharomyces cerevisiae with distinct biological functions."
Fernandes L., Rodrigues-Pousada C., Struhl K.
Mol. Cell. Biol. 17:6982-6993(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DNA-BINDING.
[15]"Crm1p mediates regulated nuclear export of a yeast AP-1-like transcription factor."
Yan C., Lee L.H., Davis L.I.
EMBO J. 17:7416-7429(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, NUCLEAR EXPORT BY CRM1, NUCLEAR EXPORT SIGNAL.
[16]"The yeast transcription factor genes YAP1 and YAP2 are subject to differential control at the levels of both translation and mRNA stability."
Vilela C., Linz B., Rodrigues-Pousada C., McCarthy J.E.
Nucleic Acids Res. 26:1150-1159(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, POST-TRANSCRIPTIONAL EXPRESSION CONTROL.
[17]"Yap1 and Skn7 control two specialized oxidative stress response regulons in yeast."
Lee J., Godon C., Lagniel G., Spector D., Garin J., Labarre J., Toledano M.B.
J. Biol. Chem. 274:16040-16046(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, COOPERATIVITY WITH SKN7, YAP1 DEPENDENT GENES.
[18]"H2O2 sensing through oxidation of the Yap1 transcription factor."
Delaunay A., Isnard A.D., Toledano M.B.
EMBO J. 19:5157-5166(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, REDUCTION BY THIOREDOXINS.
[19]"Nuclear import of the yeast AP-1-like transcription factor Yap1p is mediated by transport receptor Pse1p, and this import step is not affected by oxidative stress."
Isoyama T., Murayama A., Nomoto A., Kuge S.
J. Biol. Chem. 276:21863-21869(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, NUCLEAR IMPORT, INTERACTION WITH PSE1.
[20]"Regulation of the yeast Yap1p nuclear export signal is mediated by redox signal-induced reversible disulfide bond formation."
Kuge S., Arita M., Murayama A., Maeta K., Izawa S., Inoue Y., Nomoto A.
Mol. Cell. Biol. 21:6139-6150(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[21]"A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation."
Delaunay A., Pflieger D., Barrault M.-B., Vinh J., Toledano M.B.
Cell 111:471-481(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, OXIDATION BY HYR1/GPX3.
[22]"Yap1 accumulates in the nucleus in response to carbon stress in Saccharomyces cerevisiae."
Wiatrowski H.A., Carlson M.
Eukaryot. Cell 2:19-26(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[23]"The redox domain of the Yap1p transcription factor contains two disulfide bonds."
Wood M.J., Andrade E.C., Storz G.
Biochemistry 42:11982-11991(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, OXIDATION, DISULFIDE BONDS.
[24]"Two redox centers within Yap1 for H2O2 and thiol-reactive chemicals signaling."
Azevedo D., Tacnet F., Delaunay A., Rodrigues-Pousada C., Toledano M.B.
Free Radic. Biol. Med. 35:889-900(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ELICITOR SPECIFIC DISULFIDE BONDS.
[25]"Ybp1 is required for the hydrogen peroxide-induced oxidation of the Yap1 transcription factor."
Veal E.A., Ross S.J., Malakasi P., Peacock E., Morgan B.A.
J. Biol. Chem. 278:30896-30904(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH YBP1.
[26]"Regulation of yAP-1 nuclear localization in response to oxidative stress."
Kuge S., Jones N., Nomoto A.
EMBO J. 16:1710-1720(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-620, SUBCELLULAR LOCATION.
[27]"A large-scale study of Yap1p-dependent genes in normal aerobic and H2O2-stress conditions: the role of Yap1p in cell proliferation control in yeast."
Dumond H., Danielou N., Pinto M., Bolotin-Fukuhara M.
Mol. Microbiol. 36:830-845(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TRANSCRIPTION PROFILING.
[28]"Genomic expression programs in the response of yeast cells to environmental changes."
Gasch A.P., Spellman P.T., Kao C.M., Carmel-Harel O., Eisen M.B., Storz G., Botstein D., Brown P.O.
Mol. Biol. Cell 11:4241-4257(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TRANSCRIPTION PROFILING.
[29]"Transcription factors regulating the response to oxidative stress in yeast."
Moye-Rowley W.S.
Antioxid. Redox Signal. 4:123-140(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[30]"Thiol-based regulatory switches."
Paget M.S., Buttner M.J.
Annu. Rev. Genet. 37:91-121(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[31]"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].
[32]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-14; SER-17; THR-165; SER-204 AND SER-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58693 Genomic DNA. Translation: CAA41536.1.
X53830 Genomic DNA. Translation: CAA37827.1. Frameshift.
X60780 Genomic DNA. Translation: CAA43195.1.
X63268 Genomic DNA. Translation: CAA44917.1.
Z49810 Genomic DNA. Translation: CAA89945.1.
BK006946 Genomic DNA. Translation: DAA09892.1.
PIRS16706.
RefSeqNP_013707.1. NM_001182362.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SSENMR-A279-313[»]
B565-650[»]
ProteinModelPortalP19880.
SMRP19880. Positions 63-125, 279-313, 565-650.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35163. 172 interactions.
DIPDIP-1752N.
IntActP19880. 41 interactions.
MINTMINT-505627.

Proteomic databases

PaxDbP19880.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYML007W; YML007W; YML007W.
GeneID855005.
KEGGsce:YML007W.

Organism-specific databases

CYGDYML007w.
SGDS000004466. YAP1.

Phylogenomic databases

eggNOGNOG72873.
GeneTreeENSGT00530000069148.
HOGENOMHOG000142347.
KOK09043.
OMANEACGTK.
OrthoDBEOG7GFBHK.

Enzyme and pathway databases

BioCycYEAST:G3O-32612-MONOMER.

Gene expression databases

GenevestigatorP19880.

Family and domain databases

Gene3D1.10.238.100. 1 hit.
InterProIPR004827. bZIP.
IPR013910. TF_PAP1.
IPR023167. Yap1_redox_dom.
[Graphical view]
PfamPF00170. bZIP_1. 1 hit.
PF08601. PAP1. 1 hit.
[Graphical view]
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP19880.
NextBio978163.

Entry information

Entry nameYAP1_YEAST
AccessionPrimary (citable) accession number: P19880
Secondary accession number(s): D6VZG8, P22631, Q06840
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 1, 1993
Last modified: March 19, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: 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