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P53550 (DCP2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. 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:
mRNA-decapping enzyme subunit 2

EC=3.-.-.-
Alternative name(s):
Protein PSU1
Gene names
Name:DCP2
Synonyms:PSU1
Ordered Locus Names:YNL118C
ORF Names:N1917
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length970 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body. Ref.9 Ref.11 Ref.12 Ref.14

Cofactor

Manganese By similarity.

Subunit structure

Component of the decapping complex composed of DCP1 and DCP2. Interacts with mRNA, LSM2, LSM4 and LSM8. Interacts with EDC3. Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.16

Subcellular location

CytoplasmP-body. Note: Is concentrated in several cytoplasmic foci called P bodies (or cytoplasmic processing bodies) which represent sites of mRNA decapping and 5' to 3' exonucleotidic decay. Ref.15

Miscellaneous

Present with 8530 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the Nudix hydrolase family. DCP2 subfamily.

Contains 1 nudix hydrolase domain.

Ontologies

Keywords
   Biological processmRNA processing
Nonsense-mediated mRNA decay
   Cellular componentCytoplasm
   LigandManganese
Metal-binding
RNA-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdeadenylation-dependent decapping of nuclear-transcribed mRNA

Inferred from direct assay Ref.9Ref.11. Source: SGD

deadenylation-independent decapping of nuclear-transcribed mRNA

Inferred from mutant phenotype PubMed 15225544. Source: SGD

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of transcription initiation from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 23706738. Source: SGD

stress granule assembly

Inferred from mutant phenotype PubMed 20513766. Source: SGD

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 23706738. Source: SGD

cytoplasmic mRNA processing body

Inferred from direct assay Ref.15. Source: SGD

nucleus

Inferred from direct assay PubMed 23706738. Source: SGD

   Molecular_functionchromatin binding

Inferred from direct assay PubMed 23706738. Source: SGD

hydrolase activity

Inferred from direct assay PubMed 12486012. Source: SGD

m7G(5')pppN diphosphatase activity

Inferred from direct assay PubMed 16341225. Source: SGD

mRNA binding

Inferred from physical interaction Ref.11. Source: SGD

manganese ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DCP1Q125175EBI-270,EBI-38519
EDC3P399987EBI-270,EBI-22300

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 970970mRNA-decapping enzyme subunit 2
PRO_0000057054

Regions

Domain101 – 228128Nudix hydrolase
Motif134 – 15522Nudix box
Compositional bias345 – 43086Pro-rich
Compositional bias436 – 4394Poly-Ser

Sites

Metal binding1491Manganese By similarity
Metal binding1531Manganese By similarity

Amino acid modifications

Modified residue1161Phosphoserine Ref.17
Modified residue4391Phosphoserine Ref.18
Modified residue6771Phosphothreonine Ref.18
Modified residue6791Phosphoserine Ref.6 Ref.18
Modified residue6821Phosphoserine Ref.17 Ref.18
Modified residue7511Phosphoserine Ref.6 Ref.17 Ref.18
Modified residue7711Phosphoserine Ref.18
Modified residue7731Phosphoserine Ref.18
Modified residue7781Phosphoserine Ref.18

Natural variations

Natural variant1881V → A in strain: YJM339. Ref.3
Natural variant2881Missing in strain: V1-09, YJM269, YJM270, YJM326, YJM339, YJM627 and YJM1129. Ref.3
Natural variant3011L → H in strain: YJM280, YJM 20 and YJM339. Ref.3
Natural variant3191S → P in strain: YJM627. Ref.3
Natural variant4941D → N in strain: YJM339. Ref.3
Natural variant5051I → T in strain: SK1, V1-09, YJM269, YJM270, YJM280, YJM320, YJM326, YJM339, YJM627 and YJM1129. Ref.3
Natural variant5221G → D in strain: YJM269, YJM270, YJM326 and YJM1129. Ref.3
Natural variant5471N → T in strain: YJM280 and YJM320. Ref.3
Natural variant5671S → R in strain: YJM269, YJM270, YJM326 and YJM1129. Ref.3
Natural variant5741N → S in strain: YJM269, YJM270, YJM280, YJM320, YJM326 and YJM1129. Ref.3
Natural variant5771S → N in strain: V1-09, YJM269, YJM270, YJM280, YJM320, YJM326, YJM339 and YJM1129. Ref.3
Natural variant6221G → S in strain: V1-09 and YJM339. Ref.3
Natural variant6501D → G in strain: YJM280 and YJM320. Ref.3
Natural variant7401P → S in strain: YJM269 and YJM270. Ref.3
Natural variant8071T → A in strain: YJM 69, YJM270, YJM326 and YJM1129. Ref.3
Natural variant8231S → P in strain: YJM269, YJM270, YJM280, YJM320, YJM326 and YJM1129. Ref.3
Natural variant8351D → N in strain: YJM280 and YJM320. Ref.3
Natural variant8441G → V in strain: V1-09. Ref.3
Natural variant8511S → P in strain: YJM280, YJM320 and YJM627. Ref.3
Natural variant8541M → I in strain: YJM269, YJM270, YJM326 and YJM1129. Ref.3
Natural variant8641E → Q in strain: YJM269 and YJM270. Ref.3
Natural variant8651L → S in strain: YJM269, YJM270, YJM326 and YJM1129. Ref.3
Natural variant8661D → A in strain: YJM627.
Natural variant9091A → T in strain: YJM280 and YJM320. Ref.3
Natural variant9451I → L in strain: YJM627. Ref.3
Natural variant9511D → E in strain: V1-09. Ref.3

Experimental info

Mutagenesis601N → D in DCP2-7; impairs mRNA decay at 37 degrees Celsius; when associated with V-68 and V-142. Ref.11
Mutagenesis681I → V in DCP2-7; impairs mRNA decay at 37 degrees Celsius; when associated with D-60 and V-142. Ref.11
Mutagenesis1421D → V in DCP2-7; impairs mRNA decay at 37 degrees Celsius; when associated with D-60 and V-68. Ref.11
Sequence conflict4251P → L in AAA68866. Ref.2

Secondary structure

............................. 970
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53550 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: D53CA2C5A546FA4A

FASTA970108,667
        10         20         30         40         50         60 
MSLPLRHALE NVTSVDRILE DLLVRFIINC PNEDLSSVER ELFHFEEASW FYTDFIKLMN 

        70         80         90        100        110        120 
PTLPSLKIKS FAQLIIKLCP LVWKWDIRVD EALQQFSKYK KSIPVRGAAI FNENLSKILL 

       130        140        150        160        170        180 
VQGTESDSWS FPRGKISKDE NDIDCCIREV KEEIGFDLTD YIDDNQFIER NIQGKNYKIF 

       190        200        210        220        230        240 
LISGVSEVFN FKPQVRNEID KIEWFDFKKI SKTMYKSNIK YYLINSMMRP LSMWLRHQRQ 

       250        260        270        280        290        300 
IKNEDQLKSY AEEQLKLLLG ITKEEQIDPG RELLNMLHTA VQANSNNNAV SNGQVPSSQE 

       310        320        330        340        350        360 
LQHLKEQSGE HNQQKDQQSS FSSQQQPSIF PSLSEPFANN KNVIPPTMPM ANVFMSNPQL 

       370        380        390        400        410        420 
FATMNGQPFA PFPFMLPLTN NSNSANPIPT PVPPNFNAPP NPMAFGVPNM HNLSGPAVSQ 

       430        440        450        460        470        480 
PFSLPPAPLP RDSGYSSSSP GQLLDILNSK KPDSNVQSSK KPKLKILQRG TDLNSIKQNN 

       490        500        510        520        530        540 
NDETAHSNSQ ALLDLLKKPT SSQKIHASKP DTSFLPNDSV SGIQDAEYED FESSSDEEVE 

       550        560        570        580        590        600 
TARDERNSLN VDIGVNVMPS EKDSRRSQKE KPRNDASKTN LNASAESNSV EWGPGKSSPS 

       610        620        630        640        650        660 
TQSKQNSSVG MQNKYRQEIH IGDSDAYEVF ESSSDEEDGK KLEELEQTQD NSKLISQDIL 

       670        680        690        700        710        720 
KENNFQDGEV PHRDMPTESN KSINETVGLS STTNTVKKVP KVKILKRGET FASLANDKKA 

       730        740        750        760        770        780 
FDSSSNVSSS KDLLQMLRNP ISSTVSSNQQ SPKSQHLSGD EEIMMMLKRN SVSKPQNSEE 

       790        800        810        820        830        840 
NASTSSINDA NASELLGMLK QKEKDITAPK QPYNVDSYSQ KNSAKGLLNI LKKNDSTGYP 

       850        860        870        880        890        900 
RTEGGPSSEM STSMKRNDAT NNQELDKNST ELLNYLKPKP LNDGYENISN KDSSHELLNI 

       910        920        930        940        950        960 
LHGNKNSSAF NNNVYATDGY SLASDNNENS SNKLLNMLQN RSSAINEPNF DVRSNGTSGS 

       970 
NELLSILHRK 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a novel component of the nonsense-mediated mRNA decay pathway by use of an interacting protein screen."
He F., Jacobson A.
Genes Dev. 9:437-454(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Tzagoloff A.A.
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 24657 / D273-10B.
[3]"Sequential elimination of major-effect contributors identifies additional quantitative trait loci conditioning high-temperature growth in yeast."
Sinha H., David L., Pascon R.C., Clauder-Muenster S., Krishnakumar S., Nguyen M., Shi G., Dean J., Davis R.W., Oefner P.J., McCusker J.H., Steinmetz L.M.
Genetics 180:1661-1670(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-188; ASN-288 DEL; HIS-301; PRO-319; ASN-494; THR-505; ASP-522; THR-547; ARG-567; SER-574; ASN-577; SER-622; GLY-650; SER-740; ALA-807; PRO-823; ASN-835; VAL-844; PRO-851; ILE-854; GLN-864; SER-865; THR-909; LEU-945 AND GLU-951.
Strain: ATCC 200060 / W303, S103, SK1, V1-09, YJM 1129, YJM 269, YJM 270, YJM 320, YJM 326, YJM 339, YJM 627 and YJM230.
[4]"The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces cerevisiae reveals an unusually high number of overlapping open reading frames."
de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D., Pallavicini A., Lanfranchi G., Valle G.
Yeast 13:261-266(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. expand/collapse author list , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"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-679 AND SER-751, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[7]"Crystal structure of human Edc3 and its functional implications."
Ling S.H., Decker C.J., Walsh M.A., She M., Parker R., Song H.
Mol. Cell. Biol. 28:5965-5976(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EDC3.
[8]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[9]"The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif."
Dunckley T., Parker R.
EMBO J. 18:5411-5422(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DCP1.
[10]"Genome-wide protein interaction screens reveal functional networks involving Sm-like proteins."
Fromont-Racine M., Mayes A.E., Brunet-Simon A., Rain J.-C., Colley A., Dix I., Decourty L., Joly N., Ricard F., Beggs J.D., Legrain P.
Yeast 17:95-110(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LSM2; LSM4 AND LSM8.
[11]"Two related proteins, Edc1p and Edc2p, stimulate mRNA decapping in Saccharomyces cerevisiae."
Dunckley T., Tucker M., Parker R.
Genetics 157:27-37(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASN-60; ILE-68 AND ASP-142, INTERACTION WITH EDC1.
[12]"Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs."
Tharun S., Parker R.
Mol. Cell 8:1075-1083(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MRNA, FUNCTION OF THE DCP1-DCP2 COMPLEX.
[13]"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].
[14]"Analysis of recombinant yeast decapping enzyme."
Steiger M., Carr-Schmid A., Schwartz D.C., Kiledjian M., Parker R.
RNA 9:231-238(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE DCP1-DCP2 COMPLEX.
[15]"Decapping and decay of messenger RNA occur in cytoplasmic processing bodies."
Sheth U., Parker R.
Science 300:805-808(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[16]"Crystal structure of Dcp1p and its functional implications in mRNA decapping."
She M., Decker C.J., Sundramurthy K., Liu Y., Chen N., Parker R., Song H.
Nat. Struct. Mol. Biol. 11:249-256(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DCP1.
[17]"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-116; SER-682 AND SER-751, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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-439; THR-677; SER-679; SER-682; SER-751; SER-771; SER-773 AND SER-778, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"mRNA decapping is promoted by an RNA-binding channel in Dcp2."
Deshmukh M.V., Jones B.N., Quang-Dang D.U., Flinders J., Floor S.N., Kim C., Jemielity J., Kalek M., Darzynkiewicz E., Gross J.D.
Mol. Cell 29:324-336(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 100-245.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U31377 Genomic DNA. Translation: AAC99860.1.
L43065 Genomic DNA. Translation: AAA68866.1.
EF125216 Genomic DNA. Translation: ABN58539.1.
EF125217 Genomic DNA. Translation: ABN58548.1.
EF125218 Genomic DNA. Translation: ABN58557.1.
EF125219 Genomic DNA. Translation: ABN58566.1.
EF125220 Genomic DNA. Translation: ABN58578.1.
EF125221 Genomic DNA. Translation: ABN58584.1.
EF125222 Genomic DNA. Translation: ABN58593.1.
EF125223 Genomic DNA. Translation: ABN58602.1.
EF125224 Genomic DNA. Translation: ABN58611.1.
EF125225 Genomic DNA. Translation: ABN58620.1.
EF125226 Genomic DNA. Translation: ABN58629.1.
EF125228 Genomic DNA. Translation: ABN58647.1.
Z69382 Genomic DNA. Translation: CAA93389.1.
Z71394 Genomic DNA. Translation: CAA95998.1.
BK006947 Genomic DNA. Translation: DAA10430.1.
PIRS63059.
RefSeqNP_014281.1. NM_001182956.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JVBNMR-A100-245[»]
4K6EX-ray2.10A102-245[»]
4KG3X-ray1.70A/B/C100-245[»]
4KG4X-ray1.80A/B100-245[»]
ProteinModelPortalP53550.
SMRP53550. Positions 8-279.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35708. 140 interactions.
DIPDIP-969N.
IntActP53550. 43 interactions.
MINTMINT-385102.

Proteomic databases

PeptideAtlasP53550.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL118C; YNL118C; YNL118C.
GeneID855605.
KEGGsce:YNL118C.

Organism-specific databases

CYGDYNL118c.
SGDS000005062. DCP2.

Phylogenomic databases

GeneTreeENSGT00390000018878.
KOK12613.
OrthoDBEOG7P5TBG.

Enzyme and pathway databases

BioCycYEAST:G3O-33140-MONOMER.

Gene expression databases

GenevestigatorP53550.

Family and domain databases

Gene3D3.90.79.10. 1 hit.
InterProIPR007722. mRNA_decapping_BoxA.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamPF05026. DCP2. 1 hit.
PF00293. NUDIX. 1 hit.
[Graphical view]
SUPFAMSSF55811. SSF55811. 1 hit.
PROSITEPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP53550.
NextBio979774.

Entry information

Entry nameDCP2_YEAST
AccessionPrimary (citable) accession number: P53550
Secondary accession number(s): B0KZS6 expand/collapse secondary AC list , B0KZU4, B0KZW2, B0KZY0, B0KZY9, B0KZZ8, B0L007, D6W164, Q6LCS6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 134 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 XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: 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