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Q12149

- RRP6_YEAST

UniProt

Q12149 - RRP6_YEAST

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Protein

Exosome complex exonuclease RRP6

Gene

RRP6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Nuclear-specific catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. RRP6 has 3'-5' exonuclease activity which is not modulated upon association with Exo-9 suggesting that the complex inner RNA-binding path is not used to access its active site.4 Publications

GO - Molecular functioni

  1. 3'-5'-exoribonuclease activity Source: SGD
  2. nucleotide binding Source: InterPro
  3. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  2. histone mRNA catabolic process Source: SGD
  3. nuclear polyadenylation-dependent antisense transcript catabolic process Source: SGD
  4. nuclear polyadenylation-dependent CUT catabolic process Source: SGD
  5. nuclear polyadenylation-dependent mRNA catabolic process Source: SGD
  6. nuclear polyadenylation-dependent rRNA catabolic process Source: SGD
  7. nuclear polyadenylation-dependent snoRNA catabolic process Source: SGD
  8. nuclear polyadenylation-dependent snRNA catabolic process Source: SGD
  9. nuclear polyadenylation-dependent tRNA catabolic process Source: SGD
  10. nuclear retention of pre-mRNA at the site of transcription Source: SGD
  11. nuclear retention of pre-mRNA with aberrant 3'-ends at the site of transcription Source: SGD
  12. polyadenylation-dependent snoRNA 3'-end processing Source: SGD
  13. posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery Source: SGD
  14. U1 snRNA 3'-end processing Source: SGD
  15. U4 snRNA 3'-end processing Source: SGD
  16. U5 snRNA 3'-end processing Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33552-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Exosome complex exonuclease RRP6 (EC:3.1.13.-)
Alternative name(s):
Ribosomal RNA-processing protein 6
Gene namesi
Name:RRP6
Synonyms:UNC733
Ordered Locus Names:YOR001W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XV

Organism-specific databases

CYGDiYOR001w.
SGDiS000005527. RRP6.

Subcellular locationi

Nucleusnucleolus 4 Publications

GO - Cellular componenti

  1. nuclear exosome (RNase complex) Source: SGD
  2. nucleolus Source: SGD
  3. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Exosome, Nucleus

Pathology & Biotechi

Disruption phenotypei

Deletion mutant is impaired in growth at all temperatures and is nonviable at 37 degrees Celsius. It is defective in the 3' processing of the 5.8S rRNA and accumulates a discrete species, 5.8S + 30, that is 3' extended by about 30 nucleotides. Deletion also causes an accumulation of 7S RNA and 5' ETS and increases the level of poly(A)+ mRNA.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 733733Exosome complex exonuclease RRP6PRO_0000097456Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei138 – 1381Phosphoserine1 Publication
Modified residuei520 – 5201Phosphothreonine1 Publication
Modified residuei640 – 6401Phosphoserine1 Publication
Modified residuei645 – 6451Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12149.
PaxDbiQ12149.

Expressioni

Gene expression databases

GenevestigatoriQ12149.

Interactioni

Subunit structurei

Component of the RNA exosome complex. The catalytically inactive RNA exosome core (Exo-9) complex associates with catalytic subunits DIS3 and RRP6 in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits and peripheral S1 domain-containing components CSL4, RRP4 and RRP40 located on the top of the ring structure. RRP6 specifically is part of the nuclear form of the RNA exosome complex; the association appears to be mediated by Exo-9 and not by DIS3. Interacts with LRP1. Interacts with NPL3, NOP53 and PAP1.6 Publications

Protein-protein interaction databases

BioGridi34404. 302 interactions.
DIPiDIP-4560N.
IntActiQ12149. 27 interactions.
MINTiMINT-534618.
STRINGi4932.YOR001W.

Structurei

Secondary structure

1
733
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi132 – 1354
Helixi162 – 1654
Beta strandi173 – 1753
Helixi184 – 1896
Helixi194 – 1963
Helixi208 – 2103
Beta strandi214 – 2163
Helixi219 – 22911
Beta strandi233 – 24210
Beta strandi244 – 2485
Beta strandi250 – 2578
Beta strandi262 – 2665
Turni267 – 2737
Helixi274 – 2774
Helixi278 – 2814
Beta strandi286 – 2927
Helixi294 – 30411
Beta strandi309 – 3135
Helixi314 – 3218
Helixi328 – 3358
Turni343 – 3464
Helixi356 – 36712
Helixi369 – 38214
Helixi386 – 39813
Helixi404 – 4063
Beta strandi413 – 4164
Beta strandi421 – 4277
Helixi436 – 4383
Helixi439 – 45618
Helixi460 – 4634
Helixi466 – 47510
Helixi480 – 4845
Helixi492 – 4965
Helixi498 – 51518
Turni534 – 5363
Helixi539 – 55315
Beta strandi570 – 5723
Turni573 – 5775
Beta strandi582 – 5854
Beta strandi591 – 5944
Helixi596 – 61116
Helixi612 – 6143
Beta strandi617 – 6193

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M0Ymodel-A207-382[»]
2HBJX-ray2.10A129-536[»]
2HBKX-ray2.25A129-536[»]
2HBLX-ray2.30A129-536[»]
2HBMX-ray2.70A129-536[»]
4IFDX-ray2.80K518-693[»]
4OO1X-ray3.30J129-685[»]
ProteinModelPortaliQ12149.
SMRiQ12149. Positions 129-628.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12149.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini435 – 51581HRDCPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the exosome component 10/RRP6 family.Curated
Contains 1 HRDC domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0349.
GeneTreeiENSGT00390000015408.
HOGENOMiHOG000196525.
InParanoidiQ12149.
KOiK12591.
OMAiEYKFLHA.
OrthoDBiEOG7WT49D.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR002562. 3'-5'_exonuclease_dom.
IPR012588. Exosome-assoc_fac_Rrp6_N.
IPR010997. HRDC-like.
IPR002121. HRDC_dom.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF01612. DNA_pol_A_exo1. 1 hit.
PF00570. HRDC. 1 hit.
PF08066. PMC2NT. 1 hit.
[Graphical view]
SMARTiSM00474. 35EXOc. 1 hit.
SM00341. HRDC. 1 hit.
[Graphical view]
SUPFAMiSSF47819. SSF47819. 1 hit.
SSF53098. SSF53098. 1 hit.
PROSITEiPS50967. HRDC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12149-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTSENPDVLL SRVINVVRAA SSLASQDVDF YKNLDRGFSK DLKSKADKLA
60 70 80 90 100
DMANEIILSI DEHHESFELK EEDISDLWNN FGNIMDNLLE MSDHSLDKLN
110 120 130 140 150
CAINSKSRGS DLQYLGEFSG KNFSPTKRVE KPQLKFKSPI DNSESHPFIP
160 170 180 190 200
LLKEKPNALK PLSESLRLVD DDENNPSHYP HPYEYEIDHQ EYSPEILQIR
210 220 230 240 250
EEIPSKSWDD SVPIWVDTST ELESMLEDLK NTKEIAVDLE HHDYRSYYGI
260 270 280 290 300
VCLMQISTRE RDYLVDTLKL RENLHILNEV FTNPSIVKVF HGAFMDIIWL
310 320 330 340 350
QRDLGLYVVG LFDTYHASKA IGLPRHSLAY LLENFANFKT SKKYQLADWR
360 370 380 390 400
IRPLSKPMTA YARADTHFLL NIYDQLRNKL IESNKLAGVL YESRNVAKRR
410 420 430 440 450
FEYSKYRPLT PSSEVYSPIE KESPWKILMY QYNIPPEREV LVRELYQWRD
460 470 480 490 500
LIARRDDESP RFVMPNQLLA ALVAYTPTDV IGVVSLTNGV TEHVRQNAKL
510 520 530 540 550
LANLIRDALR NIKNTNEEAT PIPSSETKAD GILLETISVP QIRDVMERFS
560 570 580 590 600
VLCNSNISKS RAKPVTNSSI LLGKILPREE HDIAYSKDGL PNKVKTEDIR
610 620 630 640 650
IRAQNFKSAL ANLEDIIFEI EKPLVVPVKL EEIKTVDPAS APNHSPEIDN
660 670 680 690 700
LDDLVVLKKK NIQKKQPAKE KGVTEKDAVD YSKIPNILSN KPGQNNRQQK
710 720 730
KRRFDPSSSD SNGPRAAKKR RPAAKGKNLS FKR
Length:733
Mass (Da):84,039
Last modified:November 1, 1996 - v1
Checksum:iB19A0B2ED74C6DA7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti402 – 4021E → G in AAT92869. (PubMed:17322287)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z74909 Genomic DNA. Translation: CAA99189.1.
U43491 Genomic DNA. Translation: AAC49480.1.
AY692850 Genomic DNA. Translation: AAT92869.1.
BK006948 Genomic DNA. Translation: DAA10783.1.
PIRiS61984.
RefSeqiNP_014643.1. NM_001183420.1.

Genome annotation databases

EnsemblFungiiYOR001W; YOR001W; YOR001W.
GeneIDi854162.
KEGGisce:YOR001W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z74909 Genomic DNA. Translation: CAA99189.1 .
U43491 Genomic DNA. Translation: AAC49480.1 .
AY692850 Genomic DNA. Translation: AAT92869.1 .
BK006948 Genomic DNA. Translation: DAA10783.1 .
PIRi S61984.
RefSeqi NP_014643.1. NM_001183420.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M0Y model - A 207-382 [» ]
2HBJ X-ray 2.10 A 129-536 [» ]
2HBK X-ray 2.25 A 129-536 [» ]
2HBL X-ray 2.30 A 129-536 [» ]
2HBM X-ray 2.70 A 129-536 [» ]
4IFD X-ray 2.80 K 518-693 [» ]
4OO1 X-ray 3.30 J 129-685 [» ]
ProteinModelPortali Q12149.
SMRi Q12149. Positions 129-628.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34404. 302 interactions.
DIPi DIP-4560N.
IntActi Q12149. 27 interactions.
MINTi MINT-534618.
STRINGi 4932.YOR001W.

Proteomic databases

MaxQBi Q12149.
PaxDbi Q12149.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YOR001W ; YOR001W ; YOR001W .
GeneIDi 854162.
KEGGi sce:YOR001W.

Organism-specific databases

CYGDi YOR001w.
SGDi S000005527. RRP6.

Phylogenomic databases

eggNOGi COG0349.
GeneTreei ENSGT00390000015408.
HOGENOMi HOG000196525.
InParanoidi Q12149.
KOi K12591.
OMAi EYKFLHA.
OrthoDBi EOG7WT49D.

Enzyme and pathway databases

BioCyci YEAST:G3O-33552-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q12149.
NextBioi 975938.
PROi Q12149.

Gene expression databases

Genevestigatori Q12149.

Family and domain databases

Gene3Di 3.30.420.10. 1 hit.
InterProi IPR002562. 3'-5'_exonuclease_dom.
IPR012588. Exosome-assoc_fac_Rrp6_N.
IPR010997. HRDC-like.
IPR002121. HRDC_dom.
IPR012337. RNaseH-like_dom.
[Graphical view ]
Pfami PF01612. DNA_pol_A_exo1. 1 hit.
PF00570. HRDC. 1 hit.
PF08066. PMC2NT. 1 hit.
[Graphical view ]
SMARTi SM00474. 35EXOc. 1 hit.
SM00341. HRDC. 1 hit.
[Graphical view ]
SUPFAMi SSF47819. SSF47819. 1 hit.
SSF53098. SSF53098. 1 hit.
PROSITEi PS50967. HRDC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of a 30 kb fragment on the left arm of chromosome XV from Saccharomyces cerevisiae reveals 15 open reading frames, five of which correspond to previously identified genes."
    Sterky F., Holmberg A., Pettersson B., Uhlen M.
    Yeast 12:1091-1095(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Rrp6p, the yeast homologue of the human PM-Scl 100-kDa autoantigen, is essential for efficient 5.8 S rRNA 3' end formation."
    Briggs M.W., Burkard K.T.D., Butler J.S.
    J. Biol. Chem. 273:13255-13263(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "The yeast exosome and human PM-Scl are related complexes of 3'-->5' exonucleases."
    Allmang C., Petfalski E., Podtelejnikov A., Mann M., Tollervey D., Mitchell P.
    Genes Dev. 13:2148-2158(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE RNA EXOSOME COMPLEX BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  7. "A nuclear 3'-5' exonuclease involved in mRNA degradation interacts with Poly(A) polymerase and the hnRNA protein Npl3p."
    Burkard K.T.D., Butler J.S.
    Mol. Cell. Biol. 20:604-616(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION, INTERACTION WITH NPL3 AND PAP1, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  8. "Rrp47p is an exosome-associated protein required for the 3' processing of stable RNAs."
    Mitchell P., Petfalski E., Houalla R., Podtelejnikov A., Mann M., Tollervey D.
    Mol. Cell. Biol. 23:6982-6992(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRP1.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "Genome-wide mRNA surveillance is coupled to mRNA export."
    Hieronymus H., Yu M.C., Silver P.A.
    Genes Dev. 18:2652-2662(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LRP1, SUBCELLULAR LOCATION.
  12. "Reconstitution, activities, and structure of the eukaryotic RNA exosome."
    Liu Q., Greimann J.C., Lima C.D.
    Cell 127:1223-1237(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: RECONSTITUTION OF THE RNA EXOSOME COMPLEX, EXONUCLEASE ACTIVITY.
  13. Erratum
    Liu Q., Greimann J.C., Lima C.D.
    Cell 131:188-189(2007)
  14. "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-138 AND SER-645, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  15. "A single subunit, Dis3, is essentially responsible for yeast exosome core activity."
    Dziembowski A., Lorentzen E., Conti E., Seraphin B.
    Nat. Struct. Mol. Biol. 14:15-22(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH THE RNA EXOSOME, SUBUNIT, DISRUPTION PHENOTYPE.
  16. "Nop53p interacts with 5.8S rRNA co-transcriptionally, and regulates processing of pre-rRNA by the exosome."
    Granato D.C., Machado-Santelli G.M., Oliveira C.C.
    FEBS J. 275:4164-4178(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOP53.
  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 THR-520 AND SER-645, 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-640 AND SER-645, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRRP6_YEAST
AccessioniPrimary (citable) accession number: Q12149
Secondary accession number(s): D6W267, Q6B280
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2160 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3