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Q12149

- RRP6_YEAST

UniProt

Q12149 - RRP6_YEAST

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
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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

    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

    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. 301 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[»]
    ProteinModelPortaliQ12149.
    SMRiQ12149. Positions 129-516, 532-619.
    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.
    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

    MTSENPDVLL SRVINVVRAA SSLASQDVDF YKNLDRGFSK DLKSKADKLA    50
    DMANEIILSI DEHHESFELK EEDISDLWNN FGNIMDNLLE MSDHSLDKLN 100
    CAINSKSRGS DLQYLGEFSG KNFSPTKRVE KPQLKFKSPI DNSESHPFIP 150
    LLKEKPNALK PLSESLRLVD DDENNPSHYP HPYEYEIDHQ EYSPEILQIR 200
    EEIPSKSWDD SVPIWVDTST ELESMLEDLK NTKEIAVDLE HHDYRSYYGI 250
    VCLMQISTRE RDYLVDTLKL RENLHILNEV FTNPSIVKVF HGAFMDIIWL 300
    QRDLGLYVVG LFDTYHASKA IGLPRHSLAY LLENFANFKT SKKYQLADWR 350
    IRPLSKPMTA YARADTHFLL NIYDQLRNKL IESNKLAGVL YESRNVAKRR 400
    FEYSKYRPLT PSSEVYSPIE KESPWKILMY QYNIPPEREV LVRELYQWRD 450
    LIARRDDESP RFVMPNQLLA ALVAYTPTDV IGVVSLTNGV TEHVRQNAKL 500
    LANLIRDALR NIKNTNEEAT PIPSSETKAD GILLETISVP QIRDVMERFS 550
    VLCNSNISKS RAKPVTNSSI LLGKILPREE HDIAYSKDGL PNKVKTEDIR 600
    IRAQNFKSAL ANLEDIIFEI EKPLVVPVKL EEIKTVDPAS APNHSPEIDN 650
    LDDLVVLKKK NIQKKQPAKE KGVTEKDAVD YSKIPNILSN KPGQNNRQQK 700
    KRRFDPSSSD SNGPRAAKKR RPAAKGKNLS FKR 733
    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 [» ]
    ProteinModelPortali Q12149.
    SMRi Q12149. Positions 129-516, 532-619.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34404. 301 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.
    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

    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 1, 2014
    This is version 131 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