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P06104

- UBC2_YEAST

UniProt

P06104 - UBC2_YEAST

Protein

Ubiquitin-conjugating enzyme E2 2

Gene

RAD6

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 154 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
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    Functioni

    Catalyzes the covalent attachment of ubiquitin to other proteins. In association with the E3 enzyme BRE1 and LGE1, it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In association with the E3 enzyme RAD18, it catalyzes the monoubiquitination of POL30 'Lys-164', involved in postreplication repair of UV-damaged DNA. The RAD6/UBC2-RAD18 complex is also involved in prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine. In association with the E3 enzyme UBR1, is involved in N-end rule-dependent protein degradation. Also involved in sporulation.17 PublicationsPROSITE-ProRule annotation

    Catalytic activityi

    ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei88 – 881Glycyl thioester intermediate

    GO - Molecular functioni

    1. acid-amino acid ligase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. ubiquitin-protein transferase activity Source: SGD

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. chromatin silencing at telomere Source: SGD
    3. DNA-templated transcription, termination Source: SGD
    4. double-strand break repair via homologous recombination Source: SGD
    5. ER-associated ubiquitin-dependent protein catabolic process Source: SGD
    6. error-free postreplication DNA repair Source: SGD
    7. error-free translesion synthesis Source: SGD
    8. error-prone translesion synthesis Source: SGD
    9. histone monoubiquitination Source: SGD
    10. meiotic DNA double-strand break formation Source: SGD
    11. mitotic G1 DNA damage checkpoint Source: SGD
    12. protein monoubiquitination Source: SGD
    13. protein polyubiquitination Source: SGD
    14. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: SGD
    15. regulation of dipeptide transport Source: SGD
    16. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
    17. telomere maintenance via recombination Source: SGD
    18. transcription from RNA polymerase II promoter Source: SGD
    19. ubiquitin-dependent protein catabolic process via the N-end rule pathway Source: SGD

    Keywords - Molecular functioni

    Chromatin regulator, Ligase

    Keywords - Biological processi

    DNA damage, DNA repair, Sporulation, Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30566-MONOMER.
    ReactomeiREACT_189060. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-conjugating enzyme E2 2 (EC:6.3.2.19)
    Alternative name(s):
    Radiation sensitivity protein 6
    Ubiquitin carrier protein UBC2
    Ubiquitin-protein ligase UBC2
    Gene namesi
    Name:RAD6
    Synonyms:UBC2
    Ordered Locus Names:YGL058W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGL058w.
    SGDiS000003026. RAD6.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. nucleus Source: SGD
    3. Rad6-Rad18 complex Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1 – 99Missing: Prevents H3K4me3 formation. 1 Publication
    Mutagenesisi88 – 881C → A or V: Loss of activity. 3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 172172Ubiquitin-conjugating enzyme E2 2PRO_0000082540Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei120 – 1201Phosphoserine; by SGV12 Publications

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP06104.
    PeptideAtlasiP06104.

    Expressioni

    Inductioni

    Up-regulated by UV radiations and during meiosis.1 Publication

    Gene expression databases

    GenevestigatoriP06104.

    Interactioni

    Subunit structurei

    Forms a heterodimer complexes with the E3 enzymes BRE1, RAD18 and UBR1. Interacts also with UBR2, RTF1, PAF1 and the RNA polymerase II hyperphosphorylated form. The interaction with RNA polymerase II is BRE1- and PAF1-dependent.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRE1Q074574EBI-19722,EBI-31563
    RAD18P108624EBI-19722,EBI-14659
    UBR1P198123EBI-19722,EBI-19909
    UBR2Q079636EBI-19722,EBI-34338

    Protein-protein interaction databases

    BioGridi33189. 367 interactions.
    DIPiDIP-1555N.
    IntActiP06104. 13 interactions.
    MINTiMINT-394584.
    STRINGi4932.YGL058W.

    Structurei

    Secondary structure

    1
    172
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1815
    Beta strandi24 – 296
    Beta strandi32 – 4110
    Turni47 – 504
    Beta strandi52 – 587
    Turni61 – 655
    Beta strandi69 – 746
    Beta strandi85 – 873
    Helixi90 – 923
    Turni93 – 953
    Helixi102 – 11312
    Helixi124 – 1329
    Helixi134 – 15219

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AYZX-ray2.60A/B/C1-172[»]
    ProteinModelPortaliP06104.
    SMRiP06104. Positions 2-154.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06104.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi150 – 17223Asp/Glu-rich (acidic tail)Add
    BLAST

    Domaini

    The acidic-tail domain of UBC2 mediates interaction with UBR1 and UBR2, and thus is important for polyubiquitination of histones. This domain is also important for sporulation.

    Sequence similaritiesi

    Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5078.
    GeneTreeiENSGT00730000110565.
    HOGENOMiHOG000233454.
    KOiK10573.
    OMAiETVENSW.
    OrthoDBiEOG7SBP18.

    Family and domain databases

    Gene3Di3.10.110.10. 1 hit.
    InterProiIPR000608. UBQ-conjugat_E2.
    IPR023313. UBQ-conjugating_AS.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view]
    PfamiPF00179. UQ_con. 1 hit.
    [Graphical view]
    SUPFAMiSSF54495. SSF54495. 1 hit.
    PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
    PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P06104-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTPARRRLM RDFKRMKEDA PPGVSASPLP DNVMVWNAMI IGPADTPYED    50
    GTFRLLLEFD EEYPNKPPHV KFLSEMFHPN VYANGEICLD ILQNRWTPTY 100
    DVASILTSIQ SLFNDPNPAS PANVEAATLF KDHKSQYVKR VKETVEKSWE 150
    DDMDDMDDDD DDDDDDDDDE AD 172
    Length:172
    Mass (Da):19,706
    Last modified:January 1, 1988 - v1
    Checksum:i5F568DC28ABBD60F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02962 Genomic DNA. Translation: AAA34952.1.
    Z72580 Genomic DNA. Translation: CAA96761.1.
    BK006941 Genomic DNA. Translation: DAA08044.1.
    PIRiA21906.
    RefSeqiNP_011457.1. NM_001180923.1.

    Genome annotation databases

    EnsemblFungiiYGL058W; YGL058W; YGL058W.
    GeneIDi852822.
    KEGGisce:YGL058W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02962 Genomic DNA. Translation: AAA34952.1 .
    Z72580 Genomic DNA. Translation: CAA96761.1 .
    BK006941 Genomic DNA. Translation: DAA08044.1 .
    PIRi A21906.
    RefSeqi NP_011457.1. NM_001180923.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AYZ X-ray 2.60 A/B/C 1-172 [» ]
    ProteinModelPortali P06104.
    SMRi P06104. Positions 2-154.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33189. 367 interactions.
    DIPi DIP-1555N.
    IntActi P06104. 13 interactions.
    MINTi MINT-394584.
    STRINGi 4932.YGL058W.

    Proteomic databases

    PaxDbi P06104.
    PeptideAtlasi P06104.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGL058W ; YGL058W ; YGL058W .
    GeneIDi 852822.
    KEGGi sce:YGL058W.

    Organism-specific databases

    CYGDi YGL058w.
    SGDi S000003026. RAD6.

    Phylogenomic databases

    eggNOGi COG5078.
    GeneTreei ENSGT00730000110565.
    HOGENOMi HOG000233454.
    KOi K10573.
    OMAi ETVENSW.
    OrthoDBi EOG7SBP18.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    BioCyci YEAST:G3O-30566-MONOMER.
    Reactomei REACT_189060. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    EvolutionaryTracei P06104.
    NextBioi 972372.
    PROi P06104.

    Gene expression databases

    Genevestigatori P06104.

    Family and domain databases

    Gene3Di 3.10.110.10. 1 hit.
    InterProi IPR000608. UBQ-conjugat_E2.
    IPR023313. UBQ-conjugating_AS.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view ]
    Pfami PF00179. UQ_con. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54495. SSF54495. 1 hit.
    PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
    PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "RAD6 gene of Saccharomyces cerevisiae encodes a protein containing a tract of 13 consecutive aspartates."
      Reynolds P., Weber S., Prakash L.
      Proc. Natl. Acad. Sci. U.S.A. 82:168-172(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes."
      Feuermann M., de Montigny J., Potier S., Souciet J.-L.
      Yeast 13:861-869(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme."
      Jentsch S., McGrath J.P., Varshavsky A.
      Nature 329:131-134(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 77-91, FUNCTION.
    6. "Recombination and mutagenesis in rad6 mutants of Saccharomyces cerevisiae: evidence for multiple functions of the RAD6 gene."
      Montelone B.A., Prakash S., Prakash L.
      Mol. Gen. Genet. 184:410-415(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Expression of the Saccharomyces cerevisiae DNA repair gene RAD6 that encodes a ubiquitin conjugating enzyme, increases in response to DNA damage and in meiosis but remains constant during the mitotic cell cycle."
      Madura K., Prakash S., Prakash L.
      Nucleic Acids Res. 18:771-778(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    8. "Mutation of cysteine-88 in the Saccharomyces cerevisiae RAD6 protein abolishes its ubiquitin-conjugating activity and its various biological functions."
      Sung P., Prakash S., Prakash L.
      Proc. Natl. Acad. Sci. U.S.A. 87:2695-2699(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-88.
    9. "The N-end rule is mediated by the UBC2(RAD6) ubiquitin-conjugating enzyme."
      Dohmen R.J., Madura K., Bartel B., Varshavsky A.
      Proc. Natl. Acad. Sci. U.S.A. 88:7351-7355(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH UBR1.
    10. "Yeast RAD6 encoded ubiquitin conjugating enzyme mediates protein degradation dependent on the N-end-recognizing E3 enzyme."
      Sung P., Berleth E., Pickart C.M., Prakash S., Prakash L.
      EMBO J. 10:2187-2193(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "The extremely conserved amino terminus of RAD6 ubiquitin-conjugating enzyme is essential for amino-end rule-dependent protein degradation."
      Watkins J.F., Sung P., Prakash S., Prakash L.
      Genes Dev. 7:250-261(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH UBR1, MUTAGENESIS OF 1-MET--LEU-9.
    12. "Specific complex formation between yeast RAD6 and RAD18 proteins: a potential mechanism for targeting RAD6 ubiquitin-conjugating activity to DNA damage sites."
      Bailly V., Lamb J., Sung P., Prakash S., Prakash L.
      Genes Dev. 8:811-820(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RAD18 AND UBR1.
    13. "Yeast DNA repair proteins Rad6 and Rad18 form a heterodimer that has ubiquitin conjugating, DNA binding, and ATP hydrolytic activities."
      Bailly V., Lauder S., Prakash S., Prakash L.
      J. Biol. Chem. 272:23360-23365(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RAD18.
    14. "The ubiquitin-conjugating enzyme Rad6 (Ubc2) is required for silencing in Saccharomyces cerevisiae."
      Huang H., Kahana A., Gottschling D.E., Prakash L., Liebman S.W.
      Mol. Cell. Biol. 17:6693-6699(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "The E2-E3 interaction in the N-end rule pathway: the RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain."
      Xie Y., Varshavsky A.
      EMBO J. 18:6832-6844(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBR1 AND UBR2.
    16. "Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair."
      Ulrich H.D., Jentsch S.
      EMBO J. 19:3388-3397(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    17. "Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast."
      Sun Z.-W., Allis C.D.
      Nature 418:104-108(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-88 AND 1-MET--LEU-9.
    18. "RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO."
      Hoege C., Pfander B., Moldovan G.-L., Pyrowolakis G., Jentsch S.
      Nature 419:135-141(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    20. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    21. "Rad6 plays a role in transcriptional activation through ubiquitylation of histone H2B."
      Kao C.-F., Hillyer C., Tsukuda T., Henry K.W., Berger S.L., Osley M.A.
      Genes Dev. 18:184-195(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    22. "The post-replication repair RAD18 and RAD6 genes are involved in the prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine in Saccharomyces cerevisiae."
      de Padula M., Slezak G., Auffret van Der Kemp P., Boiteux S.
      Nucleic Acids Res. 32:5003-5010(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "The Bur1/Bur2 complex is required for histone H2B monoubiquitination by Rad6/Bre1 and histone methylation by COMPASS."
      Wood A., Schneider J., Dover J., Johnston M., Shilatifard A.
      Mol. Cell 20:589-599(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-120.
    24. "Histone H2B ubiquitylation is associated with elongating RNA polymerase II."
      Xiao T., Kao C.-F., Krogan N.J., Sun Z.-W., Greenblatt J.F., Osley M.A., Strahl B.D.
      Mol. Cell. Biol. 25:637-651(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RTF1; PAF1 AND THE RNA POLYMERASE II HYPERPHOSPHORYLATED FORM.
    25. "The error-free component of the RAD6/RAD18 DNA damage tolerance pathway of budding yeast employs sister-strand recombination."
      Zhang H., Lawrence C.W.
      Proc. Natl. Acad. Sci. U.S.A. 102:15954-15959(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    26. "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-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Crystal structure of the Saccharomyces cerevisiae ubiquitin-conjugating enzyme Rad6 at 2.6-A resolution."
      Worthylake D.K., Prakash S., Prakash L., Hill C.P.
      J. Biol. Chem. 273:6271-6276(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

    Entry informationi

    Entry nameiUBC2_YEAST
    AccessioniPrimary (citable) accession number: P06104
    Secondary accession number(s): D6VU83
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 154 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 2770 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3