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P52488

- UBA2_YEAST

UniProt

P52488 - UBA2_YEAST

Protein

Ubiquitin-activating enzyme E1-like

Gene

UBA2

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 139 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    The dimeric enzyme acts as a SMT3 E1 ligase. It mediates ATP-dependent activation of SMT3 and formation of a thioester with a conserved cysteine residue on AOS1.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei52 – 521ATPBy similarity
    Binding sitei76 – 761ATPBy similarity
    Metal bindingi162 – 1621ZincBy similarity
    Metal bindingi165 – 1651ZincBy similarity
    Active sitei177 – 1771Glycyl thioester intermediatePROSITE-ProRule annotation
    Metal bindingi435 – 4351ZincBy similarity
    Metal bindingi438 – 4381ZincBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi28 – 336ATPBy similarity
    Nucleotide bindingi60 – 634ATPBy similarity
    Nucleotide bindingi121 – 1266ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ligase activity Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW
    4. SUMO activating enzyme activity Source: SGD

    GO - Biological processi

    1. protein sumoylation Source: SGD

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29938-MONOMER.
    ReactomeiREACT_188767. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
    REACT_188903. SUMO is conjugated to E1 (UBA2:SAE1).
    UniPathwayiUPA00886.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-activating enzyme E1-like
    Alternative name(s):
    Polymerase-interacting protein 2
    SMT3-activating enzyme subunit 2
    Gene namesi
    Name:UBA2
    Synonyms:PIP2, UAL1
    Ordered Locus Names:YDR390C
    ORF Names:D9509.10
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR390c.
    SGDiS000002798. UBA2.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: SGD
    2. SUMO activating enzyme complex Source: SGD

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi177 – 1771C → A or S: Loss of function.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 636636Ubiquitin-activating enzyme E1-likePRO_0000194979Add
    BLAST

    Post-translational modificationi

    Multiubiquitinated in vivo.

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiP52488.
    PaxDbiP52488.
    PeptideAtlasiP52488.

    Expressioni

    Gene expression databases

    GenevestigatoriP52488.

    Interactioni

    Subunit structurei

    Heterodimer of UBA2 and AOS1. The complex binds SMT3.

    Protein-protein interaction databases

    BioGridi32451. 26 interactions.
    DIPiDIP-2296N.
    IntActiP52488. 9 interactions.
    MINTiMINT-657883.
    STRINGi4932.YDR390C.

    Structurei

    Secondary structure

    1
    636
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi442 – 4487
    Helixi450 – 4556
    Helixi458 – 46912
    Beta strandi473 – 4797
    Turni480 – 4834
    Beta strandi484 – 4885
    Turni493 – 4964
    Turni499 – 5035
    Beta strandi509 – 5157
    Beta strandi518 – 5225
    Beta strandi525 – 5317
    Beta strandi535 – 5384
    Beta strandi549 – 5513

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ONGX-ray2.30A/C439-563[»]
    3ONHX-ray1.60A439-563[»]
    ProteinModelPortaliP52488.
    SMRiP52488. Positions 19-552.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi619 – 6224Nuclear localization signalSequence Analysis

    Sequence similaritiesi

    Belongs to the ubiquitin-activating E1 family.Curated

    Phylogenomic databases

    eggNOGiCOG0476.
    GeneTreeiENSGT00550000074924.
    HOGENOMiHOG000216514.
    KOiK10685.
    OMAiPHHGNIM.
    OrthoDBiEOG7FZ07P.

    Family and domain databases

    Gene3Di1.10.3240.10. 1 hit.
    3.40.50.720. 2 hits.
    InterProiIPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    IPR023280. Ub-like_act_enz_cat_cys_dom.
    IPR000127. UBact_repeat.
    IPR019572. Ubiquitin-activating_enzyme.
    IPR018074. UBQ-activ_enz_E1_AS.
    [Graphical view]
    PfamiPF00899. ThiF. 1 hit.
    PF10585. UBA_e1_thiolCys. 1 hit.
    PF02134. UBACT. 1 hit.
    [Graphical view]
    SUPFAMiSSF69572. SSF69572. 2 hits.
    PROSITEiPS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P52488-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPRETSLVTI IGEDSYKKLR SSRCLLVGAG GIGSELLKDI ILMEFGEIHI    50
    VDLDTIDLSN LNRQFLFRQK DIKQPKSTTA VKAVQHFNNS KLVPYQGNVM 100
    DISTFPLHWF EQFDIIFNAL DNLAARRYVN KISQFLSLPL IESGTAGFDG 150
    YMQPIIPGKT ECFECTKKET PKTFPVCTIR STPSQPIHCI VWAKNFLFNQ 200
    LFASETSGNE DDNNQDWGTD DAEEIKRIKQ ETNELYELQK IIISRDASRI 250
    PEILNKLFIQ DINKLLAIEN LWKTRTKPVP LSDSQINTPT KTAQSASNSV 300
    GTIQEQISNF INITQKLMDR YPKEQNHIEF DKDDADTLEF VATAANIRSH 350
    IFNIPMKSVF DIKQIAGNII PAIATTNAIV AGASSLISLR VLNLLKYAPT 400
    TKYTDLNMAF TAKASNLSQN RYLSNPKLAP PNKNCPVCSK VCRGVIKLSS 450
    DCLNKMKLSD FVVLIREKYS YPQDISLLDA SNQRLLFDYD FEDLNDRTLS 500
    EINLGNGSII LFSDEEGDTM IRKAIELFLD VDDELPCNTC SLPDVEVPLI 550
    KANNSPSKNE EEEKNEKGAD VVATTNSHGK DGIVILDDDE GEITIDAEPI 600
    NGSKKRPVDT EISEAPSNKR TKLVNEPTNS DIVELD 636
    Length:636
    Mass (Da):71,259
    Last modified:October 1, 1996 - v1
    Checksum:iDBF800E1458B3B10
    GO

    Sequence cautioni

    The sequence CAA82980.1 differs from that shown. Reason: Frameshift at positions 180 and 268.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z48725 Genomic DNA. Translation: CAA88617.1.
    Z30326 Genomic DNA. Translation: CAA82980.1. Frameshift.
    U17263 Genomic DNA. Translation: AAB46626.1.
    U32274 Genomic DNA. Translation: AAB64832.1.
    BK006938 Genomic DNA. Translation: DAA12234.1.
    PIRiA57178.
    RefSeqiNP_010678.3. NM_001180698.3.

    Genome annotation databases

    EnsemblFungiiYDR390C; YDR390C; YDR390C.
    GeneIDi851998.
    KEGGisce:YDR390C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z48725 Genomic DNA. Translation: CAA88617.1 .
    Z30326 Genomic DNA. Translation: CAA82980.1 . Frameshift.
    U17263 Genomic DNA. Translation: AAB46626.1 .
    U32274 Genomic DNA. Translation: AAB64832.1 .
    BK006938 Genomic DNA. Translation: DAA12234.1 .
    PIRi A57178.
    RefSeqi NP_010678.3. NM_001180698.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ONG X-ray 2.30 A/C 439-563 [» ]
    3ONH X-ray 1.60 A 439-563 [» ]
    ProteinModelPortali P52488.
    SMRi P52488. Positions 19-552.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32451. 26 interactions.
    DIPi DIP-2296N.
    IntActi P52488. 9 interactions.
    MINTi MINT-657883.
    STRINGi 4932.YDR390C.

    Proteomic databases

    MaxQBi P52488.
    PaxDbi P52488.
    PeptideAtlasi P52488.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR390C ; YDR390C ; YDR390C .
    GeneIDi 851998.
    KEGGi sce:YDR390C.

    Organism-specific databases

    CYGDi YDR390c.
    SGDi S000002798. UBA2.

    Phylogenomic databases

    eggNOGi COG0476.
    GeneTreei ENSGT00550000074924.
    HOGENOMi HOG000216514.
    KOi K10685.
    OMAi PHHGNIM.
    OrthoDBi EOG7FZ07P.

    Enzyme and pathway databases

    UniPathwayi UPA00886 .
    BioCyci YEAST:G3O-29938-MONOMER.
    Reactomei REACT_188767. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
    REACT_188903. SUMO is conjugated to E1 (UBA2:SAE1).

    Miscellaneous databases

    NextBioi 970178.
    PROi P52488.

    Gene expression databases

    Genevestigatori P52488.

    Family and domain databases

    Gene3Di 1.10.3240.10. 1 hit.
    3.40.50.720. 2 hits.
    InterProi IPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    IPR023280. Ub-like_act_enz_cat_cys_dom.
    IPR000127. UBact_repeat.
    IPR019572. Ubiquitin-activating_enzyme.
    IPR018074. UBQ-activ_enz_E1_AS.
    [Graphical view ]
    Pfami PF00899. ThiF. 1 hit.
    PF10585. UBA_e1_thiolCys. 1 hit.
    PF02134. UBACT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69572. SSF69572. 2 hits.
    PROSITEi PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "An essential yeast gene encoding a homolog of ubiquitin-activating enzyme."
      Dohmen R.J., Stappen R., McGrath J.P., Forrova H., Kolarov J., Goffeau A., Varshavsky A.
      J. Biol. Chem. 270:18099-18109(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Kolarov J.
      Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. del Olmo M., Gross S., Moore C.L.
      Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 200060 / W303.
    4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. "The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer."
      Johnson E.S., Schwienhorst I., Dohmen R.J., Blobel G.
      EMBO J. 16:5509-5519(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiUBA2_YEAST
    AccessioniPrimary (citable) accession number: P52488
    Secondary accession number(s): D6VT24
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 139 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 18800 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, 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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3