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P22515

- UBA1_YEAST

UniProt

P22515 - UBA1_YEAST

Protein

Ubiquitin-activating enzyme E1 1

Gene

UBA1

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 151 (01 Oct 2014)
      Sequence version 2 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei600 – 6001Glycyl thioester intermediatePROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi444 – 47330ATPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ubiquitin activating enzyme activity Source: SGD

    GO - Biological processi

    1. protein ubiquitination Source: SGD

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31969-MONOMER.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-activating enzyme E1 1
    Gene namesi
    Name:UBA1
    Ordered Locus Names:YKL210W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XI

    Organism-specific databases

    CYGDiYKL210w.
    SGDiS000001693. UBA1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. nucleus Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 10241023Ubiquitin-activating enzyme E1 1PRO_0000194977Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei265 – 2651Phosphoserine1 Publication
    Modified residuei914 – 9141Phosphoserine1 Publication

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP22515.
    PaxDbiP22515.
    PeptideAtlasiP22515.
    PRIDEiP22515.

    Expressioni

    Gene expression databases

    GenevestigatoriP22515.

    Interactioni

    Subunit structurei

    Monomer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    UBI4P618642EBI-19703,EBI-19797From a different organism.

    Protein-protein interaction databases

    BioGridi33955. 58 interactions.
    DIPiDIP-4853N.
    IntActiP22515. 16 interactions.
    MINTiMINT-489454.
    STRINGi4932.YKL210W.

    Structurei

    Secondary structure

    1
    1024
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi16 – 2611
    Helixi28 – 347
    Beta strandi38 – 425
    Helixi46 – 5813
    Beta strandi61 – 666
    Helixi73 – 775
    Helixi84 – 863
    Helixi91 – 10010
    Beta strandi108 – 1103
    Helixi117 – 1226
    Beta strandi124 – 1285
    Helixi134 – 14714
    Beta strandi150 – 1578
    Beta strandi160 – 1667
    Beta strandi171 – 1777
    Beta strandi183 – 1897
    Beta strandi194 – 1985
    Beta strandi210 – 2156
    Helixi220 – 2234
    Beta strandi231 – 2344
    Beta strandi237 – 2393
    Helixi244 – 2463
    Beta strandi254 – 2585
    Beta strandi262 – 2643
    Helixi269 – 2746
    Helixi283 – 2875
    Helixi288 – 30518
    Turni306 – 3083
    Helixi316 – 33217
    Turni334 – 3374
    Helixi345 – 3539
    Turni354 – 3563
    Helixi360 – 37920
    Beta strandi387 – 3926
    Helixi394 – 3963
    Turni400 – 4023
    Turni407 – 4104
    Helixi418 – 4247
    Helixi426 – 4338
    Beta strandi436 – 4405
    Helixi444 – 45613
    Turni457 – 4593
    Beta strandi465 – 4695
    Helixi476 – 4805
    Helixi487 – 4893
    Helixi494 – 50512
    Helixi507 – 5093
    Turni510 – 5123
    Beta strandi513 – 5164
    Helixi522 – 5243
    Turni525 – 5273
    Helixi530 – 5345
    Beta strandi537 – 5415
    Helixi546 – 55914
    Beta strandi563 – 5697
    Beta strandi572 – 5787
    Turni580 – 5823
    Helixi586 – 5883
    Helixi599 – 6035
    Helixi609 – 62416
    Helixi626 – 63611
    Helixi640 – 6478
    Helixi651 – 66313
    Helixi669 – 68416
    Helixi686 – 6949
    Beta strandi704 – 7085
    Helixi725 – 74218
    Helixi755 – 7639
    Helixi797 – 8026
    Helixi808 – 8114
    Helixi830 – 84415
    Helixi852 – 8598
    Helixi867 – 88519
    Helixi891 – 8933
    Beta strandi896 – 9005
    Turni901 – 9044
    Beta strandi905 – 9095
    Beta strandi916 – 9194
    Beta strandi922 – 9254
    Turni926 – 9283
    Beta strandi930 – 9367
    Helixi939 – 95012
    Beta strandi953 – 9597
    Beta strandi962 – 9665
    Helixi971 – 9777
    Helixi982 – 9909
    Beta strandi1000 – 10089
    Beta strandi1019 – 10235

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3CMMX-ray2.70A/C10-1024[»]
    4NNJX-ray2.40A/C9-1024[»]
    ProteinModelPortaliP22515.
    SMRiP22515. Positions 11-1024.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22515.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati27 – 1641381-1Add
    BLAST
    Repeati425 – 5791551-2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni27 – 5795532 approximate repeatsAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ubiquitin-activating E1 family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0476.
    GeneTreeiENSGT00390000016689.
    HOGENOMiHOG000167329.
    KOiK03178.
    OMAiKFHPVKQ.
    OrthoDBiEOG7FZ07P.

    Family and domain databases

    Gene3Di1.10.3240.10. 2 hits.
    3.40.50.720. 4 hits.
    InterProiIPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    IPR018965. Ub-activating_enz_e1_C.
    IPR023280. Ub-like_act_enz_cat_cys_dom.
    IPR000127. UBact_repeat.
    IPR019572. Ubiquitin-activating_enzyme.
    IPR018075. UBQ-activ_enz_E1.
    IPR018074. UBQ-activ_enz_E1_AS.
    IPR000011. UBQ/SUMO-activ_enz_E1-like.
    [Graphical view]
    PfamiPF00899. ThiF. 2 hits.
    PF09358. UBA_e1_C. 1 hit.
    PF10585. UBA_e1_thiolCys. 1 hit.
    PF02134. UBACT. 2 hits.
    [Graphical view]
    PRINTSiPR01849. UBIQUITINACT.
    SMARTiSM00985. UBA_e1_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF69572. SSF69572. 2 hits.
    TIGRFAMsiTIGR01408. Ube1. 1 hit.
    PROSITEiPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
    PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P22515-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSNNSGLSA AGEIDESLYS RQLYVLGKEA MLKMQTSNVL ILGLKGLGVE     50
    IAKNVVLAGV KSMTVFDPEP VQLADLSTQF FLTEKDIGQK RGDVTRAKLA 100
    ELNAYVPVNV LDSLDDVTQL SQFQVVVATD TVSLEDKVKI NEFCHSSGIR 150
    FISSETRGLF GNTFVDLGDE FTVLDPTGEE PRTGMVSDIE PDGTVTMLDD 200
    NRHGLEDGNF VRFSEVEGLD KLNDGTLFKV EVLGPFAFRI GSVKEYGEYK 250
    KGGIFTEVKV PRKISFKSLK QQLSNPEFVF SDFAKFDRAA QLHLGFQALH 300
    QFAVRHNGEL PRTMNDEDAN ELIKLVTDLS VQQPEVLGEG VDVNEDLIKE 350
    LSYQARGDIP GVVAFFGGLV AQEVLKACSG KFTPLKQFMY FDSLESLPDP 400
    KNFPRNEKTT QPVNSRYDNQ IAVFGLDFQK KIANSKVFLV GSGAIGCEML 450
    KNWALLGLGS GSDGYIVVTD NDSIEKSNLN RQFLFRPKDV GKNKSEVAAE 500
    AVCAMNPDLK GKINAKIDKV GPETEEIFND SFWESLDFVT NALDNVDART 550
    YVDRRCVFYR KPLLESGTLG TKGNTQVIIP RLTESYSSSR DPPEKSIPLC 600
    TLRSFPNKID HTIAWAKSLF QGYFTDSAEN VNMYLTQPNF VEQTLKQSGD 650
    VKGVLESISD SLSSKPHNFE DCIKWARLEF EKKFNHDIKQ LLFNFPKDAK 700
    TSNGEPFWSG AKRAPTPLEF DIYNNDHFHF VVAGASLRAY NYGIKSDDSN 750
    SKPNVDEYKS VIDHMIIPEF TPNANLKIQV NDDDPDPNAN AANGSDEIDQ 800
    LVSSLPDPST LAGFKLEPVD FEKDDDTNHH IEFITACSNC RAQNYFIETA 850
    DRQKTKFIAG RIIPAIATTT SLVTGLVNLE LYKLIDNKTD IEQYKNGFVN 900
    LALPFFGFSE PIASPKGEYN NKKYDKIWDR FDIKGDIKLS DLIEHFEKDE 950
    GLEITMLSYG VSLLYASFFP PKKLKERLNL PITQLVKLVT KKDIPAHVST 1000
    MILEICADDK EGEDVEVPFI TIHL 1024
    Length:1,024
    Mass (Da):114,266
    Last modified:June 1, 1994 - v2
    Checksum:i8910804DF9156661
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti526 – 5261E → K in CAA39056. (PubMed:1989885)Curated
    Sequence conflicti736 – 7361S → N in CAA39056. (PubMed:1989885)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55386 Genomic DNA. Translation: CAA39056.1.
    Z28210 Genomic DNA. Translation: CAA82055.1.
    X15428 Genomic DNA. Translation: CAA33468.1.
    BK006944 Genomic DNA. Translation: DAA08959.1.
    PIRiS38048.
    RefSeqiNP_012712.1. NM_001179775.1.

    Genome annotation databases

    EnsemblFungiiYKL210W; YKL210W; YKL210W.
    GeneIDi853670.
    KEGGisce:YKL210W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55386 Genomic DNA. Translation: CAA39056.1 .
    Z28210 Genomic DNA. Translation: CAA82055.1 .
    X15428 Genomic DNA. Translation: CAA33468.1 .
    BK006944 Genomic DNA. Translation: DAA08959.1 .
    PIRi S38048.
    RefSeqi NP_012712.1. NM_001179775.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3CMM X-ray 2.70 A/C 10-1024 [» ]
    4NNJ X-ray 2.40 A/C 9-1024 [» ]
    ProteinModelPortali P22515.
    SMRi P22515. Positions 11-1024.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33955. 58 interactions.
    DIPi DIP-4853N.
    IntActi P22515. 16 interactions.
    MINTi MINT-489454.
    STRINGi 4932.YKL210W.

    Proteomic databases

    MaxQBi P22515.
    PaxDbi P22515.
    PeptideAtlasi P22515.
    PRIDEi P22515.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YKL210W ; YKL210W ; YKL210W .
    GeneIDi 853670.
    KEGGi sce:YKL210W.

    Organism-specific databases

    CYGDi YKL210w.
    SGDi S000001693. UBA1.

    Phylogenomic databases

    eggNOGi COG0476.
    GeneTreei ENSGT00390000016689.
    HOGENOMi HOG000167329.
    KOi K03178.
    OMAi KFHPVKQ.
    OrthoDBi EOG7FZ07P.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    BioCyci YEAST:G3O-31969-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P22515.
    NextBioi 974614.
    PROi P22515.

    Gene expression databases

    Genevestigatori P22515.

    Family and domain databases

    Gene3Di 1.10.3240.10. 2 hits.
    3.40.50.720. 4 hits.
    InterProi IPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    IPR018965. Ub-activating_enz_e1_C.
    IPR023280. Ub-like_act_enz_cat_cys_dom.
    IPR000127. UBact_repeat.
    IPR019572. Ubiquitin-activating_enzyme.
    IPR018075. UBQ-activ_enz_E1.
    IPR018074. UBQ-activ_enz_E1_AS.
    IPR000011. UBQ/SUMO-activ_enz_E1-like.
    [Graphical view ]
    Pfami PF00899. ThiF. 2 hits.
    PF09358. UBA_e1_C. 1 hit.
    PF10585. UBA_e1_thiolCys. 1 hit.
    PF02134. UBACT. 2 hits.
    [Graphical view ]
    PRINTSi PR01849. UBIQUITINACT.
    SMARTi SM00985. UBA_e1_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69572. SSF69572. 2 hits.
    TIGRFAMsi TIGR01408. Ube1. 1 hit.
    PROSITEi PS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
    PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "UBA 1: an essential yeast gene encoding ubiquitin-activating enzyme."
      McGrath J.P., Jentsch S., Varshavsky A.
      EMBO J. 10:227-236(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: ATCC 204508 / S288c.
    2. "Complete DNA sequence of yeast chromosome XI."
      Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
      , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
      Nature 369:371-378(1994) [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. "The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoprotein."
      McGrath J.P., Varshavsky A.
      Nature 340:400-404(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 940-1024.
      Strain: ATCC 204508 / S288c.
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "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-914, IDENTIFICATION BY MASS SPECTROMETRY [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].
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    10. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiUBA1_YEAST
    AccessioniPrimary (citable) accession number: P22515
    Secondary accession number(s): D6VWZ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 151 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are two active sites within the E1 molecule, allowing it to accommodate two ubiquitin moieties at a time, with a new ubiquitin forming an adenylate intermediate as the previous one is transferred to the thiol site.
    Present with 17700 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 XI
      Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

    External Data

    Dasty 3