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P25865

- UBC1_ARATH

UniProt

P25865 - UBC1_ARATH

Protein

Ubiquitin-conjugating enzyme E2 1

Gene

UBC1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.2 Publications

    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. ubiquitin-protein transferase activity Source: TAIR

    GO - Biological processi

    1. histone H2B ubiquitination Source: TAIR
    2. leaf morphogenesis Source: TAIR
    3. negative regulation of flower development Source: TAIR
    4. ubiquitin-dependent protein catabolic process Source: TAIR
    5. vegetative to reproductive phase transition of meristem Source: TAIR

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciARA:AT1G14400-MONOMER.
    ARA:GQT-2296-MONOMER.
    ReactomeiREACT_187848. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-conjugating enzyme E2 1 (EC:6.3.2.19)
    Alternative name(s):
    Ubiquitin carrier protein 1
    Ubiquitin-conjugating enzyme E2-17 kDa 1
    Ubiquitin-protein ligase 1
    Gene namesi
    Name:UBC1
    Ordered Locus Names:At1g14400
    ORF Names:F14L17.17, F14L17_35
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G14400.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi88 – 881C → S: Stabilization of the ester bond with the ubiquitin. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 152152Ubiquitin-conjugating enzyme E2 1PRO_0000082570Add
    BLAST

    Proteomic databases

    PaxDbiP25865.
    PRIDEiP25865.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.2 Publications

    Inductioni

    Not induced by heat shock.1 Publication

    Gene expression databases

    GenevestigatoriP25865.

    Interactioni

    Protein-protein interaction databases

    BioGridi23242. 2 interactions.
    IntActiP25865. 2 interactions.
    STRINGi3702.AT1G14400.1-P.

    Structurei

    Secondary structure

    1
    152
    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
    Helixi102 – 11312
    Helixi124 – 1329
    Helixi134 – 14815

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AAKX-ray2.40A1-152[»]
    ProteinModelPortaliP25865.
    SMRiP25865. Positions 1-150.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25865.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5078.
    HOGENOMiHOG000233454.
    InParanoidiP25865.
    KOiK10573.
    OMAiPVPDNVM.
    PhylomeDBiP25865.

    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.

    P25865-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTPARKRLM RDFKRLQQDP PAGISGAPQD NNIMLWNAVI FGPDDTPWDG    50
    GTFKLSLQFS EDYPNKPPTV RFVSRMFHPN IYADGSICLD ILQNQWSPIY 100
    DVAAILTSIQ SLLCDPNPNS PANSEAARMY SESKREYNRR VRDVVEQSWT 150
    AD 152
    Length:152
    Mass (Da):17,281
    Last modified:May 1, 1992 - v1
    Checksum:i896D911930C39045
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M62721 mRNA. Translation: AAA32903.1.
    L19351 Genomic DNA. Translation: AAA32897.1.
    DQ027016 mRNA. Translation: AAY44842.1.
    AC012188 Genomic DNA. Translation: AAF43940.1.
    CP002684 Genomic DNA. Translation: AEE29158.1.
    CP002684 Genomic DNA. Translation: AEE29159.1.
    AF332451 mRNA. Translation: AAG48814.1.
    AY070074 mRNA. Translation: AAL49769.1.
    AY091330 mRNA. Translation: AAM14269.1.
    AY085783 mRNA. Translation: AAM63000.1.
    AK226391 mRNA. Translation: BAE98537.1.
    Z27262 mRNA. Translation: CAA81773.1.
    PIRiS43781.
    RefSeqiNP_563951.1. NM_101307.4.
    NP_973825.1. NM_202096.2.
    UniGeneiAt.331.

    Genome annotation databases

    EnsemblPlantsiAT1G14400.1; AT1G14400.1; AT1G14400.
    AT1G14400.2; AT1G14400.2; AT1G14400.
    GeneIDi838002.
    KEGGiath:AT1G14400.

    Cross-referencesi

    Web resourcesi

    PlantsUBQ

    A functional genomics database for the ubiquitin/26S proteasome proteolytic pathway in plants

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M62721 mRNA. Translation: AAA32903.1 .
    L19351 Genomic DNA. Translation: AAA32897.1 .
    DQ027016 mRNA. Translation: AAY44842.1 .
    AC012188 Genomic DNA. Translation: AAF43940.1 .
    CP002684 Genomic DNA. Translation: AEE29158.1 .
    CP002684 Genomic DNA. Translation: AEE29159.1 .
    AF332451 mRNA. Translation: AAG48814.1 .
    AY070074 mRNA. Translation: AAL49769.1 .
    AY091330 mRNA. Translation: AAM14269.1 .
    AY085783 mRNA. Translation: AAM63000.1 .
    AK226391 mRNA. Translation: BAE98537.1 .
    Z27262 mRNA. Translation: CAA81773.1 .
    PIRi S43781.
    RefSeqi NP_563951.1. NM_101307.4.
    NP_973825.1. NM_202096.2.
    UniGenei At.331.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AAK X-ray 2.40 A 1-152 [» ]
    ProteinModelPortali P25865.
    SMRi P25865. Positions 1-150.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 23242. 2 interactions.
    IntActi P25865. 2 interactions.
    STRINGi 3702.AT1G14400.1-P.

    Proteomic databases

    PaxDbi P25865.
    PRIDEi P25865.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G14400.1 ; AT1G14400.1 ; AT1G14400 .
    AT1G14400.2 ; AT1G14400.2 ; AT1G14400 .
    GeneIDi 838002.
    KEGGi ath:AT1G14400.

    Organism-specific databases

    GeneFarmi 4743. 464.
    TAIRi AT1G14400.

    Phylogenomic databases

    eggNOGi COG5078.
    HOGENOMi HOG000233454.
    InParanoidi P25865.
    KOi K10573.
    OMAi PVPDNVM.
    PhylomeDBi P25865.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    BioCyci ARA:AT1G14400-MONOMER.
    ARA:GQT-2296-MONOMER.
    Reactomei REACT_187848. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    EvolutionaryTracei P25865.

    Gene expression databases

    Genevestigatori P25865.

    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. "Cloning of a 16-kDa ubiquitin carrier protein from wheat and Arabidopsis thaliana. Identification of functional domains by in vitro mutagenesis."
      Sullivan M.L., Vierstra R.D.
      J. Biol. Chem. 266:23878-23885(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
    2. "Homologues of wheat ubiquitin-conjugating enzymes -- TaUBC1 and TaUBC4 are encoded by small multigene families in Arabidopsis thaliana."
      Sullivan M.L., Carpenter T.B., Vierstra R.D.
      Plant Mol. Biol. 24:651-661(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. Columbia.
    3. "Genome analysis and functional characterization of the E2 and RING-type E3 ligase ubiquitination enzymes of Arabidopsis."
      Kraft E., Stone S.L., Ma L., Su N., Gao Y., Lau O.-S., Deng X.-W., Callis J.
      Plant Physiol. 139:1597-1611(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
    4. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    5. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    6. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    7. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    8. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
      , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-98.
      Strain: cv. Columbia.
      Tissue: Dry seed.
    10. "Formation of a stable adduct between ubiquitin and the Arabidopsis ubiquitin-conjugating enzyme, AtUBC1+."
      Sullivan M.L., Vierstra R.D.
      J. Biol. Chem. 268:8777-8780(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-88.
    11. "Members of two gene families encoding ubiquitin-conjugating enzymes, AtUBC1-3 and AtUBC4-6, from Arabidopsis thaliana are differentially expressed."
      Thoma S., Sullivan M.L., Vierstra R.D.
      Plant Mol. Biol. 31:493-505(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION.
    12. "Three-dimensional structure of a ubiquitin-conjugating enzyme (E2)."
      Cook W.J., Jeffrey L.C., Sullivan M.L., Vierstra R.D.
      J. Biol. Chem. 267:15116-15121(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

    Entry informationi

    Entry nameiUBC1_ARATH
    AccessioniPrimary (citable) accession number: P25865
    Secondary accession number(s): Q4TZ08
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3