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Protein

Ubiquitin-conjugating enzyme E2 1

Gene

UBC1

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

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. ATP binding Source: UniProtKB-KW
  2. ligase activity Source: UniProtKB-KW
  3. ubiquitin-like protein transferase activity Source: GO_Central
  4. ubiquitin protein ligase activity Source: GO_Central
  5. ubiquitin protein ligase binding Source: GO_Central
  6. ubiquitin-protein transferase activity Source: TAIR

GO - Biological processi

  1. DNA repair Source: GO_Central
  2. histone H2B ubiquitination Source: TAIR
  3. proteasome-mediated ubiquitin-dependent protein catabolic process Source: GO_Central
  4. protein polyubiquitination Source: GO_Central
  5. ubiquitin-dependent protein catabolic process Source: TAIR
  6. vegetative to reproductive phase transition of meristem Source: TAIR
Complete GO annotation...

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.
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 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G14400.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
Complete GO annotation...

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 – 1815Combined sources
Beta strandi24 – 296Combined sources
Beta strandi32 – 4110Combined sources
Turni47 – 504Combined sources
Beta strandi52 – 587Combined sources
Turni61 – 655Combined sources
Beta strandi69 – 746Combined sources
Beta strandi85 – 873Combined sources
Helixi90 – 923Combined sources
Helixi102 – 11312Combined sources
Helixi124 – 1329Combined sources
Helixi134 – 14815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
OMAiIVEQSWV.
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

        10         20         30         40         50
MSTPARKRLM RDFKRLQQDP PAGISGAPQD NNIMLWNAVI FGPDDTPWDG
60 70 80 90 100
GTFKLSLQFS EDYPNKPPTV RFVSRMFHPN IYADGSICLD ILQNQWSPIY
110 120 130 140 150
DVAAILTSIQ SLLCDPNPNS PANSEAARMY SESKREYNRR VRDVVEQSWT

AD
Length:152
Mass (Da):17,281
Last modified:May 1, 1992 - v1
Checksum:i896D911930C39045
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP25865.
PRIDEiP25865.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

GeneFarmi4743. 464.
TAIRiAT1G14400.

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000233454.
InParanoidiP25865.
KOiK10573.
OMAiIVEQSWV.
PhylomeDBiP25865.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciARA:AT1G14400-MONOMER.
ARA:GQT-2296-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP25865.
PROiP25865.

Gene expression databases

GenevestigatoriP25865.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 133 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.