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Protein

Ubiquitin-conjugating enzyme E2 20

Gene

UBC20

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 sitei119 – 1191Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cyclin, Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT1G50490-MONOMER.
ReactomeiREACT_273097. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_284122. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_294737. Senescence-Associated Secretory Phenotype (SASP).
REACT_295391. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_299093. Regulation of APC/C activators between G1/S and early anaphase.
REACT_301780. APC/C:Cdc20 mediated degradation of Securin.
REACT_305944. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_314276. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_318090. Separation of Sister Chromatids.
REACT_319658. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_336371. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_353749. APC-Cdc20 mediated degradation of Nek2A.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 20 (EC:6.3.2.19)
Alternative name(s):
Ubiquitin carrier protein 20
Gene namesi
Name:UBC20
Ordered Locus Names:At1g50490
ORF Names:F11F12.16, F17J6.3
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G50490.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 180180Ubiquitin-conjugating enzyme E2 20PRO_0000345186Add
BLAST

Proteomic databases

PaxDbiQ8L7T3.
PRIDEiQ8L7T3.

Expressioni

Tissue specificityi

Expressed in all tissues with cell division activities and in mature leaves.2 Publications

Developmental stagei

Expressed during the G2-M phases of the cell cycle.1 Publication

Inductioni

By the herbicide isoxaben and by biotic stresses.1 Publication

Gene expression databases

GenevestigatoriQ8L7T3.

Structurei

3D structure databases

ProteinModelPortaliQ8L7T3.
SMRiQ8L7T3. Positions 36-175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000233454.
InParanoidiQ8L7T3.
KOiK06688.
OMAiCNQEEYR.
PhylomeDBiQ8L7T3.

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.

Q8L7T3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVNGYQGN TPADPPASNG SKQPAAPTKT VDSQSVLKRL QSELMGLMMG
60 70 80 90 100
GGPGISAFPE EDNIFCWKGT ITGSKDTVFE GTEYRLSLSF SNDYPFKPPK
110 120 130 140 150
VKFETCCFHP NVDVYGNICL DILQDKWSSA YDVRTILLSI QSLLGEPNIS
160 170 180
SPLNTQAAQL WSNQEEYRKM VEKLYKPPSA
Length:180
Mass (Da):19,792
Last modified:October 1, 2002 - v1
Checksum:i0FFFF2E7347D815B
GO

Sequence cautioni

The sequence AAF87880.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG51188.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721T → I in AAM67229 (Ref. 6) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY127574 mRNA. Translation: AAM96887.1.
DQ027034 mRNA. Translation: AAY44860.1.
AC012561 Genomic DNA. Translation: AAF87880.1. Sequence problems.
AC079279 Genomic DNA. Translation: AAG51188.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE32556.1.
AK227382 mRNA. Translation: BAE99389.1.
AY088923 mRNA. Translation: AAM67229.1.
BT005855 mRNA. Translation: AAO64790.1.
PIRiD96541.
RefSeqiNP_564572.1. NM_103932.3.
UniGeneiAt.21610.
At.71081.

Genome annotation databases

EnsemblPlantsiAT1G50490.1; AT1G50490.1; AT1G50490.
GeneIDi841471.
KEGGiath:AT1G50490.

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
AY127574 mRNA. Translation: AAM96887.1.
DQ027034 mRNA. Translation: AAY44860.1.
AC012561 Genomic DNA. Translation: AAF87880.1. Sequence problems.
AC079279 Genomic DNA. Translation: AAG51188.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE32556.1.
AK227382 mRNA. Translation: BAE99389.1.
AY088923 mRNA. Translation: AAM67229.1.
BT005855 mRNA. Translation: AAO64790.1.
PIRiD96541.
RefSeqiNP_564572.1. NM_103932.3.
UniGeneiAt.21610.
At.71081.

3D structure databases

ProteinModelPortaliQ8L7T3.
SMRiQ8L7T3. Positions 36-175.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiQ8L7T3.
PRIDEiQ8L7T3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G50490.1; AT1G50490.1; AT1G50490.
GeneIDi841471.
KEGGiath:AT1G50490.

Organism-specific databases

GeneFarmi2577. 224.
TAIRiAT1G50490.

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000233454.
InParanoidiQ8L7T3.
KOiK06688.
OMAiCNQEEYR.
PhylomeDBiQ8L7T3.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciARA:AT1G50490-MONOMER.
ReactomeiREACT_273097. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_284122. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_294737. Senescence-Associated Secretory Phenotype (SASP).
REACT_295391. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_299093. Regulation of APC/C activators between G1/S and early anaphase.
REACT_301780. APC/C:Cdc20 mediated degradation of Securin.
REACT_305944. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_314276. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_318090. Separation of Sister Chromatids.
REACT_319658. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_336371. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_353749. APC-Cdc20 mediated degradation of Nek2A.

Miscellaneous databases

PROiQ8L7T3.

Gene expression databases

GenevestigatoriQ8L7T3.

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. "Molecular characterization of plant ubiquitin-conjugating enzymes belonging to the UbcP4/E2-C/UBCx/UbcH10 gene family."
    Criqui M.C., de Almeida Engler J., Camasses A., Capron A., Parmentier Y., Inze D., Genschik P.
    Plant Physiol. 130:1230-1240(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
  2. "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, INDUCTION, GENE FAMILY, NOMENCLATURE.
  3. "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.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "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.
  6. "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].
  7. "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.
  8. "Arabidopsis anaphase-promoting complexes: multiple activators and wide range of substrates might keep APC perpetually busy."
    Fueloep K., Tarayre S., Kelemen Z., Horvath G., Kevei Z., Nikovics K., Bako L., Brown S., Kondorosi A., Kondorosi E.
    Cell Cycle 4:1084-1092(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiUBC20_ARATH
AccessioniPrimary (citable) accession number: Q8L7T3
Secondary accession number(s): Q8L8L3, Q9C6Q4, Q9LPS2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: October 1, 2002
Last modified: April 1, 2015
This is version 95 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

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.