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Protein

Ubiquitin-conjugating enzyme E2 11

Gene

UBC11

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Mediates the selective degradation of short-lived and abnormal proteins.1 Publication

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei85 – 851Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ligase activity Source: UniProtKB-KW
  3. ubiquitin-protein transferase activity Source: TAIR

GO - Biological processi

  1. ubiquitin-dependent protein catabolic process 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:AT3G08690-MONOMER.
ARA:GQT-2213-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 11 (EC:6.3.2.19)
Alternative name(s):
Ubiquitin carrier protein 11
Ubiquitin-conjugating enzyme E2-17 kDa 11
Ubiquitin-protein ligase 11
Gene namesi
Name:UBC11
Ordered Locus Names:At3g08690
ORF Names:F17O14.16
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G08690.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 148148Ubiquitin-conjugating enzyme E2 11PRO_0000082579Add
BLAST

Proteomic databases

PaxDbiP35134.
PRIDEiP35134.

Expressioni

Tissue specificityi

Ubiquitously expressed. Mainly in petals.

Inductioni

Up-regulated by syringolin, a cell death-inducing chemical.1 Publication

Gene expression databases

GenevestigatoriP35134.

Interactioni

Subunit structurei

Interacts with the E3 ubiquitin-protein ligases MBR1 and MBR2.1 Publication

Protein-protein interaction databases

BioGridi5351. 6 interactions.
IntActiP35134. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliP35134.
SMRiP35134. Positions 2-146.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000233455.
InParanoidiP35134.
KOiK06689.
OMAiSAREWTH.
PhylomeDBiP35134.

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.

P35134-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASKRILKEL KDLQKDPPSN CSAGPVAEDM FHWQATIMGP PESPYAGGVF
60 70 80 90 100
LVSIHFPPDY PFKPPKVSFK TKVYHPNINS NGSICLDILK EQWSPALTIS
110 120 130 140
KVLLSICSLL TDPNPDDPLV PEIAHMYKTD RSKYESTARS WTQKYAMG
Length:148
Mass (Da):16,551
Last modified:January 24, 2001 - v2
Checksum:i74A0991115BA50EA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ027025 mRNA. Translation: AAY44851.1.
AC012562 Genomic DNA. Translation: AAG51362.1.
CP002686 Genomic DNA. Translation: AEE74664.1.
CP002686 Genomic DNA. Translation: AEE74665.1.
AY063869 mRNA. Translation: AAL36225.1.
AY091223 mRNA. Translation: AAM14162.1.
AY086109 mRNA. Translation: AAM63316.1.
AK228254 mRNA. Translation: BAF00202.1.
Z14992 mRNA. Translation: CAA78716.1.
L00641 mRNA. Translation: AAA32896.1.
PIRiS32673.
RefSeqiNP_001189841.1. NM_001202912.1.
NP_566331.1. NM_111703.3.
UniGeneiAt.202.

Genome annotation databases

EnsemblPlantsiAT3G08690.1; AT3G08690.1; AT3G08690.
AT3G08690.2; AT3G08690.2; AT3G08690.
GeneIDi820016.
KEGGiath:AT3G08690.

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
DQ027025 mRNA. Translation: AAY44851.1.
AC012562 Genomic DNA. Translation: AAG51362.1.
CP002686 Genomic DNA. Translation: AEE74664.1.
CP002686 Genomic DNA. Translation: AEE74665.1.
AY063869 mRNA. Translation: AAL36225.1.
AY091223 mRNA. Translation: AAM14162.1.
AY086109 mRNA. Translation: AAM63316.1.
AK228254 mRNA. Translation: BAF00202.1.
Z14992 mRNA. Translation: CAA78716.1.
L00641 mRNA. Translation: AAA32896.1.
PIRiS32673.
RefSeqiNP_001189841.1. NM_001202912.1.
NP_566331.1. NM_111703.3.
UniGeneiAt.202.

3D structure databases

ProteinModelPortaliP35134.
SMRiP35134. Positions 2-146.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi5351. 6 interactions.
IntActiP35134. 3 interactions.

Proteomic databases

PaxDbiP35134.
PRIDEiP35134.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G08690.1; AT3G08690.1; AT3G08690.
AT3G08690.2; AT3G08690.2; AT3G08690.
GeneIDi820016.
KEGGiath:AT3G08690.

Organism-specific databases

TAIRiAT3G08690.

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000233455.
InParanoidiP35134.
KOiK06689.
OMAiSAREWTH.
PhylomeDBiP35134.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciARA:AT3G08690-MONOMER.
ARA:GQT-2213-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

PROiP35134.

Gene expression databases

GenevestigatoriP35134.

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. "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, INDUCTION, GENE FAMILY, NOMENCLATURE.
  2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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.
  5. "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].
  6. "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.
  7. "Homologs of the essential ubiquitin conjugating enzymes UBC1, 4, and 5 in yeast are encoded by a multigene family in Arabidopsis thaliana."
    Girod P.-A., Carpenter T.B., van Nocker S., Sullivan M.L., Vierstra R.D.
    Plant J. 3:545-552(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 31-148.
    Strain: cv. Columbia.
    Tissue: Leaf.
  8. "Proteasome-mediated turnover of Arabidopsis MED25 is coupled to the activation of FLOWERING LOCUS T transcription."
    Inigo S., Giraldez A.N., Chory J., Cerdan P.D.
    Plant Physiol. 160:1662-1673(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MBR1 AND MBR2.

Entry informationi

Entry nameiUBC11_ARATH
AccessioniPrimary (citable) accession number: P35134
Secondary accession number(s): Q4TYZ9, Q9M9J1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 24, 2001
Last modified: April 29, 2015
This is version 124 of the entry and version 2 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.