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Protein

Ubiquitin-conjugating enzyme E2 34

Gene

UBC34

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.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 sitei87 – 871Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ligase activity Source: UniProtKB-KW
  3. small conjugating 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. ER-associated ubiquitin-dependent protein catabolic process Source: GO_Central
  2. protein polyubiquitination Source: GO_Central
  3. 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:AT1G17280-MONOMER.
ARA:GQT-1971-MONOMER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 34 (EC:6.3.2.19)
Alternative name(s):
Ubiquitin carrier protein 34
Gene namesi
Name:UBC34
Ordered Locus Names:At1g17280
ORF Names:F20D23.1
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G17280.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei214 – 23421HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: GO_Central
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 237237Ubiquitin-conjugating enzyme E2 34PRO_0000345199Add
BLAST

Proteomic databases

PRIDEiQ9SHI7.

Expressioni

Gene expression databases

GenevestigatoriQ9SHI7.

Interactioni

Protein-protein interaction databases

BioGridi23540. 1 interaction.
IntActiQ9SHI7. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9SHI7.
SMRiQ9SHI7. Positions 8-164.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000170329.
InParanoidiQ9SHI7.
KOiK04554.
OMAiLCKEPVP.
PhylomeDBiQ9SHI7.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9SHI7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEKACIKRL QKEYRALCKE PVSHVVARPS PNDILEWHYV LEGSEGTPFA
60 70 80 90 100
GGFYYGKIKF PPEYPYKPPG ITMTTPNGRF MTQKKICLSM SDFHPESWNP
110 120 130 140 150
MWSVSSILTG LLSFMMDTSP TTGSVNTTVI EKQRLAKSSL AFNCKTPAFR
160 170 180 190 200
KLFPEYVEKY NQQQLAEQAT TQLTTPESPQ KSDTKVESEK TIDPTKGDSE
210 220 230
GGLKERKKNN KQGLPAWIIL LLVSVFGVVM ALPLLQL
Length:237
Mass (Da):26,614
Last modified:May 1, 2000 - v1
Checksum:iFE2888F36BF8B8EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007651 Genomic DNA. Translation: AAD50006.1.
CP002684 Genomic DNA. Translation: AEE29567.1.
CP002684 Genomic DNA. Translation: AEE29568.1.
BT003073 mRNA. Translation: AAO23638.1.
AK227344 mRNA. Translation: BAE99355.1.
AY084676 mRNA. Translation: AAM61238.1.
DQ027047 mRNA. Translation: AAY44873.1.
PIRiC86309.
RefSeqiNP_001077554.1. NM_001084085.1.
NP_173172.1. NM_101590.3.
UniGeneiAt.42947.

Genome annotation databases

EnsemblPlantsiAT1G17280.1; AT1G17280.1; AT1G17280.
AT1G17280.2; AT1G17280.2; AT1G17280.
GeneIDi838300.
KEGGiath:AT1G17280.

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
AC007651 Genomic DNA. Translation: AAD50006.1.
CP002684 Genomic DNA. Translation: AEE29567.1.
CP002684 Genomic DNA. Translation: AEE29568.1.
BT003073 mRNA. Translation: AAO23638.1.
AK227344 mRNA. Translation: BAE99355.1.
AY084676 mRNA. Translation: AAM61238.1.
DQ027047 mRNA. Translation: AAY44873.1.
PIRiC86309.
RefSeqiNP_001077554.1. NM_001084085.1.
NP_173172.1. NM_101590.3.
UniGeneiAt.42947.

3D structure databases

ProteinModelPortaliQ9SHI7.
SMRiQ9SHI7. Positions 8-164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi23540. 1 interaction.
IntActiQ9SHI7. 1 interaction.

Proteomic databases

PRIDEiQ9SHI7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G17280.1; AT1G17280.1; AT1G17280.
AT1G17280.2; AT1G17280.2; AT1G17280.
GeneIDi838300.
KEGGiath:AT1G17280.

Organism-specific databases

TAIRiAT1G17280.

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000170329.
InParanoidiQ9SHI7.
KOiK04554.
OMAiLCKEPVP.
PhylomeDBiQ9SHI7.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciARA:AT1G17280-MONOMER.
ARA:GQT-1971-MONOMER.

Gene expression databases

GenevestigatoriQ9SHI7.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "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.
  4. "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.
  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. "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] OF 1-213, FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.

Entry informationi

Entry nameiUBC34_ARATH
AccessioniPrimary (citable) accession number: Q9SHI7
Secondary accession number(s): Q4TYX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: May 1, 2000
Last modified: March 4, 2015
This is version 101 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.