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P25865 (UBC1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:UBC1
Ordered Locus Names:At1g14400
ORF Names:F14L17.17, F14L17_35
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Ref.3 Ref.10

Catalytic activity

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

Pathway

Protein modification; protein ubiquitination.

Tissue specificity

Ubiquitously expressed. Ref.3 Ref.11

Induction

Not induced by heat shock. Ref.11

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 152152Ubiquitin-conjugating enzyme E2 1
PRO_0000082570

Sites

Active site881Glycyl thioester intermediate

Experimental info

Mutagenesis881C → S: Stabilization of the ester bond with the ubiquitin. Ref.10

Secondary structure

......................... 152
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25865 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 896D911930C39045

FASTA15217,281
        10         20         30         40         50         60 
MSTPARKRLM RDFKRLQQDP PAGISGAPQD NNIMLWNAVI FGPDDTPWDG GTFKLSLQFS 

        70         80         90        100        110        120 
EDYPNKPPTV RFVSRMFHPN IYADGSICLD ILQNQWSPIY DVAAILTSIQ SLLCDPNPNS 

       130        140        150 
PANSEAARMY SESKREYNRR VRDVVEQSWT AD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"Further progress towards a catalogue of all Arabidopsis genes: analysis of a set of 5000 non-redundant ESTs."
Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C., Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R., Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J. expand/collapse author list , Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D., Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P., Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.
Plant J. 9:101-124(1996) [PubMed] [Europe PMC] [Abstract]
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).
+Additional computationally mapped references.

Web resources

PlantsUBQ

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS43781.
RefSeqNP_563951.1. NM_101307.4.
NP_973825.1. NM_202096.2.
UniGeneAt.331.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AAKX-ray2.40A1-152[»]
ProteinModelPortalP25865.
SMRP25865. Positions 1-150.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid23242. 2 interactions.
IntActP25865. 2 interactions.
STRING3702.AT1G14400.1-P.

Proteomic databases

PaxDbP25865.
PRIDEP25865.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G14400.1; AT1G14400.1; AT1G14400.
AT1G14400.2; AT1G14400.2; AT1G14400.
GeneID838002.
KEGGath:AT1G14400.

Organism-specific databases

GeneFarm4743. 464.
TAIRAT1G14400.

Phylogenomic databases

eggNOGCOG5078.
HOGENOMHOG000233454.
InParanoidP25865.
KOK10573.
OMAPVPDNVM.
PhylomeDBP25865.
ProtClustDBCLSN2687804.

Enzyme and pathway databases

BioCycARA:AT1G14400-MONOMER.
ARA:GQT-2296-MONOMER.
UniPathwayUPA00143.

Gene expression databases

GenevestigatorP25865.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP25865.

Entry information

Entry nameUBC1_ARATH
AccessionPrimary (citable) accession number: P25865
Secondary accession number(s): Q4TZ08
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: February 19, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names