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P25865

- UBC1_ARATH

UniProt

P25865 - UBC1_ARATH

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Protein
Ubiquitin-conjugating enzyme E2 1
Gene
UBC1, At1g14400, F14L17.17, F14L17_35
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei88 – 881Glycyl thioester intermediate

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. acid-amino acid ligase activity Source: InterPro
  3. ubiquitin-protein transferase activity Source: TAIR
Complete GO annotation...

GO - Biological processi

  1. histone H2B ubiquitination Source: TAIR
  2. leaf morphogenesis Source: TAIR
  3. negative regulation of flower development Source: TAIR
  4. ubiquitin-dependent protein catabolic process Source: TAIR
  5. 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.
ReactomeiREACT_187848. Antigen processing: Ubiquitination & Proteasome degradation.
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: Chromosome 1

Organism-specific databases

TAIRiAT1G14400.

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 1
PRO_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

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1815
Beta strandi24 – 296
Beta strandi32 – 4110
Turni47 – 504
Beta strandi52 – 587
Turni61 – 655
Beta strandi69 – 746
Beta strandi85 – 873
Helixi90 – 923
Helixi102 – 11312
Helixi124 – 1329
Helixi134 – 14815

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AAKX-ray2.40A1-152[»]
ProteinModelPortaliP25865.
SMRiP25865. Positions 1-150.

Miscellaneous databases

EvolutionaryTraceiP25865.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000233454.
InParanoidiP25865.
KOiK10573.
OMAiPVPDNVM.
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

MSTPARKRLM RDFKRLQQDP PAGISGAPQD NNIMLWNAVI FGPDDTPWDG    50
GTFKLSLQFS EDYPNKPPTV RFVSRMFHPN IYADGSICLD ILQNQWSPIY 100
DVAAILTSIQ SLLCDPNPNS PANSEAARMY SESKREYNRR VRDVVEQSWT 150
AD 152
Length:152
Mass (Da):17,281
Last modified:May 1, 1992 - v1
Checksum:i896D911930C39045
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S43781.
RefSeqi NP_563951.1. NM_101307.4.
NP_973825.1. NM_202096.2.
UniGenei At.331.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2AAK X-ray 2.40 A 1-152 [» ]
ProteinModelPortali P25865.
SMRi P25865. Positions 1-150.
ModBasei Search...

Protein-protein interaction databases

BioGridi 23242. 2 interactions.
IntActi P25865. 2 interactions.
STRINGi 3702.AT1G14400.1-P.

Proteomic databases

PaxDbi P25865.
PRIDEi P25865.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G14400.1 ; AT1G14400.1 ; AT1G14400 .
AT1G14400.2 ; AT1G14400.2 ; AT1G14400 .
GeneIDi 838002.
KEGGi ath:AT1G14400.

Organism-specific databases

GeneFarmi 4743. 464.
TAIRi AT1G14400.

Phylogenomic databases

eggNOGi COG5078.
HOGENOMi HOG000233454.
InParanoidi P25865.
KOi K10573.
OMAi PVPDNVM.
PhylomeDBi P25865.

Enzyme and pathway databases

UniPathwayi UPA00143 .
BioCyci ARA:AT1G14400-MONOMER.
ARA:GQT-2296-MONOMER.
Reactomei REACT_187848. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

EvolutionaryTracei P25865.

Gene expression databases

Genevestigatori P25865.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF00179. UQ_con. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 126 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

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