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Protein

Ubiquitin-conjugating enzyme E2 28

Gene

UBC28

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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

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

GO - Biological processi

  1. protein ubiquitination Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT1G64230-MONOMER.
ARA:GQT-1299-MONOMER.
ARA:GQT-1300-MONOMER.
ARA:GQT-1301-MONOMER.
ARA:GQT-1302-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 28 (EC:6.3.2.19)
Alternative name(s):
Ubiquitin carrier protein 28
Gene namesi
Name:UBC28
Synonyms:UBC9A
Ordered Locus Names:At1g64230
ORF Names:F22C12.2
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G64230.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 148148Ubiquitin-conjugating enzyme E2 28PRO_0000345193Add
BLAST

Proteomic databases

PaxDbiQ94F47.
PRIDEiQ94F47.

Expressioni

Tissue specificityi

Expressed in seeds, pistils, siliques, hypocotyls and leaves.1 Publication

Gene expression databases

ExpressionAtlasiQ94F47. baseline and differential.
GenevestigatoriQ94F47.

Interactioni

Protein-protein interaction databases

BioGridi27949. 7 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ94F47.
SMRiQ94F47. Positions 1-147.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000233455.
InParanoidiQ94F47.
KOiK06689.
PhylomeDBiQ94F47.

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.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q94F47-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASKRILKEL KDLQKDPPTS CSAGPVAEDM FHWQATIMGP SDSPYSGGVF
60 70 80 90 100
LVTIHFPPDY PFKPPKVAFR TKVFHPNVNS NGSICLDILK EQWSPALTIS
110 120 130 140
KVLLSICSLL TDPNPDDPLV PEIAHMYKTD RAKYESTARS WTQKYAMG
Length:148
Mass (Da):16,510
Last modified:November 30, 2001 - v1
Checksum:iD9F89BAF1801A83F
GO

Sequence cautioni

The sequence AAF24583.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF480945 mRNA. Translation: AAM11574.1.
DQ027041 mRNA. Translation: AAY44867.1.
AC007764 Genomic DNA. Translation: AAF24583.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE34212.1.
CP002684 Genomic DNA. Translation: AEE34213.1.
AF385718 mRNA. Translation: AAK60309.1.
AY133670 mRNA. Translation: AAM91500.1.
PIRiD96666.
RefSeqiNP_001031228.1. NM_001036151.1. [Q94F47-1]
NP_564828.1. NM_105097.8. [Q94F47-1]
UniGeneiAt.24180.

Genome annotation databases

EnsemblPlantsiAT1G64230.1; AT1G64230.1; AT1G64230. [Q94F47-1]
AT1G64230.2; AT1G64230.2; AT1G64230. [Q94F47-1]
GeneIDi842728.
KEGGiath:AT1G64230.

Keywords - Coding sequence diversityi

Alternative splicing

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
AF480945 mRNA. Translation: AAM11574.1.
DQ027041 mRNA. Translation: AAY44867.1.
AC007764 Genomic DNA. Translation: AAF24583.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE34212.1.
CP002684 Genomic DNA. Translation: AEE34213.1.
AF385718 mRNA. Translation: AAK60309.1.
AY133670 mRNA. Translation: AAM91500.1.
PIRiD96666.
RefSeqiNP_001031228.1. NM_001036151.1. [Q94F47-1]
NP_564828.1. NM_105097.8. [Q94F47-1]
UniGeneiAt.24180.

3D structure databases

ProteinModelPortaliQ94F47.
SMRiQ94F47. Positions 1-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi27949. 7 interactions.

Proteomic databases

PaxDbiQ94F47.
PRIDEiQ94F47.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G64230.1; AT1G64230.1; AT1G64230. [Q94F47-1]
AT1G64230.2; AT1G64230.2; AT1G64230. [Q94F47-1]
GeneIDi842728.
KEGGiath:AT1G64230.

Organism-specific databases

TAIRiAT1G64230.

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000233455.
InParanoidiQ94F47.
KOiK06689.
PhylomeDBiQ94F47.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciARA:AT1G64230-MONOMER.
ARA:GQT-1299-MONOMER.
ARA:GQT-1300-MONOMER.
ARA:GQT-1301-MONOMER.
ARA:GQT-1302-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.

Gene expression databases

ExpressionAtlasiQ94F47. baseline and differential.
GenevestigatoriQ94F47.

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. "SINAT 5, a RING E3 ubiquitin protein ligase, promotes post-translational degradation of NAC 1 to attenuate auxin signals."
    Xie Q., Chua N.-H.
    Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, 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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.

Entry informationi

Entry nameiUBC28_ARATH
AccessioniPrimary (citable) accession number: Q94F47
Secondary accession number(s): Q9SH72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 2008
Last sequence update: November 30, 2001
Last modified: March 31, 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.