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P35131 (UBC8_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 8

EC=6.3.2.19
Alternative name(s):
UBCAT4A
Ubiquitin carrier protein 8
Ubiquitin-conjugating enzyme E2-17 kDa 8
Ubiquitin-protein ligase 8
Gene names
Name:UBC8
Synonyms:UBC4A
Ordered Locus Names:At5g41700
ORF Names:MBK23.24
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length148 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. Mediates the selective degradation of short-lived and abnormal proteins. Ref.2

Catalytic activity

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

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with CIP8, CHIP, NLA and XERICO. Ref.10 Ref.11 Ref.12 Ref.13

Tissue specificity

Highest expression in young stems, old leaves. Lowest levels in floral buds, anthers and young leaves. Ref.2

Developmental stage

Up-regulated during senescence, but not during the G0 to S phase transition. Ref.9

Induction

Not induced by heat shock or wounding. Ref.9

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35131-1)

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.
Isoform 2 (identifier: P35131-2)

The sequence of this isoform differs from the canonical sequence as follows:
     21-22: CS → CIF
Note: Derived from EST data. No experimental confirmation available.
Isoform 3 (identifier: P35131-3)

The sequence of this isoform differs from the canonical sequence as follows:
     103-148: LLSICSLLTD...RNWTQKYAMG → TLIFQKHRFS...QALLLECLCM
Note: Derived from EST data. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 148148Ubiquitin-conjugating enzyme E2 8
PRO_0000082576

Sites

Active site851Glycyl thioester intermediate By similarity

Natural variations

Alternative sequence21 – 222CS → CIF in isoform 2.
VSP_034925
Alternative sequence103 – 14846LLSIC…KYAMG → TLIFQKHRFSNVRLCSKSIA RASTFSARILLNAQALLLEC LCM in isoform 3.
VSP_034926

Experimental info

Sequence conflict721K → M in AAL34248. Ref.5
Sequence conflict801S → D in AAK44072. Ref.5
Sequence conflict801S → D in AAL66929. Ref.5
Sequence conflict801S → D in AAL15262. Ref.5
Sequence conflict801S → D in AAK96786. Ref.5
Sequence conflict801S → D in AAG40361. Ref.5
Sequence conflict981T → P in AAK44072. Ref.5
Sequence conflict981T → P in AAL66929. Ref.5
Sequence conflict981T → P in AAL15262. Ref.5
Sequence conflict981T → P in AAK96786. Ref.5
Sequence conflict981T → P in AAG40361. Ref.5
Sequence conflict1351E → K in AAM62889. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 27CAAEABBBE74972

FASTA14816,533
        10         20         30         40         50         60 
MASKRILKEL KDLQKDPPTS CSAGPVAEDM FHWQATIMGP AESPYSGGVF LVTIHFPPDY 

        70         80         90        100        110        120 
PFKPPKVAFR TKVFHPNINS NGSICLDILK EQWSPALTIS KVLLSICSLL TDPNPDDPLV 

       130        140 
PEIAHMYKTD RAKYEATARN WTQKYAMG 

« Hide

Isoform 2 [UniParc].

Checksum: 11D4DF7CB733D0B8
Show »

FASTA14916,706
Isoform 3 [UniParc].

Checksum: 4727400F23743DDD
Show »

FASTA14516,163

References

« Hide 'large scale' references
[1]"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 [GENOMIC DNA].
Strain: cv. Columbia.
Tissue: Leaf.
[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(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
[3]"Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones."
Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S.
DNA Res. 4:215-230(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-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. 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.
[6]"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].
[7]"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 1-74.
Strain: cv. Columbia.
[8]"An inventory of 1152 expressed sequence tags obtained by partial sequencing of cDNAs from Arabidopsis thaliana."
Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M., Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M., Cooke R. expand/collapse author list , Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.
Plant J. 4:1051-1061(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-148.
Strain: cv. Columbia.
Tissue: Green siliques.
[9]"Differential expression of several E2-type ubiquitin carrier protein genes at different developmental stages in Arabidopsis thaliana and Nicotiana sylvestris."
Genschik P., Durr A., Fleck J.
Mol. Gen. Genet. 244:548-556(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE, INDUCTION.
[10]"Biochemical evidence for ubiquitin ligase activity of the Arabidopsis COP1 interacting protein 8 (CIP8)."
Hardtke C.S., Okamoto H., Stoop-Myer C., Deng X.-W.
Plant J. 30:385-394(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CIP8.
[11]"AtCHIP functions as an E3 ubiquitin ligase of protein phosphatase 2A subunits and alters plant response to abscisic acid treatment."
Luo J., Shen G., Yan J., He C., Zhang H.
Plant J. 46:649-657(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHIP.
[12]"Upregulation of an Arabidopsis RING-H2 gene, XERICO, confers drought tolerance through increased abscisic acid biosynthesis."
Ko J.-H., Yang S.H., Han K.-H.
Plant J. 47:343-355(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH XERICO.
[13]"A mutation in NLA, which encodes a RING-type ubiquitin ligase, disrupts the adaptability of Arabidopsis to nitrogen limitation."
Peng M., Hannam C., Gu H., Bi Y.-M., Rothstein S.J.
Plant J. 50:320-337(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NLA.

Web resources

PlantsUBQ

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z14989 Genomic DNA. Translation: CAA78713.1.
DQ027022 mRNA. Translation: AAY44848.1.
AB005233 Genomic DNA. Translation: BAB11476.1.
CP002688 Genomic DNA. Translation: AED94711.1.
CP002688 Genomic DNA. Translation: AED94712.1.
CP002688 Genomic DNA. Translation: AED94713.1.
CP002688 Genomic DNA. Translation: AED94714.1.
CP002688 Genomic DNA. Translation: AED94715.1.
AF325009 mRNA. Translation: AAG40361.1.
AY063074 mRNA. Translation: AAL34248.1.
AF370257 mRNA. Translation: AAK44072.1.
AY054595 mRNA. Translation: AAK96786.1.
AY057631 mRNA. Translation: AAL15262.1.
AY072514 mRNA. Translation: AAL66929.1.
AY085670 mRNA. Translation: AAM62889.1.
Z37225 mRNA. Translation: CAA85527.1.
Z17692 mRNA. Translation: CAA79036.1.
RefSeqNP_001190447.1. NM_001203518.1.
NP_568595.2. NM_123535.2.
NP_851114.1. NM_180783.1.
NP_851115.1. NM_180784.1.
NP_851116.1. NM_180785.2.
UniGeneAt.23971.
At.24180.

3D structure databases

ProteinModelPortalP35131.
SMRP35131. Positions 1-147.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid19424. 14 interactions.
IntActP35131. 2 interactions.

Proteomic databases

PRIDEP35131.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G41700.1; AT5G41700.1; AT5G41700. [P35131-1]
AT5G41700.2; AT5G41700.2; AT5G41700. [P35131-1]
AT5G41700.5; AT5G41700.5; AT5G41700. [P35131-1]
GeneID834173.
KEGGath:AT5G41700.

Organism-specific databases

TAIRAT5G41700.

Phylogenomic databases

InParanoidP35131.
KOK06689.
OMANGSICLI.
PhylomeDBP35131.
ProtClustDBCLSN2680399.

Enzyme and pathway databases

BioCycARA:AT5G41700-MONOMER.
ARA:GQT-251-MONOMER.
ARA:GQT-252-MONOMER.
ARA:GQT-253-MONOMER.
ARA:GQT-254-MONOMER.
UniPathwayUPA00143.

Gene expression databases

GenevestigatorP35131.

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...

Entry information

Entry nameUBC8_ARATH
AccessionPrimary (citable) accession number: P35131
Secondary accession number(s): Q3E8J2 expand/collapse secondary AC list , Q3E8J3, Q42308, Q43276, Q4TZ02, Q8LE19
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 127 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names