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Q8GY87 (UBC26_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable ubiquitin-conjugating enzyme E2 26

EC=6.3.2.19
Alternative name(s):
Ubiquitin carrier protein 26
Gene names
Name:UBC26
Ordered Locus Names:At1g53025
ORF Names:F8L10.11, F8L10.22
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length543 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

Protein modification; protein ubiquitination.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-protein ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 543543Probable ubiquitin-conjugating enzyme E2 26
PRO_0000345191

Regions

Compositional bias9 – 124Poly-Pro

Sites

Active site3571Glycyl thioester intermediate By similarity

Experimental info

Sequence conflict1181K → E in BAC42437. Ref.4
Sequence conflict1181K → E in AAO64853. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q8GY87 [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: 91B327FE466403C6

FASTA54360,552
        10         20         30         40         50         60 
MEPDVVEIPP PPLIASGSRT RKPRKAVPEV IDVESYEFRN VGVVKDNNVV DKKNKGKAIQ 

        70         80         90        100        110        120 
VDSFSFNNVQ SHHHGSSLLN LETFQDYYGH KNIPFSEFAN QPIDVDDYSM YQDVLDPKDV 

       130        140        150        160        170        180 
PAGAEVTVPW GLNSSSKGTA KSSISIMRSQ SMKGYGTVSL ATTNVPQLWD YTLPQQNQAI 

       190        200        210        220        230        240 
YSSVSFSAVQ PQTPDVVMVT NPTPNPFSYD ASASSSHPIA AEPISSVQDS SNARKLKEEF 

       250        260        270        280        290        300 
LRDFKRFDTV EDFSDHHYAS KGKSSKQHSK NWVKKVQADW KILENDLPEA ISVRACESRM 

       310        320        330        340        350        360 
DLLRAVIIGA EGTPYHDGLF FFDIQFPDTY PSVPPNVHYH SGGLRINPNL YNCGKVCLSL 

       370        380        390        400        410        420 
LGTWAGSARE KWLPNESTML QLLVSIQALI LNEKPYFNEP GYVQSAGTAS GESKSKVYSE 

       430        440        450        460        470        480 
NVFLLSLKTM VYSIRRPPQH FEEYVQNHYF VRSHDIVKAC NAYKAGAPLG SMVKGGVQDL 

       490        500        510        520        530        540 
EEARQSGSKK FKTDVASFMQ TVVDEFVKLG VKELAEKPEP PMSNANTENQ SKKKTRKRSR 


SSR 

« Hide

References

« Hide 'large scale' references
[1]"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], GENE FAMILY, NOMENCLATURE.
[2]"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.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Functional annotation of a full-length Arabidopsis cDNA collection."
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.
Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]"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 (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.

Web resources

PlantsUBQ

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ027039 mRNA. Translation: AAY44865.1.
AC022520 Genomic DNA. Translation: AAF87864.1.
CP002684 Genomic DNA. Translation: AEE32878.1.
AK117792 mRNA. Translation: BAC42437.1.
BT005918 mRNA. Translation: AAO64853.1.
AK176042 mRNA. Translation: BAD43805.1.
PIRG96570.
RefSeqNP_001185207.1. NM_001198278.1.
UniGeneAt.37482.

3D structure databases

ProteinModelPortalQ8GY87.
SMRQ8GY87. Positions 236-509.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8GY87. 3 interactions.
STRING3702.AT1G53020.1-P.

Proteomic databases

PaxDbQ8GY87.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G53025.1; AT1G53025.1; AT1G53025.
GeneID10723113.
KEGGath:AT1G53025.

Organism-specific databases

TAIRAT1G53025.

Phylogenomic databases

eggNOGCOG5078.
HOGENOMHOG000237682.
KOK10581.
OMAWAGSARE.

Enzyme and pathway databases

BioCycARA:AT1G53025-MONOMER.
UniPathwayUPA00143.

Gene expression databases

GenevestigatorQ8GY87.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUBC26_ARATH
AccessionPrimary (citable) accession number: Q8GY87
Secondary accession number(s): Q9LNM8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: July 22, 2008
Last modified: February 19, 2014
This is version 71 of the entry and version 2 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