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Q9FZ48 (UBC36_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. 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 36

EC=6.3.2.19
Alternative name(s):
Ubiquitin carrier protein 36
Gene names
Name:UBC36
Synonyms:UBC13B, UBG13B
Ordered Locus Names:At1g16890
ORF Names:F17F16.19, F6I1.11
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length153 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Required for postreplication repair of UV-damaged DNA and for adapting root developmental programs to suboptimal availability of iron. Ref.1 Ref.6 Ref.9

Catalytic activity

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

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with yeast and human Mms2, with the RING domain of RGLG2 and with UEV1A, UEV1B, UEV1C and UEV1D. Ref.6 Ref.7 Ref.8

Tissue specificity

Ubiquitously expressed at low level. Ref.6

Induction

Not induced by iron. Ref.6 Ref.9

Miscellaneous

Partly functionally redundant with UBC35.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Coding sequence diversityAlternative splicing
   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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9FZ48-1)

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: Q9FZ48-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.
Note: Derived from EST data. May be due to an intron retention. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 153153Ubiquitin-conjugating enzyme E2 36
PRO_0000345201

Sites

Active site891Glycyl thioester intermediate By similarity

Natural variations

Alternative sequence1 – 3333Missing in isoform 2.
VSP_034932

Sequences

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

Last modified March 1, 2001. Version 1.
Checksum: 66FD614EA346EDD1

FASTA15317,220
        10         20         30         40         50         60 
MANSNLPRRI IKETQRLLSE PAPGISASPS EENMRYFNVM ILGPTQSPYE GGVFKLELFL 

        70         80         90        100        110        120 
PEEYPMAAPK VRFLTKIYHP NIDKLGRICL DILKDKWSPA LQIRTVLLSI QALLSAPNPD 

       130        140        150 
DPLSENIAKH WKSNEAEAVE TAKEWTRLYA SGA 

« Hide

Isoform 2 [UniParc].

Checksum: A9498B1FE3F0AD28
Show »

FASTA12013,631

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] (ISOFORM 1), FUNCTION, 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]"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] (ISOFORM 1).
Strain: cv. Columbia.
[5]"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] (ISOFORM 1).
[6]"Arabidopsis thaliana UBC13: implication of error-free DNA damage tolerance and Lys63-linked polyubiquitylation in plants."
Wen R., Newton L., Li G., Wang H., Xiao W.
Plant Mol. Biol. 61:241-253(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH YEAST AND HUMAN MMS2, TISSUE SPECIFICITY, INDUCTION.
[7]"Ubiquitin lysine 63 chain forming ligases regulate apical dominance in Arabidopsis."
Yin X.-J., Volk S., Ljung K., Mehlmer N., Dolezal K., Ditengou F., Hanano S., Davis S.J., Schmelzer E., Sandberg G., Teige M., Palme K., Pickart C., Bachmair A.
Plant Cell 19:1898-1911(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RGLG2.
[8]"Arabidopsis UEV1D promotes lysine-63-linked polyubiquitination and is involved in DNA damage response."
Wen R., Torres-Acosta J.A., Pastushok L., Lai X., Pelzer L., Wang H., Xiao W.
Plant Cell 20:213-227(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UEV1A; UEV1B; UEV1C AND UEV1D.
[9]"A lysine-63-linked ubiquitin chain-forming conjugase, UBC13, promotes the developmental responses to iron deficiency in Arabidopsis roots."
Li W., Schmidt W.
Plant J. 62:330-343(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION BY IRON.

Web resources

PlantsUBQ

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ027049 mRNA. Translation: AAY44875.1.
AC051629 Genomic DNA. Translation: AAF99844.1.
CP002684 Genomic DNA. Translation: AEE29515.1.
CP002684 Genomic DNA. Translation: AEE29516.1.
AY052307 mRNA. Translation: AAK96500.1.
AY061926 mRNA. Translation: AAL31253.1.
AY086780 mRNA. Translation: AAM63831.1.
PIRC86304.
RefSeqNP_564011.1. NM_101550.3.
NP_849678.1. NM_179347.1.
UniGeneAt.16052.
At.24697.

3D structure databases

ProteinModelPortalQ9FZ48.
SMRQ9FZ48. Positions 6-150.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid23500. 10 interactions.
IntActQ9FZ48. 9 interactions.
STRING3702.AT1G16890.2-P.

Proteomic databases

PaxDbQ9FZ48.
PRIDEQ9FZ48.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G16890.2; AT1G16890.2; AT1G16890. [Q9FZ48-1]
GeneID838260.
KEGGath:AT1G16890.

Organism-specific databases

TAIRAT1G16890.

Phylogenomic databases

eggNOGCOG5078.
HOGENOMHOG000233455.
InParanoidQ9FZ48.
KOK10580.
PhylomeDBQ9FZ48.
ProtClustDBCLSN2687835.

Enzyme and pathway databases

BioCycARA:AT1G16890-MONOMER.
ARA:GQT-2517-MONOMER.
ARA:GQT-718-MONOMER.
UniPathwayUPA00143.

Gene expression databases

GenevestigatorQ9FZ48.

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 nameUBC36_ARATH
AccessionPrimary (citable) accession number: Q9FZ48
Secondary accession number(s): Q3EDA7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 96 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