Q8L7T3 (UBC20_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 20
EC=6.3.2.19

Alternative name(s):
Ubiquitin carrier protein 20

Gene names

Name:	UBC20
Ordered Locus Names:	At1g50490
ORF Names:	F11F12.16, F17J6.3

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	180 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Ref.1 Ref.2
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Tissue specificity	Expressed in all tissues with cell division activities and in mature leaves. Ref.1 Ref.2
Developmental stage	Expressed during the G2-M phases of the cell cycle. Ref.8
Induction	By the herbicide isoxaben and by biotic stresses. Ref.2
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.
Sequence caution	The sequence AAF87880.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAG51188.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Ligand	ATP-binding Nucleotide-binding
Molecular function	Cyclin Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell proliferation Inferred from expression pattern Ref.1. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from sequence or structural similarity Ref.1. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 180	180	Ubiquitin-conjugating enzyme E2 20		PRO_0000345186
Sites
	Active site	119	1	Glycyl thioester intermediate By similarity
Experimental info
	Sequence conflict	72	1	T → I in AAM67229. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q8L7T3 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 0FFFF2E7347D815B	FASTA	180	19,792
	10 20 30 40 50 60 MAAVNGYQGN TPADPPASNG SKQPAAPTKT VDSQSVLKRL QSELMGLMMG GGPGISAFPE 70 80 90 100 110 120 EDNIFCWKGT ITGSKDTVFE GTEYRLSLSF SNDYPFKPPK VKFETCCFHP NVDVYGNICL 130 140 150 160 170 180 DILQDKWSSA YDVRTILLSI QSLLGEPNIS SPLNTQAAQL WSNQEEYRKM VEKLYKPPSA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of plant ubiquitin-conjugating enzymes belonging to the UbcP4/E2-C/UBCx/UbcH10 gene family." Criqui M.C., de Almeida Engler J., Camasses A., Capron A., Parmentier Y., Inze D., Genschik P. Plant Physiol. 130:1230-1240(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[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], FUNCTION, TISSUE SPECIFICITY, INDUCTION, 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(2000) [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. , 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]	"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.
[8]	"Arabidopsis anaphase-promoting complexes: multiple activators and wide range of substrates might keep APC perpetually busy." Fueloep K., Tarayre S., Kelemen Z., Horvath G., Kevei Z., Nikovics K., Bako L., Brown S., Kondorosi A., Kondorosi E. Cell Cycle 4:1084-1092(2005) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Web resources

PlantsUBQ

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

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY127574 mRNA. Translation: AAM96887.1. DQ027034 mRNA. Translation: AAY44860.1. AC012561 Genomic DNA. Translation: AAF87880.1. Sequence problems. AC079279 Genomic DNA. Translation: AAG51188.1. Sequence problems. CP002684 Genomic DNA. Translation: AEE32556.1. AK227382 mRNA. Translation: BAE99389.1. AY088923 mRNA. Translation: AAM67229.1. BT005855 mRNA. Translation: AAO64790.1.
IPI	IPI00520594.
PIR	D96541.
RefSeq	NP_564572.1. NM_103932.3.
UniGene	At.21610. At.71081.
3D structure databases
ProteinModelPortal	Q8L7T3.
SMR	Q8L7T3. Positions 36-175.
ModBase	Search...
Proteomic databases
PaxDb	Q8L7T3.
PRIDE	Q8L7T3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G50490.1; AT1G50490.1; AT1G50490.
GeneID	841471.
KEGG	ath:AT1G50490.
Organism-specific databases
GeneFarm	2577. 224.
TAIR	At1g50490.
Phylogenomic databases
eggNOG	COG5078.
HOGENOM	HOG000233454.
InParanoid	Q8L7T3.
KO	K06688.
OMA	DNLFRWI.
PhylomeDB	Q8L7T3.
ProtClustDB	CLSN2688586.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
Genevestigator	Q8L7T3.
Family and domain databases
Gene3D	3.10.110.10. 1 hit.
InterPro	IPR000608. UBQ-conjugat_E2. IPR023313. UBQ-conjugating_AS. IPR016135. UBQ-conjugating_enzyme/RWD. [Graphical view]
Pfam	PF00179. UQ_con. 1 hit. [Graphical view]
SUPFAM	SSF54495. UBQ-conjugat/RWD-like. 1 hit.
PROSITE	PS00183. UBIQUITIN_CONJUGAT_1. 1 hit. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UBC20_ARATH

Accession

Primary (citable) accession number: Q8L7T3
Secondary accession number(s): Q8L8L3, Q9C6Q4, Q9LPS2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 22, 2008
Last sequence update:	October 1, 2002
Last modified:	May 29, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program