Reviewed, UniProtKB/Swiss-Prot P35133 (UBC10_ARATH)

Names and origin

Protein names

Recommended name:
    Ubiquitin-conjugating enzyme E2 10
    EC=6.3.2.19
Alternative name(s):
    Ubiquitin-conjugating enzyme E2-17 kDa 10/12
    Ubiquitin-protein ligase 10/12
    Ubiquitin carrier protein 10/12

Gene names

Name:	UBC10
Synonyms:	UBC12
Ordered Locus Names:	At5g53300
ORF Names:	K19E1.10

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	148 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the covalent attachment of ubiquitin 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 CHIP. Ref.6
Tissue specificity	Ubiquitously expressed with the highest levels in rosette leaves, roots and petals. Ref.2
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.
Sequence caution	The sequence Z14993 differs from that shown. Reason: Miscellaneous discrepancy. Artifacts of PCR amplification. Originally thought to be UBC12 isoform.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	post-translational protein modification Inferred from electronic annotation. Source: InterPro regulation of protein metabolic process Inferred from electronic annotation. Source: InterPro ubiquitin-dependent protein catabolic process Ref.2 Inferred from direct assay. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Ref.2 Inferred from direct assay. Source: TAIR
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

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

Isoform 1 (identifier: P35133-1)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 148	148	Ubiquitin-conjugating enzyme E2 10		PRO_0000082578
Sites
	Active site	85	1	Glycyl thioester intermediate By similarity
Experimental info
	Sequence conflict	23	1	A → T in Z14993. Ref.1
	Sequence conflict	140	1	S → T in Z14993. Ref.1
	Sequence conflict	144	1	K → E in AAM63450. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 2B83EDC1AD2AE657	FASTA	148	16,537
	10 20 30 40 50 60 MASKRILKEL KDLQKDPPTS CSAGPVAEDM FHWQATIMGP SESPYAGGVF LVTIHFPPDY 70 80 90 100 110 120 PFKPPKVAFR TKVFHPNINS NGSICLDILK EQWSPALTIS KVLLSICSLL TDPNPDDPLV 130 140 PEIAHMYKTD KNKYESTARS WTQKYAMG

References

	« Hide 'large scale' referencesShow '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: 8220461] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. 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: 16339806] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
[3]	"Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence features of the regions of 1,367,185 bp covered by 19 physically assigned P1 and TAC clones." Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S. DNA Res. 5:203-216(1998) [PubMed: 9734815] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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. , 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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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].
[6]	"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: 16640601] [Abstract] Cited for: INTERACTION WITH CHIP.
+	Additional computationally mapped references.

Web resources

PlantsUBQ

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

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z14991 mRNA. Translation: CAA78715.1. L00640 mRNA. Translation: AAA32895.1. Z14993 Genomic DNA. No translation available. DQ027024 mRNA. Translation: AAY44850.1. AB013388 Genomic DNA. Translation: BAB09792.1. AF324718 mRNA. Translation: AAG40069.1. AF325005 mRNA. Translation: AAG40357.1. AF326872 mRNA. Translation: AAG41454.1. AY039566 mRNA. Translation: AAK62621.1. AY065059 mRNA. Translation: AAL57693.1. AY113937 mRNA. Translation: AAM44985.1. AY129488 mRNA. Translation: AAM91074.1. AY086447 mRNA. Translation: AAM63450.1.
IPI	IPI00547528.
PIR	S32672.
RefSeq	NP_568788.1. NP_851181.1.
UniGene	At.24357
3D structure databases
HSSP	HSSP built from PDB template 1QCQ based on UniProtKB P15731.
SMR	P35133. Positions 1-147.
ModBase	Search...
Protein-protein interaction databases
STRING	P35133.
Genome annotation databases
GeneID	835411.
GenomeReviews	Gene locus AT5G53300 in contig BA000015_GR.
KEGG	ath:AT5G53300.
Organism-specific databases
TAIR	At5g53300.
Phylogenomic databases
OMA	NDLQRDP.
Enzyme and pathway databases
BRENDA	6.3.2.19. 302.
Gene expression databases
Genevestigator	P35133.
Family and domain databases
InterPro	IPR016135. UBQ-conjugat/RWD-like. IPR000608. UBQ-conjugat_E2. [Graphical view]
Gene3D	G3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.
Pfam	PF00179. UQ_con. 1 hit. [Graphical view]
ProDom	PD000461. UBQ_conjugat. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00212. UBCc. 1 hit. [Graphical view]
PROSITE	PS00183. UBIQUITIN_CONJUGAT_1. 1 hit. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UBC10_ARATH

Accession

Primary (citable) accession number: P35133
Secondary accession number(s): P56617, Q4TZ00, Q8LCR4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	November 3, 2009
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)