ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P35133


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name UBC10_ARATH
Primary accession number P35133
Secondary accession numbers P56617 Q4TZ00 Q8LCR4
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on February 1, 1994 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 72)
Name and origin of the protein
Protein name Ubiquitin-conjugating enzyme E2 10
Synonyms EC 6.3.2.19
Ubiquitin-conjugating enzyme E2-17 kDa 10/12
Ubiquitin-protein ligase 10/12
Ubiquitin carrier protein 10/12
Gene name
Name: UBC10
Synonyms: UBC12
OrderedLocusNames: At5g53300
ORFNames: K19E1.10
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=cv. Columbia;
TISSUE=Leaf;
PubMed=8220461 [NCBI, ExPASy, EBI, Israel, Japan]
Girod P.-A., Carpenter T.B., van Nocker S., Sullivan M.L., Vierstra R.D.;
"Homologs of the essential ubiquitin conjugating enzymes UBC1, 4, and 5 in yeast are encoded by a multigene family in Arabidopsis thaliana.";
Plant J. 3:545-552(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
DOI=10.1104/pp.105.067983; PubMed=16339806 [NCBI, ExPASy, EBI, Israel, Japan]
Kraft E., Stone S.L., Ma L., Su N., Gao Y., Lau O.-S., Deng X.-W., Callis J.;
"Genome analysis and functional characterization of the E2 and RING-type E3 ligase ubiquitination enzymes of Arabidopsis.";
Plant Physiol. 139:1597-1611(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1093/dnares/5.3.203; PubMed=9734815 [NCBI, ExPASy, EBI, Israel, Japan]
Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S.;
"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.";
DNA Res. 5:203-216(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
INTERACTION WITH CHIP.
DOI=10.1111/j.1365-313X.2006.02730.x; PubMed=16640601 [NCBI, ExPASy, EBI, Israel, Japan]
Luo J., Shen G., Yan J., He C., Zhang H.;
"AtCHIP functions as an E3 ubiquitin ligase of protein phosphatase 2A subunits and alters plant response to abscisic acid treatment.";
Plant J. 46:649-657(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z14991; CAA78715.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00640; AAA32895.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z14993; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
DQ027024; AAY44850.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB013388; BAB09792.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF324718; AAG40069.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF325005; AAG40357.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF326872; AAG41454.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY039566; AAK62621.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY065059; AAL57693.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY113937; AAM44985.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY129488; AAM91074.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY086447; AAM63450.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S32672; S32672.
RefSeq NP_568788.1; -.
NP_851181.1; -.
UniGene At.24357
3D structure databases
HSSP P15731; 1QCQ. [HSSP ENTRY / PDB]
SMR P35133; 1-147.
ModBase P35133.
Organism-specific databases
TAIR At5g53300; -.
Ontologies
GO
GO:0004842; Molecular function: ubiquitin-protein ligase activity (inferred from electronic annotation from EC).
GO:0006511; Biological process: ubiquitin-dependent protein catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR016135; UBQ-conjugat/RWD-like.
IPR000608; UBQ-conjugat_E2.
Graphical view of domain structure.
Gene3D G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
PANTHER PTHR11621; UBQ-conjugat_E2; 1.
Pfam PF00179; UQ_con; 1.
Pfam graphical view of domain structure.
ProDom PD000461; UBQ_conjugat; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00212; UBCc; 1.
SMART graphical view of domain structure.
PROSITE PS00183; UBIQUITIN_CONJUGAT_1; 1.
PS50127; UBIQUITIN_CONJUGAT_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P35133.
ProtoNet P35133.
Genome annotation databases
GeneID 835411; -.
GenomeReviews BA000015_GR; AT5G53300.
KEGG ath:AT5G53300; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Ligase; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   148  148     Ubiquitin-conjugating enzyme E2 10. PRO_0000082578
ACT_SITE   85    85        Glycyl thioester intermediate (By similarity). 
CONFLICT   23    23        A -> T (in Ref. 1; Z14993). 
CONFLICT   140   140        S -> T (in Ref. 1; Z14993). 
CONFLICT   144   144        K -> E (in Ref. 4; AAM63450). 
Sequence information
Length: 148 AA [This is the length of the unprocessed precursor] Molecular weight: 16537 Da [This is the MW of the unprocessed precursor] CRC64: 2B83EDC1AD2AE657 [This is a checksum on the sequence]
        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 

P35133 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!