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UniProtKB/Swiss-Prot entry Q42541


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

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Entry information
Entry name UBC13_ARATH
Primary accession number Q42541
Secondary accession number Q4TYZ7
Integrated into Swiss-Prot on May 23, 2003
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 64)
Name and origin of the protein
Protein name Ubiquitin-conjugating enzyme E2 13
Synonyms EC 6.3.2.19
Ubiquitin-protein ligase 13
Ubiquitin carrier protein 13
Gene name
Name: UBC13
OrderedLocusNames: At3g46460
ORFNames: F18L15.180
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 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=cv. Columbia;
TISSUE=Seedling;
DOI=10.1074/jbc.271.21.12150; PubMed=8647807 [NCBI, ExPASy, EBI, Israel, Japan]
van Nocker S., Walker J.M., Vierstra R.D.;
"The Arabidopsis thaliana UBC7/13/14 genes encode a family of multiubiquitin chain-forming E2 enzymes.";
J. Biol. Chem. 271:12150-12158(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, 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=10.1038/35048706; PubMed=11130713 [NCBI, ExPASy, EBI, Israel, Japan]
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
Nature 408:820-822(2000).
[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).
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
U33758; AAC49322.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ027027; AAY44853.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133298; CAB62037.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY050368; AAK91385.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY094040; AAM16196.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T45703; T45703.
RefSeq NP_566884.1; -.
UniGene At.24542
3D structure databases
HSSP P34477; 1PZV. [HSSP ENTRY / PDB]
ModBase Q42541.
Organism-specific databases
TAIR At3g46460; -.
Gene expression databases
ArrayExpress Q42541; -.
Ontologies
GO
GO:0004842; Molecular function: ubiquitin-protein ligase activity (inferred from direct assay from TAIR).
GO:0006511; Biological process: ubiquitin-dependent protein catabolic process (inferred from direct assay from TAIR).
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 Q42541.
Genome annotation databases
GeneID 823796; -.
GenomeReviews BA000014_GR; AT3G46460.
KEGG ath:AT3G46460; -.
Other
ProtoNet Q42541.
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   166  166     Ubiquitin-conjugating enzyme E2 13. PRO_0000082587
ACT_SITE   89    89        Glycyl thioester intermediate (By similarity). 
Sequence information
Length: 166 AA [This is the length of the unprocessed precursor] Molecular weight: 18822 Da [This is the MW of the unprocessed precursor] CRC64: DCC26424275F275B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNSQACLLLQ KQLKDLCKHP VDGFSAGLVD EKNIFEWSVT IIGPPDTLYE GGFFYAIMSF 

        70         80         90        100        110        120 
PQNYPNSPPT VRFTSDIWHP NVYPDGRVCI SILHPPGDDP SGYELASERW TPVHTVESIM 

       130        140        150        160 
LSIISMLSGP NDESPANVEA AKEWREKRDE FKKKVSRCVR KSQEMF 

Q42541 in FASTA format

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View entry in raw text format (no links)
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