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UniProtKB/Swiss-Prot entry P25865


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

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Entry information
Entry name UBC1_ARATH
Primary accession number P25865
Secondary accession number Q4TZ08
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on May 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 79)
Name and origin of the protein
Protein name Ubiquitin-conjugating enzyme E2 1
Synonyms EC 6.3.2.19
Ubiquitin-conjugating enzyme E2-17 kDa 1
Ubiquitin-protein ligase 1
Ubiquitin carrier protein 1
Gene name
Name: UBC1
OrderedLocusNames: At1g14400
ORFNames: F14L17.17, F14L17_35
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 [MRNA].
STRAIN=cv. Columbia;
PubMed=1660887 [NCBI, ExPASy, EBI, Israel, Japan]
Sullivan M.L., Vierstra R.D.;
"Cloning of a 16-kDa ubiquitin carrier protein from wheat and Arabidopsis thaliana. Identification of functional domains by in vitro mutagenesis.";
J. Biol. Chem. 266:23878-23885(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1007/BF00023561; PubMed=8155884 [NCBI, ExPASy, EBI, Israel, Japan]
Sullivan M.L., Carpenter T.B., Vierstra R.D.;
"Homologues of wheat ubiquitin-conjugating enzymes -- TaUBC1 and TaUBC4 are encoded by small multigene families in Arabidopsis thaliana.";
Plant Mol. Biol. 24:651-661(1994).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[5]
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).
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
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.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-98.
STRAIN=cv. Columbia;
TISSUE=Dry seed;
DOI=10.1046/j.1365-313X.1996.09010101.x; PubMed=8580968 [NCBI, ExPASy, EBI, Israel, Japan]
Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C., Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R., Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J., Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D., Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P., Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
"Further progress towards a catalogue of all Arabidopsis genes: analysis of a set of 5000 non-redundant ESTs.";
Plant J. 9:101-124(1996).
[9]
FUNCTION, AND MUTAGENESIS OF CYS-88.
PubMed=8386169 [NCBI, ExPASy, EBI, Israel, Japan]
Sullivan M.L., Vierstra R.D.;
"Formation of a stable adduct between ubiquitin and the Arabidopsis ubiquitin-conjugating enzyme, AtUBC1+.";
J. Biol. Chem. 268:8777-8780(1993).
[10]
TISSUE SPECIFICITY, AND INDUCTION.
DOI=10.1007/BF00042223; PubMed=8790283 [NCBI, ExPASy, EBI, Israel, Japan]
Thoma S., Sullivan M.L., Vierstra R.D.;
"Members of two gene families encoding ubiquitin-conjugating enzymes, AtUBC1-3 and AtUBC4-6, from Arabidopsis thaliana are differentially expressed.";
Plant Mol. Biol. 31:493-505(1996).
[11]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
PubMed=1321826 [NCBI, ExPASy, EBI, Israel, Japan]
Cook W.J., Jeffrey L.C., Sullivan M.L., Vierstra R.D.;
"Three-dimensional structure of a ubiquitin-conjugating enzyme (E2).";
J. Biol. Chem. 267:15116-15121(1992).
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
M62721; AAA32903.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L19351; AAA32897.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ027016; AAY44842.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC012188; AAF43940.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF332451; AAG48814.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY070074; AAL49769.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY091330; AAM14269.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY085783; AAM63000.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK226391; BAE98537.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z27262; CAA81773.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S43781; S43781.
RefSeq NP_563951.1; -.
NP_973825.1; -.
UniGene At.331
3D structure databases
PDB
2AAK; X-ray; 2.40 A; A=1-152.[ExPASy / RCSB / EBI]
PDBsum 2AAK; -.
ModBase P25865.
Organism-specific databases
GeneFarm 4743; 464.
TAIR At1g14400; -.
Gene expression databases
ArrayExpress P25865; -.
Ontologies
GO
GO:0004842; Molecular function: ubiquitin-protein ligase activity (inferred from electronic annotation from EC).
GO:0043687; Biological process: post-translational protein modification (inferred from electronic annotation from InterPro).
GO:0051246; Biological process: regulation of protein metabolic process (inferred from electronic annotation from InterPro).
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 P25865.
ProtoNet P25865.
Genome annotation databases
GeneID 838002; -.
GenomeReviews CT485782_GR; AT1G14400.
KEGG ath:AT1G14400; -.
Other
LinkHub P25865; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Ligase; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   152  152     Ubiquitin-conjugating enzyme E2 1. PRO_0000082570
ACT_SITE   88    88        Glycyl thioester intermediate. 
MUTAGEN   88    88        C->S: Stabilization of the ester bond with the ubiquitin. 
HELIX   4    18  15      
STRAND   24    29  6      
STRAND   32    41  10      
TURN   47    50  4      
STRAND   52    58  7      
TURN   61    65  5      
STRAND   69    74  6      
STRAND   85    87  3      
HELIX   90    92  3      
HELIX   102   113  12      
HELIX   124   132  9      
HELIX   134   148  15      
Sequence information
Length: 152 AA [This is the length of the unprocessed precursor] Molecular weight: 17281 Da [This is the MW of the unprocessed precursor] CRC64: 896D911930C39045 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSTPARKRLM RDFKRLQQDP PAGISGAPQD NNIMLWNAVI FGPDDTPWDG GTFKLSLQFS 

        70         80         90        100        110        120 
EDYPNKPPTV RFVSRMFHPN IYADGSICLD ILQNQWSPIY DVAAILTSIQ SLLCDPNPNS 

       130        140        150 
PANSEAARMY SESKREYNRR VRDVVEQSWT AD 

P25865 in FASTA format

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View entry in raw text format (no links)
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