ID   UBC10_ARATH             Reviewed;         148 AA.
AC   P35133; P56617; Q4TZ00; Q8LCR4;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   16-JUN-2009, entry version 78.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 10;
DE            EC=6.3.2.19;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa 10/12;
DE   AltName: Full=Ubiquitin-protein ligase 10/12;
DE   AltName: Full=Ubiquitin carrier protein 10/12;
GN   Name=UBC10; Synonyms=UBC12; OrderedLocusNames=At5g53300;
GN   ORFNames=K19E1.10;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=cv. Columbia; TISSUE=Leaf;
RX   MEDLINE=94035158; PubMed=8220461;
RX   DOI=10.1046/j.1365-313X.1993.03040545.x;
RA   Girod P.-A., Carpenter T.B., van Nocker S., Sullivan M.L.,
RA   Vierstra R.D.;
RT   "Homologs of the essential ubiquitin conjugating enzymes UBC1, 4, and
RT   5 in yeast are encoded by a multigene family in Arabidopsis
RT   thaliana.";
RL   Plant J. 3:545-552(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, GENE FAMILY,
RP   AND NOMENCLATURE.
RX   PubMed=16339806; DOI=10.1104/pp.105.067983;
RA   Kraft E., Stone S.L., Ma L., Su N., Gao Y., Lau O.-S., Deng X.-W.,
RA   Callis J.;
RT   "Genome analysis and functional characterization of the E2 and RING-
RT   type E3 ligase ubiquitination enzymes of Arabidopsis.";
RL   Plant Physiol. 139:1597-1611(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=98403884; PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI.
RT   Sequence features of the regions of 1,367,185 bp covered by 19
RT   physically assigned P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   INTERACTION WITH CHIP.
RX   PubMed=16640601; DOI=10.1111/j.1365-313X.2006.02730.x;
RA   Luo J., Shen G., Yan J., He C., Zhang H.;
RT   "AtCHIP functions as an E3 ubiquitin ligase of protein phosphatase 2A
RT   subunits and alters plant response to abscisic acid treatment.";
RL   Plant J. 46:649-657(2006).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. Mediates the selective degradation of short-lived and
CC       abnormal proteins.
CC   -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC       diphosphate + protein N-ubiquityllysine.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with CHIP.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed with the highest levels
CC       in rosette leaves, roots and petals.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=Z14993; Type=Miscellaneous discrepancy; Note=Artifacts of PCR amplification. Originally thought to be UBC12 isoform;
CC   -!- WEB RESOURCE: Name=PlantsUBQ; Note=A functional genomics database
CC       for the ubiquitin/26S proteasome proteolytic pathway in plants;
CC       URL="http://plantsubq.genomics.purdue.edu/";
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DR   EMBL; Z14991; CAA78715.1; -; mRNA.
DR   EMBL; L00640; AAA32895.1; -; mRNA.
DR   EMBL; Z14993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DQ027024; AAY44850.1; -; mRNA.
DR   EMBL; AB013388; BAB09792.1; -; Genomic_DNA.
DR   EMBL; AF324718; AAG40069.1; -; mRNA.
DR   EMBL; AF325005; AAG40357.1; -; mRNA.
DR   EMBL; AF326872; AAG41454.1; -; mRNA.
DR   EMBL; AY039566; AAK62621.1; -; mRNA.
DR   EMBL; AY065059; AAL57693.1; -; mRNA.
DR   EMBL; AY113937; AAM44985.1; -; mRNA.
DR   EMBL; AY129488; AAM91074.1; -; mRNA.
DR   EMBL; AY086447; AAM63450.1; -; mRNA.
DR   IPI; IPI00547528; -.
DR   PIR; S32672; S32672.
DR   RefSeq; NP_568788.1; -.
DR   RefSeq; NP_851181.1; -.
DR   UniGene; At.24357; -.
DR   HSSP; P15731; 1QCQ.
DR   SMR; P35133; 1-147.
DR   GeneID; 835411; -.
DR   GenomeReviews; BA000015_GR; AT5G53300.
DR   KEGG; ath:AT5G53300; -.
DR   TAIR; At5g53300; -.
DR   OMA; P35133; NDLQRDP.
DR   BRENDA; 6.3.2.19; 302.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:TAIR.
DR   GO; GO:0043687; P:post-translational protein modification; IEA:InterPro.
DR   GO; GO:0051246; P:regulation of protein metabolic process; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:TAIR.
DR   InterPro; IPR016135; UBQ-conjugat/RWD-like.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   ProDom; PD000461; UBQ_conjugat; 1.
DR   SMART; SM00212; UBCc; 1.
DR   PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Ubl conjugation pathway.
FT   CHAIN         1    148       Ubiquitin-conjugating enzyme E2 10.
FT                                /FTId=PRO_0000082578.
FT   ACT_SITE     85     85       Glycyl thioester intermediate (By
FT                                similarity).
FT   CONFLICT     23     23       A -> T (in Ref. 1; Z14993).
FT   CONFLICT    140    140       S -> T (in Ref. 1; Z14993).
FT   CONFLICT    144    144       K -> E (in Ref. 4; AAM63450).
SQ   SEQUENCE   148 AA;  16537 MW;  2B83EDC1AD2AE657 CRC64;
     MASKRILKEL KDLQKDPPTS CSAGPVAEDM FHWQATIMGP SESPYAGGVF LVTIHFPPDY
     PFKPPKVAFR TKVFHPNINS NGSICLDILK EQWSPALTIS KVLLSICSLL TDPNPDDPLV
     PEIAHMYKTD KNKYESTARS WTQKYAMG
//