UBC10_ARATH
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 03-AUG-2022, entry version 167.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 10 {ECO:0000303|PubMed:16339806, ECO:0000303|PubMed:8220461};
DE EC=2.3.2.23 {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133};
DE AltName: Full=E2 ubiquitin-conjugating enzyme 10 {ECO:0000303|PubMed:16339806, ECO:0000303|PubMed:8220461};
DE AltName: Full=Ubiquitin carrier protein 10/12 {ECO:0000303|PubMed:16339806, ECO:0000303|PubMed:8220461};
DE AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa 10/12 {ECO:0000303|PubMed:16339806, ECO:0000303|PubMed:8220461};
DE AltName: Full=Ubiquitin-protein ligase 10/12 {ECO:0000303|PubMed:16339806, ECO:0000303|PubMed:8220461};
GN Name=UBC10 {ECO:0000303|PubMed:16339806, ECO:0000303|PubMed:8220461};
GN Synonyms=UBC12;
GN OrderedLocusNames=At5g53300 {ECO:0000312|Araport:AT5G53300};
GN ORFNames=K19E1.10 {ECO:0000312|EMBL:BAB09792.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=8220461; DOI=10.1046/j.1365-313x.1993.03040545.x;
RA Girod P.-A., Carpenter T.B., van Nocker S., Sullivan M.L., Vierstra R.D.;
RT "Homologs of the essential ubiquitin conjugating enzymes UBC1, 4, and 5 in
RT yeast are encoded by a multigene family in Arabidopsis thaliana.";
RL Plant J. 3:545-552(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, AND
RP 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-type E3
RT 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 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. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
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 [7]
RP INTERACTION WITH BB.
RX PubMed=16461280; DOI=10.1016/j.cub.2005.12.026;
RA Disch S., Anastasiou E., Sharma V.K., Laux T., Fletcher J.C., Lenhard M.;
RT "The E3 ubiquitin ligase BIG BROTHER controls arabidopsis organ size in a
RT dosage-dependent manner.";
RL Curr. Biol. 16:272-279(2006).
RN [8]
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).
RN [9]
RP INTERACTION WITH JMJ24.
RC STRAIN=cv. Columbia;
RX PubMed=26979329; DOI=10.1104/pp.15.01688;
RA Kabelitz T., Brzezinka K., Friedrich T., Gorka M., Graf A., Kappel C.,
RA Baeurle I.;
RT "A JUMONJI protein with E3 ligase and histone H3 binding activities affects
RT transposon silencing in Arabidopsis.";
RL Plant Physiol. 171:344-358(2016).
CC -!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. Mediates the selective
CC degradation of short-lived and abnormal proteins.
CC {ECO:0000269|PubMed:16339806}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC ProRule:PRU10133};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Interacts with CHIP and the E3 ubiquitin ligase BB. Associates
CC with the E3 ubiquitin ligase JMJ24 (PubMed:26979329).
CC {ECO:0000269|PubMed:16461280, ECO:0000269|PubMed:16640601,
CC ECO:0000269|PubMed:26979329}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P35133-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with the highest levels in
CC rosette leaves, roots and petals. {ECO:0000269|PubMed:16339806}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=Z14993; Type=Miscellaneous discrepancy; Note=Artifacts of PCR amplification. Originally thought to be UBC12 isoform.; Evidence={ECO:0000305};
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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; CP002688; AED96334.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96335.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96337.1; -; 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 PIR; S32672; S32672.
DR RefSeq; NP_001190528.1; NM_001203599.1. [P35133-1]
DR RefSeq; NP_568788.1; NM_124709.2. [P35133-1]
DR RefSeq; NP_851181.1; NM_180850.3. [P35133-1]
DR AlphaFoldDB; P35133; -.
DR SMR; P35133; -.
DR BioGRID; 20656; 11.
DR STRING; 3702.AT5G53300.1; -.
DR PaxDb; P35133; -.
DR PRIDE; P35133; -.
DR EnsemblPlants; AT5G53300.1; AT5G53300.1; AT5G53300. [P35133-1]
DR EnsemblPlants; AT5G53300.2; AT5G53300.2; AT5G53300. [P35133-1]
DR EnsemblPlants; AT5G53300.4; AT5G53300.4; AT5G53300. [P35133-1]
DR GeneID; 835411; -.
DR Gramene; AT5G53300.1; AT5G53300.1; AT5G53300. [P35133-1]
DR Gramene; AT5G53300.2; AT5G53300.2; AT5G53300. [P35133-1]
DR Gramene; AT5G53300.4; AT5G53300.4; AT5G53300. [P35133-1]
DR KEGG; ath:AT5G53300; -.
DR Araport; AT5G53300; -.
DR TAIR; locus:2154207; AT5G53300.
DR eggNOG; KOG0417; Eukaryota.
DR HOGENOM; CLU_030988_13_3_1; -.
DR InParanoid; P35133; -.
DR OMA; QMDICLL; -.
DR PhylomeDB; P35133; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P35133; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P35133; baseline and differential.
DR Genevisible; P35133; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:TAIR.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Nucleotide-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway.
FT CHAIN 1..148
FT /note="Ubiquitin-conjugating enzyme E2 10"
FT /id="PRO_0000082578"
FT DOMAIN 1..147
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 85
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT CONFLICT 23
FT /note="A -> T (in Ref. 1; Z14993)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="S -> T (in Ref. 1; Z14993)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="K -> E (in Ref. 5; AAM63450)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 148 AA; 16537 MW; 2B83EDC1AD2AE657 CRC64;
MASKRILKEL KDLQKDPPTS CSAGPVAEDM FHWQATIMGP SESPYAGGVF LVTIHFPPDY
PFKPPKVAFR TKVFHPNINS NGSICLDILK EQWSPALTIS KVLLSICSLL TDPNPDDPLV
PEIAHMYKTD KNKYESTARS WTQKYAMG
