UBC6_ARATH
ID UBC6_ARATH Reviewed; 183 AA.
AC P42750; O49739; O82365; Q4TZ03;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 6;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 6;
DE AltName: Full=Ubiquitin carrier protein 6;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-21 kDa 3;
DE AltName: Full=Ubiquitin-protein ligase 6;
GN Name=UBC6; OrderedLocusNames=At2g46030; ORFNames=T3F17.32;
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].
RC STRAIN=cv. Columbia; TISSUE=Green leaf;
RX PubMed=8155884; DOI=10.1007/bf00023561;
RA Sullivan M.L., Carpenter T.B., Vierstra R.D.;
RT "Homologues of wheat ubiquitin-conjugating enzymes -- TaUBC1 and TaUBC4 are
RT encoded by small multigene families in Arabidopsis thaliana.";
RL Plant Mol. Biol. 24:651-661(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=7948890; DOI=10.1007/bf00039553;
RA Watts F.Z., Butt N., Layfield P., Machuka J., Burke J.F., Moore A.L.;
RT "Floral expression of a gene encoding an E2-related ubiquitin-conjugating
RT protein from Arabidopsis thaliana.";
RL Plant Mol. Biol. 26:445-451(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, TISSUE SPECIFICITY, GENE
RP FAMILY, 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-type E3
RT ligase ubiquitination enzymes of Arabidopsis.";
RL Plant Physiol. 139:1597-1611(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=8790283; DOI=10.1007/bf00042223;
RA Thoma S., Sullivan M.L., Vierstra R.D.;
RT "Members of two gene families encoding ubiquitin-conjugating enzymes,
RT AtUBC1-3 and AtUBC4-6, from Arabidopsis thaliana are differentially
RT expressed.";
RL Plant Mol. Biol. 31:493-505(1996).
CC -!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. {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 -!- TISSUE SPECIFICITY: Expressed in roots, petals, sepals and silique
CC walls. {ECO:0000269|PubMed:16339806, ECO:0000269|PubMed:7948890,
CC ECO:0000269|PubMed:8790283}.
CC -!- INDUCTION: By senescence, but not by heat shock.
CC {ECO:0000269|PubMed:16339806, ECO:0000269|PubMed:8790283}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA50503.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; L19355; AAA32901.1; -; Genomic_DNA.
DR EMBL; X71381; CAA50503.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DQ027021; AAY44847.1; -; mRNA.
DR EMBL; AC005397; AAC62907.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10634.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62735.1; -; Genomic_DNA.
DR EMBL; BT005208; AAO63272.1; -; mRNA.
DR EMBL; AK228245; BAF00193.1; -; mRNA.
DR PIR; S43785; S43785.
DR PIR; S52661; S52661.
DR RefSeq; NP_001318433.1; NM_001337170.1.
DR RefSeq; NP_566062.1; NM_130166.4.
DR AlphaFoldDB; P42750; -.
DR SMR; P42750; -.
DR BioGRID; 4546; 1.
DR STRING; 3702.AT2G46030.1; -.
DR PaxDb; P42750; -.
DR PRIDE; P42750; -.
DR ProteomicsDB; 243239; -.
DR EnsemblPlants; AT2G46030.1; AT2G46030.1; AT2G46030.
DR EnsemblPlants; AT2G46030.5; AT2G46030.5; AT2G46030.
DR GeneID; 819211; -.
DR Gramene; AT2G46030.1; AT2G46030.1; AT2G46030.
DR Gramene; AT2G46030.5; AT2G46030.5; AT2G46030.
DR KEGG; ath:AT2G46030; -.
DR Araport; AT2G46030; -.
DR TAIR; locus:2062979; AT2G46030.
DR eggNOG; KOG0416; Eukaryota.
DR HOGENOM; CLU_030988_7_1_1; -.
DR InParanoid; P42750; -.
DR PhylomeDB; P42750; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P42750; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P42750; baseline and differential.
DR Genevisible; P42750; 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: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 2: Evidence at transcript level;
KW ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..183
FT /note="Ubiquitin-conjugating enzyme E2 6"
FT /id="PRO_0000082584"
FT DOMAIN 1..148
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 148..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..183
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 85
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT CONFLICT 2
FT /note="A -> S (in Ref. 1; AAA32901)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 183 AA; 20785 MW; D833BA90995EDEF2 CRC64;
MASPSKRREM DMMKLMMSDY KVDTVNDDLQ MFYVTFHGPT DSLYQGGVWK IKVELPEAYP
YKSPSVGFVN KIYHPNVDES SGAVCLDVIN QTWSPMFDLI NVFESFLPQL LLYPNPSDPF
NGEAASLLMR DRAAYELKVK EYCEKYAKPE EILSDDDDDD SMSEDGSDSD DDDDDEIVGK
ADP
