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   27-MAR-2024, entry version 159.
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.P42750; -.
DR   PaxDb; 3702-AT2G46030-1; -.
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; AT2G46030; UBC6.
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   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:TAIR.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24068; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24068:SF568; UBIQUITIN-CONJUGATING ENZYME E2 6; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
DR   Genevisible; P42750; AT.
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
//