UBC35_ARATH
ID UBC35_ARATH Reviewed; 153 AA.
AC Q94A97; Q2V4C1; Q9ZVA6;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 35;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 35;
DE AltName: Full=Ubiquitin carrier protein 35;
GN Name=UBC35; Synonyms=UBC13A, UBG13A; OrderedLocusNames=At1g78870;
GN ORFNames=F9K20.8;
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 [MRNA] (ISOFORM 1), FUNCTION, 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 FUNCTION, INTERACTION WITH YEAST AND HUMAN MMS2, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=16786304; DOI=10.1007/s11103-006-0007-x;
RA Wen R., Newton L., Li G., Wang H., Xiao W.;
RT "Arabidopsis thaliana UBC13: implication of error-free DNA damage tolerance
RT and Lys63-linked polyubiquitylation in plants.";
RL Plant Mol. Biol. 61:241-253(2006).
RN [7]
RP INTERACTION WITH RGLG2.
RX PubMed=17586653; DOI=10.1105/tpc.107.052035;
RA Yin X.-J., Volk S., Ljung K., Mehlmer N., Dolezal K., Ditengou F.,
RA Hanano S., Davis S.J., Schmelzer E., Sandberg G., Teige M., Palme K.,
RA Pickart C., Bachmair A.;
RT "Ubiquitin lysine 63 chain forming ligases regulate apical dominance in
RT Arabidopsis.";
RL Plant Cell 19:1898-1911(2007).
RN [8]
RP INTERACTION WITH UEV1A; UEV1B; UEV1C AND UEV1D.
RX PubMed=18178771; DOI=10.1105/tpc.107.051862;
RA Wen R., Torres-Acosta J.A., Pastushok L., Lai X., Pelzer L., Wang H.,
RA Xiao W.;
RT "Arabidopsis UEV1D promotes lysine-63-linked polyubiquitination and is
RT involved in DNA damage response.";
RL Plant Cell 20:213-227(2008).
RN [9]
RP FUNCTION, INDUCTION BY IRON, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20113438; DOI=10.1111/j.1365-313x.2010.04150.x;
RA Li W., Schmidt W.;
RT "A lysine-63-linked ubiquitin chain-forming conjugase, UBC13, promotes the
RT developmental responses to iron deficiency in Arabidopsis roots.";
RL Plant J. 62:330-343(2010).
CC -!- FUNCTION: Catalyzes the synthesis of non-canonical poly-ubiquitin
CC chains that are linked through 'Lys-63'. This type of poly-
CC ubiquitination does not lead to protein degradation by the proteasome.
CC Mediates transcriptional activation of target genes. Required for
CC postreplication repair of UV-damaged DNA and for adapting root
CC developmental programs to suboptimal availability of iron.
CC {ECO:0000269|PubMed:16339806, ECO:0000269|PubMed:16786304,
CC ECO:0000269|PubMed:20113438}.
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 yeast and human Mms2, with the RING domain of
CC RGLG2 and with UEV1A, UEV1B, UEV1C and UEV1D.
CC {ECO:0000269|PubMed:16786304, ECO:0000269|PubMed:17586653,
CC ECO:0000269|PubMed:18178771}.
CC -!- INTERACTION:
CC Q94A97; Q15819: UBE2V2; Xeno; NbExp=3; IntAct=EBI-994120, EBI-714329;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q94A97-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94A97-2; Sequence=VSP_034929;
CC Name=3;
CC IsoId=Q94A97-3; Sequence=VSP_034930, VSP_034931;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at low level. Mainly
CC expressed in the vasculature. {ECO:0000269|PubMed:16339806,
CC ECO:0000269|PubMed:16786304, ECO:0000269|PubMed:20113438}.
CC -!- INDUCTION: Not induced by salt, abscisic acid, mannitol, H(2)O(2), low
CC temperature, MMS or iron. {ECO:0000269|PubMed:16786304,
CC ECO:0000269|PubMed:20113438}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions or in phosphate-deficient plants. Unable to form branched
CC root hairs in response to iron-deficient conditions.
CC {ECO:0000269|PubMed:20113438}.
CC -!- MISCELLANEOUS: Partly functionally redundant with UBC36.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC83026.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ027048; AAY44874.1; -; mRNA.
DR EMBL; AC005679; AAC83026.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36165.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36166.1; -; Genomic_DNA.
DR EMBL; AY049261; AAK83603.1; -; mRNA.
DR EMBL; BT000544; AAN18113.1; -; mRNA.
DR EMBL; AY085854; AAM63067.1; -; mRNA.
DR PIR; B96818; B96818.
DR RefSeq; NP_001031298.1; NM_001036221.3. [Q94A97-3]
DR RefSeq; NP_565192.1; NM_106535.4. [Q94A97-1]
DR AlphaFoldDB; Q94A97; -.
DR SMR; Q94A97; -.
DR BioGRID; 29443; 8.
DR IntAct; Q94A97; 2.
DR STRING; 3702.AT1G78870.1; -.
DR PaxDb; Q94A97; -.
DR PRIDE; Q94A97; -.
DR ProteomicsDB; 243215; -. [Q94A97-1]
DR EnsemblPlants; AT1G78870.2; AT1G78870.2; AT1G78870. [Q94A97-1]
DR EnsemblPlants; AT1G78870.3; AT1G78870.3; AT1G78870. [Q94A97-3]
DR GeneID; 844224; -.
DR Gramene; AT1G78870.2; AT1G78870.2; AT1G78870. [Q94A97-1]
DR Gramene; AT1G78870.3; AT1G78870.3; AT1G78870. [Q94A97-3]
DR KEGG; ath:AT1G78870; -.
DR Araport; AT1G78870; -.
DR TAIR; locus:2037553; AT1G78870.
DR eggNOG; KOG0417; Eukaryota.
DR HOGENOM; CLU_030988_13_2_1; -.
DR InParanoid; Q94A97; -.
DR OMA; QWKVNES; -.
DR PhylomeDB; Q94A97; -.
DR BRENDA; 2.3.2.23; 399.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q94A97; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94A97; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031372; C:UBC13-MMS2 complex; IPI:TAIR.
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:0006301; P:postreplication repair; IGI:TAIR.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0010039; P:response to iron ion; IMP:TAIR.
DR GO; GO:0010053; P:root epidermal cell differentiation; IGI:TAIR.
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..153
FT /note="Ubiquitin-conjugating enzyme E2 35"
FT /id="PRO_0000345200"
FT DOMAIN 5..151
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 89
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT VAR_SEQ 51
FT /note="G -> GR (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034929"
FT VAR_SEQ 109..112
FT /note="SIQA -> RYMS (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_034930"
FT VAR_SEQ 113..153
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_034931"
SQ SEQUENCE 153 AA; 17192 MW; 66FDD14FA347A8D0 CRC64;
MANSNLPRRI IKETQRLLSE PAPGISASPS EDNMRYFNVM ILGPTQSPYE GGVFKLELFL
PEEYPMAAPK VRFLTKIYHP NIDKLGRICL DILKDKWSPA LQIRTVLLSI QALLSAPNPD
DPLSENIAKH WKSNEAEAVD TAKEWTRLYA SGA
