ID   UBC36_ARATH             Reviewed;         153 AA.
AC   Q9FZ48; Q3EDA7;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 36;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 36;
DE   AltName: Full=Ubiquitin carrier protein 36;
GN   Name=UBC36; Synonyms=UBC13B, UBG13B; OrderedLocusNames=At1g16890;
GN   ORFNames=F17F16.19, F6I1.11;
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, 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   [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, AND INDUCTION BY IRON.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9FZ48-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9FZ48-2; Sequence=VSP_034932;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed at low level.
CC       {ECO:0000269|PubMed:16786304}.
CC   -!- INDUCTION: Not induced by iron. {ECO:0000269|PubMed:16786304,
CC       ECO:0000269|PubMed:20113438}.
CC   -!- MISCELLANEOUS: Partly functionally redundant with UBC35.
CC   -!- MISCELLANEOUS: [Isoform 2]: 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}.
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DR   EMBL; DQ027049; AAY44875.1; -; mRNA.
DR   EMBL; AC051629; AAF99844.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29515.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29516.1; -; Genomic_DNA.
DR   EMBL; AY052307; AAK96500.1; -; mRNA.
DR   EMBL; AY061926; AAL31253.1; -; mRNA.
DR   EMBL; AY086780; AAM63831.1; -; mRNA.
DR   PIR; C86304; C86304.
DR   RefSeq; NP_564011.1; NM_101550.4. [Q9FZ48-1]
DR   RefSeq; NP_849678.1; NM_179347.2. [Q9FZ48-2]
DR   AlphaFoldDB; Q9FZ48; -.
DR   SMR; Q9FZ48; -.
DR   BioGRID; 23500; 11.
DR   IntAct; Q9FZ48; 9.
DR   STRING; 3702.Q9FZ48; -.
DR   iPTMnet; Q9FZ48; -.
DR   MetOSite; Q9FZ48; -.
DR   ProteomicsDB; 228598; -. [Q9FZ48-1]
DR   EnsemblPlants; AT1G16890.1; AT1G16890.1; AT1G16890. [Q9FZ48-2]
DR   EnsemblPlants; AT1G16890.2; AT1G16890.2; AT1G16890. [Q9FZ48-1]
DR   GeneID; 838260; -.
DR   Gramene; AT1G16890.1; AT1G16890.1; AT1G16890. [Q9FZ48-2]
DR   Gramene; AT1G16890.2; AT1G16890.2; AT1G16890. [Q9FZ48-1]
DR   KEGG; ath:AT1G16890; -.
DR   Araport; AT1G16890; -.
DR   TAIR; AT1G16890; UBC36.
DR   HOGENOM; CLU_030988_13_2_1; -.
DR   InParanoid; Q9FZ48; -.
DR   OMA; PDDYPME; -.
DR   PhylomeDB; Q9FZ48; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9FZ48; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FZ48; baseline and differential.
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:0006301; P:postreplication repair; IBA:GO_Central.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; IBA:GO_Central.
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:SF519; UBIQUITIN-CONJUGATING ENZYME E2 36; 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; Q9FZ48; AT.
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 36"
FT                   /id="PRO_0000345201"
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         1..33
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_034932"
SQ   SEQUENCE   153 AA;  17220 MW;  66FD614EA346EDD1 CRC64;
     MANSNLPRRI IKETQRLLSE PAPGISASPS EENMRYFNVM ILGPTQSPYE GGVFKLELFL
     PEEYPMAAPK VRFLTKIYHP NIDKLGRICL DILKDKWSPA LQIRTVLLSI QALLSAPNPD
     DPLSENIAKH WKSNEAEAVE TAKEWTRLYA SGA
//