UEV1C_ARATH
ID UEV1C_ARATH Reviewed; 145 AA.
AC Q9SJ44; A8MQX2; Q3EBM3;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 variant 1C;
DE Short=Ubc enzyme variant 1C;
DE AltName: Full=Protein MMS ZWEI HOMOLOG 3;
GN Name=UEV1C; Synonyms=MMZ3; OrderedLocusNames=At2g36060; ORFNames=F11F19.3;
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 [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 [2]
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 [3]
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 [4]
RP IDENTIFICATION, FUNCTION, AND SUBUNIT.
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, AND
RP INTERACTION WITH UBC35 AND UBC 36.
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Has no ubiquitin ligase activity on its own. The heterodimer
CC with UBC catalyzes the synthesis of non-canonical poly-ubiquitin chains
CC that are linked through 'Lys-63'. This type of poly-ubiquitination does
CC not lead to protein degradation by the proteasome. Mediates
CC transcriptional activation of target genes. May play a role in the
CC control of progress through the cell cycle and differentiation. May
CC play a role in the error-free DNA repair pathway and contributes to the
CC survival of cells after DNA damage. {ECO:0000269|PubMed:17586653,
CC ECO:0000269|PubMed:18178771}.
CC -!- SUBUNIT: Heterodimer with UBC35 or UBC36.
CC {ECO:0000269|PubMed:17586653}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9SJ44-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SJ44-2; Sequence=VSP_034852;
CC Name=3;
CC IsoId=Q9SJ44-3; Sequence=VSP_034853;
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, leaves, stems and
CC flowers, but not in pollen. {ECO:0000269|PubMed:18178771}.
CC -!- DEVELOPMENTAL STAGE: Detected in seedlings 6 hours post-germination,
CC but not 2 days post-germination. {ECO:0000269|PubMed:18178771}.
CC -!- INDUCTION: Not induced by stresses. {ECO:0000269|PubMed:18178771}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC007017; AAD21451.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09199.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09200.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09201.1; -; Genomic_DNA.
DR EMBL; AY062760; AAL32838.1; -; mRNA.
DR EMBL; AY093382; AAM13381.1; -; mRNA.
DR PIR; D84776; D84776.
DR RefSeq; NP_001078011.1; NM_001084542.1. [Q9SJ44-3]
DR RefSeq; NP_565834.1; NM_129165.4. [Q9SJ44-1]
DR RefSeq; NP_850259.1; NM_179928.2. [Q9SJ44-2]
DR AlphaFoldDB; Q9SJ44; -.
DR SMR; Q9SJ44; -.
DR BioGRID; 3523; 2.
DR STRING; 3702.AT2G36060.2; -.
DR iPTMnet; Q9SJ44; -.
DR MetOSite; Q9SJ44; -.
DR PaxDb; Q9SJ44; -.
DR PRIDE; Q9SJ44; -.
DR ProteomicsDB; 245290; -. [Q9SJ44-1]
DR EnsemblPlants; AT2G36060.1; AT2G36060.1; AT2G36060. [Q9SJ44-1]
DR EnsemblPlants; AT2G36060.2; AT2G36060.2; AT2G36060. [Q9SJ44-2]
DR EnsemblPlants; AT2G36060.3; AT2G36060.3; AT2G36060. [Q9SJ44-3]
DR GeneID; 818179; -.
DR Gramene; AT2G36060.1; AT2G36060.1; AT2G36060. [Q9SJ44-1]
DR Gramene; AT2G36060.2; AT2G36060.2; AT2G36060. [Q9SJ44-2]
DR Gramene; AT2G36060.3; AT2G36060.3; AT2G36060. [Q9SJ44-3]
DR KEGG; ath:AT2G36060; -.
DR Araport; AT2G36060; -.
DR TAIR; locus:2039245; AT2G36060.
DR eggNOG; KOG0896; Eukaryota.
DR InParanoid; Q9SJ44; -.
DR OMA; NLPCVDQ; -.
DR PhylomeDB; Q9SJ44; -.
DR PRO; PR:Q9SJ44; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJ44; baseline and differential.
DR Genevisible; Q9SJ44; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031372; C:UBC13-MMS2 complex; IPI:TAIR.
DR GO; GO:1902916; P:positive regulation of protein polyubiquitination; 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 Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..145
FT /note="Ubiquitin-conjugating enzyme E2 variant 1C"
FT /id="PRO_0000344628"
FT DOMAIN 12..145
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT VAR_SEQ 57
FT /note="N -> NV (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034852"
FT VAR_SEQ 99
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_034853"
SQ SEQUENCE 145 AA; 16481 MW; BB71ED6AB8FD22B1 CRC64;
MTLGSGSSVV VPRNFRLLEE LERGEKGIGD GTVSYGMDDG DDIYMRSWTG TIIGPHNTVH
EGRIYQLKLF CDKDYPEKPP TVRFHSRINM TCVNHDTGVV DSKKFGVLAN WQRQYTMEDI
LTQLKKEMAA SHNRKLVQPP EGTFF
