UEV1D_ARATH
ID UEV1D_ARATH Reviewed; 146 AA.
AC Q9SVD7; A8MSC0; Q3EAL0;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 variant 1D;
DE Short=Ubc enzyme variant 1D;
DE AltName: Full=Protein MMS ZWEI HOMOLOG 4;
GN Name=UEV1D; Synonyms=MMZ4; OrderedLocusNames=At3g52560; ORFNames=F22O6.60;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 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 [5]
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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, ALTERNATIVE SPLICING, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, INDUCTION, AND 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 [7]
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).
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.
CC Involved 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 -!- INTERACTION:
CC Q9SVD7; Q93ZF6: AIRP1; NbExp=3; IntAct=EBI-3386882, EBI-4465263;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9SVD7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SVD7-2; Sequence=VSP_034855;
CC Name=3;
CC IsoId=Q9SVD7-3; Sequence=VSP_034854, VSP_034855;
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, leaves, stems, flowers
CC and pollen. {ECO:0000269|PubMed:18178771}.
CC -!- DEVELOPMENTAL STAGE: Detected in seedlings 6 hours and 2 days post-
CC germination. {ECO:0000269|PubMed:18178771}.
CC -!- INDUCTION: Not induced by stresses. {ECO:0000269|PubMed:18178771}.
CC -!- DISRUPTION PHENOTYPE: Plants do not display apparent morphological
CC variations, but are sensitive to the DNA-damaging agent MMS.
CC {ECO:0000269|PubMed:18178771}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: 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}.
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DR EMBL; AL050300; CAB43411.1; -; Genomic_DNA.
DR EMBL; AL353912; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002686; AEE78959.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78960.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78961.1; -; Genomic_DNA.
DR EMBL; AY042846; AAK68786.1; -; mRNA.
DR EMBL; AY072492; AAL66907.1; -; mRNA.
DR EMBL; AY085609; AAM62830.1; -; mRNA.
DR PIR; T08443; T08443.
DR RefSeq; NP_001078272.1; NM_001084803.1. [Q9SVD7-3]
DR RefSeq; NP_566968.1; NM_115116.4. [Q9SVD7-1]
DR RefSeq; NP_850684.1; NM_180353.2. [Q9SVD7-2]
DR AlphaFoldDB; Q9SVD7; -.
DR SMR; Q9SVD7; -.
DR BioGRID; 9740; 11.
DR IntAct; Q9SVD7; 8.
DR iPTMnet; Q9SVD7; -.
DR PRIDE; Q9SVD7; -.
DR EnsemblPlants; AT3G52560.1; AT3G52560.1; AT3G52560. [Q9SVD7-1]
DR EnsemblPlants; AT3G52560.2; AT3G52560.2; AT3G52560. [Q9SVD7-2]
DR EnsemblPlants; AT3G52560.3; AT3G52560.3; AT3G52560. [Q9SVD7-3]
DR GeneID; 824422; -.
DR Gramene; AT3G52560.1; AT3G52560.1; AT3G52560. [Q9SVD7-1]
DR Gramene; AT3G52560.2; AT3G52560.2; AT3G52560. [Q9SVD7-2]
DR Gramene; AT3G52560.3; AT3G52560.3; AT3G52560. [Q9SVD7-3]
DR KEGG; ath:AT3G52560; -.
DR Araport; AT3G52560; -.
DR HOGENOM; CLU_063065_4_0_1; -.
DR InParanoid; Q9SVD7; -.
DR PhylomeDB; Q9SVD7; -.
DR PRO; PR:Q9SVD7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SVD7; baseline and differential.
DR Genevisible; Q9SVD7; AT.
DR GO; GO:0005634; C:nucleus; 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 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 CHAIN 1..146
FT /note="Ubiquitin-conjugating enzyme E2 variant 1D"
FT /id="PRO_0000344629"
FT DOMAIN 13..146
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT VAR_SEQ 1..37
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_034854"
FT VAR_SEQ 58
FT /note="N -> NV (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_034855"
SQ SEQUENCE 146 AA; 16533 MW; 5D0C1996649D3738 CRC64;
MTLGSGGSSV VVPRNFRLLE ELERGEKGIG DGTVSYGMDD GDDIYMRSWT GTIIGPHNTV
HEGRIYQLKL FCDKDYPEKP PTVRFHSRVN MACVNHETGV VDPKKFGLLA NWQREYTMED
ILVQLKKEMS TSHNRKLVQP PEGTCF
