UEV1A_ARATH
ID UEV1A_ARATH Reviewed; 158 AA.
AC Q93YP0; Q9LR36;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 variant 1A;
DE Short=Ubc enzyme variant 1A;
DE AltName: Full=Protein MMS ZWEI HOMOLOG 1;
GN Name=UEV1A; Synonyms=MMZ1; OrderedLocusNames=At1g23260; ORFNames=F26F24.10;
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=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 [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].
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, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP 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).
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 Probably not involved in the error-free DNA repair.
CC {ECO:0000269|PubMed:17586653, ECO:0000269|PubMed:18178771}.
CC -!- SUBUNIT: Heterodimer with UBC35 or UBC36.
CC {ECO:0000269|PubMed:17586653}.
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 and 2 days post-
CC germination. {ECO:0000269|PubMed:18178771}.
CC -!- DISRUPTION PHENOTYPE: Plants do not display MMS sensitivity during seed
CC germination. {ECO:0000269|PubMed:18178771}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF87019.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005292; AAF87019.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30365.1; -; Genomic_DNA.
DR EMBL; AY059896; AAL24378.1; -; mRNA.
DR EMBL; AY093340; AAM13339.1; -; mRNA.
DR PIR; G86366; G86366.
DR RefSeq; NP_564191.1; NM_102175.4.
DR AlphaFoldDB; Q93YP0; -.
DR SMR; Q93YP0; -.
DR BioGRID; 24174; 4.
DR IntAct; Q93YP0; 1.
DR STRING; 3702.AT1G23260.1; -.
DR PaxDb; Q93YP0; -.
DR PRIDE; Q93YP0; -.
DR ProteomicsDB; 245289; -.
DR EnsemblPlants; AT1G23260.1; AT1G23260.1; AT1G23260.
DR GeneID; 838935; -.
DR Gramene; AT1G23260.1; AT1G23260.1; AT1G23260.
DR KEGG; ath:AT1G23260; -.
DR Araport; AT1G23260; -.
DR TAIR; locus:2028085; AT1G23260.
DR eggNOG; KOG0896; Eukaryota.
DR HOGENOM; CLU_063065_4_0_1; -.
DR InParanoid; Q93YP0; -.
DR OMA; WQSSYSI; -.
DR OrthoDB; 1507995at2759; -.
DR PhylomeDB; Q93YP0; -.
DR PRO; PR:Q93YP0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93YP0; baseline and differential.
DR Genevisible; Q93YP0; AT.
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 Reference proteome.
FT CHAIN 1..158
FT /note="Ubiquitin-conjugating enzyme E2 variant 1A"
FT /id="PRO_0000344626"
FT DOMAIN 11..158
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 130..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 158 AA; 17851 MW; 619573F3DAC51974 CRC64;
MSSEEAKVVV PRNFRLLEEL ERGEKGIGDG TVSYGMDDAD DIYMQSWTGT ILGPPNTAYE
GKIFQLKLFC GKEYPESPPT VRFQTRINMA CVNPETGVVE PSLFPMLTNW RREYTMEDIL
VKLKKEMMTS HNRKLAQPPE GNEEARADPK GPAKCCVM
