UEV1B_ARATH
ID UEV1B_ARATH Reviewed; 159 AA.
AC Q9CAB6; Q8L9N0;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 variant 1B;
DE Short=Ubc enzyme variant 1B;
DE AltName: Full=Protein MMS ZWEI HOMOLOG 2;
GN Name=UEV1B; Synonyms=MMZ2; OrderedLocusNames=At1g70660; ORFNames=F5A18.16;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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, 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).
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=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9CAB6-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, leaves, stems and
CC flowers, but not in pollen. {ECO:0000269|PubMed:18178771}.
CC -!- DEVELOPMENTAL STAGE: Not detected in seedlings 6 hours or 2 days post-
CC germination. {ECO:0000269|PubMed:18178771}.
CC -!- INDUCTION: Not induced by stresses. {ECO:0000269|PubMed:18178771}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AC011663; AAG52343.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35096.1; -; Genomic_DNA.
DR EMBL; BT004011; AAO42048.1; -; mRNA.
DR EMBL; BT004943; AAO50476.1; -; mRNA.
DR EMBL; AY088344; AAM65883.1; -; mRNA.
DR PIR; H96730; H96730.
DR RefSeq; NP_564994.1; NM_105734.3. [Q9CAB6-1]
DR AlphaFoldDB; Q9CAB6; -.
DR SMR; Q9CAB6; -.
DR BioGRID; 28623; 5.
DR IntAct; Q9CAB6; 3.
DR STRING; 3702.AT1G70660.1; -.
DR PaxDb; Q9CAB6; -.
DR PRIDE; Q9CAB6; -.
DR EnsemblPlants; AT1G70660.1; AT1G70660.1; AT1G70660. [Q9CAB6-1]
DR GeneID; 843403; -.
DR Gramene; AT1G70660.1; AT1G70660.1; AT1G70660. [Q9CAB6-1]
DR KEGG; ath:AT1G70660; -.
DR Araport; AT1G70660; -.
DR TAIR; locus:2033561; AT1G70660.
DR eggNOG; KOG0896; Eukaryota.
DR InParanoid; Q9CAB6; -.
DR OrthoDB; 1507995at2759; -.
DR PhylomeDB; Q9CAB6; -.
DR PRO; PR:Q9CAB6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CAB6; baseline and differential.
DR Genevisible; Q9CAB6; AT.
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: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 CHAIN 1..159
FT /note="Ubiquitin-conjugating enzyme E2 variant 1B"
FT /id="PRO_0000344627"
FT DOMAIN 11..159
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT CONFLICT 114
FT /note="F -> Y (in Ref. 4; AAM65883)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="E -> D (in Ref. 4; AAM65883)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 159 AA; 18001 MW; 37DE94C376101290 CRC64;
MGSEEEKVVV PRNFRLLEEL ERGEKGIGDG TVSYGMDDAD DILMQSWTGT ILGPHNTAYE
GKIFQLKLFC GKDYPESPPT VRFQSRINMA CVNPENGVVD PSHFPMLSNW RREFTMEDLL
IQLKKEMMSS QNRKLAQPLE GNEEGRTDPK GLVVKCCVM
