UBC8_ARATH
ID UBC8_ARATH Reviewed; 148 AA.
AC P35131; Q3E8J2; Q3E8J3; Q42308; Q43276; Q4TZ02; Q8LE19;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 183.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 8;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 8;
DE AltName: Full=UBCAT4A;
DE AltName: Full=Ubiquitin carrier protein 8;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa 8;
DE AltName: Full=Ubiquitin-protein ligase 8;
GN Name=UBC8; Synonyms=UBC4A; OrderedLocusNames=At5g41700; ORFNames=MBK23.24;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=8220461; DOI=10.1046/j.1365-313x.1993.03040545.x;
RA Girod P.-A., Carpenter T.B., van Nocker S., Sullivan M.L., Vierstra R.D.;
RT "Homologs of the essential ubiquitin conjugating enzymes UBC1, 4, and 5 in
RT yeast are encoded by a multigene family in Arabidopsis thaliana.";
RL Plant J. 3:545-552(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, GENE
RP FAMILY, AND 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [4]
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-74.
RC STRAIN=cv. Columbia;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-148.
RC STRAIN=cv. Columbia; TISSUE=Green siliques;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [9]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=8078482; DOI=10.1007/bf00583906;
RA Genschik P., Durr A., Fleck J.;
RT "Differential expression of several E2-type ubiquitin carrier protein genes
RT at different developmental stages in Arabidopsis thaliana and Nicotiana
RT sylvestris.";
RL Mol. Gen. Genet. 244:548-556(1994).
RN [10]
RP INTERACTION WITH CIP8.
RX PubMed=12028569; DOI=10.1046/j.1365-313x.2002.01298.x;
RA Hardtke C.S., Okamoto H., Stoop-Myer C., Deng X.-W.;
RT "Biochemical evidence for ubiquitin ligase activity of the Arabidopsis COP1
RT interacting protein 8 (CIP8).";
RL Plant J. 30:385-394(2002).
RN [11]
RP INTERACTION WITH CHIP.
RX PubMed=16640601; DOI=10.1111/j.1365-313x.2006.02730.x;
RA Luo J., Shen G., Yan J., He C., Zhang H.;
RT "AtCHIP functions as an E3 ubiquitin ligase of protein phosphatase 2A
RT subunits and alters plant response to abscisic acid treatment.";
RL Plant J. 46:649-657(2006).
RN [12]
RP INTERACTION WITH XERICO.
RX PubMed=16792696; DOI=10.1111/j.1365-313x.2006.02782.x;
RA Ko J.-H., Yang S.H., Han K.-H.;
RT "Upregulation of an Arabidopsis RING-H2 gene, XERICO, confers drought
RT tolerance through increased abscisic acid biosynthesis.";
RL Plant J. 47:343-355(2006).
RN [13]
RP INTERACTION WITH NLA.
RX PubMed=17355433; DOI=10.1111/j.1365-313x.2007.03050.x;
RA Peng M., Hannam C., Gu H., Bi Y.-M., Rothstein S.J.;
RT "A mutation in NLA, which encodes a RING-type ubiquitin ligase, disrupts
RT the adaptability of Arabidopsis to nitrogen limitation.";
RL Plant J. 50:320-337(2007).
CC -!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. Mediates the selective
CC degradation of short-lived and abnormal proteins.
CC {ECO:0000269|PubMed:16339806}.
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 CIP8, CHIP, NLA and XERICO.
CC {ECO:0000269|PubMed:12028569, ECO:0000269|PubMed:16640601,
CC ECO:0000269|PubMed:16792696, ECO:0000269|PubMed:17355433}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P35131-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35131-2; Sequence=VSP_034925;
CC Name=3;
CC IsoId=P35131-3; Sequence=VSP_034926;
CC -!- TISSUE SPECIFICITY: Highest expression in young stems, old leaves.
CC Lowest levels in floral buds, anthers and young leaves.
CC {ECO:0000269|PubMed:16339806}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during senescence, but not during the
CC G0 to S phase transition. {ECO:0000269|PubMed:8078482}.
CC -!- INDUCTION: Not induced by heat shock or wounding.
CC {ECO:0000269|PubMed:8078482}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; Z14989; CAA78713.1; -; Genomic_DNA.
DR EMBL; DQ027022; AAY44848.1; -; mRNA.
DR EMBL; AB005233; BAB11476.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94711.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94712.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94713.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94714.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94715.1; -; Genomic_DNA.
DR EMBL; AF325009; AAG40361.1; -; mRNA.
DR EMBL; AY063074; AAL34248.1; -; mRNA.
DR EMBL; AF370257; AAK44072.1; -; mRNA.
DR EMBL; AY054595; AAK96786.1; -; mRNA.
DR EMBL; AY057631; AAL15262.1; -; mRNA.
DR EMBL; AY072514; AAL66929.1; -; mRNA.
DR EMBL; AY085670; AAM62889.1; -; mRNA.
DR EMBL; Z37225; CAA85527.1; -; mRNA.
DR EMBL; Z17692; CAA79036.1; -; mRNA.
DR RefSeq; NP_001190447.1; NM_001203518.1. [P35131-1]
DR RefSeq; NP_568595.2; NM_123535.2. [P35131-2]
DR RefSeq; NP_851114.1; NM_180783.2. [P35131-1]
DR RefSeq; NP_851115.1; NM_180784.2. [P35131-1]
DR RefSeq; NP_851116.1; NM_180785.2. [P35131-3]
DR PDB; 4X57; X-ray; 2.80 A; A/C=1-148.
DR PDBsum; 4X57; -.
DR AlphaFoldDB; P35131; -.
DR SMR; P35131; -.
DR BioGRID; 19424; 17.
DR IntAct; P35131; 2.
DR STRING; 3702.AT5G41700.4; -.
DR PaxDb; P35131; -.
DR ProteomicsDB; 228602; -. [P35131-1]
DR EnsemblPlants; AT5G41700.1; AT5G41700.1; AT5G41700. [P35131-1]
DR EnsemblPlants; AT5G41700.2; AT5G41700.2; AT5G41700. [P35131-1]
DR EnsemblPlants; AT5G41700.3; AT5G41700.3; AT5G41700. [P35131-3]
DR EnsemblPlants; AT5G41700.4; AT5G41700.4; AT5G41700. [P35131-2]
DR EnsemblPlants; AT5G41700.5; AT5G41700.5; AT5G41700. [P35131-1]
DR GeneID; 834173; -.
DR Gramene; AT5G41700.1; AT5G41700.1; AT5G41700. [P35131-1]
DR Gramene; AT5G41700.2; AT5G41700.2; AT5G41700. [P35131-1]
DR Gramene; AT5G41700.3; AT5G41700.3; AT5G41700. [P35131-3]
DR Gramene; AT5G41700.4; AT5G41700.4; AT5G41700. [P35131-2]
DR Gramene; AT5G41700.5; AT5G41700.5; AT5G41700. [P35131-1]
DR KEGG; ath:AT5G41700; -.
DR Araport; AT5G41700; -.
DR TAIR; locus:2160462; AT5G41700.
DR eggNOG; KOG0417; Eukaryota.
DR HOGENOM; CLU_030988_13_3_1; -.
DR InParanoid; P35131; -.
DR OMA; HAREWTH; -.
DR OrthoDB; 1337945at2759; -.
DR PhylomeDB; P35131; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P35131; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P35131; baseline and differential.
DR Genevisible; P35131; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0009960; P:endosperm development; IEP:TAIR.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:TAIR.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Nucleotide-binding;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..148
FT /note="Ubiquitin-conjugating enzyme E2 8"
FT /id="PRO_0000082576"
FT DOMAIN 1..147
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 85
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT VAR_SEQ 21..22
FT /note="CS -> CIF (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034925"
FT VAR_SEQ 103..148
FT /note="LLSICSLLTDPNPDDPLVPEIAHMYKTDRAKYEATARNWTQKYAMG -> TL
FT IFQKHRFSNVRLCSKSIARASTFSARILLNAQALLLECLCM (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_034926"
FT CONFLICT 72
FT /note="K -> M (in Ref. 5; AAL34248)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="S -> D (in Ref. 5; AAK44072/AAL66929/AAL15262/
FT AAK96786/AAG40361)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="T -> P (in Ref. 5; AAK44072/AAL66929/AAL15262/
FT AAK96786/AAG40361)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="E -> K (in Ref. 6; AAM62889)"
FT /evidence="ECO:0000305"
FT HELIX 1..15
FT /evidence="ECO:0007829|PDB:4X57"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:4X57"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:4X57"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:4X57"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:4X57"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:4X57"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:4X57"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:4X57"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:4X57"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:4X57"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:4X57"
FT HELIX 131..145
FT /evidence="ECO:0007829|PDB:4X57"
SQ SEQUENCE 148 AA; 16533 MW; 27CAAEABBBE74972 CRC64;
MASKRILKEL KDLQKDPPTS CSAGPVAEDM FHWQATIMGP AESPYSGGVF LVTIHFPPDY
PFKPPKVAFR TKVFHPNINS NGSICLDILK EQWSPALTIS KVLLSICSLL TDPNPDDPLV
PEIAHMYKTD RAKYEATARN WTQKYAMG
