UBC5_ARATH
ID UBC5_ARATH Reviewed; 185 AA.
AC P42749; Q4TZ04; Q8VXY5; Q9CAE2; Q9CAJ4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 5;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 5;
DE AltName: Full=Ubiquitin carrier protein 5;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-21 kDa 2;
DE AltName: Full=Ubiquitin-protein ligase 5;
GN Name=UBC5; OrderedLocusNames=At1g63800; ORFNames=F24D7.1, T12P18.18;
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=Green leaf;
RX PubMed=8155884; DOI=10.1007/bf00023561;
RA Sullivan M.L., Carpenter T.B., Vierstra R.D.;
RT "Homologues of wheat ubiquitin-conjugating enzymes -- TaUBC1 and TaUBC4 are
RT encoded by small multigene families in Arabidopsis thaliana.";
RL Plant Mol. Biol. 24:651-661(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, GENE 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=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 [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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=8790283; DOI=10.1007/bf00042223;
RA Thoma S., Sullivan M.L., Vierstra R.D.;
RT "Members of two gene families encoding ubiquitin-conjugating enzymes,
RT AtUBC1-3 and AtUBC4-6, from Arabidopsis thaliana are differentially
RT expressed.";
RL Plant Mol. Biol. 31:493-505(1996).
CC -!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. {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 -!- TISSUE SPECIFICITY: Expressed in developing ovules, but not in vascular
CC tissues. {ECO:0000269|PubMed:8790283}.
CC -!- INDUCTION: Not induced by heat shock. {ECO:0000269|PubMed:8790283}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; L19356; AAA32902.1; -; Genomic_DNA.
DR EMBL; DQ027020; AAY44846.1; -; mRNA.
DR EMBL; AC010852; AAG52444.1; -; Genomic_DNA.
DR EMBL; AC011622; AAG52422.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34149.1; -; Genomic_DNA.
DR EMBL; AY074347; AAL67043.1; -; mRNA.
DR EMBL; AY114061; AAM45109.1; -; mRNA.
DR EMBL; AK230439; BAF02237.1; -; mRNA.
DR PIR; A96663; A96663.
DR PIR; S43786; S43786.
DR RefSeq; NP_001321725.1; NM_001334127.1.
DR RefSeq; NP_564817.2; NM_105055.3.
DR AlphaFoldDB; P42749; -.
DR SMR; P42749; -.
DR BioGRID; 27904; 1.
DR IntAct; P42749; 1.
DR STRING; 3702.AT1G63800.1; -.
DR PaxDb; P42749; -.
DR PRIDE; P42749; -.
DR ProteomicsDB; 228658; -.
DR EnsemblPlants; AT1G63800.1; AT1G63800.1; AT1G63800.
DR GeneID; 842683; -.
DR Gramene; AT1G63800.1; AT1G63800.1; AT1G63800.
DR KEGG; ath:AT1G63800; -.
DR Araport; AT1G63800; -.
DR TAIR; locus:2026644; AT1G63800.
DR eggNOG; KOG0416; Eukaryota.
DR HOGENOM; CLU_030988_7_1_1; -.
DR InParanoid; P42749; -.
DR OrthoDB; 1301162at2759; -.
DR PhylomeDB; P42749; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P42749; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P42749; baseline and differential.
DR Genevisible; P42749; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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: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 2: Evidence at transcript level;
KW ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..185
FT /note="Ubiquitin-conjugating enzyme E2 5"
FT /id="PRO_0000082583"
FT DOMAIN 1..148
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 146..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..174
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 85
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT CONFLICT 178
FT /note="A -> R (in Ref. 1; AAA32902)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 185 AA; 21179 MW; 76AE2D7B0C34F5D8 CRC64;
MSSPSKRREM DLMKLMMSDY KVEMINDGMQ EFFVEFSGPK DSIYEGGVWK IRVELPDAYP
YKSPSVGFIT KIYHPNVDEM SGSVCLDVIN QTWSPMFDLV NVFETFLPQL LLYPNPSDPL
NGEAAALMMR DRPTYEQRVK EYCEKYAKPR ADTEEMSSDD EMSEDEYASD GDDEDDVAIA
GKLDP
