UBC27_ARATH
ID UBC27_ARATH Reviewed; 192 AA.
AC Q9FI61; Q42045;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 27;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 27;
DE AltName: Full=Ubiquitin carrier protein 27;
GN Name=UBC27; Synonyms=UBC1; OrderedLocusNames=At5g50870; ORFNames=K3K7.1;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Fu H.;
RT "Functional differentiation of ubiquitin-interacting factors from
RT Arabidopsis.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
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] OF 78-192.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RA Hoefte H.;
RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
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 -!- 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=Q9FI61-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in seeds, pistils, siliques, hypocotyls
CC and leaves. {ECO:0000269|PubMed:16339806}.
CC -!- INDUCTION: Up-regulated by syringolin, a cell death-inducing chemical.
CC {ECO:0000269|PubMed:16339806}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; DQ027040; AAY44866.1; -; mRNA.
DR EMBL; DQ677667; ABG85247.1; -; mRNA.
DR EMBL; AB017063; BAB08733.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96003.1; -; Genomic_DNA.
DR EMBL; AY065303; AAL38779.1; -; mRNA.
DR EMBL; AY096429; AAM20069.1; -; mRNA.
DR EMBL; Z25704; CAA81015.1; -; mRNA.
DR RefSeq; NP_199900.1; NM_124465.6. [Q9FI61-1]
DR AlphaFoldDB; Q9FI61; -.
DR SMR; Q9FI61; -.
DR BioGRID; 20405; 2.
DR IntAct; Q9FI61; 1.
DR STRING; 3702.AT5G50870.2; -.
DR PRIDE; Q9FI61; -.
DR ProteomicsDB; 242817; -. [Q9FI61-1]
DR EnsemblPlants; AT5G50870.1; AT5G50870.1; AT5G50870. [Q9FI61-1]
DR GeneID; 835159; -.
DR Gramene; AT5G50870.1; AT5G50870.1; AT5G50870. [Q9FI61-1]
DR KEGG; ath:AT5G50870; -.
DR Araport; AT5G50870; -.
DR eggNOG; KOG0418; Eukaryota.
DR InParanoid; Q9FI61; -.
DR OMA; HHLKGSF; -.
DR PhylomeDB; Q9FI61; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FI61; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FI61; baseline and differential.
DR Genevisible; Q9FI61; 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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR CDD; cd14312; UBA_II_E2_UBC27_like; 1.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR041974; UBC27_UBA.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00179; UQ_con; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Nucleotide-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway.
FT CHAIN 1..192
FT /note="Ubiquitin-conjugating enzyme E2 27"
FT /id="PRO_0000345192"
FT DOMAIN 2..150
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT DOMAIN 153..192
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT ACT_SITE 88
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 192 AA; 21254 MW; 154FF8B581059646 CRC64;
MIDFSRIQKE LQDCERNQDS SGIRVCPKSD NLTRLTGTIP GPIGTPYEGG TFQIDITMPD
GYPFEPPKMQ FSTKVWHPNI SSQSGAICLD ILKDQWSPAL TLKTALVSIQ ALLSAPEPKD
PQDAVVAEQY MKNYQVFVST ARYWTETFAK KSSLEEKVKR LVEMGFGDAQ VRSAIESSGG
DENLALEKLC SA
