UBC4_ARATH
ID UBC4_ARATH Reviewed; 187 AA.
AC P42748; Q4TZ05; Q9FN66;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 4;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 4;
DE AltName: Full=Ubiquitin carrier protein 4;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-21 kDa 1;
DE AltName: Full=Ubiquitin-protein ligase 4;
GN Name=UBC4; OrderedLocusNames=At5g41340; ORFNames=MYC6.5;
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(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 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 antipodal cells of developing seeds
CC and in the vascular junction between the cotyledons or leaves and the
CC hypocotyl. Not expressed in pollen. {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; L19354; AAA32900.1; -; Genomic_DNA.
DR EMBL; DQ027019; AAY44845.1; -; mRNA.
DR EMBL; AB006707; BAB08506.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94667.1; -; Genomic_DNA.
DR EMBL; AY096587; AAM20237.1; -; mRNA.
DR EMBL; AY065360; AAL38801.1; -; mRNA.
DR PIR; S43784; S43784.
DR RefSeq; NP_568589.1; NM_123499.5.
DR AlphaFoldDB; P42748; -.
DR SMR; P42748; -.
DR BioGRID; 19387; 3.
DR IntAct; P42748; 1.
DR STRING; 3702.AT5G41340.1; -.
DR PaxDb; P42748; -.
DR PRIDE; P42748; -.
DR ProteomicsDB; 228600; -.
DR EnsemblPlants; AT5G41340.1; AT5G41340.1; AT5G41340.
DR GeneID; 834136; -.
DR Gramene; AT5G41340.1; AT5G41340.1; AT5G41340.
DR KEGG; ath:AT5G41340; -.
DR Araport; AT5G41340; -.
DR TAIR; locus:2177871; AT5G41340.
DR eggNOG; KOG0416; Eukaryota.
DR HOGENOM; CLU_030988_7_1_1; -.
DR InParanoid; P42748; -.
DR OrthoDB; 1301162at2759; -.
DR PhylomeDB; P42748; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P42748; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P42748; baseline and differential.
DR Genevisible; P42748; 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..187
FT /note="Ubiquitin-conjugating enzyme E2 4"
FT /id="PRO_0000082582"
FT DOMAIN 1..148
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 145..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..181
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 132
FT /note="R -> H (in Ref. 1; AAA32900)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 187 AA; 21298 MW; B9588F0AE7C0F20A CRC64;
MSSPSKRREM DMMKLMMSDY KVETINDGMQ EFYVEFNGPK DSLYQGGVWK IRVELPDAYP
YKSPSVGFIT KIYHPNVDEL SGSVCLDVIN QTWSPMFDLV NVFETFLPQL LLYPNPSDPL
NGEAAALMMR DRPAYEQRVK EYCEKYAKPG EGSEDKSSDE ELSEEEYGSD NEDDDDDDVA
IAGKPDP
