UBC1_ARATH
ID UBC1_ARATH Reviewed; 152 AA.
AC P25865; Q4TZ08;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 168.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 1;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 1;
DE AltName: Full=Ubiquitin carrier protein 1;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa 1;
DE AltName: Full=Ubiquitin-protein ligase 1;
GN Name=UBC1; OrderedLocusNames=At1g14400; ORFNames=F14L17.17, F14L17_35;
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].
RC STRAIN=cv. Columbia;
RX PubMed=1660887; DOI=10.1016/s0021-9258(18)54365-9;
RA Sullivan M.L., Vierstra R.D.;
RT "Cloning of a 16-kDa ubiquitin carrier protein from wheat and Arabidopsis
RT thaliana. Identification of functional domains by in vitro mutagenesis.";
RL J. Biol. Chem. 266:23878-23885(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, AND
RP 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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-98.
RC STRAIN=cv. Columbia; TISSUE=Dry seed;
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 [10]
RP FUNCTION, AND MUTAGENESIS OF CYS-88.
RX PubMed=8386169; DOI=10.1016/s0021-9258(18)52941-0;
RA Sullivan M.L., Vierstra R.D.;
RT "Formation of a stable adduct between ubiquitin and the Arabidopsis
RT ubiquitin-conjugating enzyme, AtUBC1+.";
RL J. Biol. Chem. 268:8777-8780(1993).
RN [11]
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).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=1321826; DOI=10.2210/pdb1aak/pdb;
RA Cook W.J., Jeffrey L.C., Sullivan M.L., Vierstra R.D.;
RT "Three-dimensional structure of a ubiquitin-conjugating enzyme (E2).";
RL J. Biol. Chem. 267:15116-15121(1992).
CC -!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. {ECO:0000269|PubMed:16339806,
CC ECO:0000269|PubMed:8386169}.
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: Ubiquitously expressed.
CC {ECO:0000269|PubMed:16339806, 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M62721; AAA32903.1; -; mRNA.
DR EMBL; L19351; AAA32897.1; -; Genomic_DNA.
DR EMBL; DQ027016; AAY44842.1; -; mRNA.
DR EMBL; AC012188; AAF43940.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29158.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29159.1; -; Genomic_DNA.
DR EMBL; AF332451; AAG48814.1; -; mRNA.
DR EMBL; AY070074; AAL49769.1; -; mRNA.
DR EMBL; AY091330; AAM14269.1; -; mRNA.
DR EMBL; AY085783; AAM63000.1; -; mRNA.
DR EMBL; AK226391; BAE98537.1; -; mRNA.
DR EMBL; Z27262; CAA81773.1; -; mRNA.
DR PIR; S43781; S43781.
DR RefSeq; NP_563951.1; NM_101307.5.
DR RefSeq; NP_973825.1; NM_202096.2.
DR PDB; 2AAK; X-ray; 2.40 A; A=1-152.
DR PDBsum; 2AAK; -.
DR AlphaFoldDB; P25865; -.
DR SMR; P25865; -.
DR BioGRID; 23242; 3.
DR IntAct; P25865; 2.
DR STRING; 3702.AT1G14400.1; -.
DR PaxDb; P25865; -.
DR PRIDE; P25865; -.
DR ProteomicsDB; 228689; -.
DR EnsemblPlants; AT1G14400.1; AT1G14400.1; AT1G14400.
DR EnsemblPlants; AT1G14400.2; AT1G14400.2; AT1G14400.
DR GeneID; 838002; -.
DR Gramene; AT1G14400.1; AT1G14400.1; AT1G14400.
DR Gramene; AT1G14400.2; AT1G14400.2; AT1G14400.
DR KEGG; ath:AT1G14400; -.
DR Araport; AT1G14400; -.
DR TAIR; locus:2012622; AT1G14400.
DR eggNOG; KOG0419; Eukaryota.
DR HOGENOM; CLU_030988_10_2_1; -.
DR InParanoid; P25865; -.
DR OMA; EDTIWEC; -.
DR OrthoDB; 1292821at2759; -.
DR PhylomeDB; P25865; -.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; P25865; -.
DR PRO; PR:P25865; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P25865; baseline and differential.
DR Genevisible; P25865; AT.
DR GO; GO:0005829; C:cytosol; HDA: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:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0033523; P:histone H2B ubiquitination; IGI:TAIR.
DR GO; GO:0016574; P:histone ubiquitination; 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 GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IGI: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; ATP-binding; Nucleotide-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway.
FT CHAIN 1..152
FT /note="Ubiquitin-conjugating enzyme E2 1"
FT /id="PRO_0000082570"
FT DOMAIN 4..150
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 119..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 88
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MUTAGEN 88
FT /note="C->S: Stabilization of the ester bond with the
FT ubiquitin."
FT /evidence="ECO:0000269|PubMed:8386169"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:2AAK"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:2AAK"
FT STRAND 32..41
FT /evidence="ECO:0007829|PDB:2AAK"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:2AAK"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:2AAK"
FT TURN 61..65
FT /evidence="ECO:0007829|PDB:2AAK"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:2AAK"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2AAK"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:2AAK"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:2AAK"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:2AAK"
FT HELIX 134..148
FT /evidence="ECO:0007829|PDB:2AAK"
SQ SEQUENCE 152 AA; 17281 MW; 896D911930C39045 CRC64;
MSTPARKRLM RDFKRLQQDP PAGISGAPQD NNIMLWNAVI FGPDDTPWDG GTFKLSLQFS
EDYPNKPPTV RFVSRMFHPN IYADGSICLD ILQNQWSPIY DVAAILTSIQ SLLCDPNPNS
PANSEAARMY SESKREYNRR VRDVVEQSWT AD
