UBC34_ARATH
ID UBC34_ARATH Reviewed; 237 AA.
AC Q9SHI7; Q4TYX7;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 34;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 34;
DE AltName: Full=Ubiquitin carrier protein 34;
GN Name=UBC34; OrderedLocusNames=At1g17280; ORFNames=F20D23.1;
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 [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 [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-213, 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).
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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AC007651; AAD50006.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29567.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29568.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59253.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59254.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59255.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59256.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59257.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59259.1; -; Genomic_DNA.
DR EMBL; BT003073; AAO23638.1; -; mRNA.
DR EMBL; AK227344; BAE99355.1; -; mRNA.
DR EMBL; AY084676; AAM61238.1; -; mRNA.
DR EMBL; DQ027047; AAY44873.1; -; mRNA.
DR PIR; C86309; C86309.
DR RefSeq; NP_001077554.1; NM_001084085.1.
DR RefSeq; NP_001319027.1; NM_001332287.1.
DR RefSeq; NP_001321626.1; NM_001332292.1.
DR RefSeq; NP_001321627.1; NM_001332293.1.
DR RefSeq; NP_001321628.1; NM_001332288.1.
DR RefSeq; NP_001321629.1; NM_001332290.1.
DR RefSeq; NP_001321630.1; NM_001332291.1.
DR RefSeq; NP_173172.1; NM_101590.4.
DR AlphaFoldDB; Q9SHI7; -.
DR SMR; Q9SHI7; -.
DR BioGRID; 23540; 448.
DR IntAct; Q9SHI7; 449.
DR STRING; 3702.AT1G17280.1; -.
DR TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR PaxDb; Q9SHI7; -.
DR PRIDE; Q9SHI7; -.
DR ProteomicsDB; 243214; -.
DR EnsemblPlants; AT1G17280.1; AT1G17280.1; AT1G17280.
DR EnsemblPlants; AT1G17280.2; AT1G17280.2; AT1G17280.
DR EnsemblPlants; AT1G17280.3; AT1G17280.3; AT1G17280.
DR EnsemblPlants; AT1G17280.5; AT1G17280.5; AT1G17280.
DR EnsemblPlants; AT1G17280.6; AT1G17280.6; AT1G17280.
DR EnsemblPlants; AT1G17280.7; AT1G17280.7; AT1G17280.
DR EnsemblPlants; AT1G17280.8; AT1G17280.8; AT1G17280.
DR EnsemblPlants; AT1G17280.9; AT1G17280.9; AT1G17280.
DR GeneID; 838300; -.
DR Gramene; AT1G17280.1; AT1G17280.1; AT1G17280.
DR Gramene; AT1G17280.2; AT1G17280.2; AT1G17280.
DR Gramene; AT1G17280.3; AT1G17280.3; AT1G17280.
DR Gramene; AT1G17280.5; AT1G17280.5; AT1G17280.
DR Gramene; AT1G17280.6; AT1G17280.6; AT1G17280.
DR Gramene; AT1G17280.7; AT1G17280.7; AT1G17280.
DR Gramene; AT1G17280.8; AT1G17280.8; AT1G17280.
DR Gramene; AT1G17280.9; AT1G17280.9; AT1G17280.
DR KEGG; ath:AT1G17280; -.
DR Araport; AT1G17280; -.
DR TAIR; locus:2020392; AT1G17280.
DR eggNOG; KOG0894; Eukaryota.
DR HOGENOM; CLU_041481_1_0_1; -.
DR InParanoid; Q9SHI7; -.
DR PhylomeDB; Q9SHI7; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SHI7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SHI7; baseline and differential.
DR Genevisible; Q9SHI7; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0042631; P:cellular response to water deprivation; IGI:TAIR.
DR GO; GO:1902457; P:negative regulation of stomatal opening; IGI:TAIR.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; 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; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Membrane; Nucleotide-binding; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway.
FT CHAIN 1..237
FT /note="Ubiquitin-conjugating enzyme E2 34"
FT /id="PRO_0000345199"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 5..162
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 168..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 87
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ SEQUENCE 237 AA; 26614 MW; FE2888F36BF8B8EC CRC64;
MAEKACIKRL QKEYRALCKE PVSHVVARPS PNDILEWHYV LEGSEGTPFA GGFYYGKIKF
PPEYPYKPPG ITMTTPNGRF MTQKKICLSM SDFHPESWNP MWSVSSILTG LLSFMMDTSP
TTGSVNTTVI EKQRLAKSSL AFNCKTPAFR KLFPEYVEKY NQQQLAEQAT TQLTTPESPQ
KSDTKVESEK TIDPTKGDSE GGLKERKKNN KQGLPAWIIL LLVSVFGVVM ALPLLQL
