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   24-JAN-2024, entry version 145.
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.Q9SHI7; -.
DR   TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR   PaxDb; 3702-AT1G17280-1; -.
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; AT1G17280; UBC34.
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   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:TAIR.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067:SF257; UBC CORE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS50127; UBC_2; 1.
DR   Genevisible; Q9SHI7; AT.
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
//