UBC14_ARATH
ID UBC14_ARATH Reviewed; 167 AA.
AC P42747; Q4TYZ6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 14;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 14;
DE AltName: Full=TAYO29;
DE AltName: Full=UbcAt3;
DE AltName: Full=Ubiquitin carrier protein 14;
DE AltName: Full=Ubiquitin-protein ligase 14;
GN Name=UBC14; Synonyms=UBC3, UBC7; OrderedLocusNames=At3g55380;
GN ORFNames=T22E16.40;
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], AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=8078482; DOI=10.1007/bf00583906;
RA Genschik P., Durr A., Fleck J.;
RT "Differential expression of several E2-type ubiquitin carrier protein genes
RT at different developmental stages in Arabidopsis thaliana and Nicotiana
RT sylvestris.";
RL Mol. Gen. Genet. 244:548-556(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=8647807; DOI=10.1074/jbc.271.21.12150;
RA van Nocker S., Walker J.M., Vierstra R.D.;
RT "The Arabidopsis thaliana UBC7/13/14 genes encode a family of
RT multiubiquitin chain-forming E2 enzymes.";
RL J. Biol. Chem. 271:12150-12158(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] OF 1-67.
RC STRAIN=cv. Columbia;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. Involved in the formation of
CC multiubiquitin chains. Signal the protein for selective degradation.
CC {ECO:0000269|PubMed:8647807}.
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=P42747-1; Sequence=Displayed;
CC -!- DEVELOPMENTAL STAGE: Up-regulated during the G0 to S phase transition.
CC {ECO:0000269|PubMed:8078482}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; X72625; CAA51200.1; -; mRNA.
DR EMBL; U33759; AAC49323.1; -; Genomic_DNA.
DR EMBL; DQ027028; AAY44854.1; -; mRNA.
DR EMBL; AL132975; CAB75896.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79376.1; -; Genomic_DNA.
DR EMBL; AY117262; AAM51337.1; -; mRNA.
DR EMBL; AY045883; AAK76557.1; -; mRNA.
DR EMBL; AY086490; AAM63492.1; -; mRNA.
DR EMBL; Z18513; CAA79212.1; -; mRNA.
DR PIR; S46656; S46656.
DR RefSeq; NP_567020.1; NM_115396.4. [P42747-1]
DR AlphaFoldDB; P42747; -.
DR SMR; P42747; -.
DR BioGRID; 10020; 1.
DR iPTMnet; P42747; -.
DR PRIDE; P42747; -.
DR ProteomicsDB; 242593; -. [P42747-1]
DR EnsemblPlants; AT3G55380.1; AT3G55380.1; AT3G55380. [P42747-1]
DR GeneID; 824704; -.
DR Gramene; AT3G55380.1; AT3G55380.1; AT3G55380. [P42747-1]
DR KEGG; ath:AT3G55380; -.
DR Araport; AT3G55380; -.
DR HOGENOM; CLU_030988_10_1_1; -.
DR InParanoid; P42747; -.
DR OMA; FEWSITI; -.
DR PhylomeDB; P42747; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P42747; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P42747; baseline and differential.
DR Genevisible; P42747; AT.
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:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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 Acetylation; Alternative splicing; ATP-binding; Nucleotide-binding;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..167
FT /note="Ubiquitin-conjugating enzyme E2 14"
FT /id="PRO_0000082588"
FT DOMAIN 5..165
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 90
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 167 AA; 18728 MW; 15053C16A62C08BC CRC64;
MANNQASLLL QKQLKDLCKK PVDGFSAGLV DEKNVFQWSV SIMGPPDTLY EGGFFNAIMS
FPENYPVSPP TVTFTSEMWH PNVYSDGKVC ISILHPPGDD PHGYELASER WTPVHTVESI
VLSIISMLSG PNDESPANVE AAKEWRDNRA EFRKKVSRCV RRSQEML
