ID   UBQ14_ARATH             Reviewed;         305 AA.
AC   Q3E7T8; B9DFN7; O80715; P59263; Q38875; Q9LDJ2; Q9LYW1; Q9M0W3; Q9M1P9;
AC   Q9S7X3;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 2.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=Polyubiquitin 14;
DE   Contains:
DE     RecName: Full=Ubiquitin;
DE   Flags: Precursor;
GN   Name=UBQ14; OrderedLocusNames=At4g02890; ORFNames=T5J8.21;
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;
RX   PubMed=7713442; DOI=10.1093/genetics/139.2.921;
RA   Callis J., Carpenter T., Sun C.W., Vierstra R.D.;
RT   "Structure and evolution of genes encoding polyubiquitin and ubiquitin-like
RT   proteins in Arabidopsis thaliana ecotype Columbia.";
RL   Genetics 139:921-939(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
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.
CC   -!- FUNCTION: Ubiquitin exists either covalently attached to another
CC       protein, or free (unanchored). When covalently bound, it is conjugated
CC       to target proteins via an isopeptide bond either as a monomer
CC       (monoubiquitin), a polymer linked via different Lys residues of the
CC       ubiquitin (polyubiquitin chains) or a linear polymer linked via the
CC       initiator Met of the ubiquitin (linear polyubiquitin chains).
CC       Polyubiquitin chains, when attached to a target protein, have different
CC       functions depending on the Lys residue of the ubiquitin that is linked:
CC       Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated
CC       degradation) and in cell-cycle regulation; Lys-29-linked is involved in
CC       lysosomal degradation; Lys-33-linked is involved in kinase
CC       modification; Lys-48-linked is involved in protein degradation via the
CC       proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage
CC       responses. Linear polymer chains formed via attachment by the initiator
CC       Met lead to cell signaling. Ubiquitin is usually conjugated to Lys
CC       residues of target proteins, however, in rare cases, conjugation to Cys
CC       or Ser residues has been observed. When polyubiquitin is free
CC       (unanchored-polyubiquitin), it also has distinct roles, such as in
CC       activation of protein kinases, and in signaling (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3E7T8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3E7T8-2; Sequence=VSP_041601;
CC   -!- MISCELLANEOUS: Ubiquitin is encoded by 16 different genes. Ubiquitin is
CC       generally synthesized as a polyubiquitin precursor with tandem head to
CC       tail repeats. Often, there is one to three additional amino acids after
CC       the last repeat, removed in the mature protein. Alternatively,
CC       ubiquitin extension protein is synthesized as a single copy of
CC       ubiquitin fused to a ribosomal protein (either eL40 or eS31) or to a
CC       ubiquitin-related protein (either RUB1 or RUB2). Following translation,
CC       extension protein is cleaved from ubiquitin.
CC   -!- MISCELLANEOUS: For the sake of clarity sequence features are annotated
CC       only for the first chain, and are not repeated for each of the
CC       following chains.
CC   -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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; L05394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC004044; AAD15340.1; -; Genomic_DNA.
DR   EMBL; AL161495; CAB77774.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82244.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82245.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82246.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82247.1; -; Genomic_DNA.
DR   EMBL; AK316842; BAH19554.1; -; mRNA.
DR   EMBL; AY087759; AAM65295.1; -; mRNA.
DR   RefSeq; NP_001031585.1; NM_001036508.2. [Q3E7T8-2]
DR   RefSeq; NP_001118922.1; NM_001125450.2. [Q3E7T8-1]
DR   RefSeq; NP_001118936.1; NM_001125464.2. [Q3E7T8-2]
DR   RefSeq; NP_001328998.1; NM_001340547.1. [Q3E7T8-1]
DR   RefSeq; NP_567247.2; NM_116523.3. [Q3E7T8-2]
DR   RefSeq; NP_567286.1; NM_116744.4. [Q3E7T8-2]
DR   RefSeq; NP_849291.1; NM_178960.2. [Q3E7T8-2]
DR   RefSeq; NP_849292.1; NM_178961.1. [Q3E7T8-1]
DR   RefSeq; NP_974516.4; NM_202787.4. [Q3E7T8-1]
DR   AlphaFoldDB; Q3E7T8; -.
DR   SMR; Q3E7T8; -.
DR   BioGRID; 11158; 1.
DR   BioGRID; 11191; 13.
DR   BioGRID; 13437; 3.
DR   STRING; 3702.Q3E7T8; -.
DR   PaxDb; 3702-AT4G02890-3; -.
DR   EnsemblPlants; AT4G02890.1; AT4G02890.1; AT4G02890. [Q3E7T8-2]
DR   EnsemblPlants; AT4G02890.2; AT4G02890.2; AT4G02890. [Q3E7T8-2]
DR   EnsemblPlants; AT4G02890.3; AT4G02890.3; AT4G02890.
DR   EnsemblPlants; AT4G02890.4; AT4G02890.4; AT4G02890.
DR   EnsemblPlants; AT4G05050.1; AT4G05050.1; AT4G05050. [Q3E7T8-2]
DR   EnsemblPlants; AT4G05050.2; AT4G05050.2; AT4G05050. [Q3E7T8-2]
DR   EnsemblPlants; AT4G05050.3; AT4G05050.3; AT4G05050. [Q3E7T8-2]
DR   EnsemblPlants; AT4G05320.5; AT4G05320.5; AT4G05320.
DR   EnsemblPlants; AT4G05320.8; AT4G05320.8; AT4G05320.
DR   GeneID; 825847; -.
DR   GeneID; 825880; -.
DR   GeneID; 828148; -.
DR   Gramene; AT4G02890.1; AT4G02890.1; AT4G02890. [Q3E7T8-2]
DR   Gramene; AT4G02890.2; AT4G02890.2; AT4G02890. [Q3E7T8-2]
DR   Gramene; AT4G02890.3; AT4G02890.3; AT4G02890.
DR   Gramene; AT4G02890.4; AT4G02890.4; AT4G02890.
DR   Gramene; AT4G05050.1; AT4G05050.1; AT4G05050. [Q3E7T8-2]
DR   Gramene; AT4G05050.2; AT4G05050.2; AT4G05050. [Q3E7T8-2]
DR   Gramene; AT4G05050.3; AT4G05050.3; AT4G05050. [Q3E7T8-2]
DR   Gramene; AT4G05320.5; AT4G05320.5; AT4G05320.
DR   Gramene; AT4G05320.8; AT4G05320.8; AT4G05320.
DR   KEGG; ath:AT4G02890; -.
DR   KEGG; ath:AT4G05050; -.
DR   KEGG; ath:AT4G05320; -.
DR   Araport; AT4G02890; -.
DR   TAIR; AT4G02890; UBQ14.
DR   HOGENOM; CLU_010412_7_0_1; -.
DR   InParanoid; Q3E7T8; -.
DR   OrthoDB; 1017877at2759; -.
DR   PRO; PR:Q3E7T8; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q3E7T8; baseline and differential.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:TAIR.
DR   CDD; cd01803; Ubl_ubiquitin; 4.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   PANTHER; PTHR10666:SF465; POLYUBIQUITIN 3; 1.
DR   PANTHER; PTHR10666; UBIQUITIN; 1.
DR   Pfam; PF00240; ubiquitin; 4.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 4.
DR   SUPFAM; SSF54236; Ubiquitin-like; 4.
DR   PROSITE; PS00299; UBIQUITIN_1; 4.
DR   PROSITE; PS50053; UBIQUITIN_2; 4.
DR   Genevisible; Q3E7T8; AT.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Isopeptide bond; Nucleus;
KW   Reference proteome; Repeat; Ubl conjugation pathway.
FT   CHAIN           1..76
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396899"
FT   CHAIN           77..152
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396900"
FT   CHAIN           153..228
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396901"
FT   CHAIN           229..304
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396902"
FT   PROPEP          305
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000396903"
FT   DOMAIN          1..76
FT                   /note="Ubiquitin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          77..152
FT                   /note="Ubiquitin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          153..228
FT                   /note="Ubiquitin-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          229..304
FT                   /note="Ubiquitin-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CROSSLNK        76
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   VAR_SEQ         1..76
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_041601"
SQ   SEQUENCE   305 AA;  34192 MW;  901C32F1D4F3BE8F CRC64;
     MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN
     IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVESSDTID NVKAKIQDKE GIPPDQQRLI
     FAGKQLEDGR TLADYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE SSDTIDNVKA
     KIQDKEGIPP DQQRLIFAGK QLEDGRTLAD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT
     ITLEVESSDT IDNVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLADYNIQ KESTLHLVLR
     LRGGF
//