(data stored in ACNUC16935 zone)

SWISSPROT: UBQ11_ARATH

ID   UBQ11_ARATH             Reviewed;         229 AA.
AC   P0CH33; O80715; P59263; Q38875; Q9LDJ2; Q9LYW1; Q9M0W3; Q9M1P9;
AC   Q9S7X3;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   30-AUG-2017, entry version 55.
DE   RecName: Full=Polyubiquitin 11;
DE   Contains:
DE     RecName: Full=Ubiquitin;
DE   Flags: Precursor;
GN   Name=UBQ11; OrderedLocusNames=At4g05050; ORFNames=C17L7.6, T32N4.13;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=7713442;
RA   Callis J., Carpenter T., Sun C.W., Vierstra R.D.;
RT   "Structure and evolution of genes encoding polyubiquitin and
RT   ubiquitin-like 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.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   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.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- FUNCTION: Ubiquitin exists either covalently attached to another
CC       protein, or free (unanchored). When covalently bound, it is
CC       conjugated to target proteins via an isopeptide bond either as a
CC       monomer (monoubiquitin), a polymer linked via different Lys
CC       residues of the ubiquitin (polyubiquitin chains) or a linear
CC       polymer linked via the initiator Met of the ubiquitin (linear
CC       polyubiquitin chains). Polyubiquitin chains, when attached to a
CC       target protein, have different functions depending on the Lys
CC       residue of the ubiquitin that is linked: Lys-11-linked is involved
CC       in ERAD (endoplasmic reticulum-associated degradation) and in
CC       cell-cycle regulation; Lys-29-linked is involved in lysosomal
CC       degradation; Lys-33-linked is involved in kinase modification;
CC       Lys-48-linked is involved in protein degradation via the
CC       proteasome; Lys-63-linked is involved in endocytosis, and DNA-
CC       damage responses. Linear polymer chains formed via attachment by
CC       the initiator Met lead to cell signaling. Ubiquitin is usually
CC       conjugated to Lys residues of target proteins, however, in rare
CC       cases, conjugation to Cys or Ser residues has been observed. When
CC       polyubiquitin is free (unanchored-polyubiquitin), it also has
CC       distinct roles, such as in activation of protein kinases, and in
CC       signaling (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
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=P0CH33-1; Sequence=Displayed;
CC   -!- MISCELLANEOUS: Ubiquitin is encoded by 16 different genes.
CC       Ubiquitin is generally synthesized as a polyubiquitin precursor
CC       with tandem head to tail repeats. Often, there is one to three
CC       additional amino acids after the last repeat, removed in the
CC       mature protein. Alternatively, ubiquitin extension protein is
CC       synthesized as a single copy of ubiquitin fused to a ribosomal
CC       protein (either L40 or S27A) or to a ubiquitin-related protein
CC       (either RUB1 or RUB2). Following translation, extension protein is
CC       cleaved from ubiquitin.
CC   -!- MISCELLANEOUS: For the sake of clarity sequence features are
CC       annotated only for the first chain, and are not repeated for each
CC       of the following chains.
CC   -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
DR   EMBL; AF162444; AAD48980.1; -; Genomic_DNA.
DR   EMBL; AL161502; CAB81047.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82468.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82469.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82470.1; -; Genomic_DNA.
DR   EMBL; AY052661; AAK96565.1; -; mRNA.
DR   EMBL; AY054281; AAL06940.1; -; mRNA.
DR   EMBL; AY057530; AAL09770.1; -; mRNA.
DR   EMBL; AY098958; AAM19968.1; -; mRNA.
DR   RefSeq; NP_001031585.1; NM_001036508.2. [P0CH33-1]
DR   RefSeq; NP_001118936.1; NM_001125464.2. [P0CH33-1]
DR   RefSeq; NP_567247.2; NM_116523.3. [P0CH33-1]
DR   RefSeq; NP_567286.1; NM_116744.4. [P0CH33-1]
DR   RefSeq; NP_849291.1; NM_178960.2. [P0CH33-1]
DR   UniGene; At.24970; -.
DR   UniGene; At.25274; -.
DR   UniGene; At.47590; -.
DR   UniGene; At.48785; -.
DR   UniGene; At.74401; -.
DR   UniGene; At.74780; -.
DR   ProteinModelPortal; P0CH33; -.
DR   SMR; P0CH33; -.
DR   BioGrid; 11158; 1.
DR   BioGrid; 13437; 3.
DR   STRING; 3702.AT4G05050.1; -.
DR   PaxDb; P0CH33; -.
DR   PRIDE; P0CH33; -.
DR   ProMEX; P0CH33; -.
DR   EnsemblPlants; AT4G02890.1; AT4G02890.1; AT4G02890. [P0CH33-1]
DR   EnsemblPlants; AT4G02890.2; AT4G02890.2; AT4G02890. [P0CH33-1]
DR   EnsemblPlants; AT4G05050.1; AT4G05050.1; AT4G05050. [P0CH33-1]
DR   EnsemblPlants; AT4G05050.2; AT4G05050.2; AT4G05050. [P0CH33-1]
DR   EnsemblPlants; AT4G05050.3; AT4G05050.3; AT4G05050. [P0CH33-1]
DR   GeneID; 825847; -.
DR   GeneID; 828148; -.
DR   Gramene; AT4G02890.1; AT4G02890.1; AT4G02890.
DR   Gramene; AT4G02890.2; AT4G02890.2; AT4G02890.
DR   Gramene; AT4G05050.1; AT4G05050.1; AT4G05050.
DR   Gramene; AT4G05050.2; AT4G05050.2; AT4G05050.
DR   Gramene; AT4G05050.3; AT4G05050.3; AT4G05050.
DR   KEGG; ath:AT4G02890; -.
DR   KEGG; ath:AT4G05050; -.
DR   Araport; AT4G05050; -.
DR   TAIR; locus:2138386; AT4G05050.
DR   eggNOG; KOG0001; Eukaryota.
DR   eggNOG; COG5272; LUCA.
DR   InParanoid; P0CH33; -.
DR   KO; K08770; -.
DR   Reactome; R-ATH-110312; Translesion synthesis by REV1.
DR   Reactome; R-ATH-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR   Reactome; R-ATH-110320; Translesion Synthesis by POLH.
DR   Reactome; R-ATH-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-ATH-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR   Reactome; R-ATH-382556; ABC-family proteins mediated transport.
DR   Reactome; R-ATH-446652; Interleukin-1 signaling.
DR   Reactome; R-ATH-450302; activated TAK1 mediates p38 MAPK activation.
DR   Reactome; R-ATH-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR   Reactome; R-ATH-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR   Reactome; R-ATH-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-ATH-5632684; Hedgehog 'on' state.
DR   Reactome; R-ATH-5655862; Translesion synthesis by POLK.
DR   Reactome; R-ATH-5656121; Translesion synthesis by POLI.
DR   Reactome; R-ATH-5656169; Termination of translesion DNA synthesis.
DR   Reactome; R-ATH-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-ATH-5689603; UCH proteinases.
DR   Reactome; R-ATH-5689877; Josephin domain DUBs.
DR   Reactome; R-ATH-5689880; Ub-specific processing proteases.
DR   Reactome; R-ATH-5689901; Metalloprotease DUBs.
DR   Reactome; R-ATH-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-ATH-5696394; DNA Damage Recognition in GG-NER.
DR   Reactome; R-ATH-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-ATH-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR   Reactome; R-ATH-5696400; Dual Incision in GG-NER.
DR   Reactome; R-ATH-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-ATH-6782135; Dual incision in TC-NER.
DR   Reactome; R-ATH-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-ATH-68949; Orc1 removal from chromatin.
DR   Reactome; R-ATH-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-ATH-69229; Ubiquitin-dependent degradation of Cyclin D1.
DR   Reactome; R-ATH-69231; Cyclin D associated events in G1.
DR   Reactome; R-ATH-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-ATH-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-ATH-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR   Reactome; R-ATH-901032; ER Quality Control Compartment (ERQC).
DR   Reactome; R-ATH-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   Reactome; R-ATH-917937; Iron uptake and transport.
DR   Reactome; R-ATH-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:P0CH33; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; P0CH33; baseline and differential.
DR   Genevisible; P0CH33; AT.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:TAIR.
DR   InterPro; IPR019956; Ubiquitin.
DR   InterPro; IPR029071; Ubiquitin-rel_dom.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR000626; Ubiquitin_dom.
DR   Pfam; PF00240; ubiquitin; 3.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 3.
DR   SUPFAM; SSF54236; SSF54236; 3.
DR   PROSITE; PS00299; UBIQUITIN_1; 3.
DR   PROSITE; PS50053; UBIQUITIN_2; 3.
PE   2: Evidence at transcript level;
DR   PRODOM; Q9S7X3.
DR   SWISS-2DPAGE; Q9S7X3.
KW   Alternative splicing; Complete proteome; Cytoplasm; Isopeptide bond;
KW   Nucleus; Reference proteome; Repeat; Ubl conjugation pathway.
FT   CHAIN         1     76       Ubiquitin.
FT                                /FTId=PRO_0000396895.
FT   CHAIN        77    152       Ubiquitin.
FT                                /FTId=PRO_0000396896.
FT   CHAIN       153    228       Ubiquitin.
FT                                /FTId=PRO_0000396897.
FT   PROPEP      229    229       {ECO:0000305}.
FT                                /FTId=PRO_0000396898.
FT   DOMAIN        1     76       Ubiquitin-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00214}.
FT   DOMAIN       77    152       Ubiquitin-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00214}.
FT   DOMAIN      153    228       Ubiquitin-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00214}.
FT   CROSSLNK     76     76       Glycyl lysine isopeptide (Gly-Lys)
FT                                (interchain with K-? in acceptor
FT                                proteins). {ECO:0000255|PROSITE-
FT                                ProRule:PRU00214}.
SQ   SEQUENCE   229 AA;  25685 MW;  DECF8BB1742D009E CRC64;
     MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN
     IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVESSDTID NVKAKIQDKE GIPPDQQRLI
     FAGKQLEDGR TLADYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE SSDTIDNVKA
     KIQDKEGIPP DQQRLIFAGK QLEDGRTLAD YNIQKESTLH LVLRLRGGF
//

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