(data stored in ACNUC16935 zone)

HOGENOM: ARATH_4_PE436

ID   ARATH_4_PE436                        STANDARD;      PRT;   229 AA.
AC   ARATH_4_PE436;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Polyubiquitin 11;Contains: RecName: Full=Ubiquitin;Flags:
DE   Precursor; (ARATH_4.PE436).
GN   Name=UBQ11; OrderedLocusNames=At4g05050; ORFNames=C17L7.6, T32N4.13;
OS   ARABIDOPSIS THALIANA.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; rosids;
OC   eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ARATH_4.PE436.
CC       Arabidopsis thaliana chromosome 4 TAIR10 full sequence 1..18585056
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:UBQ11_ARATH
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).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
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 an ubiquitin-related protein
CC       (either RUB1 or RUB2). Following translation, extension protein is
CC       cleaved from ubiquitin.
CC   -!- MISCELLANEOUS: For a better understanding, features related to
CC       ubiquitin are only indicated for the first chain.
CC   -!- SIMILARITY: Belongs to the ubiquitin family.
CC   -!- SIMILARITY: Contains 3 ubiquitin-like domains.
CC   -!- GENE_FAMILY: HOG000233942 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Arabidopsis_thaliana;AT4G02890;AT4G02890.1;AT4G02890.1.
DR   EMBL; AF035383; - ;
DR   EMBL; AF162444; - ;
DR   EMBL; AK226406; - ;
DR   EMBL; AL161502; - ;
DR   EMBL; AY042884; - ;
DR   EMBL; AY052661; - ;
DR   EMBL; AY054281; - ;
DR   EMBL; AY057530; - ;
DR   EMBL; AY086967; - ;
DR   EMBL; AY098958; - ;
DR   EMBL; BT001165; - ;
DR   EMBL; DQ793132; - ;
DR   EMBL; DQ793134; - ;
DR   EMBL; Z29165; - ;
DR   UniProtKB/Swiss-Prot; P0CH33; O80715; P59263; Q38875; Q9LDJ2; Q9LYW1; Q9M0W3; Q9M1P9; -.
DR   UniProtKB/Swiss-Prot; Q9S7X3; -.
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   IPI; IPI00528294; -.
DR   RefSeq; NP_001031585.1; NM_001036508.1.
DR   RefSeq; NP_001118936.1; NM_001125464.2.
DR   RefSeq; NP_567247.2; NM_116523.3.
DR   RefSeq; NP_567286.1; NM_116744.3.
DR   RefSeq; NP_849291.1; NM_178960.2.
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   UniGene; At.74796; -.
DR   UniGene; At.75097; -.
DR   ProteinModelPortal; P0CH33; -.
DR   SMR; P0CH33; 1-226.
DR   EnsemblPlants; AT4G02890.1; AT4G02890.1; AT4G02890.
DR   EnsemblPlants; AT4G02890.2; AT4G02890.2; AT4G02890.
DR   EnsemblPlants; AT4G02890.3; AT4G02890.3; AT4G02890.
DR   EnsemblPlants; AT4G02890.4; AT4G02890.4; AT4G02890.
DR   EnsemblPlants; AT4G05050.1; AT4G05050.1; AT4G05050.
DR   EnsemblPlants; AT4G05050.2; AT4G05050.2; AT4G05050.
DR   EnsemblPlants; AT4G05050.3; AT4G05050.3; AT4G05050.
DR   EnsemblPlants; AT4G05320.1; AT4G05320.1; AT4G05320.
DR   EnsemblPlants; AT4G05320.2; AT4G05320.2; AT4G05320.
DR   EnsemblPlants; AT4G05320.3; AT4G05320.3; AT4G05320.
DR   EnsemblPlants; AT4G05320.4; AT4G05320.4; AT4G05320.
DR   EnsemblPlants; AT4G05320.5; AT4G05320.5; AT4G05320.
DR   EnsemblPlants; AT4G05320.6; AT4G05320.6; AT4G05320.
DR   GeneID; 825847; -.
DR   GeneID; 828148; -.
DR   GenomeReviews; CT486007_GR; AT4G02890.
DR   GenomeReviews; CT486007_GR; AT4G05050.
DR   KEGG; ath:AT4G02890; -.
DR   KEGG; ath:AT4G05050; -.
DR   TAIR; At4g05050; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000626; Ubiquitin.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_subgr.
DR   InterPro; IPR019955; Ubiquitin_supergroup.
DR   Pfam; PF00240; ubiquitin; 3.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 3.
DR   PROSITE; PS00299; UBIQUITIN_1; 3.
DR   PROSITE; PS50053; UBIQUITIN_2; 3.
DR   HOGENOMDNA; ARATH_4.PE436; -.
KW   AT4G02890pg.C_scaffold_1320000031; AT4G02890.1.C_scaffold_1320000031;
KW   A6XI99; A6XIA1; O64955; Q42214; Q8H0Y0; Q8LBW0; Q94B30; AF035383;
KW   AK226406; AL161502; AY042884; AY052661; AY054281; AY057530; AY086967;
KW   BT001165; DQ793132; DQ793134; Z29165;
KW   Alternative splicing; Complete proteome; Cytoplasm; Isopeptide bond;
KW   Nucleus; Reference proteome; Repeat; Ubl conjugation;
KW   Ubl conjugation pathway.
SQ   SEQUENCE   229 AA;  UNKNOWN MW;  UNKNOWN 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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