(data stored in ACNUC16935 zone)

HOGENOM: ARATH_5_PE3932

ID   ARATH_5_PE3932                       STANDARD;      PRT;   322 AA.
AC   ARATH_5_PE3932; Q9FHQ6;
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 9;Contains: RecName: Full=Ubiquitin-related
DE   1;Contains: RecName: Full=Ubiquitin-related 2;Contains: RecName:
DE   Full=Ubiquitin-related 3;Contains: RecName: Full=Ubiquitin-related
DE   4;Flags: Precursor; (ARATH_5.PE3932).
GN   Name=UBQ9; OrderedLocusNames=At5g37640; ORFNames=K12B20.90;
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_5.PE3932.
CC       Arabidopsis thaliana chromosome 5 TAIR10 full sequence 1..26975502
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:UBQ9_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   -!- 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   -!- SIMILARITY: Belongs to the ubiquitin family.
CC   -!- SIMILARITY: Contains 4 ubiquitin-like domains.
CC   -!- GENE_FAMILY: HOG000233942 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Arabidopsis_thaliana;AT5G37640;AT5G37640.1;AT5G37640.1.
DR   EMBL; AB018107; - ;
DR   UniProtKB/Swiss-Prot; Q9FHQ6; -.
DR   EMBL; AB018107; BAB08310.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94213.1; -; Genomic_DNA.
DR   IPI; IPI00533118; -.
DR   PIR; S55244; S55244.
DR   RefSeq; NP_568552.1; NM_123123.1.
DR   UniGene; At.65595; -.
DR   HSSP; Q862M4; 1AAR.
DR   ProteinModelPortal; Q9FHQ6; -.
DR   SMR; Q9FHQ6; 2-307.
DR   STRING; Q9FHQ6; -.
DR   PRIDE; Q9FHQ6; -.
DR   EnsemblPlants; AT5G37640.1; AT5G37640.1; AT5G37640.
DR   GeneID; 833742; -.
DR   GenomeReviews; BA000015_GR; AT5G37640.
DR   KEGG; ath:AT5G37640; -.
DR   NMPDR; fig|3702.1.peg.25451; -.
DR   TAIR; At5g37640; -.
DR   eggNOG; KOG0001; -.
DR   GeneTree; EPGT00070000028244; -.
DR   InParanoid; Q9FHQ6; -.
DR   OMA; GREMSQD; -.
DR   PhylomeDB; Q9FHQ6; -.
DR   Genevestigator; Q9FHQ6; -.
DR   GO; GO:0005618; C:cell wall; IDA:TAIR.
DR   GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR   GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
DR   InterPro; IPR000626; Ubiquitin.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_subgr.
DR   InterPro; IPR019955; Ubiquitin_supergroup.
DR   Pfam; PF00240; ubiquitin; 4.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 4.
DR   PROSITE; PS00299; UBIQUITIN_1; 4.
DR   PROSITE; PS50053; UBIQUITIN_2; 4.
DR   HOGENOMDNA; ARATH_5.PE3932; -.
KW   AT5G37640pg.C_scaffold_1320000031; AT5G37640.10C_scaffold_1320000031;
KW   AB018107;
KW   Complete proteome; Cytoplasm; Isopeptide bond; Nucleus;
KW   Reference proteome; Repeat; Ubl conjugation pathway.
SQ   SEQUENCE   322 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSMQIHAKTL TEKTITIDVV SSDTINNVKA KIQDIEGIPL DQQRLIFSGK LLDDGRTLAD
     YSIQKDSILH LALRLRGGMQ IFVKTLTGKT ITLEVESSDT IDNVKAKIQD KEGVPPDQQR
     LIFAGKQLDD GRTLADYNIQ KESTLHLVLR LRGGMQIFVR TLTRKTIALE VESSDTTDNV
     KAKIQDKEGI PPDQQRLIFA GKQLEDGRTL ADYNIQKEST LHLVLRLCGG MQIFVNTLTG
     KTITLEVESS DTIDNVKAKI QDKERIQPDQ QRLIFAGEQL EDGYYTLADY NIQKESTLHL
     VLRLRGGECF GFIFLFLLCF NS
//

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