(data stored in ACNUC16935 zone)

HOGENOM: ORYSJ_12_PE3974

ID   ORYSJ_12_PE3974                      STANDARD;      PRT;   129 AA.
AC   ORYSJ_12_PE3974;
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=Ubiquitin-40S ribosomal protein S27a-1;Contains: RecName:
DE   Full=Ubiquitin;Contains: RecName: Full=40S ribosomal protein
DE   S27a-1;Flags: Precursor; (ORYSJ_12.PE3974).
GN   Name=RPS27AA; OrderedLocusNames=Os01g0328400, LOC_Os01g22490;
OS   ORYZA SATIVA JAPONICA GROUP.
OC   cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina;
OC   Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta;
OC   Liliopsida; commelinids; Poales; Poaceae; BEP clade; Ehrhartoideae;
OC   Oryzeae; Oryza.
OX   NCBI_TaxID=39947;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ORYSJ_12.PE3974.
CC       Oryza sativa Japonica Group chromosome 9 MSU6 full sequence 1..23011239
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:R27AA_ORYSJ
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-48-linked is involved
CC       in protein degradation via the proteasome; Lys-63-linked is
CC       involved in endocytosis, and DNA-damage responses. Linear polymer
CC       chains formed via attachment by the initiator Met lead to cell
CC       signaling. Ubiquitin is usually conjugated to Lys residues of
CC       target proteins, however, in rare cases, conjugation to Cys or Ser
CC       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   -!- FUNCTION: Ribosomal protein RSP27a-1 is a component of the 40S
CC       subunit of the ribosome.
CC   -!- SUBUNIT: Ribosomal protein RSP27a-1 is part of the 40S ribosomal
CC       subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm (By similarity).
CC       Nucleus (By similarity).
CC   -!- MISCELLANEOUS: Ubiquitin is generally synthesized as a
CC       polyubiquitin precursor with tandem head to tail repeats. Often,
CC       there is one to three additional amino-acids after the last
CC       repeat, removed in the mature protein. Alternatively, ubiquitin
CC       extension protein is synthesized as a single copy of ubiquitin
CC       fused to a ribosomal protein (either L40 or S27A) or to an
CC       ubiquitin-related protein (either RUB1 or RUB2). Following
CC       translation, extension protein is cleaved from ubiquitin.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin
CC       family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the ribosomal
CC       protein S27Ae family.
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC   -!- GENE_FAMILY: HOG000233942 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Oryza_sativa_japonica_group;LOC_OS09G39500;LOC_OS09G39500.1;LOC_OS09G39500.1.
DR   UniProtKB/Swiss-Prot; Q9ARZ9; O82079; P03993; P69321; Q652Q2; Q67UR4; Q69P70; Q6ATC2; -.
DR   UniProtKB/Swiss-Prot; Q7XN78; Q8S5Y3; Q9AR09; -.
DR   EMBL; AP002971; BAB39294.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF04829.1; -; Genomic_DNA.
DR   EMBL; CM000138; EAZ11698.1; -; Genomic_DNA.
DR   EMBL; AK061988; BAG88191.1; -; mRNA.
DR   RefSeq; NP_001042915.1; NM_001049450.1.
DR   UniGene; Os.28209; -.
DR   UniGene; Os.37856; -.
DR   HSSP; Q862M4; 1AAR.
DR   ProteinModelPortal; Q9ARZ9; -.
DR   STRING; Q9ARZ9; -.
DR   PRIDE; Q9ARZ9; -.
DR   EnsemblPlants; LOC_Os01g22490.1; LOC_Os01g22490.1; LOC_Os01g22490.
DR   GeneID; 4326977; -.
DR   KEGG; osa:4326977; -.
DR   NMPDR; fig|39947.1.peg.342; -.
DR   Gramene; Q9ARZ9; -.
DR   GeneTree; EPGT00050000007995; -.
DR   OMA; QYCGRCH; -.
DR   PhylomeDB; Q9ARZ9; -.
DR   ProtClustDB; CLSN2682087; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR002906; Ribosomal_S27a.
DR   InterPro; IPR000626; Ubiquitin.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_subgr.
DR   InterPro; IPR019955; Ubiquitin_supergroup.
DR   Pfam; PF01599; Ribosomal_S27; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
DR   HOGENOMDNA; ORYSJ_12.PE3974; -.
KW   LOC_Os09g395008286.scaffold_90100000011;
KW   P35296; P69321; A6N0G0; B8BEN6; Q10PH1;
KW   Cytoplasm; Isopeptide bond; Metal-binding; Nucleus; Ribonucleoprotein;
KW   Ribosomal protein; Ubl conjugation; Zinc; Zinc-finger.
SQ   SEQUENCE   129 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN
     IQKESTLHLV LRLRGGIIEP SLQALARKYN QDKMICRKCY ARLHPRAVNC RKKKCGHSNQ
     LRPKKKIKN
//

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