(data stored in ACNUC16935 zone)

HOGENOM: PIG2_66_PE12

ID   PIG2_66_PE12                         STANDARD;      PRT;   128 AA.
AC   PIG2_66_PE12;
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-60S ribosomal protein L40;AltName:
DE   Full=CEP52;AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion
DE   product 1;Contains: RecName: Full=Ubiquitin;Contains: RecName: Full=60S
DE   ribosomal protein L40;Flags: Precursor; (PIG2_66.PE12).
GN   Name=UBA52; Synonyms=UBCEP2;
OS   SUS SCROFA.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Laurasiatheria; Cetartiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PIG2_66.PE12.
CC       Sus scrofa chromosome 2 Sscrofa9 partial sequence 62352253..63352252
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:RL40_PIG
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-6-linked may be
CC       involved in DNA repair; Lys-11-linked is involved in ERAD
CC       (endoplasmic reticulum-associated degradation) and in cell-cycle
CC       regulation; Lys-29-linked is involved in lysosomal degradation;
CC       Lys-33-linked is involved in kinase modification; Lys-48-linked is
CC       involved in protein degradation via the proteasome; Lys-63-linked
CC       is involved in endocytosis, DNA-damage responses as well as in
CC       signaling processes leading to activation of the transcription
CC       factor NF-kappa-B. 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   -!- FUNCTION: Ribosomal protein L40 is a component of the 60S subunit
CC       of the ribosome.
CC   -!- SUBUNIT: Ribosomal protein L40 is part of the 60S ribosomal
CC       subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm (By similarity).
CC       Nucleus (By similarity).
CC   -!- SUBCELLULAR LOCATION: 60S ribosomal protein L40: Cytoplasm (By
CC       similarity).
CC   -!- MISCELLANEOUS: Ubiquitin is encoded by 4 different genes. UBA52
CC       and RPS27A genes code for a single copy of ubiquitin fused to the
CC       ribosomal proteins L40 and S27a, respectively. UBB and UBC genes
CC       code for a polyubiquitin precursor with exact head to tail
CC       repeats, the number of repeats differ between species and strains.
CC   -!- MISCELLANEOUS: For a better understanding, features related to
CC       ubiquitin are only indicated for the first chain.
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 L40e family.
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC   -!- GENE_FAMILY: HOG000233942 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Sus_scrofa;ENSSSCG00000013907;ENSSSCT00000015193;ENSSSCP00000014787.
DR   EMBL; F14530; - ;
DR   EMBL; F14869; - ;
DR   EMBL; M18159; - ;
DR   EMBL; U72496; - ;
DR   UniProtKB/Swiss-Prot; P63053; P02248; P02249; P02250; P62974; Q29120; Q29203; Q29252; -.
DR   UniProtKB/Swiss-Prot; Q91887; Q91888; Q95260; -.
DR   EMBL; U72496; AAB52914.1; -; mRNA.
DR   PIR; A29584; A29584.
DR   RefSeq; NP_999376.1; NM_214211.1.
DR   UniGene; Ssc.638; -.
DR   ProteinModelPortal; P63053; -.
DR   SMR; P63053; 1-76, 89-128.
DR   STRING; P63053; -.
DR   Ensembl; ENSSSCT00000015193; ENSSSCP00000014787; ENSSSCG00000013907.
DR   GeneID; 397418; -.
DR   KEGG; ssc:397418; -.
DR   CTD; 7311; -.
DR   GeneTree; ENSGT00600000084479; -.
DR   OMA; YNCEKMI; -.
DR   OrthoDB; EOG4V1726; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR001975; Ribosomal_L40e.
DR   InterPro; IPR000626; Ubiquitin.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_subgr.
DR   InterPro; IPR019955; Ubiquitin_supergroup.
DR   Pfam; PF01020; Ribosomal_L40e; 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; PIG2_66.PE12; -.
KW   ENSSSCG00000013907820036002503210000011;
KW   RL40_PIG; UBIQ_PIG; F14530; F14869; M18159; U72496;
KW   Acetylation; Complete proteome; Cytoplasm; Isopeptide bond;
KW   Methylation; Nucleus; Phosphoprotein; Ribonucleoprotein;
KW   Ribosomal protein; Ubl conjugation.
SQ   SEQUENCE   128 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
     IQKESTLHLV LRLRGGIIEP SLRQLAQKYN CDKMICRKCY ARLHPRAVNC RKKKCGHTNN
     LRPKKKVK
//

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