(data stored in ACNUC16935 zone)

HOGENOM: RABIT17_46_PE48

ID   RABIT17_46_PE48                      STANDARD;      PRT;   81 AA.
AC   RABIT17_46_PE48; Q4PLJ0;
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=NEDD8;AltName: Full=Neddylin;AltName: Full=Ubiquitin-like
DE   protein Nedd8;Flags: Precursor; (RABIT17_46.PE48).
GN   Name=NEDD8;
OS   ORYCTOLAGUS CUNICULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RABIT17_46.PE48.
CC       Oryctolagus cuniculus chromosome 17 oryCun2 partial sequence
CC       43434537..44434536 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:NEDD8_RABIT
CC   -!- FUNCTION: Ubiquitin-like protein which plays an important role in
CC       cell cycle control and embryogenesis. Covalent attachment to its
CC       substrates requires prior activation by the E1 complex UBE1C-
CC       APPBP1 and linkage to the E2 enzyme UBE2M. Attachment of NEDD8 to
CC       cullins activates their associated E3 ubiquitin ligase activity,
CC       and thus promotes polyubiquitination and proteasomal degradation
CC       of cyclins and other regulatory proteins (By similarity).
CC   -!- SUBUNIT: Directly interacts with NUB1 and AHR. Covalently attached
CC       to cullins and p53 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Mainly nuclear (By
CC       similarity).
CC   -!- PTM: Cleavage of precursor form by UCHL3 or SENP8 is necessary for
CC       function (By similarity).
CC   -!- SIMILARITY: Belongs to the ubiquitin family.
CC   -!- GENE_FAMILY: HOG000233942 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Oryctolagus_cuniculus;ENSOCUG00000002910;ENSOCUT00000002907;ENSOCUP00000002526.
DR   EMBL; DQ067448; - ;
DR   UniProtKB/Swiss-Prot; Q4PLJ0; -.
DR   EMBL; DQ067448; AAY67833.1; -; mRNA.
DR   RefSeq; NP_001075681.1; NM_001082212.1.
DR   UniGene; Ocu.6280; -.
DR   ProteinModelPortal; Q4PLJ0; -.
DR   SMR; Q4PLJ0; 1-76.
DR   STRING; Q4PLJ0; -.
DR   PRIDE; Q4PLJ0; -.
DR   Ensembl; ENSOCUT00000002907; ENSOCUP00000002526; ENSOCUG00000002910.
DR   GeneID; 100009008; -.
DR   CTD; 4738; -.
DR   eggNOG; maNOG23639; -.
DR   GeneTree; ENSGT00560000077356; -.
DR   OMA; DYKVQGG; -.
DR   OrthoDB; EOG4N04GQ; -.
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; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
DR   HOGENOMDNA; RABIT17_46.PE48; -.
KW   ENSOCUG00000002910820036002503210000011;
KW   NEDD8_RABIT; DQ067448;
KW   Acetylation; Isopeptide bond; Nucleus; Ubl conjugation pathway.
SQ   SEQUENCE   81 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLIKVKTLTG KEIEIDIEPT DKVERIKERV EEKEGIPPQQ QRLIYSGKQM NDEKTAADYK
     ILGGSVLHLV LALRGGGGLR Q
//

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