(data stored in ACNUC16935 zone)

HOGENOM: HS14_PE348

ID   HS14_PE348                           STANDARD;      PRT;   81 AA.
AC   HS14_PE348; Q15843; Q3SXN8; Q6LES6;
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=Neural precursor
DE   cell expressed developmentally down-regulated protein 8;
DE   Short=NEDD-8;AltName: Full=Ubiquitin-like protein Nedd8;Flags: Precursor;
DE   (HS14.PE348).
GN   Name=NEDD8;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS14.PE348.
CC       Homo sapiens chromosome 14 GRCh37  sequence 1..107289540 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:NEDD8_HUMAN
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.
CC   -!- SUBUNIT: Directly interacts with NUB1 and AHR. Covalently attached
CC       to cullins and p53.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Mainly nuclear.
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle,
CC       spleen, thymus, prostate, testis, ovary, colon and leukocytes.
CC   -!- PTM: Cleavage of precursor form by UCHL3 or SENP8 is necessary for
CC       function.
CC   -!- SIMILARITY: Belongs to the ubiquitin family.
CC   -!- GENE_FAMILY: HOG000233942 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000129559;ENST00000250495;ENSP00000250495.
DR   EMBL; BC104200; - ;
DR   EMBL; BC104201; - ;
DR   EMBL; BC104664; - ;
DR   EMBL; CR407662; - ;
DR   EMBL; D23662; - ;
DR   UniProtKB/Swiss-Prot; Q15843; Q3SXN8; Q6LES6; -.
DR   EMBL; D23662; BAA04889.1; -; mRNA.
DR   EMBL; CR407662; CAG28590.1; -; mRNA.
DR   EMBL; BC104200; AAI04201.1; -; mRNA.
DR   EMBL; BC104201; AAI04202.1; -; mRNA.
DR   EMBL; BC104664; AAI04665.1; -; mRNA.
DR   IPI; IPI00020008; -.
DR   RefSeq; NP_006147.1; NM_006156.2.
DR   UniGene; Hs.531064; -.
DR   PDB; 1NDD; X-ray; 1.60 A; A/B/C/D=1-76.
DR   PDB; 1R4M; X-ray; 3.00 A; I/J/K/L=1-76.
DR   PDB; 1R4N; X-ray; 3.60 A; I/J/K/L=1-76.
DR   PDB; 1XT9; X-ray; 2.20 A; B=1-76.
DR   PDB; 2BKR; X-ray; 1.90 A; B=1-76.
DR   PDB; 2KO3; NMR; -; A=1-76.
DR   PDB; 2NVU; X-ray; 2.80 A; I/J=1-76.
DR   PDB; 3DBH; X-ray; 2.85 A; I/J/K/L=1-76.
DR   PDB; 3DBL; X-ray; 2.90 A; I/J/K/L=1-76.
DR   PDB; 3DBR; X-ray; 3.05 A; I/J/K/L=1-76.
DR   PDB; 3DQV; X-ray; 3.00 A; A/B=1-76.
DR   PDB; 3GZN; X-ray; 3.00 A; I/J=1-76.
DR   PDBsum; 1NDD; -.
DR   PDBsum; 1R4M; -.
DR   PDBsum; 1R4N; -.
DR   PDBsum; 1XT9; -.
DR   PDBsum; 2BKR; -.
DR   PDBsum; 2KO3; -.
DR   PDBsum; 2NVU; -.
DR   PDBsum; 3DBH; -.
DR   PDBsum; 3DBL; -.
DR   PDBsum; 3DBR; -.
DR   PDBsum; 3DQV; -.
DR   PDBsum; 3GZN; -.
DR   ProteinModelPortal; Q15843; -.
DR   SMR; Q15843; 1-76.
DR   DIP; DIP-29266N; -.
DR   IntAct; Q15843; 17.
DR   MINT; MINT-268324; -.
DR   STRING; Q15843; -.
DR   PhosphoSite; Q15843; -.
DR   PeptideAtlas; Q15843; -.
DR   PRIDE; Q15843; -.
DR   Ensembl; ENST00000250495; ENSP00000250495; ENSG00000129559.
DR   GeneID; 4738; -.
DR   KEGG; hsa:4738; -.
DR   UCSC; uc001wnn.2; human.
DR   CTD; 4738; -.
DR   GeneCards; GC14M004801; -.
DR   H-InvDB; HIX0202089; -.
DR   HGNC; HGNC:7732; NEDD8.
DR   HPA; CAB004082; -.
DR   MIM; 603171; gene.
DR   neXtProt; NX_Q15843; -.
DR   PharmGKB; PA31537; -.
DR   eggNOG; prNOG21659; -.
DR   GeneTree; ENSGT00560000077356; -.
DR   InParanoid; Q15843; -.
DR   OMA; DYKVQGG; -.
DR   OrthoDB; EOG4N04GQ; -.
DR   PhylomeDB; Q15843; -.
DR   NextBio; 18272; -.
DR   PMAP-CutDB; Q15843; -.
DR   ArrayExpress; Q15843; -.
DR   Bgee; Q15843; -.
DR   CleanEx; HS_NEDD8; -.
DR   Genevestigator; Q15843; -.
DR   GermOnline; ENSG00000129559; Homo sapiens.
DR   GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR   GO; GO:0045116; P:protein neddylation; IDA:MGI.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc.
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; HS14.PE348; -.
KW   ENSG000001295591755old_1320000031; ENSP000002504957901old_1320000031;
KW   BC104200; BC104201; BC104664; CR407662; D23662;
KW   3D-structure; Acetylation; Complete proteome;
KW   Direct protein sequencing; Isopeptide bond; Nucleus;
KW   Reference proteome; Ubl conjugation pathway.
SQ   SEQUENCE   81 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLIKVKTLTG KEIEIDIEPT DKVERIKERV EEKEGIPPQQ QRLIYSGKQM NDEKTAADYK
     ILGGSVLHLV LALRGGGGLR Q
//

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