NEDD8_RAT
ID NEDD8_RAT Reviewed; 81 AA.
AC Q71UE8;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=NEDD8;
DE AltName: Full=Neddylin;
DE AltName: Full=Ubiquitin-like protein NEDD8;
DE Flags: Precursor;
GN Name=Nedd8;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=GK; TISSUE=Kidney;
RA Page R.A.;
RT "Isolation of a novel ubiquitin-like protein from the diabetic kidney.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 61-74, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
CC -!- FUNCTION: Ubiquitin-like protein which plays an important role in cell
CC cycle control and embryogenesis via its conjugation to a limited number
CC of cellular proteins, such as cullins or p53/TP53. Attachment of NEDD8
CC to cullins is critical for the recruitment of E2 to the cullin-RING-
CC based E3 ubiquitin-protein ligase complex, thus facilitating
CC polyubiquitination and proteasomal degradation of cyclins and other
CC regulatory proteins. Attachment of NEDD8 to p53/TP53 inhibits p53/TP53
CC transcriptional activity. Covalent attachment to its substrates
CC requires prior activation by the E1 complex UBE1C-APPBP1 and linkage to
CC the E2 enzyme UBE2M. {ECO:0000250|UniProtKB:Q15843}.
CC -!- SUBUNIT: Interacts with AHR; interaction is direct. Interacts with
CC NUB1; interaction is direct. {ECO:0000250|UniProtKB:Q15843}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15843}.
CC Note=Mainly nuclear. {ECO:0000250|UniProtKB:Q15843}.
CC -!- PTM: Cleavage of precursor form by UCHL3 or SENP8 is necessary for
CC function. {ECO:0000250|UniProtKB:Q15843}.
CC -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR EMBL; AF095740; AAC64189.1; -; mRNA.
DR EMBL; BC084728; AAH84728.1; -; mRNA.
DR RefSeq; NP_620233.1; NM_138878.2.
DR AlphaFoldDB; Q71UE8; -.
DR BMRB; Q71UE8; -.
DR SMR; Q71UE8; -.
DR BioGRID; 247523; 2.
DR DIP; DIP-60385N; -.
DR IntAct; Q71UE8; 2.
DR STRING; 10116.ENSRNOP00000061284; -.
DR iPTMnet; Q71UE8; -.
DR PhosphoSitePlus; Q71UE8; -.
DR jPOST; Q71UE8; -.
DR PaxDb; Q71UE8; -.
DR PRIDE; Q71UE8; -.
DR Ensembl; ENSRNOT00000064916; ENSRNOP00000061284; ENSRNOG00000019895.
DR GeneID; 25490; -.
DR KEGG; rno:25490; -.
DR UCSC; RGD:3158; rat.
DR CTD; 4738; -.
DR RGD; 3158; Nedd8.
DR eggNOG; KOG0005; Eukaryota.
DR GeneTree; ENSGT00940000155856; -.
DR HOGENOM; CLU_010412_6_4_1; -.
DR InParanoid; Q71UE8; -.
DR OrthoDB; 1536766at2759; -.
DR PhylomeDB; Q71UE8; -.
DR TreeFam; TF300072; -.
DR Reactome; R-RNO-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-RNO-5689603; UCH proteinases.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-917937; Iron uptake and transport.
DR PRO; PR:Q71UE8; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000019895; Expressed in Ammon's horn and 20 other tissues.
DR ExpressionAtlas; Q71UE8; baseline and differential.
DR Genevisible; Q71UE8; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0045116; P:protein neddylation; IDA:RGD.
DR GO; GO:0030162; P:regulation of proteolysis; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IDA:RGD.
DR CDD; cd01806; Ubl_NEDD8; 1.
DR InterPro; IPR038738; Nedd8-like.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Isopeptide bond; Nucleus;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..76
FT /note="NEDD8"
FT /id="PRO_0000042773"
FT PROPEP 77..81
FT /evidence="ECO:0000250|UniProtKB:Q15843"
FT /id="PRO_0000042774"
FT REGION 70..72
FT /note="Interaction with UBE1C"
FT /evidence="ECO:0000250|UniProtKB:Q15843"
FT SITE 8
FT /note="Interaction with UBE1C"
FT /evidence="ECO:0000250|UniProtKB:Q15843"
FT SITE 44
FT /note="Interaction with UBE1C"
FT /evidence="ECO:0000250|UniProtKB:Q15843"
FT MOD_RES 48
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29595"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ SEQUENCE 81 AA; 8972 MW; DC339102BE4725D2 CRC64;
MLIKVKTLTG KEIEIDIEPT DKVERIKERV EEKEGIPPQQ QRLIYSGKQM NDEKTAADYK
ILGGSVLHLV LALRGGGGLG Q
