DCN1_CAEEL
ID DCN1_CAEEL Reviewed; 295 AA.
AC Q9U3C8; Q9U3C9;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Defective in cullin neddylation protein 1;
GN Name=dcn-1; ORFNames=H38K22.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP CUL-3; NED-8 AND UBIQUITIN.
RX PubMed=15988528; DOI=10.1038/nature03662;
RA Kurz T., Oezlue N., Rudolf F., O'Rourke S.M., Luke B., Hofmann K.,
RA Hyman A.A., Bowerman B., Peter M.;
RT "The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C.
RT elegans and S. cerevisiae.";
RL Nature 435:1257-1261(2005).
CC -!- FUNCTION: Required for neddylation of cullin components of SCF-type E3
CC ubiquitin ligase complexes. Neddylation of cullins play an essential
CC role in the regulation of SCF-type complexes activity. Does not act by
CC preventing deneddylation, but rather facilitates neddylation, possibly
CC by acting with rbx-1 to recruit the Nedd8-charged E2 enzyme to the
CC cullin component of SCF-type complexes. {ECO:0000269|PubMed:15988528}.
CC -!- SUBUNIT: Interacts with the cullin cul-3. Interacts with ubiquitin via
CC its UBA-like domain. Interacts with ned-8/nedd8.
CC {ECO:0000269|PubMed:15988528}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15988528}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q9U3C8-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q9U3C8-2; Sequence=VSP_015319;
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DR EMBL; AL024499; CAB54261.2; -; Genomic_DNA.
DR EMBL; AL024499; CAB54260.2; -; Genomic_DNA.
DR PIR; T23140; T23140.
DR PIR; T23141; T23141.
DR RefSeq; NP_497866.2; NM_065465.5. [Q9U3C8-1]
DR RefSeq; NP_497867.2; NM_065466.5.
DR AlphaFoldDB; Q9U3C8; -.
DR SMR; Q9U3C8; -.
DR BioGRID; 40792; 12.
DR IntAct; Q9U3C8; 2.
DR STRING; 6239.H38K22.2a; -.
DR EPD; Q9U3C8; -.
DR PaxDb; Q9U3C8; -.
DR PeptideAtlas; Q9U3C8; -.
DR EnsemblMetazoa; H38K22.2a.1; H38K22.2a.1; WBGene00010428. [Q9U3C8-1]
DR EnsemblMetazoa; H38K22.2a.2; H38K22.2a.2; WBGene00010428. [Q9U3C8-1]
DR EnsemblMetazoa; H38K22.2b.1; H38K22.2b.1; WBGene00010428. [Q9U3C8-2]
DR GeneID; 175556; -.
DR KEGG; cel:CELE_H38K22.2; -.
DR UCSC; H38K22.2a; c. elegans. [Q9U3C8-1]
DR CTD; 175556; -.
DR WormBase; H38K22.2a; CE33527; WBGene00010428; dcn-1. [Q9U3C8-1]
DR WormBase; H38K22.2b; CE33528; WBGene00010428; dcn-1. [Q9U3C8-2]
DR eggNOG; KOG3077; Eukaryota.
DR GeneTree; ENSGT00940000168836; -.
DR InParanoid; Q9U3C8; -.
DR OMA; FTQTGEQ; -.
DR OrthoDB; 1418097at2759; -.
DR PhylomeDB; Q9U3C8; -.
DR Reactome; R-CEL-8951664; Neddylation.
DR PRO; PR:Q9U3C8; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00010428; Expressed in embryo and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IDA:WormBase.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0032182; F:ubiquitin-like protein binding; IBA:GO_Central.
DR GO; GO:0030953; P:astral microtubule organization; IMP:WormBase.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:WormBase.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0030163; P:protein catabolic process; IMP:WormBase.
DR GO; GO:0045116; P:protein neddylation; IMP:UniProtKB.
DR Gene3D; 1.10.238.200; -; 1.
DR InterPro; IPR014764; DCN-prot.
DR InterPro; IPR042460; DCN1-like_PONY.
DR InterPro; IPR005176; PONY_dom.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR12281; PTHR12281; 1.
DR Pfam; PF03556; Cullin_binding; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS51229; DCUN1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..295
FT /note="Defective in cullin neddylation protein 1"
FT /id="PRO_0000129507"
FT DOMAIN 8..45
FT /note="UBA-like"
FT DOMAIN 60..272
FT /note="DCUN1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00574"
FT VAR_SEQ 1..64
FT /note="MNRLKSDQKTKLRQFVQWTQVTEAVSLNFLAKANWNIEYAMTLYFDNPNLFA
FT GSTPQPSVDRSN -> MNRLKSDQKTK (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_015319"
SQ SEQUENCE 295 AA; 34133 MW; F5C50912727235E4 CRC64;
MNRLKSDQKT KLRQFVQWTQ VTEAVSLNFL AKANWNIEYA MTLYFDNPNL FAGSTPQPSV
DRSNIERLFN QYVDPKDKVG EKRMGPHGIN RLLTDLGYEA TDRRVLVLAW KFTAQTQCEF
SLDEWVKGMT ALQADTVQNL RQRIDSINSG LESDKAKFHE LYLFAFNYAK SAACRNLDLE
TAICCWDVLF GQRSTIMTQW IDFLWAQENA AASRLAQNVG ASNAKQFKSV WISRDTWNLF
WDFILLSKPD LSDYDDEGAW PVLIDQFVDY CRENLNYPKP GNASNDQQME TPSYY
