CUL1_CAEEL
ID CUL1_CAEEL Reviewed; 780 AA.
AC Q17389; Q18985;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Cullin-1;
DE Short=CUL-1;
DE AltName: Full=Abnormal cell lineage protein 19;
GN Name=cul-1; Synonyms=lin-19; ORFNames=D2045.6;
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 [MRNA].
RC STRAIN=Bristol N2;
RX PubMed=8681378; DOI=10.1016/s0092-8674(00)81267-2;
RA Kipreos E.T., Lander L.E., Wing J.P., He W.W., Hedgecock E.M.;
RT "cul-1 is required for cell cycle exit in C. elegans and identifies a novel
RT gene family.";
RL Cell 85:829-839(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [3]
RP INTERACTION WITH SKR-1; SKR-2; SKR-3; SKR-4; SKR-7; SKR-8; SKR-9 AND
RP SKR-10.
RX PubMed=11864566; DOI=10.1016/s0960-9822(02)00657-7;
RA Yamanaka A., Yada M., Imaki H., Koga M., Ohshima Y., Nakayama K.;
RT "Multiple Skp1-related proteins in Caenorhabditis elegans: diverse patterns
RT of interaction with Cullins and F-box proteins.";
RL Curr. Biol. 12:267-275(2002).
RN [4]
RP INTERACTION WITH RPM-1; FSN-1 AND SKR-1.
RX PubMed=15208641; DOI=10.1038/nature02647;
RA Liao E.H., Hung W., Abrams B., Zhen M.;
RT "An SCF-like ubiquitin ligase complex that controls presynaptic
RT differentiation.";
RL Nature 430:345-350(2004).
RN [5]
RP FUNCTION.
RX PubMed=17392428; DOI=10.1073/pnas.0700638104;
RA Ghazi A., Henis-Korenblit S., Kenyon C.;
RT "Regulation of Caenorhabditis elegans lifespan by a proteasomal E3 ligase
RT complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5947-5952(2007).
CC -!- FUNCTION: Probable core component of multiple cullin-RING-based SCF
CC (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complexes which mediate
CC the ubiquitination and subsequent proteasomal degradation of target
CC proteins. As a scaffold protein may contribute to catalysis through
CC positioning of the substrate and the ubiquitin-conjugating enzyme.
CC Required for developmentally programmed transitions from the G1 phase
CC of the cell cycle to the G0 phase or the apoptotic pathway.
CC {ECO:0000269|PubMed:17392428}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin
CC ligase complex composed of cul-1, fsn-1, rpm-1 and skr-1
CC (PubMed:15208641). Interacts with Skp1-related proteins skr-1, skr-2,
CC skr-3, skr-4, skr-7, skr-8, skr-9 and skr-10 (PubMed:11864566).
CC {ECO:0000269|PubMed:11864566, ECO:0000269|PubMed:15208641}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DEVELOPMENTAL STAGE: Highest levels in embryos and lower levels in
CC larvae and adults.
CC -!- PTM: Neddylated; which enhances the ubiquitination activity of SCF.
CC {ECO:0000250|UniProtKB:Q13616}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
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DR EMBL; U58083; AAC47120.1; -; mRNA.
DR EMBL; Z35639; CAA84695.2; -; Genomic_DNA.
DR PIR; T20365; T20365.
DR RefSeq; NP_499309.1; NM_066908.4.
DR AlphaFoldDB; Q17389; -.
DR SMR; Q17389; -.
DR BioGRID; 41658; 35.
DR ComplexPortal; CPX-958; SCF-rpm-1 ubiquitin ligase complex.
DR IntAct; Q17389; 2.
DR STRING; 6239.D2045.6; -.
DR EPD; Q17389; -.
DR PaxDb; Q17389; -.
DR PeptideAtlas; Q17389; -.
DR EnsemblMetazoa; D2045.6.1; D2045.6.1; WBGene00000836.
DR GeneID; 176466; -.
DR KEGG; cel:CELE_D2045.6; -.
DR UCSC; D2045.6; c. elegans.
DR CTD; 176466; -.
DR WormBase; D2045.6; CE29089; WBGene00000836; cul-1.
DR eggNOG; KOG2166; Eukaryota.
DR GeneTree; ENSGT00940000154774; -.
DR HOGENOM; CLU_004747_6_1_1; -.
DR InParanoid; Q17389; -.
DR OMA; GVYTAVH; -.
DR OrthoDB; 1040292at2759; -.
DR PhylomeDB; Q17389; -.
DR Reactome; R-CEL-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-CEL-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-CEL-68949; Orc1 removal from chromatin.
DR Reactome; R-CEL-69231; Cyclin D associated events in G1.
DR Reactome; R-CEL-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-CEL-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-CEL-8951664; Neddylation.
DR Reactome; R-CEL-917937; Iron uptake and transport.
DR Reactome; R-CEL-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q17389; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000836; Expressed in embryo and 4 other tissues.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:ComplexPortal.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:WormBase.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:WormBase.
DR GO; GO:0010826; P:negative regulation of centrosome duplication; IMP:UniProtKB.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:WormBase.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0008361; P:regulation of cell size; IMP:WormBase.
DR GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR GO; GO:0090128; P:regulation of synapse maturation; IC:ComplexPortal.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0042594; P:response to starvation; IMP:UniProtKB.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR045093; Cullin.
DR InterPro; IPR016157; Cullin_CS.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11932; PTHR11932; 1.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR SMART; SM00182; CULLIN; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
DR SUPFAM; SSF75632; SSF75632; 1.
DR PROSITE; PS01256; CULLIN_1; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Isopeptide bond; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..780
FT /note="Cullin-1"
FT /id="PRO_0000119780"
FT CROSSLNK 724
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000250|UniProtKB:Q13616"
SQ SEQUENCE 780 AA; 89527 MW; 38A5C2EE0A7CC881 CRC64;
MTNSEPRRMT CDSEVVWKKL QDGLDVAYRR ENMAPKDYMT LYTSVYDYCT SITLSTSRRD
GEDGRAESST PARTAGADFV GHEMYQRVEE YVKAYVIAVC EKGAELSGED LLKYYTTEWE
NFRISSKVMD GIFAYLNRHW IRRELDEGHE NIYMVYTLAL VVWKRNLFND LKDKVIDAML
ELIRSERTGS MINSRYISGV VECLVELGVD DSETDAKKDA ETKKLAVYKE FFEVKFLEAT
RGFYTQEAAN FLSNGGNVTD YMIKVETRLN QEDDRCQLYL NSSTKTPLAT CCESVLISNQ
LDFLQRHFGG LLVDKRDDDL SRMFKLCDRV PNGLDELRKS LENHIAKEGH QALERVAMEA
ATDAKLYVKT LLEVHERYQS LVNRSFKNEP GFMQSLDKAA TSFINNNAVT KRAPPQAQLT
KSAELLARYC DQLLRKSSKM PDEAELEELQ TKIMVVFKYI DDKDVFSKFY TKMFSKRLIS
ELSASDEAEA NFITKLKSMC GYEYTARLSK MVNDTQVSKD LTADFKEKKA DMLGQKSVEF
NVLVLSSGSW PTFPTTPITL PQQLSKTIEI FGQFYNEKFN GRRLTWVYSQ SRGEITSTAF
PKKYVFTATT AQMCTMLLFN EQDSYTVEQI AAATKMDEKS APAIVGSLIK NLVLKADTEL
QKEDEVPMTA TVSLNKAYMN KKVRVDLSKF TMKQDAVRDT ENVQKNVEED RKSVISACIV
RIMKTRKRVQ HQQLMTEVIT QLSGRFKPKV EMIKRCIGSL IEKEYMLRTE GQKDLYEYLA
