CUL3_MOUSE
ID CUL3_MOUSE Reviewed; 768 AA.
AC Q9JLV5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Cullin-3;
DE Short=CUL-3;
GN Name=Cul3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Levy N., Agulnik A.I., Boettger-Tong H., Bishop C.E.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 SUBCELLULAR LOCATION, INTERACTION WITH CYCE, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=10500095; DOI=10.1101/gad.13.18.2375;
RA Singer J.D., Gurian-West M., Clurman B., Roberts J.M.;
RT "Cullin-3 targets cyclin E for ubiquitination and controls S phase in
RT mammalian cells.";
RL Genes Dev. 13:2375-2387(1999).
RN [4]
RP FUNCTION OF THE BCR(KEAP1) COMPLEX.
RX PubMed=12193649; DOI=10.1073/pnas.172398899;
RA Dinkova-Kostova A.T., Holtzclaw W.D., Cole R.N., Itoh K., Wakabayashi N.,
RA Katoh Y., Yamamoto M., Talalay P.;
RT "Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating
RT induction of phase 2 enzymes that protect against carcinogens and
RT oxidants.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11908-11913(2002).
RN [5]
RP FUNCTION OF THE BCR(KEAP1) COMPLEX.
RX PubMed=14764894; DOI=10.1073/pnas.0307301101;
RA Wakabayashi N., Dinkova-Kostova A.T., Holtzclaw W.D., Kang M.I.,
RA Kobayashi A., Yamamoto M., Kensler T.W., Talalay P.;
RT "Protection against electrophile and oxidant stress by induction of the
RT phase 2 response: fate of cysteines of the Keap1 sensor modified by
RT inducers.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2040-2045(2004).
RN [6]
RP FUNCTION OF THE BCR(KEAP1) COMPLEX, AND IDENTIFICATION IN THE BCR(KEAP1)
RP COMPLEX.
RX PubMed=15282312; DOI=10.1128/mcb.24.16.7130-7139.2004;
RA Kobayashi A., Kang M.I., Okawa H., Ohtsuji M., Zenke Y., Chiba T.,
RA Igarashi K., Yamamoto M.;
RT "Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3
RT ligase to regulate proteasomal degradation of Nrf2.";
RL Mol. Cell. Biol. 24:7130-7139(2004).
RN [7]
RP TISSUE SPECIFICITY, AND INTERACTION WITH KLHL10.
RX PubMed=16162871; DOI=10.1095/biolreprod.105.045484;
RA Wang S., Zheng H., Esaki Y., Kelly F., Yan W.;
RT "Cullin3 is a KLHL10-interacting protein preferentially expressed during
RT late spermiogenesis.";
RL Biol. Reprod. 74:102-108(2006).
RN [8]
RP IDENTIFICATION IN THE BCR(KEAP1) COMPLEX.
RX PubMed=16790436; DOI=10.1074/jbc.m601119200;
RA McMahon M., Thomas N., Itoh K., Yamamoto M., Hayes J.D.;
RT "Dimerization of substrate adaptors can facilitate cullin-mediated
RT ubiquitylation of proteins by a 'tethering' mechanism: a two-site
RT interaction model for the Nrf2-Keap1 complex.";
RL J. Biol. Chem. 281:24756-24768(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22358839; DOI=10.1038/nature10822;
RA Jin L., Pahuja K.B., Wickliffe K.E., Gorur A., Baumgartel C., Schekman R.,
RA Rape M.;
RT "Ubiquitin-dependent regulation of COPII coat size and function.";
RL Nature 482:495-500(2012).
RN [11]
RP IDENTIFICATION IN THE BCR(KEAP1) COMPLEX.
RX PubMed=27697860; DOI=10.1128/mcb.00389-16;
RA Iso T., Suzuki T., Baird L., Yamamoto M.;
RT "Absolute Amounts and Status of the Nrf2-Keap1-Cul3 Complex within Cells.";
RL Mol. Cell. Biol. 36:3100-3112(2016).
RN [12]
RP STRUCTURE BY NMR OF 678-768.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the cullin-3 homologue.";
RL Submitted (OCT-2003) to the PDB data bank.
CC -!- FUNCTION: Core component of multiple cullin-RING-based BCR (BTB-CUL3-
CC RBX1) E3 ubiquitin-protein ligase complexes which mediate the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins (By similarity). BCR complexes and ARIH1 collaborate in tandem
CC to mediate ubiquitination of target proteins (By similarity). As a
CC scaffold protein may contribute to catalysis through positioning of the
CC substrate and the ubiquitin-conjugating enzyme (By similarity). The E3
CC ubiquitin-protein ligase activity of the complex is dependent on the
CC neddylation of the cullin subunit and is inhibited by the association
CC of the deneddylated cullin subunit with TIP120A/CAND1 (By similarity).
CC The functional specificity of the BCR complex depends on the BTB
CC domain-containing protein as the substrate recognition component (By
CC similarity). BCR(KLHL42) is involved in ubiquitination of KATNA1 (By
CC similarity). BCR(SPOP) is involved in ubiquitination of BMI1/PCGF4,
CC BRMS1, MACROH2A1 and DAXX, GLI2 and GLI3 (By similarity). Can also form
CC a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase
CC complex containing homodimeric SPOPL or the heterodimer formed by SPOP
CC and SPOPL; these complexes have lower ubiquitin ligase activity (By
CC similarity). BCR(KLHL9-KLHL13) controls the dynamic behavior of AURKB
CC on mitotic chromosomes and thereby coordinates faithful mitotic
CC progression and completion of cytokinesis (By similarity). BCR(KLHL12)
CC is involved in ER-Golgi transport by regulating the size of COPII
CC coats, thereby playing a key role in collagen export, which is required
CC for embryonic stem (ES) cells division: BCR(KLHL12) acts by mediating
CC monoubiquitination of SEC31 (SEC31A or SEC31B) (PubMed:22358839).
CC BCR(KLHL3) acts as a regulator of ion transport in the distal nephron;
CC by mediating ubiquitination of WNK4 (By similarity). The BCR(KLHL20) E3
CC ubiquitin ligase complex is involved in interferon response and
CC anterograde Golgi to endosome transport: it mediates both
CC ubiquitination leading to degradation and 'Lys-33'-linked
CC ubiquitination (By similarity). The BCR(KLHL21) E3 ubiquitin ligase
CC complex regulates localization of the chromosomal passenger complex
CC (CPC) from chromosomes to the spindle midzone in anaphase and mediates
CC the ubiquitination of AURKB (By similarity). The BCR(KLHL22) ubiquitin
CC ligase complex mediates monoubiquitination of PLK1, leading to PLK1
CC dissociation from phosphoreceptor proteins and subsequent removal from
CC kinetochores, allowing silencing of the spindle assembly checkpoint
CC (SAC) and chromosome segregation. The BCR(KLHL22) ubiquitin ligase
CC complex is also responsible for the amino acid-stimulated 'Lys-48'
CC polyubiquitination and proteasomal degradation of DEPDC5. Through the
CC degradation of DEPDC5, releases the GATOR1 complex-mediated inhibition
CC of the TORC1 pathway (By similarity). The BCR(KLHL25) ubiquitin ligase
CC complex is involved in translational homeostasis by mediating
CC ubiquitination and subsequent degradation of hypophosphorylated
CC EIF4EBP1 (4E-BP1) (By similarity). The BCR(KBTBD8) complex acts by
CC mediating monoubiquitination of NOLC1 and TCOF1, leading to remodel the
CC translational program of differentiating cells in favor of neural crest
CC specification (By similarity). Involved in ubiquitination of cyclin E
CC and of cyclin D1 (in vitro) thus involved in regulation of G1/S
CC transition (By similarity). Involved in the ubiquitination of KEAP1,
CC ENC1 and KLHL41 (By similarity). In concert with ATF2 and RBX1,
CC promotes degradation of KAT5 thereby attenuating its ability to
CC acetylate and activate ATM (By similarity). The BCR(KCTD17) E3
CC ubiquitin ligase complex mediates ubiquitination and degradation of
CC TCHP, a down-regulator of cilium assembly, thereby inducing
CC ciliogenesis (By similarity). The BCR(KLHL24) E3 ubiquitin ligase
CC complex mediates ubiquitination of KRT14, controls KRT14 levels during
CC keratinocytes differentiation, and is essential for skin integrity (By
CC similarity). The BCR(KLHL18) E3 ubiquitin ligase complex mediates the
CC ubiquitination of AURKA leading to its activation at the centrosome
CC which is required for initiating mitotic entry (By similarity). The
CC BCR(KEAP1) E3 ubiquitin ligase complex acts as a key sensor of
CC oxidative and electrophilic stress by mediating ubiquitination and
CC degradation of NFE2L2/NRF2, a transcription factor regulating
CC expression of many cytoprotective genes (PubMed:12193649,
CC PubMed:14764894, PubMed:15282312). As part of the CUL3(KBTBD6/7) E3
CC ubiquitin ligase complex functions mediates 'Lys-48' ubiquitination and
CC proteasomal degradation of TIAM1. By controlling the ubiquitination of
CC that RAC1 guanine exchange factors (GEF), regulates RAC1 signal
CC transduction and downstream biological processes including the
CC organization of the cytoskeleton, cell migration and cell proliferation
CC (By similarity). {ECO:0000250|UniProtKB:Q13618,
CC ECO:0000269|PubMed:12193649, ECO:0000269|PubMed:14764894,
CC ECO:0000269|PubMed:15282312, ECO:0000269|PubMed:22358839}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Forms neddylation-dependent homodimers (By similarity).
CC Component of multiple BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase
CC complexes formed of CUL3, RBX1 and a variable BTB domain-containing
CC protein acting as both, adapter to cullin and substrate recognition
CC subunit (By similarity). The BCR complex may be active as a
CC heterodimeric complex, in which NEDD8, covalently attached to one CUL3
CC molecule, binds to the C-terminus of a second CUL3 molecule (By
CC similarity). Interacts with RBX1, RNF7 and TIP120A/CAND1 (By
CC similarity). Part of the BCR(SPOP) containing SPOP, and of BCR
CC containing homodimeric SPOPL or the heterodimer formed by SPOP and
CC SPOPL (By similarity). Part of the probable BCR(KLHL9-KLHL13) complex
CC with BTB domain proteins KLHL9 and KLHL13 (By similarity). Part of the
CC BCR(KLHL41) complex containing KLHL41 (By similarity). Component of the
CC BCR(KLHL12) E3 ubiquitin ligase complex, at least composed of CUL3 and
CC KLHL12 and RBX1 (By similarity). Component of the BCR(KLHL3) E3
CC ubiquitin ligase complex, at least composed of CUL3 and KLHL3 and RBX1
CC (By similarity). Part of the BCR(ENC1) complex containing ENC1 (By
CC similarity). Part of a complex consisting of BMI1/PCGF4, CUL3 and SPOP
CC (By similarity). Part of a complex consisting of BRMS1, CUL3 and SPOP
CC (By similarity). Component of the BCR(KLHL21) E3 ubiquitin ligase
CC complex, at least composed of CUL3, KLHL21 and RBX1 (By similarity).
CC Component of the BCR(KLHL22) E3 ubiquitin ligase complex, at least
CC composed of CUL3, KLHL22 and RBX1 (By similarity). Component of the
CC BCR(KLHL25) E3 ubiquitin ligase complex, at least composed of CUL3,
CC KLHL25 and RBX1 (By similarity). Part of a complex consisting of
CC MACROH2A1, CUL3 and SPOP (By similarity). Component of the BCR(KLHL42)
CC E3 ubiquitin ligase complex, at least composed of CUL3 and KLHL42 (By
CC similarity). Component of the BCR(KBTBD8) E3 ubiquitin ligase complex,
CC at least composed of CUL3, KBTBD8 and RBX1 (By similarity). Interacts
CC with KLHL42 (via the BTB domain) (By similarity). Interacts with
CC KATNA1; the interaction is enhanced by KLHL42 (By similarity).
CC Interacts with KCTD5, KLHL9, KLHL11, KLHL13, GAN, ZBTB16, KLHL3,
CC KLHL15, KLHL20, KLHL36, GMCL2, BTBD1 (By similarity). Part of a complex
CC that contains CUL3, RBX1 and GAN (By similarity). Interacts (via BTB
CC domain) with KLHL17; the interaction regulates surface GRIK2 expression
CC (By similarity). Interacts with KCTD7 (By similarity). Part of the
CC BCR(GAN) complex containing GAN (By similarity). Part of the BCR(KEAP1)
CC complex containing KEAP1 (PubMed:15282312, PubMed:16790436,
CC PubMed:27697860). Interacts with KAT5 and ATF2 (By similarity).
CC Interacts with KCTD17 in the BCR(KCTD17) E3 ubiquitin ligase complex,
CC at least composed of CUL3, KCTD17 and RBX1 (By similarity). Interacts
CC (when neddylated) with ARIH1; leading to activate the E3 ligase
CC activity of ARIH1 (By similarity). Interacts with COPS9 (By
CC similarity). Interacts with PPP2R5B; this interaction is indirect and
CC mediated through KLHL15-binding and leads to PPP2R5B proteasomal
CC degradation (By similarity). Interacts with RBBP8/CtIP; this
CC interaction is indirect and mediated through KLHL15-binding and leads
CC to RBBP8 proteasomal degradation (By similarity). Interacts with KLHL24
CC in the BCR(KLHL24) E3 ubiquitin ligase complex, composed of CUL3, RBX1
CC and KLHL24 (By similarity). Interacts with RHOBTB2 (By similarity).
CC Interacts with CYCE (PubMed:10500095). Interacts with KLHL10
CC (PubMed:16162871). Interacts with AURKA and KLHL18 (via BTB domain) (By
CC similarity). Interacts (unneddylated form) with DCUN1D1, DCUN1D2,
CC DCUN1D3, DCUN1D4 and DCUN1D5; these interactions promote the cullin
CC neddylation (By similarity). Component of a BCR3 (BTB-CUL3-RBX1) E3
CC ubiquitin ligase complex, also named Cul3-RING ubiquitin ligase complex
CC CUL3(KBTBD6/7), composed of CUL3, RBX1, KBTBD6 and KBTBD7 (By
CC similarity). {ECO:0000250|UniProtKB:Q13618,
CC ECO:0000269|PubMed:10500095, ECO:0000269|PubMed:15282312,
CC ECO:0000269|PubMed:16162871, ECO:0000269|PubMed:16790436,
CC ECO:0000269|PubMed:27697860}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10500095}. Golgi
CC apparatus {ECO:0000269|PubMed:10500095}. Cell projection, cilium,
CC flagellum {ECO:0000250|UniProtKB:Q13618}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q13618}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q13618}. Cytoplasm. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q13618}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q13618}. Note=Detected along the length of the
CC sperm flagellum and in the cytoplasm of the germ cells. Predominantly
CC found in the nucleus in interphase cells, found at the centrosome at
CC late G2 or prophase, starts accumulating at the spindle poles in
CC prometaphase and stays on the spindle poles and the mitotic spindle at
CC metaphase. {ECO:0000250|UniProtKB:Q13618}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in brain,
CC spleen and testis. In the testis, it is mainly expressed in spermatids.
CC {ECO:0000269|PubMed:10500095, ECO:0000269|PubMed:16162871}.
CC -!- PTM: Neddylated. Attachment of NEDD8 is required for the E3 ubiquitin-
CC protein ligase activity of the BCR complex. Deneddylated via its
CC interaction with the COP9 signalosome (CSN) complex.
CC {ECO:0000250|UniProtKB:Q13618}.
CC -!- DISRUPTION PHENOTYPE: Null deficient mice are not viable.
CC Extraembryonic ectoderm shows a greatly increased number of cells in S
CC phase. In the trophectoderm cells are blocked to entry into S phase.
CC Embryonic stem (ES) cells form tightly packed cell clusters with
CC prominent actin cables and aberrant adhesions. ES cells are retained in
CC proliferation, yet retain their pluripotency.
CC {ECO:0000269|PubMed:10500095, ECO:0000269|PubMed:22358839}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF129738; AAF36500.1; -; mRNA.
DR EMBL; BC027304; AAH27304.1; -; mRNA.
DR CCDS; CCDS15094.1; -.
DR RefSeq; NP_001300657.1; NM_001313728.1.
DR RefSeq; NP_057925.1; NM_016716.5.
DR PDB; 1IUY; NMR; -; A=678-768.
DR PDBsum; 1IUY; -.
DR AlphaFoldDB; Q9JLV5; -.
DR SMR; Q9JLV5; -.
DR BioGRID; 205013; 126.
DR CORUM; Q9JLV5; -.
DR IntAct; Q9JLV5; 50.
DR STRING; 10090.ENSMUSP00000130738; -.
DR iPTMnet; Q9JLV5; -.
DR PhosphoSitePlus; Q9JLV5; -.
DR EPD; Q9JLV5; -.
DR jPOST; Q9JLV5; -.
DR MaxQB; Q9JLV5; -.
DR PaxDb; Q9JLV5; -.
DR PRIDE; Q9JLV5; -.
DR ProteomicsDB; 285434; -.
DR Antibodypedia; 3632; 411 antibodies from 40 providers.
DR DNASU; 26554; -.
DR Ensembl; ENSMUST00000163119; ENSMUSP00000130738; ENSMUSG00000004364.
DR GeneID; 26554; -.
DR KEGG; mmu:26554; -.
DR UCSC; uc007brc.1; mouse.
DR CTD; 8452; -.
DR MGI; MGI:1347360; Cul3.
DR VEuPathDB; HostDB:ENSMUSG00000004364; -.
DR eggNOG; KOG2166; Eukaryota.
DR GeneTree; ENSGT00940000155066; -.
DR HOGENOM; CLU_004747_7_1_1; -.
DR InParanoid; Q9JLV5; -.
DR OMA; MFKDMTI; -.
DR OrthoDB; 1040292at2759; -.
DR PhylomeDB; Q9JLV5; -.
DR TreeFam; TF105858; -.
DR Reactome; R-MMU-4641258; Degradation of DVL.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-MMU-9013422; RHOBTB1 GTPase cycle.
DR Reactome; R-MMU-9706019; RHOBTB3 ATPase cycle.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 26554; 30 hits in 74 CRISPR screens.
DR ChiTaRS; Cul3; mouse.
DR EvolutionaryTrace; Q9JLV5; -.
DR PRO; PR:Q9JLV5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9JLV5; protein.
DR Bgee; ENSMUSG00000004364; Expressed in spermatid and 255 other tissues.
DR ExpressionAtlas; Q9JLV5; baseline and differential.
DR Genevisible; Q9JLV5; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005827; C:polar microtubule; ISS:UniProtKB.
DR GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0030332; F:cyclin binding; IPI:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0005112; F:Notch binding; ISO:MGI.
DR GO; GO:0031208; F:POZ domain binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; ISS:MGI.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0048208; P:COPII vesicle coating; ISS:UniProtKB.
DR GO; GO:0040016; P:embryonic cleavage; IMP:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0044346; P:fibroblast apoptotic process; IMP:MGI.
DR GO; GO:0007369; P:gastrulation; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0072576; P:liver morphogenesis; IMP:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:MGI.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0071630; P:nuclear protein quality control by the ubiquitin-proteasome system; ISS:UniProtKB.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:1901992; P:positive regulation of mitotic cell cycle phase transition; ISS:UniProtKB.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; ISS:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IGI:MGI.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
DR GO; GO:0030163; P:protein catabolic process; IMP:MGI.
DR GO; GO:0031648; P:protein destabilization; ISO:MGI.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0017145; P:stem cell division; IMP:UniProtKB.
DR GO; GO:0043149; P:stress fiber assembly; ISS:UniProtKB.
DR GO; GO:0001831; P:trophectodermal cellular morphogenesis; IMP:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI.
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 3D-structure; Acetylation; Cell cycle; Cell division; Cell projection;
KW Cilium; Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW ER-Golgi transport; Flagellum; Golgi apparatus; Isopeptide bond; Mitosis;
KW Nucleus; Phosphoprotein; Reference proteome; Transport; Ubl conjugation;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13618"
FT CHAIN 2..768
FT /note="Cullin-3"
FT /id="PRO_0000119794"
FT REGION 2..41
FT /note="Interaction with KLHL18"
FT /evidence="ECO:0000250|UniProtKB:Q13618"
FT REGION 677..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q13618"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13618"
FT CROSSLNK 712
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000250|UniProtKB:Q13616"
FT TURN 699..701
FT /evidence="ECO:0007829|PDB:1IUY"
FT HELIX 702..714
FT /evidence="ECO:0007829|PDB:1IUY"
FT STRAND 716..718
FT /evidence="ECO:0007829|PDB:1IUY"
FT HELIX 719..729
FT /evidence="ECO:0007829|PDB:1IUY"
FT HELIX 738..750
FT /evidence="ECO:0007829|PDB:1IUY"
FT STRAND 753..756
FT /evidence="ECO:0007829|PDB:1IUY"
FT STRAND 761..766
FT /evidence="ECO:0007829|PDB:1IUY"
SQ SEQUENCE 768 AA; 88948 MW; 841E20407BD076A3 CRC64;
MSNLSKGTGS RKDTKMRIRA FPMTMDEKYV NSIWDLLKNA IQEIQRKNNS GLSFEELYRN
AYTMVLHKHG EKLYTGLREV VTEHLINKVR EDVLNSLNNN FLQTLNQAWN DHQTAMVMIR
DILMYMDRVY VQQNNVENVY NLGLIIFRDQ VVRYGCIRDH LRQTLLDMIA RERKGEVVDR
GAIRNACQML MILGLEGRSV YEEDFEAPFL EMSAEFFQME SQKFLAENSA SVYIKKVEAR
INEEIERVMH CLDKSTEEPI VKVVERELIS KHMKTIVEME NSGLVHMLKN GKTEDLACMY
KLFSRVPNGL KTMCECMSCY LREQGKALVS EEGEGKNPVD YIQGLLDLKS RFDRFLQESF
NNDRLFKQTI AGDFEYFLNL NSRSPEYLSL FIDDKLKKGV KGLTEQEVET ILDKAMVLFR
FMQEKDVFER YYKQHLARRL LTNKSVSDDS EKNMISKLKT ECGCQFTSKL EGMFRDMSIS
NTTMDEFRQH LQATGVSLGG VDLTVRVLTT GYWPTQSATP KCNIPPAPRH AFEIFRRFYL
AKHSGRQLTL QHHMGSADLN ATFYGPVKKE DGSEVGVGGA QVTGSNTRKH ILQVSTFQMT
ILMLFNNREK YTFEEIQQET DIPERELVRA LQSLACGKPT QRVLTKEPKS KEIESGHIFT
VNDQFTSKLH RVKIQTVAAK QGESDPERKE TRQKVDDDRK HEIEAAIVRI MKSRKKMQHN
VLVAEVTQQL KARFLPSPVV IKKRIEGLIE REYLARTPED RKVYTYVA
