CUL3_RAT
ID CUL3_RAT Reviewed; 768 AA.
AC B5DF89;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Cullin-3;
GN Name=Cul3;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-768.
RC TISSUE=Lung;
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 INTERACTION WITH KLHL17.
RX PubMed=17062563; DOI=10.1074/jbc.m608194200;
RA Salinas G.D., Blair L.A., Needleman L.A., Gonzales J.D., Chen Y., Li M.,
RA Singer J.D., Marshall J.;
RT "Actinfilin is a Cul3 substrate adaptor, linking GluR6 kainate receptor
RT subunits to the ubiquitin-proteasome pathway.";
RL J. Biol. Chem. 281:40164-40173(2006).
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. BCR complexes and ARIH1 collaborate in tandem to mediate
CC ubiquitination of target proteins (By similarity). As a scaffold
CC protein may contribute to catalysis through positioning of the
CC substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-
CC protein ligase activity of the complex is dependent on the neddylation
CC of the cullin subunit and is inhibited by the association of the
CC deneddylated cullin subunit with TIP120A/CAND1 (By similarity). The
CC functional specificity of the BCR complex depends on the BTB domain-
CC containing protein as the substrate recognition component. BCR(KLHL42)
CC is involved in ubiquitination of KATNA1. BCR(SPOP) is involved in
CC ubiquitination of BMI1/PCGF4, BRMS1, MACROH2A1 and DAXX, GLI2 and GLI3.
CC Can also form a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-
CC protein ligase complex containing homodimeric SPOPL or the heterodimer
CC formed by SPOP and SPOPL; these complexes have lower ubiquitin ligase
CC activity. BCR(KLHL9-KLHL13) controls the dynamic behavior of AURKB on
CC mitotic chromosomes and thereby coordinates faithful mitotic
CC progression and completion of cytokinesis. BCR(KLHL12) is involved in
CC ER-Golgi transport by regulating the size of COPII coats, thereby
CC playing a key role in collagen export, which is required for embryonic
CC stem (ES) cells division: BCR(KLHL12) acts by mediating
CC monoubiquitination of SEC31 (SEC31A or SEC31B). BCR(KLHL3) acts as a
CC regulator of ion transport in the distal nephron; by mediating
CC ubiquitination of WNK4. The BCR(KLHL20) E3 ubiquitin ligase complex is
CC involved in interferon response and anterograde Golgi to endosome
CC transport: it mediates both ubiquitination leading to degradation and
CC 'Lys-33'-linked ubiquitination. 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. The BCR(KLHL22) ubiquitin ligase complex
CC mediates monoubiquitination of PLK1, leading to PLK1 dissociation from
CC phosphoreceptor proteins and subsequent removal from kinetochores,
CC allowing silencing of the spindle assembly checkpoint (SAC) and
CC chromosome segregation. The BCR(KLHL22) ubiquitin ligase complex is
CC 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. The BCR(KLHL25) ubiquitin ligase complex is
CC involved in translational homeostasis by mediating ubiquitination and
CC subsequent degradation of hypophosphorylated EIF4EBP1 (4E-BP1). The
CC BCR(KBTBD8) complex acts by mediating monoubiquitination of NOLC1 and
CC TCOF1, leading to remodel the translational program of differentiating
CC cells in favor of neural crest specification. Involved in
CC ubiquitination of cyclin E and of cyclin D1 (in vitro) thus involved in
CC regulation of G1/S transition. Involved in the ubiquitination of KEAP1,
CC ENC1 and KLHL41. In concert with ATF2 and RBX1, promotes degradation of
CC KAT5 thereby attenuating its ability to acetylate and activate ATM. The
CC BCR(KCTD17) E3 ubiquitin ligase complex mediates ubiquitination and
CC degradation of TCHP, a down-regulator of cilium assembly, thereby
CC inducing ciliogenesis (By similarity). The BCR(KLHL24) E3 ubiquitin
CC ligase complex mediates ubiquitination of KRT14, controls KRT14 levels
CC during keratinocytes differentiation, and is essential for skin
CC integrity (By similarity). The BCR(KLHL18) E3 ubiquitin ligase complex
CC mediates the ubiquitination of AURKA leading to its activation at the
CC centrosome which is required for initiating mitotic entry (By
CC similarity). The BCR(KEAP1) E3 ubiquitin ligase complex acts as a key
CC sensor of oxidative and electrophilic stress by mediating
CC ubiquitination and degradation of NFE2L2/NRF2, a transcription factor
CC regulating expression of many cytoprotective genes (By similarity). As
CC part of the CUL3(KBTBD6/7) E3 ubiquitin ligase complex functions
CC mediates 'Lys-48' ubiquitination and proteasomal degradation of TIAM1.
CC By controlling the ubiquitination of that RAC1 guanine exchange factors
CC (GEF), regulates RAC1 signal transduction and downstream biological
CC processes including the organization of the cytoskeleton, cell
CC migration and cell proliferation (By similarity).
CC {ECO:0000250|UniProtKB:Q13618, ECO:0000250|UniProtKB:Q9JLV5}.
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, CYCE 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 (By similarity). vInteracts with KLHL10 (By
CC similarity). Interacts with KAT5 and ATF2 (By similarity). Interacts
CC with KCTD17 in the BCR(KCTD17) E3 ubiquitin ligase complex, at least
CC composed of CUL3, KCTD17 and RBX1 (By similarity). Interacts (when
CC neddylated) with ARIH1; leading to activate the E3 ligase activity of
CC ARIH1 (By similarity). Interacts with COPS9 (By similarity). Interacts
CC with PPP2R5B; this interaction is indirect and mediated through KLHL15-
CC binding and leads to PPP2R5B proteasomal degradation (By similarity).
CC Interacts with RBBP8/CtIP; this interaction is indirect and mediated
CC through KLHL15-binding and leads to RBBP8 proteasomal degradation (By
CC similarity). Interacts with KLHL24 in the BCR(KLHL24) E3 ubiquitin
CC ligase complex, composed of CUL3, RBX1 and KLHL24 (By similarity).
CC Interacts with RHOBTB2 (By similarity). Interacts (via BTB domain) with
CC KLHL17; the interaction regulates surface GRIK2 expression
CC (PubMed:17062563). 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:17062563}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13618}. Golgi
CC apparatus {ECO:0000250|UniProtKB:Q13618}. 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 -!- 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 -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI68969.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; BC168969; AAI68969.1; ALT_INIT; mRNA.
DR RefSeq; XP_008765448.1; XM_008767226.2.
DR RefSeq; XP_017451863.1; XM_017596374.1.
DR RefSeq; XP_017451864.1; XM_017596375.1.
DR AlphaFoldDB; B5DF89; -.
DR SMR; B5DF89; -.
DR BioGRID; 257002; 3.
DR CORUM; B5DF89; -.
DR IntAct; B5DF89; 1.
DR STRING; 10116.ENSRNOP00000021528; -.
DR iPTMnet; B5DF89; -.
DR PhosphoSitePlus; B5DF89; -.
DR jPOST; B5DF89; -.
DR PaxDb; B5DF89; -.
DR PeptideAtlas; B5DF89; -.
DR PRIDE; B5DF89; -.
DR GeneID; 301555; -.
DR UCSC; RGD:1308190; rat.
DR CTD; 8452; -.
DR RGD; 1308190; Cul3.
DR eggNOG; KOG2166; Eukaryota.
DR InParanoid; B5DF89; -.
DR OrthoDB; 1040292at2759; -.
DR PhylomeDB; B5DF89; -.
DR TreeFam; TF105858; -.
DR Reactome; R-RNO-4641258; Degradation of DVL.
DR Reactome; R-RNO-5632684; Hedgehog 'on' state.
DR Reactome; R-RNO-5658442; Regulation of RAS by GAPs.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-RNO-9013422; RHOBTB1 GTPase cycle.
DR Reactome; R-RNO-9706019; RHOBTB3 ATPase cycle.
DR Reactome; R-RNO-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:B5DF89; -.
DR Proteomes; UP000002494; Unplaced.
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; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005827; C:polar microtubule; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005112; F:Notch binding; ISO:RGD.
DR GO; GO:0031208; F:POZ domain binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; ISO:RGD.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0000902; P:cell morphogenesis; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0044346; P:fibroblast apoptotic process; ISO:RGD.
DR GO; GO:0007369; P:gastrulation; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0072576; P:liver morphogenesis; ISO:RGD.
DR GO; GO:0000278; P:mitotic cell cycle; ISO:RGD.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISO:RGD.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:RGD.
DR GO; GO:0031648; P:protein destabilization; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0017145; P:stem cell division; ISS:UniProtKB.
DR GO; GO:0043149; P:stress fiber assembly; ISO:RGD.
DR GO; GO:0001831; P:trophectodermal cellular morphogenesis; ISO:RGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; ISO:RGD.
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 Acetylation; Cell cycle; Cell division; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; ER-Golgi transport;
KW Flagellum; Golgi apparatus; Isopeptide bond; Mitosis; Nucleus;
KW 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_0000395993"
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"
SQ SEQUENCE 768 AA; 88932 MW; 7CEF981391733E52 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 KTMCECMSSY 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
