CUL1_MOUSE
ID CUL1_MOUSE Reviewed; 776 AA.
AC Q9WTX6; Q9WUI7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Cullin-1;
DE Short=CUL-1;
GN Name=Cul1;
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], FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH
RP PHOSPHORYLATED NFKBIA; SKP1 AND BTRC.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=10097128; DOI=10.1073/pnas.96.7.3859;
RA Hatakeyama S., Kitagawa M., Nakayama K., Shirane M., Matsumoto M.,
RA Hattori K., Higashi H., Nakano H., Okumura K., Onoe K., Good R.A.,
RA Nakayama K.;
RT "Ubiquitin-dependent degradation of IkappaBalpha is mediated by a ubiquitin
RT ligase Skp1/Cul 1/F-box protein FWD1.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3859-3863(1999).
RN [2]
RP ERRATUM OF PUBMED:10097128.
RA Hatakeyama S., Kitagawa M., Nakayama K., Shirane M., Matsumoto M.,
RA Hattori K., Higashi H., Nakano H., Okumura K., Onoe K., Good R.A.,
RA Nakayama K.;
RL Proc. Natl. Acad. Sci. U.S.A. 96:6571-6571(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Filippov V., Filippova M., Gill S.S.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NIH Swiss; TISSUE=Embryo;
RX PubMed=10508527; DOI=10.1038/13886;
RA Dealy M.J., Nguyen K.V.T., Lo J., Gstaiger M., Krek W., Elson D.,
RA Arbeit J., Kipreos E.T., Johnson R.S.;
RT "Loss of Cul1 results in early embryonic lethality and dysregulation of
RT cyclin E.";
RL Nat. Genet. 23:245-248(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [6]
RP TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=9663463;
RA Michel J.J., Xiong Y.;
RT "Human CUL-1, but not other cullin family members, selectively interacts
RT with SKP1 to form a complex with SKP2 and cyclin A.";
RL Cell Growth Differ. 9:435-449(1998).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH BTRC AND SKP1.
RX PubMed=11735228; DOI=10.1006/geno.2001.6658;
RA Maruyama S., Hatakeyama S., Nakayama K., Ishida N., Kawakami K.,
RA Nakayama K.;
RT "Characterization of a mouse gene (Fbxw6) that encodes a homologue of
RT Caenorhabditis elegans SEL-10.";
RL Genomics 78:214-222(2001).
RN [8]
RP INTERACTION WITH COPS2.
RX PubMed=11967155; DOI=10.1016/s0960-9822(02)00791-1;
RA Yang X., Menon S., Lykke-Andersen K., Tsuge T., Xiao D., Wang X.,
RA Rodriguez-Suarez R.J., Zhang H., Wei N.;
RT "The COP9 signalosome inhibits p27(kip1) degradation and impedes G1-S phase
RT progression via deneddylation of SCF Cul1.";
RL Curr. Biol. 12:667-672(2002).
RN [9]
RP FUNCTION, SUBUNIT, AND PATHWAY.
RX PubMed=12140560; DOI=10.1038/nature00890;
RA Yoshida Y., Chiba T., Tokunaga F., Kawasaki H., Iwai K., Suzuki T., Ito Y.,
RA Matsuoka K., Yoshida M., Tanaka K., Tai T.;
RT "E3 ubiquitin ligase that recognizes sugar chains.";
RL Nature 418:438-442(2002).
RN [10]
RP INTERACTION WITH CUL7 AND FBXW8.
RX PubMed=16880526; DOI=10.1128/mcb.00595-06;
RA Tsunematsu R., Nishiyama M., Kotoshiba S., Saiga T., Kamura T.,
RA Nakayama K.I.;
RT "Fbxw8 is essential for Cul1-Cul7 complex formation and for placental
RT development.";
RL Mol. Cell. Biol. 26:6157-6169(2006).
RN [11]
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 [12]
RP INTERACTION WITH MURINE CYTOMEGALOVIRUS M48 (MICROBIAL INFECTION),
RP DENEDDYLATION BY MURINE CYTOMEGALOVIRUS M48, AND NEDDYLATION.
RX PubMed=20190741; DOI=10.1038/ncb2035;
RA Gastaldello S., Hildebrand S., Faridani O., Callegari S., Palmkvist M.,
RA Di Guglielmo C., Masucci M.G.;
RT "A deneddylase encoded by Epstein-Barr virus promotes viral DNA replication
RT by regulating the activity of cullin-RING ligases.";
RL Nat. Cell Biol. 12:351-361(2010).
RN [13]
RP IDENTIFICATION IN THE SCF(FBXL3) COMPLEX, AND FUNCTION.
RX PubMed=23452855; DOI=10.1016/j.cell.2013.01.055;
RA Yoo S.H., Mohawk J.A., Siepka S.M., Shan Y., Huh S.K., Hong H.K.,
RA Kornblum I., Kumar V., Koike N., Xu M., Nussbaum J., Liu X., Chen Z.,
RA Chen Z.J., Green C.B., Takahashi J.S.;
RT "Competing E3 ubiquitin ligases govern circadian periodicity by degradation
RT of CRY in nucleus and cytoplasm.";
RL Cell 152:1091-1105(2013).
RN [14]
RP IDENTIFICATION IN THE SCF(FBXL21) COMPLEX, AND FUNCTION.
RX PubMed=23452856; DOI=10.1016/j.cell.2013.01.054;
RA Hirano A., Yumimoto K., Tsunematsu R., Matsumoto M., Oyama M.,
RA Kozuka-Hata H., Nakagawa T., Lanjakornsiripan D., Nakayama K.I., Fukada Y.;
RT "FBXL21 regulates oscillation of the circadian clock through ubiquitination
RT and stabilization of cryptochromes.";
RL Cell 152:1106-1118(2013).
RN [15]
RP INTERACTION WITH KAT7.
RX PubMed=23319590; DOI=10.1074/jbc.m112.426882;
RA Zou C., Chen Y., Smith R.M., Snavely C., Li J., Coon T.A., Chen B.B.,
RA Zhao Y., Mallampalli R.K.;
RT "SCF(Fbxw15) mediates histone acetyltransferase binding to origin
RT recognition complex (HBO1) ubiquitin-proteasomal degradation to regulate
RT cell proliferation.";
RL J. Biol. Chem. 288:6306-6316(2013).
RN [16]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-63, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Core component of multiple cullin-RING-based SCF (SKP1-CUL1-
CC F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the
CC ubiquitination of proteins involved in cell cycle progression, signal
CC transduction and transcription. SCF complexes and ARIH1 collaborate in
CC tandem to mediate ubiquitination of target proteins. In the SCF
CC complex, serves as a rigid scaffold that organizes the SKP1-F-box
CC protein and RBX1 subunits. May contribute to catalysis through
CC positioning of the substrate and the ubiquitin-conjugating enzyme. The
CC E3 ubiquitin-protein ligase activity of the complex is dependent on the
CC neddylation of the cullin subunit and exchange of the substrate
CC recognition component is mediated by TIP120A/CAND1. The functional
CC specificity of the SCF complex depends on the F-box protein as
CC substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct
CC ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11)
CC directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs
CC ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and
CC probably NFKB2. SCF(BTRC) and/or SCF(FBXW11) direct ubiquitination of
CC CEP68. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip
CC and is involved in regulation of G1/S transition. SCF(SKP2) directs
CC ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and
CC probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E,
CC NOTCH1 released notch intracellular domain (NICD), and probably PSEN1.
CC SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs
CC ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and
CC DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO1) directs
CC ubiquitination of BCL6 and DTL but does not seem to direct
CC ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA
CC at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-
CC RELA dimer to translocate into the nucleus and to activate
CC transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3)
CC and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9)
CC directs ubiquitination of TTI1 and TELO2. SCF(FBXO10) directs
CC ubiquitination of BCL2. {ECO:0000250|UniProtKB:Q13616,
CC ECO:0000269|PubMed:12140560, ECO:0000269|PubMed:23452855}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:12140560}.
CC -!- SUBUNIT: Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin-
CC protein ligase complexes formed of CUL1, SKP1, RBX1 and a variable F-
CC box domain-containing protein as substrate-specific subunit
CC (PubMed:10097128, PubMed:12140560, PubMed:16880526, PubMed:23452855,
CC PubMed:23452856). Component of the SCF(FBXW11) complex containing
CC FBXW11. Component of the SCF(SKP2) complex containing SKP2, in which it
CC interacts directly with SKP1, SKP2 and RBX1. Component of the
CC SCF(FBXW2) complex containing FBXW2. Component of the SCF(FBXO32)
CC complex containing FBXO32. Component of the probable SCF(FBXO7) complex
CC containing FBXO7. Component of the SCF(FBXO10) complex containing
CC FBXO10. Component of the SCF(FBXO11) complex containing FBXO11.
CC Component of the SCF(FBXO25) complex containing FBXO25. Component of
CC the SCF(FBXO33) complex containing FBXO33. Component of the probable
CC SCF(FBXO4) complex containing FBXO4. Component of the SCF(FBXO44)
CC complex, composed of SKP1, CUL1 and FBXO44 (By similarity). Component
CC of the SCF(BTRC) complex, composed of SKP1, CUL1 and BTRC
CC (PubMed:10097128, PubMed:11735228). This complex binds phosphorylated
CC NFKBIA (PubMed:10097128). Part of a SCF complex consisting of CUL1,
CC RBX1, SKP1 and FBXO2. Component of a SCF(SKP2)-like complex containing
CC CUL1, SKP1, TRIM21 and SKP2. Component of the SCF(FBXO17) complex,
CC composed of SKP1, CUL1 and FBXO17. Component of the SCF(FBXO27)
CC complex, composed of SKP1, CUL1 and FBXO27. Component of the SCF(CCNF)
CC complex consisting of CUL1, RBX1, SKP1 and CCNF (By similarity).
CC Interacts with CCNF (By similarity). Component of the SCF(FBXL3)
CC complex composed of CUL1, SKP1, RBX1 and FBXL3. Component of the
CC SCF(FBXL21) complex composed of CUL1, SKP1, RBX1 and FBXL21. Component
CC of the SCF(FBXO9) composed of CUL1, SKP1, RBX1 and FBXO9. Component of
CC the SCF(FBXW7) composed of CUL1, SKP1, RBX1 and FBXW7. Interacts with
CC CHEK2; mediates CHEK2 ubiquitination and regulates its function. Part
CC of a complex with TIP120A/CAND1 and RBX1. The unneddylated form
CC interacts with TIP120A/CAND1 and the interaction mediates the exchange
CC of the F-box substrate-specific subunit. Can self-associate (By
CC similarity). Interacts with FBXW8 (PubMed:16880526). Interacts with
CC RNF7 (By similarity). Interacts with CUL7; the interaction seems to be
CC mediated by FBXW8 (PubMed:16880526). Interacts with TRIM21 (By
CC similarity). Interacts with COPS2 (PubMed:11967155). Interacts with
CC DCUN1D1 and UBE2M. Interacts with DCUN1D3. Interacts with DCUN1D4 (By
CC similarity). Identified in a complex with RBX1 and GLMN (By
CC similarity). Interacts with CEP68 as part of the SCF(FBXW11) complex;
CC the interaction is probably mediated by FBXW11 and the complex also
CC contains CDK5RAP2 and PCNT. Interacts (when neddylated) with ARIH1;
CC leading to activate the E3 ligase activity of ARIH1. Interacts with
CC COPS9. Interacts with UBXN1 (By similarity). Interacts with KAT7,
CC probably as part of an SCF complex; the interaction mediates KAT7
CC ubiquitination (PubMed:23319590). Interacts with NOTCH2 (By
CC similarity). Part of a complex that contains DCUN1D5, CUL1 and RBX1;
CC this interaction is bridged by CUL1 (By similarity). Interacts
CC (unneddylated form) with DCUN1D1, DCUN1D2, DCUN1D3, DCUN1D4 and
CC DCUN1D5; these interactions promote the cullin neddylation (By
CC similarity). {ECO:0000250|UniProtKB:Q13616,
CC ECO:0000269|PubMed:10097128, ECO:0000269|PubMed:11735228,
CC ECO:0000269|PubMed:11967155, ECO:0000269|PubMed:12140560,
CC ECO:0000269|PubMed:16880526, ECO:0000269|PubMed:23319590,
CC ECO:0000269|PubMed:23452855, ECO:0000269|PubMed:23452856}.
CC -!- SUBUNIT: (Microbial infection) Interacts with murine cytomegalovirus
CC M48. {ECO:0000269|PubMed:20190741}.
CC -!- INTERACTION:
CC Q9WTX6; O94888: UBXN7; Xeno; NbExp=3; IntAct=EBI-1551052, EBI-1993627;
CC Q9WTX6; P55072: VCP; Xeno; NbExp=2; IntAct=EBI-1551052, EBI-355164;
CC -!- TISSUE SPECIFICITY: Embryo fibroblasts and embryo preadipocytes.
CC {ECO:0000269|PubMed:9663463}.
CC -!- PTM: Neddylated; which enhances the ubiquitination activity of SCF.
CC Deneddylated via its interaction with the COP9 signalosome (CSN)
CC complex. {ECO:0000269|PubMed:20190741}.
CC -!- PTM: (Microbial infection) Deneddylated by murine cytomegalovirus M48
CC leading to a S-phase-like environment that is required for efficient
CC replication of the viral genome. {ECO:0000269|PubMed:20190741}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
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DR EMBL; AF083216; AAD16038.1; -; mRNA.
DR EMBL; AF176910; AAD52657.1; -; mRNA.
DR EMBL; AF136441; AAD34471.1; -; mRNA.
DR EMBL; BC029260; AAH29260.1; -; mRNA.
DR CCDS; CCDS20095.1; -.
DR RefSeq; NP_036172.1; NM_012042.3.
DR RefSeq; XP_006506251.1; XM_006506188.3.
DR RefSeq; XP_006506252.1; XM_006506189.3.
DR RefSeq; XP_006506253.1; XM_006506190.3.
DR AlphaFoldDB; Q9WTX6; -.
DR SMR; Q9WTX6; -.
DR BioGRID; 205088; 100.
DR CORUM; Q9WTX6; -.
DR DIP; DIP-39799N; -.
DR IntAct; Q9WTX6; 41.
DR MINT; Q9WTX6; -.
DR STRING; 10090.ENSMUSP00000031697; -.
DR iPTMnet; Q9WTX6; -.
DR PhosphoSitePlus; Q9WTX6; -.
DR EPD; Q9WTX6; -.
DR MaxQB; Q9WTX6; -.
DR PaxDb; Q9WTX6; -.
DR PeptideAtlas; Q9WTX6; -.
DR PRIDE; Q9WTX6; -.
DR ProteomicsDB; 279208; -.
DR Antibodypedia; 3630; 550 antibodies from 42 providers.
DR DNASU; 26965; -.
DR Ensembl; ENSMUST00000031697; ENSMUSP00000031697; ENSMUSG00000029686.
DR GeneID; 26965; -.
DR KEGG; mmu:26965; -.
DR UCSC; uc009bsz.1; mouse.
DR CTD; 8454; -.
DR MGI; MGI:1349658; Cul1.
DR VEuPathDB; HostDB:ENSMUSG00000029686; -.
DR eggNOG; KOG2166; Eukaryota.
DR GeneTree; ENSGT00940000154774; -.
DR HOGENOM; CLU_004747_6_1_1; -.
DR InParanoid; Q9WTX6; -.
DR OMA; GVYTAVH; -.
DR OrthoDB; 1040292at2759; -.
DR PhylomeDB; Q9WTX6; -.
DR TreeFam; TF101151; -.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-1170546; Prolactin receptor signaling.
DR Reactome; R-MMU-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-MMU-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-69231; Cyclin D associated events in G1.
DR Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-917937; Iron uptake and transport.
DR Reactome; R-MMU-9708530; Regulation of BACH1 activity.
DR Reactome; R-MMU-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 26965; 17 hits in 74 CRISPR screens.
DR ChiTaRS; Cul1; mouse.
DR PRO; PR:Q9WTX6; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9WTX6; protein.
DR Bgee; ENSMUSG00000029686; Expressed in secondary oocyte and 274 other tissues.
DR ExpressionAtlas; Q9WTX6; baseline and differential.
DR Genevisible; Q9WTX6; MM.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:1990452; C:Parkin-FBXW7-Cul1 ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IC:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:MGI.
DR GO; GO:0006513; P:protein monoubiquitination; IGI:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IC:MGI.
DR Gene3D; 1.10.10.10; -; 2.
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 Host-virus interaction; Isopeptide bond; Methylation; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..776
FT /note="Cullin-1"
FT /id="PRO_0000119788"
FT MOD_RES 63
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 720
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000250|UniProtKB:Q13616"
FT CONFLICT 74
FT /note="K -> R (in Ref. 3; AAD34471)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="T -> S (in Ref. 3; AAD34471)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="Q -> H (in Ref. 3; AAD34471)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="G -> R (in Ref. 3; AAD34471)"
FT /evidence="ECO:0000305"
FT CONFLICT 640..663
FT /note="LQILLKSKLLVLEDENANVDEVEL -> YRFTEVEIAGLRDEMPMLMRWM
FT (in Ref. 3; AAD34471)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 776 AA; 89692 MW; 3E1F8B63C6E498F4 CRC64;
MSSNRSQNPH GLKQIGLDQI WDDLRAGIQQ VYTRQSMAKS RYMELYTHVY NYCTSVHQSN
QARGAGVPPS KSKKGQTPGG AQFVGLELYK RLKEFLKNYL TNLLKDGEDL MDESVLKFYT
QQWEDYRFSS KVLNGICAYL NRHWVRRECD EGRKGIYEIY SLALVTWRDC LFRPLNKQVT
NAVLKLIEKE RNGETINTRL ISGVVQSYVE LGLNEDDAFA KGPTLTVYKE SFESQFLADT
ERFYTRESTE FLQQNPVTEY MKKAEARLLE EQRRVQVYLH ESTQDELARK CEQVLIEKHL
EIFHTEFQNL LDADKNEDLG RMYNLVSRIQ DGLGELKKLL ETHIHNQGLA AIEKCGEAAL
NDPKMYVQTV LDVHKKYNAL VMSAFNNDAG FVAALDKACG RFINNNAVTK MAQSSSKSPE
LLARYCDSLL KKSSKNPEEA ELEDTLNQVM VVFKYIEDKD VFQKFYAKML AKRLVHQNSA
SDDAEASMIS KLKQACGFEY TSKLQRMFQD IGVSKDLNEQ FKKHLTNSEP LDLDFSIQVL
SSGSWPFQQS CTFALPSELE RSYQRFTAFY ASRHSGRKLT WLYQLSKGEL VTNCFKNRYT
LQASTFQMAI LLQYNTEDAY TVQQLTDSTQ IKMDILAQVL QILLKSKLLV LEDENANVDE
VELKPDTLIK LYLGYKNKKL RVNINVPMKT EQKQEQETTH KNIEEDRKLL IQAAIVRIMK
MRKVLKHQQL LGEVLTQLSS RFKPRVPVIK KCIDILIEKE YLERVDGEKD TYSYLA
