ID E9Q4T8_MOUSE Unreviewed; 702 AA. AC E9Q4T8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAR-2024, entry version 83. DE SubName: Full=Cullin 3 {ECO:0000313|Ensembl:ENSMUSP00000131891.2}; GN Name=Cul3 {ECO:0000313|Ensembl:ENSMUSP00000131891.2, GN ECO:0000313|MGI:MGI:1347360}; 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 {ECO:0000313|Ensembl:ENSMUSP00000131891.2, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000131891.2, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000131891.2, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [3] {ECO:0000313|Ensembl:ENSMUSP00000131891.2} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000131891.2}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000256|ARBA:ARBA00004906}. CC -!- SIMILARITY: Belongs to the cullin family. CC {ECO:0000256|ARBA:ARBA00006019, ECO:0000256|PROSITE-ProRule:PRU00330, CC ECO:0000256|RuleBase:RU003829}. 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 AlphaFoldDB; E9Q4T8; -. DR SMR; E9Q4T8; -. DR jPOST; E9Q4T8; -. DR MaxQB; E9Q4T8; -. DR PeptideAtlas; E9Q4T8; -. DR ProteomicsDB; 361327; -. DR Antibodypedia; 3632; 476 antibodies from 40 providers. DR Ensembl; ENSMUST00000164108.8; ENSMUSP00000131891.2; ENSMUSG00000004364.15. DR AGR; MGI:1347360; -. DR MGI; MGI:1347360; Cul3. DR VEuPathDB; HostDB:ENSMUSG00000004364; -. DR GeneTree; ENSGT00940000155066; -. DR UniPathway; UPA00143; -. DR ChiTaRS; Cul3; mouse. DR Proteomes; UP000000589; Chromosome 1. DR Bgee; ENSMUSG00000004364; Expressed in spermatid and 259 other cell types or tissues. DR ExpressionAtlas; E9Q4T8; baseline and differential. DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IEA:InterPro. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro. DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. DR Gene3D; 1.20.1310.10; Cullin Repeats; 4. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; CULLIN; 1. DR PANTHER; PTHR11932:SF168; CULLIN-3; 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; SSF75632; Cullin homology domain; 1. DR SUPFAM; SSF74788; Cullin repeat-like; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS01256; CULLIN_1; 1. DR PROSITE; PS50069; CULLIN_2; 1. PE 1: Evidence at protein level; KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499}; KW Proteomics identification {ECO:0007829|EPD:E9Q4T8, KW ECO:0007829|MaxQB:E9Q4T8}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}; KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}. FT DOMAIN 317..569 FT /note="Cullin family profile" FT /evidence="ECO:0000259|PROSITE:PS50069" FT REGION 611..632 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 616..632 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 702 AA; 81111 MW; 09608E18C7E70FB0 CRC64; MSNLSKGTGS RKDTKMRIRA FPVREDVLNS LNNNFLQTLN QAWNDHQTAM VMIRDILMYM DRVYVQQNNV ENVYNLGLII FRDQVVRYGC IRDHLRQTLL DMIARERKGE VVDRGAIRNA CQMLMILGLE GRSVYEEDFE APFLEMSAEF FQMESQKFLA ENSASVYIKK VEARINEEIE RVMHCLDKST EEPIVKVVER ELISKHMKTI VEMENSGLVH MLKNGKTEDL ACMYKLFSRV PNGLKTMCEC MSCYLREQGK ALVSEEGEGK NPVDYIQGLL DLKSRFDRFL QESFNNDRLF KQTIAGDFEY FLNLNSRSPE YLSLFIDDKL KKGVKGLTEQ EVETILDKAM VLFRFMQEKD VFERYYKQHL ARRLLTNKSV SDDSEKNMIS KLKTECGCQF TSKLEGMFRD MSISNTTMDE FRQHLQATGV SLGGVDLTVR VLTTGYWPTQ SATPKCNIPP APRHAFEIFR RFYLAKHSGR QLTLQHHMGS ADLNATFYGP VKKEDGSEVG VGGAQVTGSN TRKHILQVST FQMTILMLFN NREKYTFEEI QQETDIPERE LVRALQSLAC GKPTQRVLTK EPKSKEIESG HIFTVNDQFT SKLHRVKIQT VAAKQGESDP ERKETRQKVD DDRKHEIEAA IVRIMKSRKK MQHNVLVAEV TQQLKARFLP SPVVIKKRIE GLIEREYLAR TPEDRKVYTY VA //