ID CUL5_MOUSE Reviewed; 780 AA. AC Q9D5V5; Q8BMQ6; Q8BV53; Q8C098; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 07-APR-2021, entry version 158. DE RecName: Full=Cullin-5; DE Short=CUL-5; GN Name=Cul5; 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 [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RC TISSUE=Brain, Medulla oblongata, Ovary, Testis, and Uterus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Olfactory epithelium; 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 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 [4] RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-384, AND FUNCTION. RX PubMed=23806657; DOI=10.1016/j.jmb.2013.06.015; RA Muniz J.R., Guo K., Kershaw N.J., Ayinampudi V., von Delft F., Babon J.J., RA Bullock A.N.; RT "Molecular architecture of the ankyrin SOCS box family of Cul5-dependent E3 RT ubiquitin ligases."; RL J. Mol. Biol. 425:3166-3177(2013). CC -!- FUNCTION: Core component of multiple SCF-like ECS (Elongin BC-Cullin CC 2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which CC mediate the ubiquitination and subsequent proteasomal degradation of CC target proteins. As a scaffold protein may contribute to catalysis CC through positioning of the substrate and the ubiquitin-conjugating CC enzyme. The functional specificity of the E3 ubiquitin-protein ligase CC complex depends on the variable substrate recognition component. CC ECS(SOCS1) seems to direct ubiquitination of JAK2. Seems to be involved CC in proteosomal degradation of p53/TP53 stimulated by adenovirus E1B-55 CC kDa protein. May form a cell surface vasopressin receptor. CC {ECO:0000269|PubMed:23806657}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Component of multiple ECS (Elongin BC-CUL2/5-SOCS-box protein) CC E3 ubiquitin-protein ligase complexes formed of CUL5, Elongin BC (ELOB CC and ELOC), RBX2 and a variable SOCS box domain-containing protein as CC substrate-specific recognition component. Component of the probable CC ECS(LRRC41) complex with the substrate recognition component LRRC41. CC Component of the probable ECS(SOCS1) complex with the substrate CC recognition component SOCS1. Component of the probable ECS(WSB1) CC complex with the substrate recognition subunit WSB1. Component of the CC probable ECS(SOCS3) complex with the substrate recognition component CC SOCS3. Component of the probable ECS(SPSB1) complex with the substrate CC recognition component SPSB1. Component of the probable ECS(SPSB2) CC complex with the substrate recognition component SPSB2. Component of CC the probable ECS(SPSB4) complex with the substrate recognition CC component SPSB4. Component of the probable ECS(RAB40C) complex with the CC substrate recognition subunit RAB40C. May also form complexes CC containing CUL5, elongin BC complex (ELOB and ELOC), RBX1 and ELOA. May CC also form complexes containing CUL5, Elongin BC (ELOB and ELOC), RBX1 CC and VHL. Interacts with RNF7/RBX2, LRRC41, SOCS3, SPSB1, SPSB2, SPSB4 CC and RAB40C. Interacts with ASB1, ASB2, ASB6, ASB7 and ASB12. Interacts CC (when neddylated) with ARIH2; leading to activate the E3 ligase CC activity of ARIH1. Interacts with NOS2 in the presence of SPSB1 or CC SPSB2 or SPSB4 (By similarity). Interacts with ERCC6; the interaction CC is induced by DNA damaging agents or inhibitors of RNA polymerase II CC elongation (By similarity). Interacts with ELOA (via BC-box) (By CC similarity). Interacts (unneddylated form) with DCUN1D1, DCUN1D2, CC DCUN1D3, DCUN1D4 and DCUN1D5; these interactions promote the cullin CC neddylation (By similarity). {ECO:0000250|UniProtKB:Q93034}. CC -!- PTM: Neddylated; which enhances the ubiquitination activity of SCF and CC prevents binding of the inhibitor CAND1. Deneddylated via its CC interaction with the COP9 signalosome (CSN). CC {ECO:0000250|UniProtKB:Q93034}. 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; AK014894; BAB29609.1; -; mRNA. DR EMBL; AK030306; BAC26889.1; -; mRNA. DR EMBL; AK031955; BAC27621.1; -; mRNA. DR EMBL; AK046030; BAC32575.1; -; mRNA. DR EMBL; AK080305; BAC37872.1; -; mRNA. DR EMBL; BC075710; AAH75710.1; -; mRNA. DR CCDS; CCDS40638.2; -. DR RefSeq; NP_001155090.1; NM_001161618.1. DR RefSeq; NP_082083.2; NM_027807.3. DR PDB; 2WZK; X-ray; 2.05 A; A=1-384. DR PDBsum; 2WZK; -. DR SMR; Q9D5V5; -. DR BioGRID; 217689; 50. DR CORUM; Q9D5V5; -. DR IntAct; Q9D5V5; 2. DR STRING; 10090.ENSMUSP00000034529; -. DR iPTMnet; Q9D5V5; -. DR PhosphoSitePlus; Q9D5V5; -. DR EPD; Q9D5V5; -. DR MaxQB; Q9D5V5; -. DR PaxDb; Q9D5V5; -. DR PRIDE; Q9D5V5; -. DR ProteomicsDB; 284062; -. DR GeneID; 75717; -. DR KEGG; mmu:75717; -. DR UCSC; uc009pmj.1; mouse. DR CTD; 8065; -. DR MGI; MGI:1922967; Cul5. DR eggNOG; KOG2285; Eukaryota. DR InParanoid; Q9D5V5; -. DR OrthoDB; 1040292at2759; -. DR PhylomeDB; Q9D5V5; -. DR BRENDA; 6.3.2.19; 3474. DR Reactome; R-MMU-8863795; Downregulation of ERBB2 signaling. DR Reactome; R-MMU-8951664; Neddylation. DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 75717; 7 hits in 54 CRISPR screens. DR ChiTaRS; Cul5; mouse. DR EvolutionaryTrace; Q9D5V5; -. DR PRO; PR:Q9D5V5; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q9D5V5; protein. DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; ISO:MGI. DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central. DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central. DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IMP:MGI. DR GO; GO:0016567; P:protein ubiquitination; IGI:MGI. DR GO; GO:0021942; P:radial glia guided migration of Purkinje cell; IMP:MGI. DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:MGI. DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR Gene3D; 1.10.10.10; -; 1. 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 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; Isopeptide bond; Phosphoprotein; Reference proteome; KW Ubl conjugation; Ubl conjugation pathway. FT CHAIN 1..780 FT /note="Cullin-5" FT /id="PRO_0000119798" FT MOD_RES 34 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q93034" FT MOD_RES 210 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q93034" FT CROSSLNK 724 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in NEDD8)" FT /evidence="ECO:0000250|UniProtKB:Q13616" FT CONFLICT 573 FT /note="W -> C (in Ref. 1; BAC27621)" FT /evidence="ECO:0000305" FT HELIX 15..31 FT /evidence="ECO:0007744|PDB:2WZK" FT HELIX 37..53 FT /evidence="ECO:0007744|PDB:2WZK" FT HELIX 57..81 FT /evidence="ECO:0007744|PDB:2WZK" FT HELIX 86..103 FT /evidence="ECO:0007744|PDB:2WZK" FT TURN 104..108 FT /evidence="ECO:0007744|PDB:2WZK" FT HELIX 109..111 FT /evidence="ECO:0007744|PDB:2WZK" FT HELIX 112..115 FT /evidence="ECO:0007744|PDB:2WZK" FT HELIX 134..146 FT /evidence="ECO:0007744|PDB:2WZK" FT HELIX 148..167 FT /evidence="ECO:0007744|PDB:2WZK" FT HELIX 175..186 FT /evidence="ECO:0007744|PDB:2WZK" FT HELIX 196..200 FT /evidence="ECO:0007744|PDB:2WZK" FT HELIX 202..248 FT /evidence="ECO:0007744|PDB:2WZK" FT HELIX 257..269 FT /evidence="ECO:0007744|PDB:2WZK" FT HELIX 271..273 FT /evidence="ECO:0007744|PDB:2WZK" FT HELIX 274..278 FT /evidence="ECO:0007744|PDB:2WZK" FT HELIX 281..286 FT /evidence="ECO:0007744|PDB:2WZK" FT HELIX 290..300 FT /evidence="ECO:0007744|PDB:2WZK" FT HELIX 308..329 FT /evidence="ECO:0007744|PDB:2WZK" FT HELIX 330..332 FT /evidence="ECO:0007744|PDB:2WZK" FT TURN 333..335 FT /evidence="ECO:0007744|PDB:2WZK" FT HELIX 337..359 FT /evidence="ECO:0007744|PDB:2WZK" FT HELIX 363..382 FT /evidence="ECO:0007744|PDB:2WZK" SQ SEQUENCE 780 AA; 90974 MW; C6EE7A1AF1038C0D CRC64; MATSNLLKNK GSLQFEDKWD FMHPIVLKLL RQESVTKQQW FDLFSDVHAV CLWDDKGSSK IHQALKEDIL EFIKQAQARV LSHQDDTALL KAYIVEWRKF FTQCDILPKP FCQLEVTLLG KQSSNKKSNM EDSIVRKLML DTWNESIFSN IKNRLQDSAM KLVHAERLGE AFDSQLVIGV RESYVNLCSN PEDKLQIYRD NFEKAYLDST ERFYRTQAPS YLQQNGVQNY MKYADAKLKE EEKRALRYLE TRRECNSVEA LMECCVNALV TSFKETILAE CQGMIKRNET EKLHLMFSLM DKVPNGIEPM LKDLEEHIIS AGLADMVAAA ETITTDSEKY VEQLLTLFNR FSKLVKEAFQ DDPRFLTARD KAYKAVVNDA TIFKLELPLK QKGVGLKTQP ESKCPELLAN YCDMLLRKTP LSKKLTSEEI EAKLKEVLLV LKYVQNKDVF MRYHKAHLTR RLILDISADS EIEENMVEWL REVGMPADYV NKLARMFQDI KVSEDLNQAF KEMHKNNKLA LPADSVNIKI LNAGAWSRSS EKVFVSLPTE LEDLIPEVEE FYKKNHSGRK LHWHHLMSNG IITFKNEVGQ YDLEVTTFQL AVLFAWNQRP REKISFENLK LATELPDAEL RRTLWSLVAF PKLKRQVLLY DPQVNSPKDF TEGTLFSVNQ DFSLIKNAKV QKRGKINLIG RLQLTTERMR EEENEGIVQL RILRTQEAII QIMKMRKKIS NAQLQTELVE ILKNMFLPQK KMIKEQMEWL IEHRYIRRDE ADINTFIYMA //