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 05-OCT-2016, entry version 130. DE RecName: Full=Cullin-5; DE Short=CUL-5; GN Name=Cul5; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: 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, RC Pancreas, 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 RT 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., RA Babon J.J., Bullock A.N.; RT "Molecular architecture of the ankyrin SOCS box family of Cul5- RT dependent E3 ubiquitin ligases."; RL J. Mol. Biol. 425:3166-3177(2013). CC -!- FUNCTION: Core component of multiple SCF-like ECS (Elongin BC- CC Cullin 2/5-SOCS-box protein) E3 ubiquitin-protein ligase CC complexes, which mediate the ubiquitination and subsequent CC proteasomal degradation of target proteins. As a scaffold protein CC may contribute to catalysis through positioning of the substrate CC and the ubiquitin-conjugating enzyme. The functional specificity CC of the E3 ubiquitin-protein ligase complex depends on the variable CC substrate recognition component. ECS(SOCS1) seems to direct CC ubiquitination of JAK2. Seems to be involved in proteosomal CC degradation of p53/TP53 stimulated by adenovirus E1B-55 kDa CC 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 CC protein) E3 ubiquitin-protein ligase complexes formed of CUL5, the CC Elongin BC (TCEB1 and TCEB2), RBX2 and a variable SOCS box domain- CC containing protein as substrate-specific recognition component. CC Component of the probable ECS(LRRC41) complex with the substrate CC recognition component LRRC41. Component of the probable ECS(SOCS1) CC complex with the substrate recognition component SOCS1. Component CC of the probable ECS(WSB1) complex with the substrate recognition CC subunit WSB1. Component of the probable ECS(SOCS3) complex with CC the substrate recognition component SOCS3. Component of the CC probable ECS(SPSB1) complex with the substrate recognition CC component SPSB1. Component of the probable ECS(SPSB2) complex with CC the substrate recognition component SPSB2. Component of the CC probable ECS(SPSB4) complex with the substrate recognition CC component SPSB4. Component of the probable ECS(RAB40C) complex CC with the substrate recognition subunit RAB40C. May also form CC complexes containing CUL5, Elongin BC (TCEB1 and TCEB2), RBX1 and CC TCEB3. May also form complexes containing CUL5, elongin BC complex CC (TCEB1 and TCEB2), RBX1 and VHL. Interacts with RNF7/RBX2, LRRC41, CC SOCS3, SPSB1, SPSB2, SPSB4 and RAB40C. Interacts with ASB1, ASB2, CC ASB6, ASB7 and ASB12 (By similarity). {ECO:0000250}. CC -!- PTM: Neddylated; which enhances the ubiquitination activity of SCF CC and prevents binding of the inhibitor CAND1. Deneddylated via its CC interaction with the COP9 signalosome (CSN) complex (By CC similarity). {ECO:0000250}. 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 RefSeq; NP_001155090.1; NM_001161618.1. DR RefSeq; NP_082083.2; NM_027807.3. DR UniGene; Mm.218910; -. DR UniGene; Mm.491606; -. DR PDB; 2WZK; X-ray; 2.05 A; A=1-384. DR PDBsum; 2WZK; -. DR ProteinModelPortal; Q9D5V5; -. DR SMR; Q9D5V5; 10-386, 15-780, 196-694. DR BioGrid; 217689; 16. DR IntAct; Q9D5V5; 2. DR STRING; 10090.ENSMUSP00000034529; -. DR iPTMnet; Q9D5V5; -. DR PhosphoSite; Q9D5V5; -. DR EPD; Q9D5V5; -. DR MaxQB; Q9D5V5; -. DR PaxDb; Q9D5V5; -. DR PRIDE; Q9D5V5; -. 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 eggNOG; COG5647; LUCA. DR HOGENOM; HOG000007610; -. DR HOVERGEN; HBG099672; -. DR InParanoid; Q9D5V5; -. DR KO; K10612; -. DR PhylomeDB; Q9D5V5; -. DR BRENDA; 6.3.2.19; 3474. DR UniPathway; UPA00143; -. DR EvolutionaryTrace; Q9D5V5; -. DR PRO; PR:Q9D5V5; -. DR Proteomes; UP000000589; Unplaced. DR Bgee; ENSMUSG00000032030; -. DR CleanEx; MM_CUL5; -. DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; ISO:MGI. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI. 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:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR GO; GO:0021942; P:radial glia guided migration of Purkinje cell; IMP:MGI. DR Gene3D; 1.10.10.10; -; 2. DR InterPro; IPR016157; Cullin_CS. DR InterPro; IPR016158; Cullin_homology. DR InterPro; IPR001373; Cullin_N. DR InterPro; IPR019559; Cullin_neddylation_domain. DR InterPro; IPR016159; Cullin_repeat-like_dom. DR InterPro; IPR011991; WHTH_DNA-bd_dom. 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; Complete proteome; Isopeptide bond; Phosphoprotein; KW Reference proteome; Ubl conjugation; Ubl conjugation pathway. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9JJ31}. FT CHAIN 2 780 Cullin-5. FT /FTId=PRO_0000119798. FT MOD_RES 34 34 Phosphoserine. FT {ECO:0000250|UniProtKB:Q93034}. FT MOD_RES 210 210 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q93034}. FT CROSSLNK 724 724 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in NEDD8). FT {ECO:0000250}. FT CONFLICT 573 573 W -> C (in Ref. 1; BAC27621). FT {ECO:0000305}. FT HELIX 15 31 {ECO:0000244|PDB:2WZK}. FT HELIX 37 53 {ECO:0000244|PDB:2WZK}. FT HELIX 57 81 {ECO:0000244|PDB:2WZK}. FT HELIX 86 103 {ECO:0000244|PDB:2WZK}. FT TURN 104 108 {ECO:0000244|PDB:2WZK}. FT HELIX 109 111 {ECO:0000244|PDB:2WZK}. FT HELIX 112 115 {ECO:0000244|PDB:2WZK}. FT HELIX 134 146 {ECO:0000244|PDB:2WZK}. FT HELIX 148 167 {ECO:0000244|PDB:2WZK}. FT HELIX 175 186 {ECO:0000244|PDB:2WZK}. FT HELIX 196 200 {ECO:0000244|PDB:2WZK}. FT HELIX 202 248 {ECO:0000244|PDB:2WZK}. FT HELIX 257 269 {ECO:0000244|PDB:2WZK}. FT HELIX 271 273 {ECO:0000244|PDB:2WZK}. FT HELIX 274 278 {ECO:0000244|PDB:2WZK}. FT HELIX 281 286 {ECO:0000244|PDB:2WZK}. FT HELIX 290 300 {ECO:0000244|PDB:2WZK}. FT HELIX 308 329 {ECO:0000244|PDB:2WZK}. FT HELIX 330 332 {ECO:0000244|PDB:2WZK}. FT TURN 333 335 {ECO:0000244|PDB:2WZK}. FT HELIX 337 359 {ECO:0000244|PDB:2WZK}. FT HELIX 363 382 {ECO:0000244|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 //