CUL5_MOUSE
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 25-MAY-2022, entry version 162.
DE RecName: Full=Cullin-5 {ECO:0000305};
DE Short=CUL-5 {ECO:0000305};
GN Name=Cul5 {ECO:0000303|PubMed:23806657, ECO:0000312|MGI:MGI:1922967};
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-Cullin 2/5-
CC SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate
CC the ubiquitination and subsequent proteasomal degradation of target
CC proteins (PubMed:23806657). As a scaffold protein may contribute to
CC catalysis through positioning of the substrate and the ubiquitin-
CC conjugating enzyme. The functional specificity of the E3 ubiquitin-
CC protein ligase complex depends on the variable substrate recognition
CC component. ECS(SOCS1) seems to direct ubiquitination of JAK2.
CC ECS(KLHDC1) complex is part of the DesCEND (destruction via C-end
CC degrons) pathway and mediates ubiquitination and degradation of
CC truncated SELENOS selenoprotein produced by failed UGA/Sec decoding,
CC which ends with a glycine. May form a cell surface vasopressin receptor
CC (By similarity). {ECO:0000250|UniProtKB:Q93034,
CC ECO:0000269|PubMed:23806657}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q93034}.
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. Component of the probable
CC ECS(KLHDC1) complex with the substrate recognition component KLHDC1.
CC May also form complexes containing CUL5, elongin BC complex (ELOB and
CC ELOC), RBX1 and ELOA. May also form complexes containing CUL5, Elongin
CC BC (ELOB and ELOC), RBX1 and VHL. Interacts with RNF7/RBX2, LRRC41,
CC SOCS3, SPSB1, SPSB2, SPSB4 and RAB40C. Interacts with ASB1, ASB2, ASB6,
CC ASB7 and ASB12. Interacts (when neddylated) with ARIH2; leading to
CC activate the E3 ligase activity of ARIH1. Interacts with NOS2 in the
CC presence of SPSB1 or SPSB2 or SPSB4. Interacts with ERCC6; the
CC interaction is induced by DNA damaging agents or inhibitors of RNA
CC polymerase II elongation. Interacts with ELOA (via BC-box). Interacts
CC (unneddylated form) with DCUN1D1, DCUN1D2, DCUN1D3, DCUN1D4 and
CC DCUN1D5; these interactions promote the cullin neddylation.
CC {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}.
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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 AlphaFoldDB; Q9D5V5; -.
DR SMR; Q9D5V5; -.
DR BioGRID; 217689; 53.
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 DNASU; 75717; -.
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 Reactome; R-MMU-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 75717; 9 hits in 72 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:0005829; C:cytosol; TAS:Reactome.
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:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
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: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; 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 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:0007829|PDB:2WZK"
FT HELIX 37..53
FT /evidence="ECO:0007829|PDB:2WZK"
FT HELIX 57..81
FT /evidence="ECO:0007829|PDB:2WZK"
FT HELIX 86..103
FT /evidence="ECO:0007829|PDB:2WZK"
FT TURN 104..108
FT /evidence="ECO:0007829|PDB:2WZK"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:2WZK"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:2WZK"
FT HELIX 134..146
FT /evidence="ECO:0007829|PDB:2WZK"
FT HELIX 148..167
FT /evidence="ECO:0007829|PDB:2WZK"
FT HELIX 175..186
FT /evidence="ECO:0007829|PDB:2WZK"
FT HELIX 196..200
FT /evidence="ECO:0007829|PDB:2WZK"
FT HELIX 202..248
FT /evidence="ECO:0007829|PDB:2WZK"
FT HELIX 257..269
FT /evidence="ECO:0007829|PDB:2WZK"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:2WZK"
FT HELIX 274..278
FT /evidence="ECO:0007829|PDB:2WZK"
FT HELIX 281..286
FT /evidence="ECO:0007829|PDB:2WZK"
FT HELIX 290..300
FT /evidence="ECO:0007829|PDB:2WZK"
FT HELIX 308..329
FT /evidence="ECO:0007829|PDB:2WZK"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:2WZK"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:2WZK"
FT HELIX 337..359
FT /evidence="ECO:0007829|PDB:2WZK"
FT HELIX 363..382
FT /evidence="ECO:0007829|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
