CUL5_HUMAN
ID CUL5_HUMAN Reviewed; 780 AA.
AC Q93034; A8K960; O14766; Q9BZC6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Cullin-5 {ECO:0000305};
DE Short=CUL-5 {ECO:0000305};
DE AltName: Full=Vasopressin-activated calcium-mobilizing receptor 1 {ECO:0000303|PubMed:9037604};
DE Short=VACM-1 {ECO:0000303|PubMed:9037604};
GN Name=CUL5 {ECO:0000303|PubMed:10230407, ECO:0000312|HGNC:HGNC:2556};
GN Synonyms=VACM1 {ECO:0000303|PubMed:9037604};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=9037604; DOI=10.1101/gr.7.1.71;
RA Byrd P.J., Stankovic T., McConville C.M., Smith A.D., Cooper P.R.,
RA Taylor A.M.R.;
RT "Identification and analysis of expression of human VACM-1, a cullin gene
RT family member located on chromosome 11q22-23.";
RL Genome Res. 7:71-75(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Longo K.A., North W.G., Du J., Fay M.J.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Kanaya K., Kamitani T.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [7]
RP INTERACTION WITH RBX1 AND RNF7.
RX PubMed=10230407; DOI=10.1016/s1097-2765(00)80482-7;
RA Ohta T., Michel J.J., Schottelius A.J., Xiong Y.;
RT "ROC1, a homolog of APC11, represents a family of cullin partners with an
RT associated ubiquitin ligase activity.";
RL Mol. Cell 3:535-541(1999).
RN [8]
RP NEDDYLATION.
RX PubMed=10597293; DOI=10.1038/sj.onc.1203093;
RA Hori T., Osaka F., Chiba T., Miyamoto C., Okabayashi K., Shimbara N.,
RA Kato S., Tanaka K.;
RT "Covalent modification of all members of human cullin family proteins by
RT NEDD8.";
RL Oncogene 18:6829-6834(1999).
RN [9]
RP FUNCTION, IDENTIFICATION IN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX WITH
RP LRRC41, IDENTIFICATION IN A COMPLEX WITH ELOA, IDENTIFICATION IN A COMPLEX
RP WITH SOCS1, AND IDENTIFICATION IN A COMPLEX WITH WSB1.
RX PubMed=11384984; DOI=10.1074/jbc.m103093200;
RA Kamura T., Burian D., Yan Q., Schmidt S.L., Lane W.S., Querido E.,
RA Branton P.E., Shilatifard A., Conaway R.C., Conaway J.W.;
RT "Muf1, a novel elongin BC-interacting leucine-rich repeat protein that can
RT assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase.";
RL J. Biol. Chem. 276:29748-29753(2001).
RN [10]
RP FUNCTION (MICROBIAL INFECTION), IDENTIFICATION IN COMPLEX WITH HUMAN
RP ADENOVIRUS 5 PROTEINS E1B-55K AND E4-ORF6 (MICROBIAL INFECTION), AND
RP NEDDYLATION.
RX PubMed=12186903; DOI=10.1128/jvi.76.18.9194-9206.2002;
RA Harada J.N., Shevchenko A., Shevchenko A., Pallas D.C., Berk A.J.;
RT "Analysis of the adenovirus E1B-55K-anchored proteome reveals its link to
RT ubiquitination machinery.";
RL J. Virol. 76:9194-9206(2002).
RN [11]
RP INTERACTION WITH HIV-1 VIF (MICROBIAL INFECTION).
RX PubMed=15574592; DOI=10.1101/gad.1249904;
RA Mehle A., Goncalves J., Santa-Marta M., McPike M., Gabuzda D.;
RT "Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-
RT Cul5 complex that promotes APOBEC3G degradation.";
RL Genes Dev. 18:2861-2866(2004).
RN [12]
RP FUNCTION, IDENTIFICATION IN THE ECS(LRRC41) COMPLEX, IDENTIFICATION IN THE
RP ECS(SOCS3) COMPLEX, IDENTIFICATION IN THE ECS(SPSB1) COMPLEX,
RP IDENTIFICATION IN THE ECS(SPSB2) COMPLEX, IDENTIFICATION IN THE ECS(SPSB4)
RP COMPLEX, IDENTIFICATION IN THE ECS(RAB40C) COMPLEX, IDENTIFICATION IN THE
RP ECS(WSB1) COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION
RP WITH LRRC41; SOCS3; SPSB1; SPSB2; SPSB4; WSB1 AND RAB40C.
RX PubMed=15601820; DOI=10.1101/gad.1252404;
RA Kamura T., Maenaka K., Kotoshiba S., Matsumoto M., Kohda D., Conaway R.C.,
RA Conaway J.W., Nakayama K.I.;
RT "VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1
RT and Cul5-Rbx2 modules of ubiquitin ligases.";
RL Genes Dev. 18:3055-3065(2004).
RN [13]
RP INTERACTION WITH ASB1; ASB2; ASB6; ASB7 AND ASB12.
RX PubMed=16325183; DOI=10.1016/j.febslet.2005.11.016;
RA Kohroki J., Nishiyama T., Nakamura T., Masuho Y.;
RT "ASB proteins interact with cullin5 and Rbx2 to form E3 ubiquitin ligase
RT complexes.";
RL FEBS Lett. 579:6796-6802(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP INTERACTION WITH ASB2.
RX PubMed=21119685; DOI=10.1038/cr.2010.165;
RA Nie L., Zhao Y., Wu W., Yang Y.Z., Wang H.C., Sun X.H.;
RT "Notch-induced Asb2 expression promotes protein ubiquitination by forming
RT non-canonical E3 ligase complexes.";
RL Cell Res. 21:754-769(2011).
RN [17]
RP INTERACTION WITH NOS2.
RX PubMed=21199876; DOI=10.1074/jbc.m110.190678;
RA Nishiya T., Matsumoto K., Maekawa S., Kajita E., Horinouchi T.,
RA Fujimuro M., Ogasawara K., Uehara T., Miwa S.;
RT "Regulation of inducible nitric-oxide synthase by the SPRY domain- and SOCS
RT box-containing proteins.";
RL J. Biol. Chem. 286:9009-9019(2011).
RN [18]
RP INTERACTION WITH HERPES VIRUS 8 PROTEIN LANA1 (MICROBIAL INFECTION).
RX PubMed=21697472; DOI=10.1128/jvi.00733-11;
RA Li X., Liang D., Lin X., Robertson E.S., Lan K.;
RT "Kaposi's sarcoma-associated herpesvirus-encoded latency-associated nuclear
RT antigen reduces interleukin-8 expression in endothelial cells and impairs
RT neutrophil chemotaxis by degrading nuclear p65.";
RL J. Virol. 85:8606-8615(2011).
RN [19]
RP INTERACTION WITH ARIH2, AND NEDDYLATION.
RX PubMed=24076655; DOI=10.1038/emboj.2013.209;
RA Kelsall I.R., Duda D.M., Olszewski J.L., Hofmann K., Knebel A.,
RA Langevin F., Wood N., Wightman M., Schulman B.A., Alpi A.F.;
RT "TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-
RT RING ligase complexes.";
RL EMBO J. 32:2848-2860(2013).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP INTERACTION WITH DCUN1D1; DCUN1D2; DCUN1D3; DCUN1D4 AND DCUN1D5.
RX PubMed=23201271; DOI=10.1016/j.str.2012.10.013;
RA Monda J.K., Scott D.C., Miller D.J., Lydeard J., King D., Harper J.W.,
RA Bennett E.J., Schulman B.A.;
RT "Structural conservation of distinctive N-terminal acetylation-dependent
RT interactions across a family of mammalian NEDD8 ligation enzymes.";
RL Structure 21:42-53(2013).
RN [22]
RP INTERACTION WITH MOLLUSCUM CONTAGIOSUM VIRUS PROTEIN MC132 (MICROBIAL
RP INFECTION).
RX PubMed=26041281; DOI=10.1128/jvi.00799-15;
RA Brady G., Haas D.A., Farrell P.J., Pichlmair A., Bowie A.G.;
RT "Poxvirus protein MC132 from molluscum contagiosum virus inhibits NF-B
RT activation by targeting p65 for degradation.";
RL J. Virol. 89:8406-8415(2015).
RN [23]
RP INTERACTION WITH DCUN1D1; DCUN1D2; DCUN1D3; DCUN1D4 AND DCUN1D5.
RX PubMed=26906416; DOI=10.1242/jcs.181784;
RA Keuss M.J., Thomas Y., Mcarthur R., Wood N.T., Knebel A., Kurz T.;
RT "Characterization of the mammalian family of DCN-type NEDD8 E3 ligases.";
RL J. Cell Sci. 129:1441-1454(2016).
RN [24]
RP INTERACTION WITH ERCC6 AND ELOA.
RX PubMed=28292928; DOI=10.1074/jbc.c117.777946;
RA Weems J.C., Slaughter B.D., Unruh J.R., Boeing S., Hall S.M., McLaird M.B.,
RA Yasukawa T., Aso T., Svejstrup J.Q., Conaway J.W., Conaway R.C.;
RT "Cockayne syndrome B protein regulates recruitment of the Elongin A
RT ubiquitin ligase to sites of DNA damage.";
RL J. Biol. Chem. 292:6431-6437(2017).
RN [25]
RP FUNCTION, PATHWAY, AND IDENTIFICATION IN A E3 UBIQUITIN-PROTEIN LIGASE
RP COMPLEX CONTAINING KLHDC1.
RX PubMed=32200094; DOI=10.1016/j.isci.2020.100970;
RA Okumura F., Fujiki Y., Oki N., Osaki K., Nishikimi A., Fukui Y.,
RA Nakatsukasa K., Kamura T.;
RT "Cul5-type ubiquitin ligase KLHDC1 contributes to the elimination of
RT truncated SELENOS produced by failed UGA/Sec decoding.";
RL IScience 23:100970-100970(2020).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 401-780 IN COMPLEX WITH NEDD8 AND
RP RBX1, AND NEDDYLATION AT LYS-724.
RX PubMed=18805092; DOI=10.1016/j.cell.2008.07.022;
RA Duda D.M., Borg L.A., Scott D.C., Hunt H.W., Hammel M., Schulman B.A.;
RT "Structural insights into NEDD8 activation of cullin-RING ligases:
RT conformational control of conjugation.";
RL Cell 134:995-1006(2008).
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:11384984, PubMed:15601820). As a scaffold protein may
CC contribute to catalysis through positioning of the substrate and the
CC ubiquitin-conjugating enzyme (PubMed:11384984, PubMed:15601820). The
CC functional specificity of the E3 ubiquitin-protein ligase complex
CC depends on the variable substrate recognition component
CC (PubMed:11384984, PubMed:15601820). ECS(SOCS1) seems to direct
CC ubiquitination of JAK2 (PubMed:11384984). ECS(KLHDC1) complex is part
CC of the DesCEND (destruction via C-end degrons) pathway and mediates
CC ubiquitination and degradation of truncated SELENOS selenoprotein
CC produced by failed UGA/Sec decoding, which ends with a glycine
CC (PubMed:32200094). May form a cell surface vasopressin receptor
CC (PubMed:9037604). {ECO:0000269|PubMed:11384984,
CC ECO:0000269|PubMed:15601820, ECO:0000269|PubMed:32200094,
CC ECO:0000269|PubMed:9037604}.
CC -!- FUNCTION: (Microbial infection) Seems to be involved in proteosomal
CC degradation of p53/TP53 stimulated by adenovirus E1B-55 kDa protein.
CC {ECO:0000269|PubMed:12186903}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:11384984, ECO:0000269|PubMed:15601820,
CC ECO:0000269|PubMed:32200094}.
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 (PubMed:11384984,
CC PubMed:15601820). Component of the probable ECS(LRRC41) complex with
CC the substrate recognition component LRRC41 (PubMed:11384984). Component
CC of the probable ECS(SOCS1) complex with the substrate recognition
CC component SOCS1 (PubMed:11384984). Component of the probable ECS(WSB1)
CC complex with the substrate recognition subunit WSB1 (PubMed:15601820).
CC Component of the probable ECS(SOCS3) complex with the substrate
CC recognition component SOCS3 (PubMed:15601820). Component of the
CC probable ECS(SPSB1) complex with the substrate recognition component
CC SPSB1 (PubMed:15601820). Component of the probable ECS(SPSB2) complex
CC with the substrate recognition component SPSB2 (PubMed:15601820).
CC Component of the probable ECS(SPSB4) complex with the substrate
CC recognition component SPSB4 (PubMed:15601820). Component of the
CC probable ECS(RAB40C) complex with the substrate recognition subunit
CC RAB40C (PubMed:15601820). Component of the probable ECS(KLHDC1) complex
CC with the substrate recognition component KLHDC1 (PubMed:32200094). May
CC also form complexes containing CUL5, elongin BC complex (ELOB and
CC ELOC), RBX1 and ELOA (PubMed:11384984). May also form complexes
CC containing CUL5, Elongin BC (ELOB and ELOC), RBX1 and VHL
CC (PubMed:10230407, PubMed:18805092). Interacts with RNF7/RBX2, LRRC41,
CC SOCS3, SPSB1, SPSB2, SPSB4 and RAB40C (PubMed:15601820). Interacts with
CC ASB1, ASB2, ASB6, ASB7 and ASB12 (PubMed:16325183, PubMed:21119685).
CC Interacts (when neddylated) with ARIH2; leading to activate the E3
CC ligase activity of ARIH1 (PubMed:24076655). Interacts with NOS2 in the
CC presence of SPSB1 or SPSB2 or SPSB4 (PubMed:21199876). Interacts with
CC ERCC6; the interaction is induced by DNA damaging agents or inhibitors
CC of RNA polymerase II elongation (PubMed:28292928). Interacts with ELOA
CC (via BC-box) (PubMed:28292928). Interacts (unneddylated form) with
CC DCUN1D1, DCUN1D2, DCUN1D3, DCUN1D4 and DCUN1D5; these interactions
CC promote the cullin neddylation (PubMed:23201271, PubMed:26906416).
CC {ECO:0000269|PubMed:10230407, ECO:0000269|PubMed:11384984,
CC ECO:0000269|PubMed:15601820, ECO:0000269|PubMed:16325183,
CC ECO:0000269|PubMed:18805092, ECO:0000269|PubMed:21199876,
CC ECO:0000269|PubMed:23201271, ECO:0000269|PubMed:24076655,
CC ECO:0000269|PubMed:26906416, ECO:0000269|PubMed:28292928,
CC ECO:0000269|PubMed:32200094}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via the substrate recognition
CC component) with HIV-1 Vif. {ECO:0000269|PubMed:12186903}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via the substrate recognition
CC component) with human adenovirus 5 proteins E1B-55K and E4-orf6.
CC {ECO:0000269|PubMed:12186903}.
CC -!- SUBUNIT: (Microbial infection) Interacts with herpes virus 8 protein
CC LANA1; this interaction promotes the degradation of NF-kappa-B
CC component RELA. {ECO:0000269|PubMed:21697472}.
CC -!- SUBUNIT: (Microbial infection) Interacts with molluscum contagiosum
CC virus protein MC132; this interaction promotes the degradation of NF-
CC kappa-B component RELA. {ECO:0000269|PubMed:26041281}.
CC -!- INTERACTION:
CC Q93034; O95376: ARIH2; NbExp=12; IntAct=EBI-1057139, EBI-711158;
CC Q93034; Q9Y576: ASB1; NbExp=6; IntAct=EBI-1057139, EBI-2323092;
CC Q93034; Q96Q27-2: ASB2; NbExp=3; IntAct=EBI-1057139, EBI-28950233;
CC Q93034; Q9NWX5: ASB6; NbExp=9; IntAct=EBI-1057139, EBI-6425205;
CC Q93034; Q9H672: ASB7; NbExp=3; IntAct=EBI-1057139, EBI-3916346;
CC Q93034; Q9NPC3: CCNB1IP1; NbExp=3; IntAct=EBI-1057139, EBI-745269;
CC Q93034; O95273: CCNDBP1; NbExp=4; IntAct=EBI-1057139, EBI-748961;
CC Q93034; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-1057139, EBI-3866319;
CC Q93034; P04626: ERBB2; NbExp=2; IntAct=EBI-1057139, EBI-641062;
CC Q93034; Q08379: GOLGA2; NbExp=3; IntAct=EBI-1057139, EBI-618309;
CC Q93034; P42858: HTT; NbExp=10; IntAct=EBI-1057139, EBI-466029;
CC Q93034; Q5T7N3: KANK4; NbExp=3; IntAct=EBI-1057139, EBI-9355810;
CC Q93034; P62877: RBX1; NbExp=3; IntAct=EBI-1057139, EBI-398523;
CC Q93034; Q9UBF6: RNF7; NbExp=8; IntAct=EBI-1057139, EBI-398632;
CC Q93034; O14508: SOCS2; NbExp=9; IntAct=EBI-1057139, EBI-617737;
CC Q93034; O41974: GAMMAHV.ORF73; Xeno; NbExp=2; IntAct=EBI-1057139, EBI-6933128;
CC Q93034; P12504: vif; Xeno; NbExp=11; IntAct=EBI-1057139, EBI-779991;
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:0000269|PubMed:10597293, ECO:0000269|PubMed:12186903,
CC ECO:0000269|PubMed:18805092, ECO:0000269|PubMed:24076655}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
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DR EMBL; X81882; CAA57465.1; -; mRNA.
DR EMBL; AF017061; AAB70253.1; -; mRNA.
DR EMBL; AF327710; AAK07472.1; -; mRNA.
DR EMBL; AK292575; BAF85264.1; -; mRNA.
DR EMBL; CH471065; EAW67102.1; -; Genomic_DNA.
DR EMBL; BC063306; AAH63306.1; -; mRNA.
DR CCDS; CCDS31668.1; -.
DR RefSeq; NP_003469.2; NM_003478.4.
DR PDB; 3DPL; X-ray; 2.60 A; C=401-780.
DR PDB; 3DQV; X-ray; 3.00 A; C/D=401-780.
DR PDB; 4JGH; X-ray; 3.00 A; D=10-386.
DR PDB; 4N9F; X-ray; 3.30 A; 3/9/C/I/O/U/V/f/l/r/w/x=12-321.
DR PDB; 6V9I; EM; 5.20 A; C=2-780.
DR PDB; 7ONI; EM; 3.40 A; C=1-780.
DR PDBsum; 3DPL; -.
DR PDBsum; 3DQV; -.
DR PDBsum; 4JGH; -.
DR PDBsum; 4N9F; -.
DR PDBsum; 6V9I; -.
DR PDBsum; 7ONI; -.
DR AlphaFoldDB; Q93034; -.
DR SMR; Q93034; -.
DR BioGRID; 113743; 510.
DR CORUM; Q93034; -.
DR DIP; DIP-43696N; -.
DR IntAct; Q93034; 373.
DR MINT; Q93034; -.
DR STRING; 9606.ENSP00000376808; -.
DR iPTMnet; Q93034; -.
DR PhosphoSitePlus; Q93034; -.
DR BioMuta; CUL5; -.
DR DMDM; 14917099; -.
DR EPD; Q93034; -.
DR jPOST; Q93034; -.
DR MassIVE; Q93034; -.
DR MaxQB; Q93034; -.
DR PaxDb; Q93034; -.
DR PeptideAtlas; Q93034; -.
DR PRIDE; Q93034; -.
DR ProteomicsDB; 75673; -.
DR Antibodypedia; 990; 243 antibodies from 35 providers.
DR DNASU; 8065; -.
DR Ensembl; ENST00000393094.7; ENSP00000376808.2; ENSG00000166266.14.
DR Ensembl; ENST00000531427.5; ENSP00000435376.1; ENSG00000166266.14.
DR GeneID; 8065; -.
DR KEGG; hsa:8065; -.
DR MANE-Select; ENST00000393094.7; ENSP00000376808.2; NM_003478.6; NP_003469.2.
DR UCSC; uc001pjv.4; human.
DR CTD; 8065; -.
DR DisGeNET; 8065; -.
DR GeneCards; CUL5; -.
DR HGNC; HGNC:2556; CUL5.
DR HPA; ENSG00000166266; Low tissue specificity.
DR MIM; 601741; gene.
DR neXtProt; NX_Q93034; -.
DR OpenTargets; ENSG00000166266; -.
DR PharmGKB; PA27052; -.
DR VEuPathDB; HostDB:ENSG00000166266; -.
DR eggNOG; KOG2285; Eukaryota.
DR GeneTree; ENSGT00940000156648; -.
DR HOGENOM; CLU_004747_5_0_1; -.
DR InParanoid; Q93034; -.
DR OMA; YRENFEA; -.
DR OrthoDB; 1040292at2759; -.
DR PhylomeDB; Q93034; -.
DR TreeFam; TF105874; -.
DR PathwayCommons; Q93034; -.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q93034; -.
DR SIGNOR; Q93034; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 8065; 44 hits in 1135 CRISPR screens.
DR ChiTaRS; CUL5; human.
DR EvolutionaryTrace; Q93034; -.
DR GeneWiki; CUL5; -.
DR GenomeRNAi; 8065; -.
DR Pharos; Q93034; Tbio.
DR PRO; PR:Q93034; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q93034; protein.
DR Bgee; ENSG00000166266; Expressed in secondary oocyte and 219 other tissues.
DR ExpressionAtlas; Q93034; baseline and differential.
DR Genevisible; Q93034; HS.
DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0090734; C:site of DNA damage; IDA:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; TAS:ProtInc.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:Reactome.
DR GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:ProtInc.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:ProtInc.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR IDEAL; IID00519; -.
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; Host-virus interaction; Isopeptide bond; Phosphoprotein;
KW Receptor; Reference proteome; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..780
FT /note="Cullin-5"
FT /id="PRO_0000119797"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 210
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 724
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000269|PubMed:18805092"
FT CONFLICT 9
FT /note="N -> D (in Ref. 2; AAB70253)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="S -> F (in Ref. 2; AAB70253)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="E -> G (in Ref. 2; AAB70253)"
FT /evidence="ECO:0000305"
FT CONFLICT 32..34
FT /note="QES -> RDF (in Ref. 2; AAB70253)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="Q -> R (in Ref. 2; AAB70253)"
FT /evidence="ECO:0000305"
FT CONFLICT 50..52
FT /note="VCL -> FCF (in Ref. 2; AAB70253)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="D -> DF (in Ref. 2; AAB70253)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="Q -> P (in Ref. 1; CAA57465)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="L -> F (in Ref. 1; CAA57465)"
FT /evidence="ECO:0000305"
FT CONFLICT 651
FT /note="E -> D (in Ref. 1; CAA57465)"
FT /evidence="ECO:0000305"
FT HELIX 15..30
FT /evidence="ECO:0007829|PDB:4JGH"
FT HELIX 37..53
FT /evidence="ECO:0007829|PDB:4JGH"
FT HELIX 57..81
FT /evidence="ECO:0007829|PDB:4JGH"
FT HELIX 86..103
FT /evidence="ECO:0007829|PDB:4JGH"
FT TURN 104..108
FT /evidence="ECO:0007829|PDB:4JGH"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:4JGH"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:4JGH"
FT HELIX 134..146
FT /evidence="ECO:0007829|PDB:4JGH"
FT HELIX 148..167
FT /evidence="ECO:0007829|PDB:4JGH"
FT HELIX 175..186
FT /evidence="ECO:0007829|PDB:4JGH"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:4JGH"
FT HELIX 202..224
FT /evidence="ECO:0007829|PDB:4JGH"
FT HELIX 227..248
FT /evidence="ECO:0007829|PDB:4JGH"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:4JGH"
FT HELIX 257..269
FT /evidence="ECO:0007829|PDB:4JGH"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:4JGH"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:4JGH"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:4JGH"
FT HELIX 281..286
FT /evidence="ECO:0007829|PDB:4JGH"
FT HELIX 290..300
FT /evidence="ECO:0007829|PDB:4JGH"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:4N9F"
FT HELIX 310..333
FT /evidence="ECO:0007829|PDB:4JGH"
FT HELIX 337..357
FT /evidence="ECO:0007829|PDB:4JGH"
FT TURN 358..361
FT /evidence="ECO:0007829|PDB:4JGH"
FT HELIX 363..377
FT /evidence="ECO:0007829|PDB:4JGH"
FT HELIX 405..416
FT /evidence="ECO:0007829|PDB:3DPL"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:3DPL"
FT HELIX 420..423
FT /evidence="ECO:0007829|PDB:3DPL"
FT HELIX 427..438
FT /evidence="ECO:0007829|PDB:3DPL"
FT HELIX 439..443
FT /evidence="ECO:0007829|PDB:3DPL"
FT HELIX 447..463
FT /evidence="ECO:0007829|PDB:3DPL"
FT HELIX 470..482
FT /evidence="ECO:0007829|PDB:3DPL"
FT HELIX 487..513
FT /evidence="ECO:0007829|PDB:3DPL"
FT HELIX 523..525
FT /evidence="ECO:0007829|PDB:3DPL"
FT STRAND 526..532
FT /evidence="ECO:0007829|PDB:3DPL"
FT HELIX 533..536
FT /evidence="ECO:0007829|PDB:3DPL"
FT HELIX 549..552
FT /evidence="ECO:0007829|PDB:3DPL"
FT HELIX 555..563
FT /evidence="ECO:0007829|PDB:3DPL"
FT STRAND 566..573
FT /evidence="ECO:0007829|PDB:3DPL"
FT HELIX 575..577
FT /evidence="ECO:0007829|PDB:3DPL"
FT STRAND 579..585
FT /evidence="ECO:0007829|PDB:3DPL"
FT STRAND 590..596
FT /evidence="ECO:0007829|PDB:3DPL"
FT HELIX 597..603
FT /evidence="ECO:0007829|PDB:3DPL"
FT HELIX 604..606
FT /evidence="ECO:0007829|PDB:3DPL"
FT STRAND 607..609
FT /evidence="ECO:0007829|PDB:7ONI"
FT HELIX 616..623
FT /evidence="ECO:0007829|PDB:3DPL"
FT HELIX 627..638
FT /evidence="ECO:0007829|PDB:3DPL"
FT STRAND 647..652
FT /evidence="ECO:0007829|PDB:3DPL"
FT HELIX 657..659
FT /evidence="ECO:0007829|PDB:3DPL"
FT STRAND 665..668
FT /evidence="ECO:0007829|PDB:3DPL"
FT STRAND 674..687
FT /evidence="ECO:0007829|PDB:3DPL"
FT TURN 690..693
FT /evidence="ECO:0007829|PDB:3DPL"
FT HELIX 697..723
FT /evidence="ECO:0007829|PDB:3DPL"
FT STRAND 726..729
FT /evidence="ECO:0007829|PDB:3DPL"
FT HELIX 731..741
FT /evidence="ECO:0007829|PDB:3DPL"
FT TURN 742..745
FT /evidence="ECO:0007829|PDB:3DPL"
FT HELIX 750..762
FT /evidence="ECO:0007829|PDB:3DPL"
FT STRAND 765..769
FT /evidence="ECO:0007829|PDB:3DPL"
FT STRAND 772..778
FT /evidence="ECO:0007829|PDB:3DPL"
SQ SEQUENCE 780 AA; 90955 MW; 57463CB4ED76E303 CRC64;
MATSNLLKNK GSLQFEDKWD FMRPIVLKLL RQESVTKQQW FDLFSDVHAV CLWDDKGPAK
IHQALKEDIL EFIKQAQARV LSHQDDTALL KAYIVEWRKF FTQCDILPKP FCQLEITLMG
KQGSNKKSNV 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 EPQVNSPKDF
TEGTLFSVNQ EFSLIKNAKV QKRGKINLIG RLQLTTERMR EEENEGIVQL RILRTQEAII
QIMKMRKKIS NAQLQTELVE ILKNMFLPQK KMIKEQIEWL IEHKYIRRDE SDINTFIYMA
