ID CUL9_HUMAN Reviewed; 2517 AA. AC Q8IWT3; O75188; Q5TCY3; Q68CP2; Q68D92; Q8N3W9; Q9BU56; DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 2. DT 24-JAN-2024, entry version 189. DE RecName: Full=Cullin-9; DE Short=CUL-9; DE AltName: Full=UbcH7-associated protein 1; DE AltName: Full=p53-associated parkin-like cytoplasmic protein; GN Name=CUL9; Synonyms=H7AP1, KIAA0708, PARC; 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] (ISOFORM 1), PROTEIN SEQUENCE OF 786-791; RP 2419-2431 AND 2432-2445, INTERACTION WITH TP53, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, AND FUNCTION. RC TISSUE=Cervix carcinoma; RX PubMed=12526791; DOI=10.1016/s0092-8674(02)01255-2; RA Nikolaev A.Y., Li M., Puskas N., Qin J., Gu W.; RT "Parc: a cytoplasmic anchor for p53."; RL Cell 112:29-40(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Testis; RA Rose S.A., Ardley H.C., Tan N.G., Scott G.B., Markham A.F., Robinson P.A.; RT "UbcH7 associated protein, H7AP1. A new member of the Parkin/Ariadne E3 RT ubiquitin Ligase (PAUL) family."; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Amygdala, and Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). 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] OF 1-662 (ISOFORM 2), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 528-662 (ISOFORMS 1/2). RC TISSUE=Chondrocyte, and Thymus; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 765-2517 (ISOFORM 1). RC TISSUE=Brain; RX PubMed=9734811; DOI=10.1093/dnares/5.3.169; RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., RA Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. X. The RT complete sequences of 100 new cDNA clones from brain which can code for RT large proteins in vitro."; RL DNA Res. 5:169-176(1998). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1554-2517 (ISOFORM 1). RC TISSUE=Lung; 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 [9] RP INTERACTION WITH UBCH7 AND UBCH8. RX PubMed=10521492; DOI=10.1074/jbc.274.43.30963; RA Moynihan T.P., Ardley H.C., Nuber U., Rose S.A., Jones P.F., Markham A.F., RA Scheffner M., Robinson P.A.; RT "The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with RING RT finger/IBR motif-containing domains of HHARI and H7-AP1."; RL J. Biol. Chem. 274:30963-30968(1999). RN [10] RP INTERACTION WITH CUL7. RX PubMed=15964813; DOI=10.1128/mcb.25.13.5579-5589.2005; RA Skaar J.R., Arai T., DeCaprio J.A.; RT "Dimerization of CUL7 and PARC is not required for all CUL7 functions and RT mouse development."; RL Mol. Cell. Biol. 25:5579-5589(2005). RN [11] RP FUNCTION, INTERACTION WITH CUL7; RBX1 AND TP53, AND NEDDYLATION. RX PubMed=17332328; DOI=10.1158/0008-5472.can-06-3241; RA Skaar J.R., Florens L., Tsutsumi T., Arai T., Tron A., Swanson S.K., RA Washburn M.P., DeCaprio J.A.; RT "PARC and CUL7 form atypical cullin RING ligase complexes."; RL Cancer Res. 67:2006-2014(2007). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-976; SER-1457 AND SER-2436, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [13] RP FUNCTION, AND INTERACTION WITH CUL7 AND RBX1. RX PubMed=24793696; DOI=10.1016/j.molcel.2014.03.046; RA Li Z., Pei X.H., Yan J., Yan F., Cappell K.M., Whitehurst A.W., Xiong Y.; RT "CUL9 mediates the functions of the 3M complex and ubiquitylates survivin RT to maintain genome integrity."; RL Mol. Cell 54:805-819(2014). CC -!- FUNCTION: Core component of a Cul9-RING ubiquitin-protein ligase CC complex, a complex that mediates ubiquitination and subsequent CC degradation of BIRC5 and is required to maintain microtubule dynamics CC and genome integrity. Acts downstream of the 3M complex, which inhibits CC CUL9 activity, leading to prevent ubiquitination of BIRC5 CC (PubMed:24793696). Cytoplasmic anchor protein in p53/TP53-associated CC protein complex. Regulates the subcellular localization of p53/TP53 and CC subsequent function (PubMed:12526791, PubMed:17332328). CC {ECO:0000269|PubMed:12526791, ECO:0000269|PubMed:17332328, CC ECO:0000269|PubMed:24793696}. CC -!- SUBUNIT: Part of a Cul9-RING complex at least composed of CUL9 and CC RBX1. Interacts with CUL7: interaction with CUL7 component of the 3M CC complex leads to inhibition of CUL9 activity. The CUL7-CUL9 heterodimer CC seems to interact specifically with TP53. Forms a complex with p53/TP53 CC in the cytoplasm of unstressed cells. Interacts with UBCH7 and UBCH8. CC {ECO:0000269|PubMed:10521492, ECO:0000269|PubMed:12526791, CC ECO:0000269|PubMed:15964813, ECO:0000269|PubMed:17332328, CC ECO:0000269|PubMed:24793696}. CC -!- INTERACTION: CC Q8IWT3; P04637: TP53; NbExp=13; IntAct=EBI-311123, EBI-366083; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12526791}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8IWT3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8IWT3-3; Sequence=VSP_009573; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues with highest CC expression in testis brain and kidney. {ECO:0000269|PubMed:12526791}. CC -!- DOMAIN: The IBR domain is required for interaction with UBCH7 and CC UBCH8. CC -!- PTM: In vitro, self-ubiquitination in the presence of E1, E2 and CC ubiquitin. CC -!- PTM: Neddylated. {ECO:0000269|PubMed:17332328}. CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE- CC ProRule:PRU00330}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC85207.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305}; CC Sequence=BAC86090.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305}; 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; AY145132; AAN61516.1; -; mRNA. DR EMBL; AJ318215; CAC85756.1; -; mRNA. DR EMBL; CR749511; CAH18328.1; -; mRNA. DR EMBL; CR749841; CAH18696.1; -; mRNA. DR EMBL; AL133375; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX04163.1; -; Genomic_DNA. DR EMBL; AK125228; BAC86090.1; ALT_SEQ; mRNA. DR EMBL; AK129649; BAC85207.1; ALT_SEQ; mRNA. DR EMBL; AB014608; BAA31683.3; -; mRNA. DR EMBL; BC002879; AAH02879.2; -; mRNA. DR CCDS; CCDS4890.1; -. [Q8IWT3-1] DR PIR; T00350; T00350. DR RefSeq; NP_055904.1; NM_015089.3. [Q8IWT3-1] DR PDB; 2JUF; NMR; -; A=366-466. DR PDBsum; 2JUF; -. DR AlphaFoldDB; Q8IWT3; -. DR BMRB; Q8IWT3; -. DR SMR; Q8IWT3; -. DR BioGRID; 116736; 175. DR CORUM; Q8IWT3; -. DR IntAct; Q8IWT3; 16. DR MINT; Q8IWT3; -. DR STRING; 9606.ENSP00000252050; -. DR iPTMnet; Q8IWT3; -. DR PhosphoSitePlus; Q8IWT3; -. DR BioMuta; CUL9; -. DR DMDM; 57015409; -. DR EPD; Q8IWT3; -. DR jPOST; Q8IWT3; -. DR MassIVE; Q8IWT3; -. DR MaxQB; Q8IWT3; -. DR PaxDb; 9606-ENSP00000252050; -. DR PeptideAtlas; Q8IWT3; -. DR ProteomicsDB; 70891; -. [Q8IWT3-1] DR ProteomicsDB; 70892; -. [Q8IWT3-3] DR Pumba; Q8IWT3; -. DR Antibodypedia; 3078; 176 antibodies from 28 providers. DR DNASU; 23113; -. DR Ensembl; ENST00000252050.9; ENSP00000252050.4; ENSG00000112659.14. [Q8IWT3-1] DR GeneID; 23113; -. DR KEGG; hsa:23113; -. DR MANE-Select; ENST00000252050.9; ENSP00000252050.4; NM_015089.4; NP_055904.1. DR UCSC; uc003ouk.4; human. [Q8IWT3-1] DR AGR; HGNC:15982; -. DR CTD; 23113; -. DR DisGeNET; 23113; -. DR GeneCards; CUL9; -. DR HGNC; HGNC:15982; CUL9. DR HPA; ENSG00000112659; Low tissue specificity. DR MIM; 607489; gene. DR neXtProt; NX_Q8IWT3; -. DR OpenTargets; ENSG00000112659; -. DR PharmGKB; PA164718328; -. DR VEuPathDB; HostDB:ENSG00000112659; -. DR eggNOG; KOG1815; Eukaryota. DR GeneTree; ENSGT00940000153954; -. DR InParanoid; Q8IWT3; -. DR OMA; KPWKPNH; -. DR OrthoDB; 4161627at2759; -. DR PhylomeDB; Q8IWT3; -. DR TreeFam; TF101154; -. DR PathwayCommons; Q8IWT3; -. DR Reactome; R-HSA-8951664; Neddylation. DR SignaLink; Q8IWT3; -. DR SIGNOR; Q8IWT3; -. DR BioGRID-ORCS; 23113; 18 hits in 1192 CRISPR screens. DR ChiTaRS; CUL9; human. DR EvolutionaryTrace; Q8IWT3; -. DR GeneWiki; PARC_(gene); -. DR GenomeRNAi; 23113; -. DR Pharos; Q8IWT3; Tbio. DR PRO; PR:Q8IWT3; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q8IWT3; Protein. DR Bgee; ENSG00000112659; Expressed in right testis and 184 other cell types or tissues. DR ExpressionAtlas; Q8IWT3; baseline and differential. DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0061630; F:ubiquitin protein ligase activity; TAS:Reactome. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB. DR GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:UniProtKB. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. DR CDD; cd20347; BRcat_RBR_CUL9; 1. DR CDD; cd20359; Rcat_RBR_CUL9; 1. DR CDD; cd16624; RING-HC_RBR_CUL9; 1. DR Gene3D; 1.20.120.1750; -; 1. DR Gene3D; 2.30.30.30; -; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR004939; APC_su10/DOC_dom. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR047561; BRcat_RBR_CUL9. DR InterPro; IPR021097; CPH_domain. 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; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR002867; IBR_dom. DR InterPro; IPR047560; Rcat_RBR_CUL9. DR InterPro; IPR014722; Rib_uL2_dom2. DR InterPro; IPR047562; RING-HC_RBR_CUL9. DR InterPro; IPR044066; TRIAD_supradom. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR22771; CULLIN AND GALACTOSE-BINDING DOMAIN-CONTAINING; 1. DR PANTHER; PTHR22771:SF2; CULLIN-9; 1. DR Pfam; PF03256; ANAPC10; 1. DR Pfam; PF11515; Cul7; 1. DR Pfam; PF00888; Cullin; 1. DR Pfam; PF01485; IBR; 2. DR SMART; SM01337; APC10; 1. DR SMART; SM00884; Cullin_Nedd8; 1. DR SMART; SM00647; IBR; 2. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF75632; Cullin homology domain; 1. DR SUPFAM; SSF49785; Galactose-binding domain-like; 1. DR SUPFAM; SSF57850; RING/U-box; 2. DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1. DR PROSITE; PS01256; CULLIN_1; 1. DR PROSITE; PS50069; CULLIN_2; 1. DR PROSITE; PS51284; DOC; 1. DR PROSITE; PS51873; TRIAD; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; Q8IWT3; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Coiled coil; Cytoplasm; KW Direct protein sequencing; Metal-binding; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Repeat; Transferase; Ubl conjugation; KW Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1..2517 FT /note="Cullin-9" FT /id="PRO_0000119815" FT DOMAIN 1143..1322 FT /note="DOC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00614" FT ZN_FING 2070..2120 FT /note="RING-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT ZN_FING 2140..2203 FT /note="IBR-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT ZN_FING 2236..2265 FT /note="RING-type 2; atypical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT REGION 276..296 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 576..639 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1432..1466 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1664..1685 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2066..2283 FT /note="TRIAD supradomain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT REGION 2442..2517 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 1649..1691 FT /evidence="ECO:0000255" FT COILED 2365..2385 FT /evidence="ECO:0000255" FT COMPBIAS 276..291 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 590..627 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1665..1685 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2460..2517 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 2249 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 1363..1370 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT BINDING 2070 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2073 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2088 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2090 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2093 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2096 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2115 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2120 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2160 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2166 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2181 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2184 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2189 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2192 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2198 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2203 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2236 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2239 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2254 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2257 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2262 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2265 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2273 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 2279 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT MOD_RES 976 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1457 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2436 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 418..527 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_009573" FT VARIANT 2058 FT /note="H -> P (in dbSNP:rs2273709)" FT /id="VAR_048844" FT VARIANT 2180 FT /note="T -> I (in dbSNP:rs11962520)" FT /id="VAR_048845" FT CONFLICT 527 FT /note="E -> G (in Ref. 3; CAH18696)" FT /evidence="ECO:0000305" FT CONFLICT 663 FT /note="E -> K (in Ref. 1; AAN61516)" FT /evidence="ECO:0000305" FT CONFLICT 1171 FT /note="E -> K (in Ref. 3; CAH18328)" FT /evidence="ECO:0000305" FT CONFLICT 1230 FT /note="M -> T (in Ref. 3; CAH18328)" FT /evidence="ECO:0000305" FT CONFLICT 1268 FT /note="N -> S (in Ref. 3; CAH18328)" FT /evidence="ECO:0000305" FT CONFLICT 1277 FT /note="R -> H (in Ref. 3; CAH18328)" FT /evidence="ECO:0000305" FT CONFLICT 1830..1857 FT /note="Missing (in Ref. 3; CAH18696)" FT /evidence="ECO:0000305" FT CONFLICT 2049 FT /note="L -> P (in Ref. 3; CAH18696)" FT /evidence="ECO:0000305" FT CONFLICT 2058..2059 FT /note="HQ -> PL (in Ref. 3; CAH18696)" FT /evidence="ECO:0000305" FT CONFLICT 2345 FT /note="V -> VV (in Ref. 5; EAX04163)" FT /evidence="ECO:0000305" FT HELIX 376..382 FT /evidence="ECO:0007829|PDB:2JUF" FT STRAND 388..393 FT /evidence="ECO:0007829|PDB:2JUF" FT STRAND 403..408 FT /evidence="ECO:0007829|PDB:2JUF" FT STRAND 411..413 FT /evidence="ECO:0007829|PDB:2JUF" FT STRAND 416..420 FT /evidence="ECO:0007829|PDB:2JUF" FT TURN 421..424 FT /evidence="ECO:0007829|PDB:2JUF" FT STRAND 425..429 FT /evidence="ECO:0007829|PDB:2JUF" FT HELIX 431..433 FT /evidence="ECO:0007829|PDB:2JUF" SQ SEQUENCE 2517 AA; 281229 MW; 42387A55DCC52EAF CRC64; MVGERHAGDL MVPLGPRLQA YPEELIRQRP GHDGHPEYLI RWSVLKCGEV GKVGVEEGKA EHILMWLSAP EVYANCPGLL GERALSKGLQ HEPAGVSGSF PRDPGGLDEV AMGEMEADVQ ALVRRAARQL AESGTPSLTA AVLHTIHVLS AYASIGPLTG VFRETGALDL LMHMLCNPEP QIRRSAGKML QALAAHDAGS RAHVLLSLSQ QDGIEQHMDF DSRYTLLELF AETTSSEEHC MAFEGIHLPQ IPGKLLFSLV KRYLCVTSLL DQLNSSPELG AGDQSSPCAT REKSRGQREL EFSMAVGNLI SELVRSMGWA RNLSEQGMSP PRPTRSIFQP YISGPSLLLP TIVTTPRRQG WVFRQRSEFS SRSGYGEYVQ QTLQPGMRVR MLDDYEEISA GDEGEFRQSN NGIPPVQVFW QSTGRTYWVH WHMLEILGPE EATEDKASAA VEKGAGATVL GTAFPSWDWN PMDGLYPLPY LQPEPQKNER VGYLTQAEWW ELLFFIKKLD LCEQQPIFQN LWKNLDETLG EKALGEISVS VEMAESLLQV LSSRFEGSTL NDLLNSQIYT KYGLLSNEPS SSSTSRNHSC TPDPEEESKS EASFSEEETE SLKAKAEAPK TEAEPTKTRT ETPMAQSDSQ LFNQLLVTEG MTLPTEMKEA ASEMARALRG PGPRSSLDQH VAAVVATVQI SSLDTNLQLS GLSALSQAVE EVTERDHPLV RPDRSLREKL VKMLVELLTN QVGEKMVVVQ ALRLLYLLMT KHEWRPLFAR EGGIYAVLVC MQEYKTSVLV QQAGLAALKM LAVASSSEIP TFVTGRDSIH SLFDAQMTRE IFASIDSATR PGSESLLLTV PAAVILMLNT EGCSSAARNG LLLLNLLLCN HHTLGDQIIT QELRDTLFRH SGIAPRTEPM PTTRTILMML LNRYSEPPGS PERAALETPI IQGQDGSPEL LIRSLVGGPS AELLLDLERV LCREGSPGGA VRPLLKRLQQ ETQPFLLLLR TLDAPGPNKT LLLSVLRVIT RLLDFPEAMV LPWHEVLEPC LNCLSGPSSD SEIVQELTCF LHRLASMHKD YAVVLCCLGA KEILSKVLDK HSAQLLLGCE LRDLVTECEK YAQLYSNLTS SILAGCIQMV LGQIEDHRRT HQPINIPFFD VFLRHLCQGS SVEVKEDKCW EKVEVSSNPH RASKLTDHNP KTYWESNGST GSHYITLHMH RGVLVRQLTL LVASEDSSYM PARVVVFGGD STSCIGTELN TVNVMPSASR VILLENLNRF WPIIQIRIKR CQQGGIDTRV RGVEVLGPKP TFWPLFREQL CRRTCLFYTI RAQAWSRDIA EDHRRLLQLC PRLNRVLRHE QNFADRFLPD DEAAQALGKT CWEALVSPLV QNITSPDAEG VSALGWLLDQ YLEQRETSRN PLSRAASFAS RVRRLCHLLV HVEPPPGPSP EPSTRPFSKN SKGRDRSPAP SPVLPSSSLR NITQCWLSVV QEQVSRFLAA AWRAPDFVPR YCKLYEHLQR AGSELFGPRA AFMLALRSGF SGALLQQSFL TAAHMSEQFA RYIDQQIQGG LIGGAPGVEM LGQLQRHLEP IMVLSGLELA TTFEHFYQHY MADRLLSFGS SWLEGAVLEQ IGLCFPNRLP QLMLQSLSTS EELQRQFHLF QLQRLDKLFL EQEDEEEKRL EEEEEEEEEE EAEKELFIED PSPAISILVL SPRCWPVSPL CYLYHPRKCL PTEFCDALDR FSSFYSQSQN HPVLDMGPHR RLQWTWLGRA ELQFGKQILH VSTVQMWLLL KFNQTEEVSV ETLLKDSDLS PELLLQALVP LTSGNGPLTL HEGQDFPHGG VLRLHEPGPQ RSGEALWLIP PQAYLNVEKD EGRTLEQKRN LLSCLLVRIL KAHGEKGLHI DQLVCLVLEA WQKGPNPPGT LGHTVAGGVA CTSTDVLSCI LHLLGQGYVK RRDDRPQILM YAAPEPMGPC RGQADVPFCG SQSETSKPSP EAVATLASLQ LPAGRTMSPQ EVEGLMKQTV RQVQETLNLE PDVAQHLLAH SHWGAEQLLQ SYSEDPEPLL LAAGLCVHQA QAVPVRPDHC PVCVSPLGCD DDLPSLCCMH YCCKSCWNEY LTTRIEQNLV LNCTCPIADC PAQPTGAFIR AIVSSPEVIS KYEKALLRGY VESCSNLTWC TNPQGCDRIL CRQGLGCGTT CSKCGWASCF NCSFPEAHYP ASCGHMSQWV DDGGYYDGMS VEAQSKHLAK LISKRCPSCQ APIEKNEGCL HMTCAKCNHG FCWRCLKSWK PNHKDYYNCS AMVSKAARQE KRFQDYNERC TFHHQAREFA VNLRNRVSAI HEVPPPRSFT FLNDACQGLE QARKVLAYAC VYSFYSQDAE YMDVVEQQTE NLELHTNALQ ILLEETLLRC RDLASSLRLL RADCLSTGME LLRRIQERLL AILQHSAQDF RVGLQSPSVE AWEAKGPNMP GSQPQASSGP EAEEEEEDDE DDVPEWQQDE FDEELDNDSF SYDESENLDQ ETFFFGDEEE DEDEAYD //