CUL9_HUMAN
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 03-AUG-2022, entry version 181.
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=5; 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};
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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; 167.
DR CORUM; Q8IWT3; -.
DR IntAct; Q8IWT3; 14.
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; Q8IWT3; -.
DR PeptideAtlas; Q8IWT3; -.
DR PRIDE; Q8IWT3; -.
DR ProteomicsDB; 70891; -. [Q8IWT3-1]
DR ProteomicsDB; 70892; -. [Q8IWT3-3]
DR Antibodypedia; 3078; 165 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 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; 469819at2759; -.
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 1114 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 182 other tissues.
DR ExpressionAtlas; Q8IWT3; baseline and differential.
DR Genevisible; Q8IWT3; HS.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase 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 Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021097; CPH_domain.
DR InterPro; IPR031222; CUL9.
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; IPR014722; Rib_L2_dom2.
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:SF2; PTHR22771:SF2; 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; SSF48371; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF75632; SSF75632; 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.
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
