ID CDCA3_HUMAN Reviewed; 268 AA. AC Q99618; A8K5V6; D3DUS6; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 27-MAR-2024, entry version 165. DE RecName: Full=Cell division cycle-associated protein 3; DE AltName: Full=Gene-rich cluster protein C8; DE AltName: Full=Trigger of mitotic entry protein 1; DE Short=TOME-1; GN Name=CDCA3; Synonyms=C8, GRCC8, TOME1; 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]. RX PubMed=12188893; DOI=10.2174/1568009013334241; RA Walker M.G.; RT "Drug target discovery by gene expression analysis: cell cycle genes."; RL Curr. Cancer Drug Targets 1:73-83(2001). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Brain; RX PubMed=9074930; DOI=10.1101/gr.7.3.268; RA Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.; RT "Large-scale sequencing in human chromosome 12p13: experimental and RT computational gene structure determination."; RL Genome Res. 7:268-280(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [4] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta, and Testis; 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-209, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; THR-202 AND SER-209, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-209, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-31; THR-37; SER-44; RP SER-64; THR-76; SER-87; SER-199 AND SER-209, AND IDENTIFICATION BY MASS RP 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND SER-199, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-199 AND SER-209, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-68; THR-76; SER-87; RP SER-94 AND SER-209, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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). CC -!- FUNCTION: F-box-like protein which is required for entry into mitosis. CC Acts by participating in E3 ligase complexes that mediate the CC ubiquitination and degradation of WEE1 kinase at G2/M phase (By CC similarity). {ECO:0000250}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Interacts with SKP1. Part of a SCF (SKP1-cullin-F-box) protein CC ligase complex (By similarity). {ECO:0000250}. CC -!- INTERACTION: CC Q99618; Q9GZU7: CTDSP1; NbExp=10; IntAct=EBI-739534, EBI-751587; CC Q99618; O14595: CTDSP2; NbExp=10; IntAct=EBI-739534, EBI-2802973; CC Q99618; O15194-2: CTDSPL; NbExp=4; IntAct=EBI-739534, EBI-12134515; CC Q99618; Q13077: TRAF1; NbExp=6; IntAct=EBI-739534, EBI-359224; CC Q99618; Q12933: TRAF2; NbExp=7; IntAct=EBI-739534, EBI-355744; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. CC -!- DOMAIN: The KEN box is required for the association with the APC/C-Cdh1 CC complex. {ECO:0000250}. CC -!- PTM: Ubiquitinated and degraded by the APC/C-Cdh1 complex. CC {ECO:0000250}. 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; BG354576; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; U47924; AAB51327.1; -; Genomic_DNA. DR EMBL; AK291421; BAF84110.1; -; mRNA. DR EMBL; CH471116; EAW88728.1; -; Genomic_DNA. DR EMBL; CH471116; EAW88729.1; -; Genomic_DNA. DR EMBL; BC002551; AAH02551.1; -; mRNA. DR EMBL; BC036512; AAH36512.1; -; mRNA. DR CCDS; CCDS8565.1; -. DR RefSeq; NP_001284532.1; NM_001297603.2. DR RefSeq; NP_001284533.1; NM_001297604.2. DR RefSeq; NP_001317948.1; NM_001331019.1. DR RefSeq; NP_112589.1; NM_031299.6. DR AlphaFoldDB; Q99618; -. DR BioGRID; 123657; 194. DR IntAct; Q99618; 74. DR MINT; Q99618; -. DR STRING; 9606.ENSP00000442068; -. DR GlyGen; Q99618; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q99618; -. DR PhosphoSitePlus; Q99618; -. DR BioMuta; CDCA3; -. DR DMDM; 74732787; -. DR EPD; Q99618; -. DR jPOST; Q99618; -. DR MassIVE; Q99618; -. DR MaxQB; Q99618; -. DR PaxDb; 9606-ENSP00000442068; -. DR PeptideAtlas; Q99618; -. DR ProteomicsDB; 78361; -. DR Pumba; Q99618; -. DR Antibodypedia; 11223; 223 antibodies from 33 providers. DR DNASU; 83461; -. DR Ensembl; ENST00000535406.5; ENSP00000446339.1; ENSG00000111665.12. DR Ensembl; ENST00000538862.7; ENSP00000442068.1; ENSG00000111665.12. DR GeneID; 83461; -. DR KEGG; hsa:83461; -. DR MANE-Select; ENST00000538862.7; ENSP00000442068.1; NM_031299.7; NP_112589.1. DR UCSC; uc001qrg.3; human. DR AGR; HGNC:14624; -. DR CTD; 83461; -. DR DisGeNET; 83461; -. DR GeneCards; CDCA3; -. DR HGNC; HGNC:14624; CDCA3. DR HPA; ENSG00000111665; Tissue enhanced (lymphoid tissue, retina). DR MalaCards; CDCA3; -. DR MIM; 607749; gene. DR neXtProt; NX_Q99618; -. DR OpenTargets; ENSG00000111665; -. DR PharmGKB; PA26276; -. DR VEuPathDB; HostDB:ENSG00000111665; -. DR eggNOG; ENOG502S7V2; Eukaryota. DR GeneTree; ENSGT00390000017343; -. DR InParanoid; Q99618; -. DR OMA; KITGRAW; -. DR OrthoDB; 5399400at2759; -. DR PhylomeDB; Q99618; -. DR TreeFam; TF101068; -. DR PathwayCommons; Q99618; -. DR SignaLink; Q99618; -. DR SIGNOR; Q99618; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 83461; 149 hits in 1159 CRISPR screens. DR ChiTaRS; CDCA3; human. DR GeneWiki; CDCA3; -. DR GenomeRNAi; 83461; -. DR Pharos; Q99618; Tbio. DR PRO; PR:Q99618; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q99618; Protein. DR Bgee; ENSG00000111665; Expressed in ventricular zone and 127 other cell types or tissues. DR ExpressionAtlas; Q99618; baseline and differential. DR GO; GO:0005912; C:adherens junction; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. DR InterPro; IPR038832; CDCA3. DR PANTHER; PTHR34756; CELL DIVISION CYCLE-ASSOCIATED PROTEIN 3; 1. DR PANTHER; PTHR34756:SF1; CELL DIVISION CYCLE-ASSOCIATED PROTEIN 3; 1. DR Genevisible; Q99618; HS. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Cytoplasm; Mitosis; Phosphoprotein; KW Reference proteome; Ubl conjugation; Ubl conjugation pathway. FT CHAIN 1..268 FT /note="Cell division cycle-associated protein 3" FT /id="PRO_0000287708" FT REGION 1..232 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 91..120 FT /note="F-box-like" FT REGION 247..268 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 258..260 FT /note="KEN box" FT COMPBIAS 74..88 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 133..148 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 158..224 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 250..268 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 29 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 31 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 37 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 44 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 64 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 68 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 76 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 87 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 94 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 199 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231" FT MOD_RES 202 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18220336" FT MOD_RES 209 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 212 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q99M54" SQ SEQUENCE 268 AA; 28998 MW; 48933FA7FF57112C CRC64; MGSAKSVPVT PARPPPHNKH LARVADPRSP SAGILRTPIQ VESSPQPGLP AGEQLEGLKH AQDSDPRSPT LGIARTPMKT SSGDPPSPLV KQLSEVFETE DSKSNLPPEP VLPPEAPLSS ELDLPLGTQL SVEEQMPPWN QTEFPSKQVF SKEEARQPTE TPVASQSSDK PSRDPETPRS SGSMRNRWKP NSSKVLGRSP LTILQDDNSP GTLTLRQGKR PSPLSENVSE LKEGAILGTG RLLKTGGRAW EQGQDHDKEN QHFPLVES //