CDCA3_HUMAN
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 03-AUG-2022, entry version 156.
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}.
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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; 158.
DR IntAct; Q99618; 48.
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; Q99618; -.
DR PeptideAtlas; Q99618; -.
DR PRIDE; Q99618; -.
DR ProteomicsDB; 78361; -.
DR Antibodypedia; 11223; 202 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 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; GHNKENQ; -.
DR OrthoDB; 1398970at2759; -.
DR PhylomeDB; Q99618; -.
DR TreeFam; TF101068; -.
DR PathwayCommons; Q99618; -.
DR SignaLink; Q99618; -.
DR SIGNOR; Q99618; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 83461; 127 hits in 1083 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 125 other tissues.
DR ExpressionAtlas; Q99618; baseline and differential.
DR Genevisible; Q99618; HS.
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; PTHR34756; 1.
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
