CDC6_HUMAN
ID CDC6_HUMAN Reviewed; 560 AA.
AC Q99741; Q8TB30;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Cell division control protein 6 homolog;
DE AltName: Full=CDC6-related protein;
DE AltName: Full=Cdc18-related protein;
DE Short=HsCdc18;
DE AltName: Full=p62(cdc6);
DE Short=HsCDC6;
GN Name=CDC6; Synonyms=CDC18L;
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=8990175; DOI=10.1073/pnas.94.1.142;
RA Williams R.S., Shohet R.V., Stillman B.;
RT "A human protein related to yeast Cdc6p.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:142-147(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH
RP PCNA; ORC1 AND CYCLIN-CDK.
RX PubMed=9566895; DOI=10.1128/mcb.18.5.2758;
RA Saha P., Chen J., Thome K.C., Lawlis S.J., Hou Z.H., Hendricks M.,
RA Parvin J.D., Dutta A.;
RT "Human CDC6/Cdc18 associates with Orc1 and cyclin-cdk and is selectively
RT eliminated from the nucleus at the onset of S phase.";
RL Mol. Cell. Biol. 18:2758-2767(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-238; ASN-295; MET-299;
RP HIS-378 AND ILE-441.
RG NIEHS SNPs program;
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-441.
RC TISSUE=Brain;
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 [5]
RP INTERACTION WITH CDT1.
RX PubMed=14672932; DOI=10.1074/jbc.m311933200;
RA Cook J.G., Chasse D.A.D., Nevins J.R.;
RT "The regulated association of Cdt1 with minichromosome maintenance proteins
RT and Cdc6 in mammalian cells.";
RL J. Biol. Chem. 279:9625-9633(2004).
RN [6]
RP INTERACTION WITH HUWE1.
RX PubMed=17567951; DOI=10.1091/mbc.e07-02-0173;
RA Hall J.R., Kow E., Nevis K.R., Lu C.K., Luce K.S., Zhong Q., Cook J.G.;
RT "Cdc6 stability is regulated by the Huwe1 ubiquitin ligase after DNA
RT damage.";
RL Mol. Biol. Cell 18:3340-3350(2007).
RN [7]
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 [8]
RP INTERACTION WITH TTC4.
RX PubMed=18320024; DOI=10.1371/journal.pone.0001737;
RA Crevel G., Bennett D., Cotterill S.;
RT "The human TPR protein TTC4 is a putative Hsp90 co-chaperone which
RT interacts with CDC6 and shows alterations in transformed cells.";
RL PLoS ONE 3:E0001737-E0001737(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-127, 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP INTERACTION WITH ANKRD17.
RX PubMed=23711367; DOI=10.1016/j.febslet.2013.05.037;
RA Menning M., Kufer T.A.;
RT "A role for the Ankyrin repeat containing protein Ankrd17 in Nod1- and
RT Nod2-mediated inflammatory responses.";
RL FEBS Lett. 587:2137-2142(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-106, AND
RP 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 [14]
RP INTERACTION WITH GRWD1.
RX PubMed=25990725; DOI=10.1093/nar/gkv509;
RA Sugimoto N., Maehara K., Yoshida K., Yasukouchi S., Osano S., Watanabe S.,
RA Aizawa M., Yugawa T., Kiyono T., Kurumizaka H., Ohkawa Y., Fujita M.;
RT "Cdt1-binding protein GRWD1 is a novel histone-binding protein that
RT facilitates MCM loading through its influence on chromatin architecture.";
RL Nucleic Acids Res. 43:5898-5911(2015).
RN [15]
RP FUNCTION, INTERACTION WITH CCNF AND CDH1, SUBCELLULAR LOCATION,
RP UBIQUITINATION, AND MUTAGENESIS OF SER-54; SER-74 AND SER-106.
RX PubMed=26818844; DOI=10.1038/ncomms10530;
RA Walter D., Hoffmann S., Komseli E.S., Rappsilber J., Gorgoulis V.,
RA Soerensen C.S.;
RT "SCF(Cyclin F)-dependent degradation of CDC6 suppresses DNA re-
RT replication.";
RL Nat. Commun. 7:10530-10530(2016).
RN [16]
RP VARIANT MGORS5 ARG-323.
RX PubMed=21358632; DOI=10.1038/ng.775;
RA Bicknell L.S., Bongers E.M., Leitch A., Brown S., Schoots J., Harley M.E.,
RA Aftimos S., Al-Aama J.Y., Bober M., Brown P.A., van Bokhoven H., Dean J.,
RA Edrees A.Y., Feingold M., Fryer A., Hoefsloot L.H., Kau N., Knoers N.V.,
RA Mackenzie J., Opitz J.M., Sarda P., Ross A., Temple I.K., Toutain A.,
RA Wise C.A., Wright M., Jackson A.P.;
RT "Mutations in the pre-replication complex cause Meier-Gorlin syndrome.";
RL Nat. Genet. 43:356-359(2011).
CC -!- FUNCTION: Involved in the initiation of DNA replication. Also
CC participates in checkpoint controls that ensure DNA replication is
CC completed before mitosis is initiated.
CC -!- SUBUNIT: Interacts with PCNA, ORC1, cyclin-CDK (PubMed:9566895).
CC Interacts with HUWE1 (PubMed:17567951). Interacts with ANKRD17
CC (PubMed:23711367). Interacts with GRWD1; origin binding of GRWD1 is
CC dependent on CDC6 (PubMed:25990725). Interacts with CDT1; are mutually
CC dependent on one another for loading MCM complexes onto chromatin
CC (PubMed:14672932). Interacts with TTC4 (PubMed:18320024). Interacts
CC (via Cy motif) with CCNF; the interaction takes place during G2 and M
CC phase (PubMed:26818844). Interacts with CDH1 (PubMed:26818844).
CC {ECO:0000269|PubMed:14672932, ECO:0000269|PubMed:17567951,
CC ECO:0000269|PubMed:18320024, ECO:0000269|PubMed:23711367,
CC ECO:0000269|PubMed:25990725, ECO:0000269|PubMed:26818844,
CC ECO:0000269|PubMed:9566895}.
CC -!- INTERACTION:
CC Q99741; P06493: CDK1; NbExp=2; IntAct=EBI-374862, EBI-444308;
CC Q99741; P38936: CDKN1A; NbExp=2; IntAct=EBI-374862, EBI-375077;
CC Q99741; Q9H211: CDT1; NbExp=3; IntAct=EBI-374862, EBI-456953;
CC Q99741; P53350: PLK1; NbExp=6; IntAct=EBI-374862, EBI-476768;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26818844,
CC ECO:0000269|PubMed:9566895}. Cytoplasm {ECO:0000269|PubMed:9566895}.
CC Note=The protein is nuclear in G1 and cytoplasmic in S-phase cells
CC (PubMed:9566895). {ECO:0000269|PubMed:9566895}.
CC -!- PTM: Ubiquitinated by the SCF(CCNF) E3 ubiquitin-protein ligase
CC complex. {ECO:0000269|PubMed:26818844}.
CC -!- DISEASE: Meier-Gorlin syndrome 5 (MGORS5) [MIM:613805]: A syndrome
CC characterized by bilateral microtia, aplasia/hypoplasia of the
CC patellae, and severe intrauterine and postnatal growth retardation with
CC short stature and poor weight gain. Additional clinical findings
CC include anomalies of cranial sutures, microcephaly, apparently low-set
CC and simple ears, microstomia, full lips, highly arched or cleft palate,
CC micrognathia, genitourinary tract anomalies, and various skeletal
CC anomalies. While almost all cases have primordial dwarfism with
CC substantial prenatal and postnatal growth retardation, not all cases
CC have microcephaly, and microtia and absent/hypoplastic patella are
CC absent in some. Despite the presence of microcephaly, intellect is
CC usually normal. {ECO:0000269|PubMed:21358632}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CDC6/cdc18 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CDC6ID40014ch17q21.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/cdc6/";
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DR EMBL; U77949; AAB38317.1; -; mRNA.
DR EMBL; AF022109; AAC52071.1; -; mRNA.
DR EMBL; AY150310; AAN10296.1; -; Genomic_DNA.
DR EMBL; BC025232; AAH25232.1; -; mRNA.
DR CCDS; CCDS11365.1; -.
DR RefSeq; NP_001245.1; NM_001254.3.
DR PDB; 2CCH; X-ray; 1.70 A; E/F=89-100.
DR PDB; 2CCI; X-ray; 2.70 A; F/I=71-100.
DR PDB; 4I5L; X-ray; 2.43 A; B/E=70-90.
DR PDB; 4I5N; X-ray; 2.80 A; B/E=70-90.
DR PDBsum; 2CCH; -.
DR PDBsum; 2CCI; -.
DR PDBsum; 4I5L; -.
DR PDBsum; 4I5N; -.
DR AlphaFoldDB; Q99741; -.
DR SMR; Q99741; -.
DR BioGRID; 107426; 117.
DR CORUM; Q99741; -.
DR DIP; DIP-28154N; -.
DR ELM; Q99741; -.
DR IntAct; Q99741; 45.
DR MINT; Q99741; -.
DR STRING; 9606.ENSP00000209728; -.
DR ChEMBL; CHEMBL2311228; -.
DR GlyGen; Q99741; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99741; -.
DR PhosphoSitePlus; Q99741; -.
DR BioMuta; CDC6; -.
DR DMDM; 50400620; -.
DR EPD; Q99741; -.
DR jPOST; Q99741; -.
DR MassIVE; Q99741; -.
DR MaxQB; Q99741; -.
DR PaxDb; Q99741; -.
DR PeptideAtlas; Q99741; -.
DR PRIDE; Q99741; -.
DR ProteomicsDB; 78452; -.
DR Antibodypedia; 16461; 809 antibodies from 42 providers.
DR DNASU; 990; -.
DR Ensembl; ENST00000209728.9; ENSP00000209728.4; ENSG00000094804.12.
DR Ensembl; ENST00000649662.1; ENSP00000497345.1; ENSG00000094804.12.
DR GeneID; 990; -.
DR KEGG; hsa:990; -.
DR MANE-Select; ENST00000209728.9; ENSP00000209728.4; NM_001254.4; NP_001245.1.
DR UCSC; uc002huj.2; human.
DR CTD; 990; -.
DR DisGeNET; 990; -.
DR GeneCards; CDC6; -.
DR HGNC; HGNC:1744; CDC6.
DR HPA; ENSG00000094804; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; CDC6; -.
DR MIM; 602627; gene.
DR MIM; 613805; phenotype.
DR neXtProt; NX_Q99741; -.
DR OpenTargets; ENSG00000094804; -.
DR Orphanet; 2554; Ear-patella-short stature syndrome.
DR PharmGKB; PA26271; -.
DR VEuPathDB; HostDB:ENSG00000094804; -.
DR eggNOG; KOG2227; Eukaryota.
DR GeneTree; ENSGT00530000063498; -.
DR HOGENOM; CLU_012774_3_0_1; -.
DR InParanoid; Q99741; -.
DR OMA; DMLGIIN; -.
DR OrthoDB; 935804at2759; -.
DR PhylomeDB; Q99741; -.
DR TreeFam; TF101051; -.
DR PathwayCommons; Q99741; -.
DR Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
DR Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
DR Reactome; R-HSA-68689; CDC6 association with the ORC:origin complex.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-68962; Activation of the pre-replicative complex.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69205; G1/S-Specific Transcription.
DR SignaLink; Q99741; -.
DR SIGNOR; Q99741; -.
DR BioGRID-ORCS; 990; 721 hits in 1091 CRISPR screens.
DR ChiTaRS; CDC6; human.
DR EvolutionaryTrace; Q99741; -.
DR GeneWiki; CDC6; -.
DR GenomeRNAi; 990; -.
DR Pharos; Q99741; Tbio.
DR PRO; PR:Q99741; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q99741; protein.
DR Bgee; ENSG00000094804; Expressed in ventricular zone and 112 other tissues.
DR ExpressionAtlas; Q99741; baseline and differential.
DR Genevisible; Q99741; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; IDA:BHF-UCL.
DR GO; GO:0000922; C:spindle pole; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR GO; GO:0019900; F:kinase binding; IPI:BHF-UCL.
DR GO; GO:0000166; F:nucleotide binding; TAS:ProtInc.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1904385; P:cellular response to angiotensin; IEA:Ensembl.
DR GO; GO:1904117; P:cellular response to vasopressin; IEA:Ensembl.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; TAS:ProtInc.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0008156; P:negative regulation of DNA replication; TAS:ProtInc.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IDA:BHF-UCL.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP:BHF-UCL.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IMP:BHF-UCL.
DR GO; GO:0007089; P:traversing start control point of mitotic cell cycle; TAS:ProtInc.
DR CDD; cd08768; Cdc6_C; 1.
DR DisProt; DP01703; -.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR IDEAL; IID00099; -.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041083; AAA_lid_10.
DR InterPro; IPR016314; Cdc6/18.
DR InterPro; IPR015163; Cdc6_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF13401; AAA_22; 1.
DR Pfam; PF17872; AAA_lid_10; 1.
DR Pfam; PF09079; Cdc6_C; 1.
DR PIRSF; PIRSF001767; Cdc6; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01074; Cdc6_C; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Cytoplasm;
KW Disease variant; DNA replication; Dwarfism; Mitosis; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..560
FT /note="Cell division control protein 6 homolog"
FT /id="PRO_0000150979"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 93..100
FT /note="Cy"
FT /evidence="ECO:0000303|PubMed:26818844"
FT COMPBIAS 25..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 202..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 67
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O89033"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O89033"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O89033"
FT VARIANT 238
FT /note="T -> A (in dbSNP:rs4135010)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_019349"
FT VARIANT 295
FT /note="D -> N (in dbSNP:rs4135012)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_019350"
FT VARIANT 299
FT /note="T -> M (in dbSNP:rs4135013)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_019351"
FT VARIANT 323
FT /note="T -> R (in MGORS5; dbSNP:rs387906842)"
FT /evidence="ECO:0000269|PubMed:21358632"
FT /id="VAR_065493"
FT VARIANT 378
FT /note="R -> H (in dbSNP:rs4135016)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_019352"
FT VARIANT 441
FT /note="V -> I (in dbSNP:rs13706)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_019353"
FT MUTAGEN 54
FT /note="S->A: Does not change protein stability after CHX
FT addition during mitosis; when associated with A-74 and A-
FT 106."
FT /evidence="ECO:0000269|PubMed:26818844"
FT MUTAGEN 54
FT /note="S->D: Does not change protein stability after CHX
FT addition during mitosis; when associated with D-74 and D-
FT 106."
FT /evidence="ECO:0000269|PubMed:26818844"
FT MUTAGEN 74
FT /note="S->A: Does not change protein stability after CHX
FT addition during mitosis; when associated with A-54 and A-
FT 106."
FT /evidence="ECO:0000269|PubMed:26818844"
FT MUTAGEN 74
FT /note="S->D: Does not change protein stability after CHX
FT addition during mitosis; when associated with D-54 and D-
FT 106."
FT /evidence="ECO:0000269|PubMed:26818844"
FT MUTAGEN 93..100
FT /note="Missing: Disrupts the interaction with CCNF. Does
FT not disrupt the interaction with CDH1. Increases protein
FT stability."
FT /evidence="ECO:0000269|PubMed:26818844"
FT MUTAGEN 106
FT /note="S->A: Does not change protein stability after CHX
FT addition during mitosis; when associated with A-54 and A-
FT 74."
FT /evidence="ECO:0000269|PubMed:26818844"
FT MUTAGEN 106
FT /note="S->D: Does not change protein stability after CHX
FT addition during mitosis; when associated with D-54 and D-
FT 74."
FT /evidence="ECO:0000269|PubMed:26818844"
SQ SEQUENCE 560 AA; 62720 MW; 3ED7DE4AF80CB017 CRC64;
MPQTRSQAQA TISFPKRKLS RALNKAKNSS DAKLEPTNVQ TVTCSPRVKA LPLSPRKRLG
DDNLCNTPHL PPCSPPKQGK KENGPPHSHT LKGRRLVFDN QLTIKSPSKR ELAKVHQNKI
LSSVRKSQEI TTNSEQRCPL KKESACVRLF KQEGTCYQQA KLVLNTAVPD RLPAREREMD
VIRNFLREHI CGKKAGSLYL SGAPGTGKTA CLSRILQDLK KELKGFKTIM LNCMSLRTAQ
AVFPAIAQEI CQEEVSRPAG KDMMRKLEKH MTAEKGPMIV LVLDEMDQLD SKGQDVLYTL
FEWPWLSNSH LVLIGIANTL DLTDRILPRL QAREKCKPQL LNFPPYTRNQ IVTILQDRLN
QVSRDQVLDN AAVQFCARKV SAVSGDVRKA LDVCRRAIEI VESDVKSQTI LKPLSECKSP
SEPLIPKRVG LIHISQVISE VDGNRMTLSQ EGAQDSFPLQ QKILVCSLML LIRQLKIKEV
TLGKLYEAYS KVCRKQQVAA VDQSECLSLS GLLEARGILG LKRNKETRLT KVFFKIEEKE
IEHALKDKAL IGNILATGLP
