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 27-MAR-2024, entry version 199. 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="https://atlasgeneticsoncology.org/gene/40014/CDC6"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/cdc6/"; 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; 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; 120. 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; 9606-ENSP00000209728; -. DR PeptideAtlas; Q99741; -. DR ProteomicsDB; 78452; -. DR Pumba; Q99741; -. DR Antibodypedia; 16461; 920 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 AGR; HGNC:1744; -. 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; NCEVIDT; -. DR OrthoDB; 118994at2759; -. 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; 752 hits in 1170 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 114 other cell types or tissues. DR ExpressionAtlas; Q99741; baseline and differential. 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:0016887; F:ATP hydrolysis activity; IEA:InterPro. 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: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: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; cd00009; AAA; 1. DR CDD; cd08768; Cdc6_C; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 PANTHER; PTHR10763:SF26; CELL DIVISION CONTROL PROTEIN 6 HOMOLOG; 1. DR PANTHER; PTHR10763; CELL DIVISION CONTROL PROTEIN 6-RELATED; 1. 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR Genevisible; Q99741; HS. 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 FT A-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 FT D-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 FT A-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 FT D-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 FT A-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 FT D-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 //