ID CAF1A_HUMAN Reviewed; 956 AA. AC Q13111; Q6NXG5; Q7Z7K3; Q9UJY8; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2018, sequence version 3. DT 27-MAR-2024, entry version 207. DE RecName: Full=Chromatin assembly factor 1 subunit A {ECO:0000305}; DE Short=CAF-1 subunit A; DE AltName: Full=Chromatin assembly factor I p150 subunit; DE Short=CAF-I 150 kDa subunit; DE Short=CAF-I p150; DE Short=hp150; GN Name=CHAF1A {ECO:0000312|HGNC:HGNC:1910}; Synonyms=CAF, CAF1P150; 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 [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND RP 3), AND VARIANT VAL-923. RX PubMed=11250073; DOI=10.1016/s0378-1119(01)00335-3; RA Dong H., Lin W., Zhang C.-K., Xiong H., Fu G., Jin W.-R., Chen R., Chen Z., RA Qi Z.-T., Huang G.M.; RT "Genomic sequence and expression analyses of human chromatin assembly RT factor 1 p150 gene."; RL Gene 264:187-196(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Ovary; 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-956 (ISOFORM 1), AND VARIANT VAL-923. RC TISSUE=Cervix adenocarcinoma; RX PubMed=7600578; DOI=10.1016/s0092-8674(05)80015-7; RA Kaufman P.D., Kobayashi R., Kessler N., Stillman B.; RT "The p150 and p60 subunits of chromatin assembly factor I: a molecular link RT between newly synthesized histones and DNA replication."; RL Cell 81:1105-1114(1995). RN [5] RP INTERACTION WITH PCNA, AND SUBCELLULAR LOCATION. RX PubMed=10052459; DOI=10.1016/s0092-8674(00)80661-3; RA Shibahara K., Stillman B.; RT "Replication-dependent marking of DNA by PCNA facilitates CAF-1-coupled RT inheritance of chromatin."; RL Cell 96:575-585(1999). RN [6] RP INTERACTION WITH PCNA. RX PubMed=10648606; DOI=10.1128/mcb.20.4.1206-1218.2000; RA Moggs J.G., Grandi P., Quivy J.P., Jonsson Z.O., Hubscher U., Becker P.B., RA Almouzni G.; RT "A CAF-1-PCNA-mediated chromatin assembly pathway triggered by sensing DNA RT damage."; RL Mol. Cell. Biol. 20:1206-1218(2000). RN [7] RP REVIEW. RX PubMed=10893180; DOI=10.1242/jcs.113.15.2647; RA Ridgway P., Almouzni G.; RT "CAF-1 and the inheritance of chromatin states: at the crossroads of DNA RT replication and repair."; RL J. Cell Sci. 113:2647-2658(2000). RN [8] RP HOMODIMERIZATION. RX PubMed=11296234; DOI=10.1093/emboj/20.8.2015; RA Quivy J.-P., Grandi P., Almouzni G.; RT "Dimerization of the largest subunit of chromatin assembly factor 1: RT importance in vitro and during Xenopus early development."; RL EMBO J. 20:2015-2027(2001). RN [9] RP INTERACTION WITH MBD1. RX PubMed=12697822; DOI=10.1128/mcb.23.9.3226-3236.2003; RA Reese B.E., Bachman K.E., Baylin S.B., Rountree M.R.; RT "The methyl-CpG binding protein MBD1 interacts with the p150 subunit of RT chromatin assembly factor 1."; RL Mol. Cell. Biol. 23:3226-3236(2003). RN [10] RP RETRACTED PAPER, FUNCTION, AND INTERACTION WITH MBD1 AND SETDB1. RX PubMed=15327775; DOI=10.1016/j.molcel.2004.06.043; RA Sarraf S.A., Stancheva I.; RT "Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9 RT by SETDB1 to DNA replication and chromatin assembly."; RL Mol. Cell 15:595-605(2004). RN [11] RP RETRACTION NOTICE OF PUBMED:15327775. RX PubMed=30849389; DOI=10.1016/j.molcel.2019.02.023; RA Sarraf S.A., Stancheva I.; RT "Retraction Notice to: Methyl-CpG Binding Protein MBD1 Couples Histone H3 RT Methylation at Lysine 9 by SETDB1 to DNA Replication and Chromatin RT Assembly."; RL Mol. Cell 73:1084-1084(2019). RN [12] RP INTERACTION WITH CBX5. RX PubMed=15882967; DOI=10.1016/j.bbrc.2005.04.016; RA Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III; RT "The mammalian heterochromatin protein 1 binds diverse nuclear proteins RT through a common motif that targets the chromoshadow domain."; RL Biochem. Biophys. Res. Commun. 331:929-937(2005). RN [13] 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION BY RP 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; THR-722; SER-772; RP SER-775; SER-873 AND SER-951, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [16] 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 [17] 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 [18] RP INTERACTION WITH CBX5, AND MUTAGENESIS OF VAL-240 AND LEU-242. RX PubMed=20562864; DOI=10.1038/ncb2075; RA Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N., RA Kimura H., Obuse C.; RT "Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms RT through Aurora B activation."; RL Nat. Cell Biol. 12:719-727(2010). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-138; SER-141; RP SER-143; SER-224; THR-722; SER-772; THR-865; SER-873 AND SER-951, 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-141; SER-143; RP SER-206; THR-722; SER-772; SER-775 AND SER-951, AND IDENTIFICATION BY MASS RP 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-206; SER-310; RP SER-772; SER-803; SER-868 AND SER-873, AND IDENTIFICATION BY MASS RP 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 [22] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-182, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [23] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-182, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-182, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [25] RP INTERACTION WITH HISTONES H3.1; H3.2 AND H3.1T. RX PubMed=33857403; DOI=10.1016/j.molcel.2021.03.041; RA Hammond C.M., Bao H., Hendriks I.A., Carraro M., Garcia-Nieto A., Liu Y., RA Reveron-Gomez N., Spanos C., Chen L., Rappsilber J., Nielsen M.L., RA Patel D.J., Huang H., Groth A.; RT "DNAJC9 integrates heat shock molecular chaperones into the histone RT chaperone network."; RL Mol. Cell 0:0-0(2021). CC -!- FUNCTION: Core component of the CAF-1 complex, a complex that is CC thought to mediate chromatin assembly in DNA replication and DNA CC repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 CC performs the first step of the nucleosome assembly process, bringing CC newly synthesized histones H3 and H4 to replicating DNA; histones CC H2A/H2B can bind to this chromatin precursor subsequent to DNA CC replication to complete the histone octamer. It may play a role in CC heterochromatin maintenance in proliferating cells by bringing newly CC synthesized cbx proteins to heterochromatic DNA replication foci. CC {ECO:0000250|UniProtKB:Q5R1T0}. CC -!- SUBUNIT: Homodimer. Part of the CAF-1 complex that contains RBBP4, CC CHAF1B and CHAF1A. CHAF1A binds directly to CHAF1B. Only minor amounts CC of RBBP4 are complexed with CHAF1A and CHAF1B in G1 phase. CHAF1A binds CC directly to PCNA and to CBX1. Interacts with MBD1 (PubMed:12697822). CC Interacts directly with CBX5 via the PxVxL motif. Interacts with CBX5. CC Interacts with histones H3.1, H3.2 and H3.1t (PubMed:33857403). CC {ECO:0000269|PubMed:10052459, ECO:0000269|PubMed:10648606, CC ECO:0000269|PubMed:12697822, ECO:0000269|PubMed:15882967, CC ECO:0000269|PubMed:20562864, ECO:0000269|PubMed:33857403}. CC -!- INTERACTION: CC Q13111; P45973: CBX5; NbExp=8; IntAct=EBI-1020839, EBI-78219; CC Q13111; Q13111: CHAF1A; NbExp=3; IntAct=EBI-1020839, EBI-1020839; CC Q13111; Q99684: GFI1; NbExp=4; IntAct=EBI-1020839, EBI-949368; CC Q13111; P84243: H3-3B; NbExp=2; IntAct=EBI-1020839, EBI-120658; CC Q13111; Q71DI3: H3C15; NbExp=2; IntAct=EBI-1020839, EBI-750650; CC Q13111; Q9UIS9: MBD1; NbExp=3; IntAct=EBI-1020839, EBI-867196; CC Q13111; A8MW99: MEI4; NbExp=3; IntAct=EBI-1020839, EBI-19944212; CC Q13111; P16333: NCK1; NbExp=2; IntAct=EBI-1020839, EBI-389883; CC Q13111; A8MTQ0: NOTO; NbExp=3; IntAct=EBI-1020839, EBI-17490746; CC Q13111; P26367: PAX6; NbExp=3; IntAct=EBI-1020839, EBI-747278; CC Q13111; P12004: PCNA; NbExp=4; IntAct=EBI-1020839, EBI-358311; CC Q13111; P27986: PIK3R1; NbExp=2; IntAct=EBI-1020839, EBI-79464; CC Q13111; P78424: POU6F2; NbExp=3; IntAct=EBI-1020839, EBI-12029004; CC Q13111; Q04864: REL; NbExp=3; IntAct=EBI-1020839, EBI-307352; CC Q13111; Q04864-2: REL; NbExp=3; IntAct=EBI-1020839, EBI-10829018; CC Q13111; Q9UHV2: SERTAD1; NbExp=3; IntAct=EBI-1020839, EBI-748601; CC Q13111; P51692: STAT5B; NbExp=3; IntAct=EBI-1020839, EBI-1186119; CC Q13111; P15884: TCF4; NbExp=3; IntAct=EBI-1020839, EBI-533224; CC Q13111; P15884-3: TCF4; NbExp=3; IntAct=EBI-1020839, EBI-13636688; CC Q13111; Q96RU7: TRIB3; NbExp=5; IntAct=EBI-1020839, EBI-492476; CC Q13111; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-1020839, EBI-4395669; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10052459}. Note=DNA CC replication foci. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Experimental confirmation may be lacking for some isoforms.; CC Name=1; CC IsoId=Q13111-1; Sequence=Displayed; CC Name=2; CC IsoId=Q13111-2; Sequence=VSP_004149, VSP_004150; CC Name=3; CC IsoId=Q13111-3; Sequence=VSP_004151; CC -!- DEVELOPMENTAL STAGE: Active complex is found in G1, S and G2 phases. CC -!- DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is CC required for interaction with chromoshadow domains. This motif requires CC additional residues -7, -6, +4 and +5 of the central Val which contact CC the chromoshadow domain. CC -!- SIMILARITY: Belongs to the CHAF1A family. {ECO:0000305}. CC -!- CAUTION: Was reported to form, during DNA replication, a S phase- CC specific complex that would facilitate methylation of H3 'Lys-9' during CC replication-coupled chromatin assembly and vould be at least composed CC of the CAF-1 subunit CHAF1A, MBD1 and SETDB1 (PubMed:15327775). CC However, this paper has been retracted because some data, results and CC conclusions are not reliable (PubMed:30849389). CC {ECO:0000269|PubMed:15327775, ECO:0000269|PubMed:30849389}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA76736.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF04291.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH52620.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH52620.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 426.; Evidence={ECO:0000305}; 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; AF190465; AAF04291.1; ALT_INIT; Genomic_DNA. DR EMBL; AC011498; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF459577; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC052620; AAH52620.1; ALT_SEQ; mRNA. DR EMBL; BC067093; AAH67093.1; -; mRNA. DR EMBL; U20979; AAA76736.1; ALT_INIT; mRNA. DR CCDS; CCDS32875.1; -. [Q13111-1] DR PIR; A56731; A56731. DR RefSeq; NP_005474.2; NM_005483.2. [Q13111-1] DR PDB; 7Y5K; X-ray; 3.48 A; A=442-714. DR PDB; 7Y5L; X-ray; 3.42 A; A/D=442-714. DR PDB; 7Y5O; X-ray; 3.57 A; A/D=442-714. DR PDB; 7Y5U; EM; 3.80 A; A=442-853. DR PDB; 7Y5V; EM; 6.10 A; A/F=442-853. DR PDB; 7Y60; EM; 3.80 A; K=442-853. DR PDB; 7Y61; EM; 5.60 A; K/M=442-853. DR PDB; 8IQF; EM; 4.60 A; A/F=1-956. DR PDB; 8IQG; EM; 3.50 A; A=1-956. DR PDB; 8J6S; EM; 3.80 A; K=1-956. DR PDB; 8J6T; EM; 6.60 A; K/M=1-956. DR PDBsum; 7Y5K; -. DR PDBsum; 7Y5L; -. DR PDBsum; 7Y5O; -. DR PDBsum; 7Y5U; -. DR PDBsum; 7Y5V; -. DR PDBsum; 7Y60; -. DR PDBsum; 7Y61; -. DR PDBsum; 8IQF; -. DR PDBsum; 8IQG; -. DR PDBsum; 8J6S; -. DR PDBsum; 8J6T; -. DR AlphaFoldDB; Q13111; -. DR EMDB; EMD-33625; -. DR EMDB; EMD-33626; -. DR EMDB; EMD-33630; -. DR EMDB; EMD-33631; -. DR EMDB; EMD-35660; -. DR EMDB; EMD-35661; -. DR EMDB; EMD-36013; -. DR EMDB; EMD-36014; -. DR SASBDB; Q13111; -. DR SMR; Q13111; -. DR BioGRID; 115349; 201. DR ComplexPortal; CPX-569; Chromatin assembly factor 1 complex. DR CORUM; Q13111; -. DR DIP; DIP-31135N; -. DR ELM; Q13111; -. DR IntAct; Q13111; 64. DR MINT; Q13111; -. DR STRING; 9606.ENSP00000301280; -. DR GlyGen; Q13111; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q13111; -. DR PhosphoSitePlus; Q13111; -. DR SwissPalm; Q13111; -. DR BioMuta; CHAF1A; -. DR DMDM; 229462842; -. DR EPD; Q13111; -. DR jPOST; Q13111; -. DR MassIVE; Q13111; -. DR MaxQB; Q13111; -. DR PaxDb; 9606-ENSP00000301280; -. DR PeptideAtlas; Q13111; -. DR ProteomicsDB; 59160; -. [Q13111-1] DR ProteomicsDB; 59161; -. [Q13111-2] DR ProteomicsDB; 59162; -. [Q13111-3] DR Pumba; Q13111; -. DR Antibodypedia; 4198; 286 antibodies from 33 providers. DR DNASU; 10036; -. DR Ensembl; ENST00000301280.10; ENSP00000301280.4; ENSG00000167670.16. [Q13111-1] DR GeneID; 10036; -. DR KEGG; hsa:10036; -. DR MANE-Select; ENST00000301280.10; ENSP00000301280.4; NM_005483.3; NP_005474.2. DR UCSC; uc002mal.4; human. [Q13111-1] DR AGR; HGNC:1910; -. DR CTD; 10036; -. DR DisGeNET; 10036; -. DR GeneCards; CHAF1A; -. DR HGNC; HGNC:1910; CHAF1A. DR HPA; ENSG00000167670; Tissue enhanced (bone). DR MIM; 601246; gene. DR neXtProt; NX_Q13111; -. DR OpenTargets; ENSG00000167670; -. DR PharmGKB; PA26446; -. DR VEuPathDB; HostDB:ENSG00000167670; -. DR eggNOG; KOG4364; Eukaryota. DR GeneTree; ENSGT00440000034888; -. DR HOGENOM; CLU_014846_0_0_1; -. DR InParanoid; Q13111; -. DR OMA; DPWAQDK; -. DR OrthoDB; 10904at2759; -. DR PhylomeDB; Q13111; -. DR TreeFam; TF350377; -. DR PathwayCommons; Q13111; -. DR SignaLink; Q13111; -. DR SIGNOR; Q13111; -. DR BioGRID-ORCS; 10036; 769 hits in 1168 CRISPR screens. DR ChiTaRS; CHAF1A; human. DR GeneWiki; CHAF1A; -. DR GenomeRNAi; 10036; -. DR Pharos; Q13111; Tbio. DR PRO; PR:Q13111; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q13111; Protein. DR Bgee; ENSG00000167670; Expressed in secondary oocyte and 202 other cell types or tissues. DR ExpressionAtlas; Q13111; baseline and differential. DR GO; GO:0033186; C:CAF-1 complex; IDA:UniProtKB. DR GO; GO:0000785; C:chromatin; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; TAS:ProtInc. DR GO; GO:0070087; F:chromo shadow domain binding; IPI:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IDA:GO_Central. DR GO; GO:0006334; P:nucleosome assembly; IDA:GO_Central. DR InterPro; IPR029105; CAF1-p150_C2. DR InterPro; IPR029091; CAF1_p150_N. DR InterPro; IPR022043; CAF1A. DR PANTHER; PTHR15272:SF0; CHROMATIN ASSEMBLY FACTOR 1 SUBUNIT A; 1. DR PANTHER; PTHR15272; CHROMATIN ASSEMBLY FACTOR 1 SUBUNIT A CAF-1 SUBUNIT A; 1. DR Pfam; PF11600; CAF-1_p150; 1. DR Pfam; PF15539; CAF1-p150_C2; 1. DR Pfam; PF15557; CAF1-p150_N; 1. DR Pfam; PF12253; CAF1A; 1. DR Genevisible; Q13111; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell cycle; Chaperone; DNA damage; KW DNA repair; DNA replication; Isopeptide bond; Nucleus; Phosphoprotein; KW Reference proteome; Ubl conjugation. FT CHAIN 1..956 FT /note="Chromatin assembly factor 1 subunit A" FT /id="PRO_0000089276" FT REGION 1..314 FT /note="Binds to CBX1 chromo shadow domain" FT REGION 1..49 FT /note="Binds to PCNA" FT REGION 45..65 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 122..155 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 188..222 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 250..432 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 599..639 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 642..678 FT /note="Necessary for homodimerization and competence for FT chromatin assembly" FT REGION 660..956 FT /note="Binds to p60" FT REGION 765..790 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 844..873 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 933..956 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 233..246 FT /note="PxVxL motif" FT COMPBIAS 279..294 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 324..432 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 599..633 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 768..785 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 844..870 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 65 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:21406692" FT MOD_RES 123 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 138 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 141 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 143 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 206 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 224 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 310 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 722 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 772 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 775 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 803 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 865 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 868 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 873 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 951 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT CROSSLNK 182 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 182 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT VAR_SEQ 710..749 FT /note="CFLETLPAQEEQTPKASKRERRDEQILAQLLPLLHGNVNG -> HWVHPESR FT GDVCRTLRVSSPQSRYLNRLNSCVKSTLSCFT (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_004149" FT VAR_SEQ 750..956 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_004150" FT VAR_SEQ 772..944 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_004151" FT VARIANT 167 FT /note="D -> V (in dbSNP:rs35651457)" FT /id="VAR_055329" FT VARIANT 239 FT /note="M -> V (in dbSNP:rs2230635)" FT /id="VAR_055330" FT VARIANT 850 FT /note="K -> R (in dbSNP:rs8100525)" FT /id="VAR_055331" FT VARIANT 923 FT /note="A -> V (in dbSNP:rs9352)" FT /evidence="ECO:0000269|PubMed:11250073, FT ECO:0000269|PubMed:7600578" FT /id="VAR_055332" FT VARIANT 950 FT /note="A -> S (in dbSNP:rs243383)" FT /id="VAR_055333" FT MUTAGEN 240 FT /note="V->E: Abolishes interaction with CBX5; when FT associated with E-242." FT /evidence="ECO:0000269|PubMed:20562864" FT MUTAGEN 242 FT /note="L->E: Abolishes interaction with CBX5; when FT associated with E-240." FT /evidence="ECO:0000269|PubMed:20562864" FT CONFLICT 775 FT /note="S -> T (in Ref. 4; AAA76736)" FT /evidence="ECO:0000305" FT STRAND 477..479 FT /evidence="ECO:0007829|PDB:7Y5L" FT HELIX 491..501 FT /evidence="ECO:0007829|PDB:7Y5L" FT HELIX 508..513 FT /evidence="ECO:0007829|PDB:7Y5L" FT STRAND 538..543 FT /evidence="ECO:0007829|PDB:7Y5L" FT HELIX 551..554 FT /evidence="ECO:0007829|PDB:7Y5L" FT STRAND 558..561 FT /evidence="ECO:0007829|PDB:7Y5L" FT STRAND 570..572 FT /evidence="ECO:0007829|PDB:7Y5L" FT TURN 591..593 FT /evidence="ECO:0007829|PDB:7Y5L" FT HELIX 600..603 FT /evidence="ECO:0007829|PDB:7Y5K" FT STRAND 614..620 FT /evidence="ECO:0007829|PDB:8IQG" FT STRAND 630..632 FT /evidence="ECO:0007829|PDB:8IQG" FT HELIX 636..646 FT /evidence="ECO:0007829|PDB:8IQG" FT STRAND 659..663 FT /evidence="ECO:0007829|PDB:7Y5L" FT HELIX 665..674 FT /evidence="ECO:0007829|PDB:7Y5L" FT STRAND 684..686 FT /evidence="ECO:0007829|PDB:7Y5L" FT STRAND 694..696 FT /evidence="ECO:0007829|PDB:7Y5L" FT HELIX 698..705 FT /evidence="ECO:0007829|PDB:7Y5L" SQ SEQUENCE 956 AA; 106910 MW; 90617F8FE8DB7FD0 CRC64; MLEELECGAP GARGAATAMD CKDRPAFPVK KLIQARLPFK RLNLVPKGKA DDMSDDQGTS VQSKSPDLEA SLDTLENNCH VGSDIDFRPK LVNGKGPLDN FLRNRIETSI GQSTVIIDLT EDSNEQPDSL VDHNKLNSEA SPSREAINGQ REDTGDQQGL LKAIQNDKLA FPGETLSDIP CKTEEEGVGC GGAGRRGDSQ ECSPRSCPEL TSGPRMCPRK EQDSWSEAGG ILFKGKVPMV VLQDILAVRP PQIKSLPATP QGKNMTPESE VLESFPEEDS VLSHSSLSSP SSTSSPEGPP APPKQHSSTS PFPTSTPLRR ITKKFVKGST EKNKLRLQRD QERLGKQLKL RAEREEKEKL KEEAKRAKEE AKKKKEEEKE LKEKERREKR EKDEKEKAEK QRLKEERRKE RQEALEAKLE EKRKKEEEKR LREEEKRIKA EKAEITRFFQ KPKTPQAPKT LAGSCGKFAP FEIKEHMVLA PRRRTAFHPD LCSQLDQLLQ QQSGEFSFLK DLKGRQPLRS GPTHVSTRNA DIFNSDVVIV ERGKGDGVPE RRKFGRMKLL QFCENHRPAY WGTWNKKTAL IRARDPWAQD TKLLDYEVDS DEEWEEEEPG ESLSHSEGDD DDDMGEDEDE DDGFFVPHGY LSEDEGVTEE CADPENHKVR QKLKAKEWDE FLAKGKRFRV LQPVKIGCVW AADRDCAGDD LKVLQQFAAC FLETLPAQEE QTPKASKRER RDEQILAQLL PLLHGNVNGS KVIIREFQEH CRRGLLSNHT GSPRSPSTTY LHTPTPSEDA AIPSKSRLKR LISENSVYEK RPDFRMCWYV HPQVLQSFQQ EHLPVPCQWS YVTSVPSAPK EDSGSVPSTG PSQGTPISLK RKSAGSMCIT QFMKKRRHDG QIGAEDMDGF QADTEEEEEE EGDCMIVDVP DAAEVQAPCG AASGAGGGVG VDTGKATLTA SPLGAS //