CAF1A_HUMAN
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 03-AUG-2022, entry version 198.
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};
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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 AlphaFoldDB; Q13111; -.
DR BioGRID; 115349; 173.
DR ComplexPortal; CPX-569; Chromatin assembly factor 1 complex.
DR CORUM; Q13111; -.
DR DIP; DIP-31135N; -.
DR ELM; Q13111; -.
DR IntAct; Q13111; 65.
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 BioMuta; CHAF1A; -.
DR DMDM; 229462842; -.
DR EPD; Q13111; -.
DR jPOST; Q13111; -.
DR MassIVE; Q13111; -.
DR MaxQB; Q13111; -.
DR PaxDb; Q13111; -.
DR PeptideAtlas; Q13111; -.
DR PRIDE; Q13111; -.
DR ProteomicsDB; 59160; -. [Q13111-1]
DR ProteomicsDB; 59161; -. [Q13111-2]
DR ProteomicsDB; 59162; -. [Q13111-3]
DR Antibodypedia; 4198; 243 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 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; CKWTYLT; -.
DR OrthoDB; 1362011at2759; -.
DR PhylomeDB; Q13111; -.
DR TreeFam; TF350377; -.
DR PathwayCommons; Q13111; -.
DR SignaLink; Q13111; -.
DR SIGNOR; Q13111; -.
DR BioGRID-ORCS; 10036; 737 hits in 1091 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 200 other tissues.
DR ExpressionAtlas; Q13111; baseline and differential.
DR Genevisible; Q13111; HS.
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:0031497; P:chromatin assembly; IDA:UniProtKB.
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:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR InterPro; IPR029105; CAF1-p150_C2.
DR InterPro; IPR029091; CAF1_p150_N.
DR InterPro; IPR022043; CAF1A.
DR Pfam; PF15539; CAF1-p150_C2; 1.
DR Pfam; PF15557; CAF1-p150_N; 1.
DR Pfam; PF12253; CAF1A; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Chaperone; DNA damage; DNA repair;
KW 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"
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
