ID   CAF1B_HUMAN             Reviewed;         559 AA.
AC   Q13112; Q99548;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   28-JAN-2026, entry version 232.
DE   RecName: Full=Chromatin assembly factor 1 subunit B {ECO:0000305};
DE            Short=CAF-1 subunit B;
DE   AltName: Full=Chromatin assembly factor I p60 subunit;
DE            Short=CAF-I 60 kDa subunit;
DE            Short=CAF-I p60;
DE   AltName: Full=M-phase phosphoprotein 7;
GN   Name=CHAF1B {ECO:0000312|HGNC:HGNC:1911};
GN   Synonyms=CAF1A, CAF1P60, MPHOSPH7, MPP7;
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], AND PROTEIN SEQUENCE OF 100-123.
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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Shibuya K., Kudoh J., Minoshima S., Kawasaki K., Nakatoh E., Shintani A.,
RA   Asakawa S., Shimizu N.;
RT   "Genomic sequencing of 1.2-Mb region on human chromosome 21q22.2.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10830953; DOI=10.1038/35012518;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA   Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA   Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA   Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA   Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA   Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA   Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA   Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA   Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA   Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA   Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 474-559, AND PHOSPHORYLATION.
RC   TISSUE=Lymphoblast;
RX   PubMed=8885239; DOI=10.1091/mbc.7.9.1455;
RA   Matsumoto-Taniura N., Pirollet F., Monroe R., Gerace L., Westendorf J.M.;
RT   "Identification of novel M phase phosphoproteins by expression cloning.";
RL   Mol. Biol. Cell 7:1455-1469(1996).
RN   [6]
RP   FUNCTION.
RX   PubMed=9813080; DOI=10.1083/jcb.143.3.563;
RA   Martini E., Roche D.M., Marheineke K., Verreault A., Almouzni G.;
RT   "Recruitment of phosphorylated chromatin assembly factor 1 to chromatin
RT   after UV irradiation of human cells.";
RL   J. Cell Biol. 143:563-575(1998).
RN   [7]
RP   SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX   PubMed=9614144; DOI=10.1074/jbc.273.24.15279;
RA   Marheineke K., Krude T.;
RT   "Nucleosome assembly activity and intracellular localization of human CAF-1
RT   changes during the cell division cycle.";
RL   J. Biol. Chem. 273:15279-15286(1998).
RN   [8]
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   [9]
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   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [11]
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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-419; SER-429; THR-433 AND
RP   SER-538, AND IDENTIFICATION BY 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   [13]
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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429, AND IDENTIFICATION BY
RP   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   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-494, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409 AND SER-458, 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   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND IDENTIFICATION BY
RP   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   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394; THR-419; SER-429;
RP   THR-433 AND SER-458, 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).
RN   [20]
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: Acts as a component of the histone chaperone complex
CC       chromatin assembly factor 1 (CAF-1), which assembles histone octamers
CC       onto DNA during replication and repair. CAF-1 performs the first step
CC       of the nucleosome assembly process, bringing newly synthesized histones
CC       H3 and H4 to replicating DNA; histones H2A/H2B can bind to this
CC       chromatin precursor subsequent to DNA replication to complete the
CC       histone octamer. {ECO:0000269|PubMed:9813080}.
CC   -!- SUBUNIT: Subunit of the CAF-1 complex that contains RBBP4, CHAF1B and
CC       CHAF1A. CHAF1A binds directly to CHAF1B. Only minor amounts of RBBP4
CC       are complexed with CHAF1A and CHAF1B in G1 phase. In G2 and S phase
CC       also monomeric CHAF1B is detected. Interacts with histones H3.1, H3.2
CC       and H3.1t (PubMed:33857403). {ECO:0000250|UniProtKB:Q5R1S9,
CC       ECO:0000269|PubMed:33857403}.
CC   -!- INTERACTION:
CC       Q13112; Q9Y294: ASF1A; NbExp=3; IntAct=EBI-1052944, EBI-749553;
CC       Q13112; Q9NVP2: ASF1B; NbExp=7; IntAct=EBI-1052944, EBI-1055650;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9614144}. Cytoplasm
CC       {ECO:0000269|PubMed:9614144}. Note=DNA replication foci. Cytoplasmic in
CC       M phase.
CC   -!- DEVELOPMENTAL STAGE: Active complex is found in G1, S and G2 phases.
CC   -!- PTM: Differentially phosphorylated during cell cycle. During mitosis
CC       the p60 subunit of inactive CAF-1 is hyperphosphorylated and displaced
CC       into the cytosol. Progressivly dephosphorylated from G1 to S and G2
CC       phase. Phosphorylated p60 is recruited to chromatin undergoing DNA
CC       repair after UV irradiation in G1, S or G2 phases.
CC       {ECO:0000269|PubMed:8885239, ECO:0000269|PubMed:9614144}.
CC   -!- SIMILARITY: Belongs to the WD repeat HIR1 family. {ECO:0000305}.
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DR   EMBL; U20980; AAA76737.1; -; mRNA.
DR   EMBL; AP000694; BAA89426.1; -; Genomic_DNA.
DR   EMBL; AP001725; BAA95549.1; -; Genomic_DNA.
DR   EMBL; BC021218; AAH21218.1; -; mRNA.
DR   EMBL; X98262; CAA66915.1; -; mRNA.
DR   CCDS; CCDS13644.1; -.
DR   PIR; B56731; B56731.
DR   RefSeq; NP_005432.1; NM_005441.3.
DR   PDB; 7Y5K; X-ray; 3.48 A; B=1-419.
DR   PDB; 7Y5L; X-ray; 3.42 A; B/E=1-419.
DR   PDB; 7Y5O; X-ray; 3.57 A; B/E=1-419.
DR   PDB; 7Y5U; EM; 3.80 A; B=1-419.
DR   PDB; 7Y5V; EM; 6.10 A; B/G=1-419.
DR   PDB; 7Y60; EM; 3.80 A; L=1-419.
DR   PDB; 7Y61; EM; 5.60 A; L/N=1-419.
DR   PDB; 8IQF; EM; 4.60 A; B/G=1-559.
DR   PDB; 8IQG; EM; 3.50 A; B=1-559.
DR   PDB; 8J6S; EM; 3.80 A; L=1-559.
DR   PDB; 8J6T; EM; 6.60 A; L/N=1-559.
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; Q13112; -.
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   SMR; Q13112; -.
DR   BioGRID; 113846; 179.
DR   ComplexPortal; CPX-569; Chromatin assembly factor 1 complex.
DR   CORUM; Q13112; -.
DR   DIP; DIP-29243N; -.
DR   FunCoup; Q13112; 2143.
DR   IntAct; Q13112; 69.
DR   MINT; Q13112; -.
DR   STRING; 9606.ENSP00000315700; -.
DR   GlyGen; Q13112; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q13112; -.
DR   MetOSite; Q13112; -.
DR   PhosphoSitePlus; Q13112; -.
DR   SwissPalm; Q13112; -.
DR   BioMuta; CHAF1B; -.
DR   DMDM; 3121829; -.
DR   jPOST; Q13112; -.
DR   MassIVE; Q13112; -.
DR   PaxDb; 9606-ENSP00000315700; -.
DR   PeptideAtlas; Q13112; -.
DR   ProteomicsDB; 59163; -.
DR   Pumba; Q13112; -.
DR   Antibodypedia; 8327; 324 antibodies from 36 providers.
DR   DNASU; 8208; -.
DR   Ensembl; ENST00000314103.6; ENSP00000315700.4; ENSG00000159259.9.
DR   GeneID; 8208; -.
DR   KEGG; hsa:8208; -.
DR   MANE-Select; ENST00000314103.6; ENSP00000315700.4; NM_005441.3; NP_005432.1.
DR   UCSC; uc002yvj.4; human.
DR   AGR; HGNC:1911; -.
DR   ClinPGx; PA26447; -.
DR   CTD; 8208; -.
DR   DisGeNET; 8208; -.
DR   GeneCards; CHAF1B; -.
DR   HGNC; HGNC:1911; CHAF1B.
DR   HPA; ENSG00000159259; Tissue enhanced (skeletal).
DR   MalaCards; CHAF1B; -.
DR   MIM; 601245; gene.
DR   OpenTargets; ENSG00000159259; -.
DR   VEuPathDB; HostDB:ENSG00000159259; -.
DR   eggNOG; KOG1009; Eukaryota.
DR   GeneTree; ENSGT00550000074968; -.
DR   HOGENOM; CLU_010127_5_2_1; -.
DR   InParanoid; Q13112; -.
DR   OMA; CTTPEIS; -.
DR   OrthoDB; 71227at2759; -.
DR   PAN-GO; Q13112; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; Q13112; -.
DR   PathwayCommons; Q13112; -.
DR   SignaLink; Q13112; -.
DR   SIGNOR; Q13112; -.
DR   Agora; ENSG00000159259; -.
DR   BioGRID-ORCS; 8208; 822 hits in 1153 CRISPR screens.
DR   ChiTaRS; CHAF1B; human.
DR   GeneWiki; CHAF1B; -.
DR   GenomeRNAi; 8208; -.
DR   Pharos; Q13112; Tbio.
DR   PRO; PR:Q13112; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   RNAct; Q13112; protein.
DR   Bgee; ENSG00000159259; Expressed in secondary oocyte and 112 other cell types or tissues.
DR   GO; GO:0033186; C:CAF-1 complex; IDA:UniProtKB.
DR   GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0042393; F:histone binding; NAS:UniProtKB.
DR   GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
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   FunFam; 2.130.10.10:FF:000248; Chromatin assembly factor 1 subunit B; 1.
DR   FunFam; 2.130.10.10:FF:001187; Chromatin assembly factor-1 p105 subunit; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR055410; Beta-prop_CAF1B_HIR1.
DR   InterPro; IPR029129; CAF1_p60_C.
DR   InterPro; IPR045145; PTHR15271.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001632; WD40_G-protein_beta-like.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR15271; CHROMATIN ASSEMBLY FACTOR 1 SUBUNIT B; 1.
DR   PANTHER; PTHR15271:SF4; CHROMATIN ASSEMBLY FACTOR 1 SUBUNIT B; 1.
DR   Pfam; PF24105; Beta-prop_CAF1B_HIR1; 1.
DR   Pfam; PF15512; CAF-1_p60_C; 1.
DR   PRINTS; PR00319; GPROTEINB.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell cycle; Chaperone; Chromatin regulator;
KW   Cytoplasm; Direct protein sequencing; DNA damage; DNA repair;
KW   DNA replication; Nucleus; Phosphoprotein; Proteomics identification;
KW   Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..559
FT                   /note="Chromatin assembly factor 1 subunit B"
FT                   /id="PRO_0000050896"
FT   REPEAT          11..54
FT                   /note="WD 1"
FT   REPEAT          64..103
FT                   /note="WD 2"
FT   REPEAT          127..166
FT                   /note="WD 3"
FT   REPEAT          169..208
FT                   /note="WD 4"
FT   REPEAT          228..279
FT                   /note="WD 5"
FT   REPEAT          299..340
FT                   /note="WD 6"
FT   REPEAT          344..385
FT                   /note="WD 7"
FT   REGION          386..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..444
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..526
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..552
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         394
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         409
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         419
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         429
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT   MOD_RES         433
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         458
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         494
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         495
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         509
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         521
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         531
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         538
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   VARIANT         506
FT                   /note="K -> Q (in dbSNP:rs74900401)"
FT                   /id="VAR_053387"
FT   CONFLICT        494
FT                   /note="K -> N (in Ref. 5; CAA66915)"
FT                   /evidence="ECO:0000305"
FT   STRAND          2..5
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   TURN            10..13
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          16..21
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          27..36
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          41..48
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          54..62
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          69..74
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          76..80
FT                   /evidence="ECO:0007829|PDB:8IQG"
FT   STRAND          81..85
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          90..95
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          119..125
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          132..137
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          141..148
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          153..157
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   TURN            158..161
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          162..167
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          174..179
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          183..190
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          195..199
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   TURN            200..202
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          204..209
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          211..213
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   HELIX           218..220
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          224..228
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          246..272
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          274..276
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          278..282
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          288..299
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          309..311
FT                   /evidence="ECO:0007829|PDB:7Y5K"
FT   STRAND          314..330
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          338..343
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          349..354
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          358..365
FT                   /evidence="ECO:0007829|PDB:7Y5L"
FT   STRAND          366..368
FT                   /evidence="ECO:0007829|PDB:8IQG"
FT   STRAND          370..374
FT                   /evidence="ECO:0007829|PDB:7Y5L"
SQ   SEQUENCE   559 AA;  61493 MW;  AD1846CC81B8DC9F CRC64;
     MKVITCEIAW HNKEPVYSLD FQHGTAGRIH RLASAGVDTN VRIWKVEKGP DGKAIVEFLS
     NLARHTKAVN VVRFSPTGEI LASGGDDAVI LLWKVNDNKE PEQIAFQDED EAQLNKENWT
     VVKTLRGHLE DVYDICWATD GNLMASASVD NTAIIWDVSK GQKISIFNEH KSYVQGVTWD
     PLGQYVATLS CDRVLRVYSI QKKRVAFNVS KMLSGIGAEG EARSYRMFHD DSMKSFFRRL
     SFTPDGSLLL TPAGCVESGE NVMNTTYVFS RKNLKRPIAH LPCPGKATLA VRCCPVYFEL
     RPVVETGVEL MSLPYRLVFA VASEDSVLLY DTQQSFPFGY VSNIHYHTLS DISWSSDGAF
     LAISSTDGYC SFVTFEKDEL GIPLKEKPVL NMRTPDTAKK TKSQTHRGSS PGPRPVEGTP
     ASRTQDPSSP GTTPPQARQA PAPTVIRDPP SITPAVKSPL PGPSEEKTLQ PSSQNTKAHP
     SRRVTLNTLQ AWSKTTPRRI NLTPLKTDTP PSSVPTSVIS TPSTEEIQSE TPGDAQGSPP
     ELKRPRLDEN KGGTESLDP
//