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Chromatin assembly factor 1 subunit B (CAF-1 subunit B) (Chromatin assembly factor I p60 subunit) (CAF-I 60 kDa subunit) (CAF-I p60) (M-phase phosphoprotein 7)

 CAF1B_HUMAN             Reviewed;         559 AA.
Q13112; Q99548;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 187.
RecName: Full=Chromatin assembly factor 1 subunit B;
Short=CAF-1 subunit B;
AltName: Full=Chromatin assembly factor I p60 subunit;
Short=CAF-I 60 kDa subunit;
Short=CAF-I p60;
AltName: Full=M-phase phosphoprotein 7;
Name=CHAF1B; Synonyms=CAF1A, CAF1P60, MPHOSPH7, MPP7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 100-123.
PubMed=7600578; DOI=10.1016/S0092-8674(05)80015-7;
Kaufman P.D., Kobayashi R., Kessler N., Stillman B.;
"The p150 and p60 subunits of chromatin assembly factor I: a molecular
link between newly synthesized histones and DNA replication.";
Cell 81:1105-1114(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Shibuya K., Kudoh J., Minoshima S., Kawasaki K., Nakatoh E.,
Shintani A., Asakawa S., Shimizu N.;
"Genomic sequencing of 1.2-Mb region on human chromosome 21q22.2.";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 474-559, AND PHOSPHORYLATION.
TISSUE=Lymphoblast;
PubMed=8885239; DOI=10.1091/mbc.7.9.1455;
Matsumoto-Taniura N., Pirollet F., Monroe R., Gerace L.,
Westendorf J.M.;
"Identification of novel M phase phosphoproteins by expression
cloning.";
Mol. Biol. Cell 7:1455-1469(1996).
[6]
FUNCTION.
PubMed=9813080; DOI=10.1083/jcb.143.3.563;
Martini E., Roche D.M., Marheineke K., Verreault A., Almouzni G.;
"Recruitment of phosphorylated chromatin assembly factor 1 to
chromatin after UV irradiation of human cells.";
J. Cell Biol. 143:563-575(1998).
[7]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=9614144; DOI=10.1074/jbc.273.24.15279;
Marheineke K., Krude T.;
"Nucleosome assembly activity and intracellular localization of human
CAF-1 changes during the cell division cycle.";
J. Biol. Chem. 273:15279-15286(1998).
[8]
REVIEW.
PubMed=10893180;
Ridgway P., Almouzni G.;
"CAF-1 and the inheritance of chromatin states: at the crossroads of
DNA replication and repair.";
J. Cell Sci. 113:2647-2658(2000).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-419; SER-429; THR-433
AND SER-538, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-494, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409 AND SER-458, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394; THR-419; SER-429;
THR-433 AND SER-458, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Complex that is thought to mediate chromatin assembly in
DNA replication and DNA repair. Assembles histone octamers onto
replicating DNA in vitro. CAF-1 performs the first step of the
nucleosome assembly process, bringing newly synthesized histones
H3 and H4 to replicating DNA; histones H2A/H2B can bind to this
chromatin precursor subsequent to DNA replication to complete the
histone octamer. {ECO:0000269|PubMed:9813080}.
-!- SUBUNIT: Subunit of the CAF-1 complex that contains RBBP4, CHAF1B
and CHAF1A. CHAF1A binds directly to CHAF1B. Only minor amounts of
RBBP4 are complexed with CHAF1A and CHAF1B in G1 phase. In G2 and
S phase also monomeric CHAF1B is detected.
-!- INTERACTION:
Q9Y294:ASF1A; NbExp=2; IntAct=EBI-1052944, EBI-749553;
Q9NVP2:ASF1B; NbExp=2; IntAct=EBI-1052944, EBI-1055650;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9614144}.
Cytoplasm {ECO:0000269|PubMed:9614144}. Note=DNA replication foci.
Cytoplasmic in M phase.
-!- DEVELOPMENTAL STAGE: Active complex is found in G1, S and G2
phases.
-!- PTM: Differentially phosphorylated during cell cycle. During
mitosis the p60 subunit of inactive CAF-1 is hyperphosphorylated
and displaced into the cytosol. Progressivly dephosphorylated from
G1 to S and G2 phase. Phosphorylated p60 is recruited to chromatin
undergoing DNA repair after UV irradiation in G1, S or G2 phases.
{ECO:0000269|PubMed:8885239, ECO:0000269|PubMed:9614144}.
-!- SIMILARITY: Belongs to the WD repeat HIR1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U20980; AAA76737.1; -; mRNA.
EMBL; AP000694; BAA89426.1; -; Genomic_DNA.
EMBL; AP001725; BAA95549.1; -; Genomic_DNA.
EMBL; BC021218; AAH21218.1; -; mRNA.
EMBL; X98262; CAA66915.1; -; mRNA.
CCDS; CCDS13644.1; -.
PIR; B56731; B56731.
RefSeq; NP_005432.1; NM_005441.2.
RefSeq; XP_016883966.1; XM_017028477.1.
RefSeq; XP_016883967.1; XM_017028478.1.
UniGene; Hs.75238; -.
ProteinModelPortal; Q13112; -.
BioGrid; 113846; 51.
CORUM; Q13112; -.
DIP; DIP-29243N; -.
IntAct; Q13112; 30.
MINT; MINT-3027086; -.
STRING; 9606.ENSP00000315700; -.
iPTMnet; Q13112; -.
PhosphoSitePlus; Q13112; -.
BioMuta; CHAF1B; -.
DMDM; 3121829; -.
EPD; Q13112; -.
MaxQB; Q13112; -.
PaxDb; Q13112; -.
PeptideAtlas; Q13112; -.
PRIDE; Q13112; -.
DNASU; 8208; -.
Ensembl; ENST00000314103; ENSP00000315700; ENSG00000159259.
GeneID; 8208; -.
KEGG; hsa:8208; -.
UCSC; uc002yvj.4; human.
CTD; 8208; -.
DisGeNET; 8208; -.
EuPathDB; HostDB:ENSG00000159259.7; -.
GeneCards; CHAF1B; -.
HGNC; HGNC:1911; CHAF1B.
HPA; CAB033604; -.
HPA; HPA021679; -.
MIM; 601245; gene.
neXtProt; NX_Q13112; -.
OpenTargets; ENSG00000159259; -.
PharmGKB; PA26447; -.
eggNOG; KOG1009; Eukaryota.
eggNOG; ENOG410XPU4; LUCA.
GeneTree; ENSGT00550000074968; -.
HOGENOM; HOG000183312; -.
HOVERGEN; HBG050780; -.
InParanoid; Q13112; -.
KO; K10751; -.
OMA; VYDICWT; -.
OrthoDB; EOG091G0FIG; -.
PhylomeDB; Q13112; -.
TreeFam; TF313062; -.
SignaLink; Q13112; -.
SIGNOR; Q13112; -.
GeneWiki; CHAF1B; -.
GenomeRNAi; 8208; -.
PRO; PR:Q13112; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000159259; -.
CleanEx; HS_CHAF1B; -.
CleanEx; HS_MPP7; -.
Genevisible; Q13112; HS.
GO; GO:0033186; C:CAF-1 complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; NAS:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; TAS:ProtInc.
GO; GO:0042393; F:histone binding; IBA:GO_Central.
GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0031497; P:chromatin assembly; IDA:UniProtKB.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0006335; P:DNA replication-dependent nucleosome assembly; IDA:UniProtKB.
GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.130.10.10; -; 2.
InterPro; IPR029129; CAF1_p60_C.
InterPro; IPR001632; Gprotein_B.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF15512; CAF-1_p60_C; 1.
Pfam; PF00400; WD40; 3.
PRINTS; PR00319; GPROTEINB.
SMART; SM00320; WD40; 5.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 1.
PROSITE; PS50082; WD_REPEATS_2; 3.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Acetylation; Cell cycle; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA damage; DNA repair; DNA replication;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Transcription; Transcription regulation; WD repeat.
CHAIN 1 559 Chromatin assembly factor 1 subunit B.
/FTId=PRO_0000050896.
REPEAT 11 54 WD 1.
REPEAT 64 103 WD 2.
REPEAT 127 166 WD 3.
REPEAT 169 208 WD 4.
REPEAT 228 279 WD 5.
REPEAT 299 340 WD 6.
REPEAT 344 385 WD 7.
MOD_RES 394 394 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 409 409 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 419 419 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 429 429 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 433 433 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 458 458 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 494 494 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 495 495 Phosphothreonine. {ECO:0000255}.
MOD_RES 509 509 Phosphothreonine. {ECO:0000255}.
MOD_RES 521 521 Phosphothreonine. {ECO:0000255}.
MOD_RES 531 531 Phosphothreonine. {ECO:0000255}.
MOD_RES 538 538 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VARIANT 506 506 K -> Q (in dbSNP:rs74900401).
/FTId=VAR_053387.
CONFLICT 494 494 K -> N (in Ref. 5; CAA66915).
{ECO:0000305}.
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


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