CAF1B_MOUSE
ID CAF1B_MOUSE Reviewed; 572 AA.
AC Q9D0N7;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
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;
GN Name=Chaf1b {ECO:0000312|MGI:MGI:1314881};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436 AND SER-456, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Complex that is thought to mediate chromatin assembly in DNA
CC replication and DNA repair. Assembles histone octamers onto replicating
CC DNA in vitro. CAF-1 performs the first step of the nucleosome assembly
CC process, bringing newly synthesized histones H3 and H4 to replicating
CC DNA; histones H2A/H2B can bind to this chromatin precursor subsequent
CC to DNA replication to complete the histone octamer (By similarity).
CC {ECO:0000250|UniProtKB:Q13112, ECO:0000250|UniProtKB:Q5R1S9}.
CC -!- SUBUNIT: Subunit of the CAF-1 complex that contains RBBP4, CHAF1B and
CC CHAF1A. CHAF1A binds directly to CHAF1B (By similarity). Interacts with
CC histones H3.1, H3.2 and H3.1t (By similarity).
CC {ECO:0000250|UniProtKB:Q13112, ECO:0000250|UniProtKB:Q5R1S9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13112}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q13112}. Note=DNA replication foci. Cytoplasmic
CC in M phase. {ECO:0000250|UniProtKB:Q13112}.
CC -!- SIMILARITY: Belongs to the WD repeat HIR1 family. {ECO:0000305}.
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DR EMBL; AK011243; BAB27490.1; -; mRNA.
DR EMBL; BC013532; AAH13532.1; -; mRNA.
DR CCDS; CCDS28344.1; -.
DR RefSeq; NP_082359.1; NM_028083.4.
DR RefSeq; XP_006522910.1; XM_006522847.3.
DR AlphaFoldDB; Q9D0N7; -.
DR SMR; Q9D0N7; -.
DR BioGRID; 225873; 3.
DR ComplexPortal; CPX-570; Chromatin assembly factor 1 complex.
DR IntAct; Q9D0N7; 2.
DR MINT; Q9D0N7; -.
DR STRING; 10090.ENSMUSP00000023666; -.
DR iPTMnet; Q9D0N7; -.
DR PhosphoSitePlus; Q9D0N7; -.
DR EPD; Q9D0N7; -.
DR jPOST; Q9D0N7; -.
DR MaxQB; Q9D0N7; -.
DR PaxDb; Q9D0N7; -.
DR PeptideAtlas; Q9D0N7; -.
DR PRIDE; Q9D0N7; -.
DR ProteomicsDB; 265274; -.
DR Antibodypedia; 8327; 318 antibodies from 35 providers.
DR DNASU; 110749; -.
DR Ensembl; ENSMUST00000023666; ENSMUSP00000023666; ENSMUSG00000022945.
DR Ensembl; ENSMUST00000117099; ENSMUSP00000113684; ENSMUSG00000022945.
DR GeneID; 110749; -.
DR KEGG; mmu:110749; -.
DR UCSC; uc008aac.1; mouse.
DR CTD; 8208; -.
DR MGI; MGI:1314881; Chaf1b.
DR VEuPathDB; HostDB:ENSMUSG00000022945; -.
DR eggNOG; KOG1009; Eukaryota.
DR GeneTree; ENSGT00550000074968; -.
DR HOGENOM; CLU_010127_5_2_1; -.
DR InParanoid; Q9D0N7; -.
DR OMA; CTIAVRC; -.
DR OrthoDB; 685536at2759; -.
DR PhylomeDB; Q9D0N7; -.
DR TreeFam; TF313062; -.
DR BioGRID-ORCS; 110749; 43 hits in 111 CRISPR screens.
DR ChiTaRS; Chaf1b; mouse.
DR PRO; PR:Q9D0N7; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9D0N7; protein.
DR Bgee; ENSMUSG00000022945; Expressed in hindlimb bud and 213 other tissues.
DR ExpressionAtlas; Q9D0N7; baseline and differential.
DR Genevisible; Q9D0N7; MM.
DR GO; GO:0033186; C:CAF-1 complex; ISS:UniProtKB.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0031497; P:chromatin assembly; ISS: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; ISO:MGI.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR029129; CAF1_p60_C.
DR InterPro; IPR001632; Gprotein_B.
DR InterPro; IPR045145; PTHR15271.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR15271; PTHR15271; 1.
DR Pfam; PF15512; CAF-1_p60_C; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00319; GPROTEINB.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 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 Acetylation; Cell cycle; Cytoplasm; DNA damage; DNA repair;
KW DNA replication; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; WD repeat.
FT CHAIN 1..572
FT /note="Chromatin assembly factor 1 subunit B"
FT /id="PRO_0000050897"
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 301..347
FT /note="WD 6"
FT REPEAT 351..392
FT /note="WD 7"
FT REGION 403..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 401
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13112"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13112"
FT MOD_RES 426
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13112"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 440
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13112"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13112"
FT MOD_RES 501
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13112"
FT MOD_RES 502
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 510
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 572 AA; 63132 MW; 03C2BC263591FF72 CRC64;
MKVITCEIAW HNKEPVYSLD FQHGATWKIH RLASAGVDTA VRIWKLERGP DGKAIVEFLS
NLARHTKAVN VVRFSPTGEI LASGGDDAVI LLWKMNDSKE PEQIAFQDEE EAQLNKENWT
VVKTLRGHLE DVYDICWATD GNLMTSASVD NTVIIWDVSK GQKISIFNEH KSYVQGVTWD
PLGQYIATLS CDRVLRIYNT QKKRVAFNIS KMLSGQGPEG EARSFRMFHD DSMKSFFRRL
SFTPDGSLLL TPAGCMESGE NVTNTTYVFS RKHLKRPIAH LPCPGKATLA VRCCPVYFEL
RPVAETEKAS EEPSPELVNL PYRMVFAVAS EDSVLLYDTQ QSFPFGYVSN IHYHTLSDIS
WSSDGAFLAI SSTDGYCTFV TFEKGELGIP LKEKPVLSIR TPDTAKKAKN QTHQGSSPGS
RSVEGTPSNR TQDPSSPCTT PSPTTQSPAP SAIKDSPSAI PAGKSPLPQP SEEKTLQPAG
QNMKAPQPRR VTLNTLQTWG KTAPRRINLT PLKTDTVPNP QPNSGTAPST EEVQPEAPGE
PPEEPPELKR PRLEEREGDA QNLAPDDSSK TV
