CHRC1_MOUSE
ID CHRC1_MOUSE Reviewed; 129 AA.
AC Q9JKP8; Q91VG2;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Chromatin accessibility complex protein 1;
DE Short=CHRAC-1;
DE AltName: Full=DNA polymerase epsilon subunit p15;
DE AltName: Full=NF-YC-like protein;
DE AltName: Full=YC-like protein 1;
DE Short=YCL1;
GN Name=Chrac1;
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 [MRNA].
RC TISSUE=B-cell lymphoma;
RX PubMed=11000277; DOI=10.1093/nar/28.19.3830;
RA Bolognese F., Imbriano C., Caretti G., Mantovani R.;
RT "Cloning and characterization of the histone-fold proteins YBL1 and YCL1.";
RL Nucleic Acids Res. 28:3830-3838(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland, and Testis;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, 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: Forms a complex with DNA polymerase epsilon subunit POLE3 and
CC binds naked DNA, which is then incorporated into chromatin, aided by
CC the nucleosome remodeling activity of ISWI/SNF2H and ACF1. Does not
CC enhance nucleosome sliding activity of the ACF-5 ISWI chromatin
CC remodeling complex (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9NRG0}.
CC -!- SUBUNIT: Heterodimer with POLE3; binds to DNA (By similarity).
CC Component of the CHRAC ISWI chromatin remodeling complex at least
CC composed of SMARCA5/SNF2H, BAZ1A/ACF1, CHRAC1 and POLE3; the complex
CC preferentially binds DNA through the CHRAC1-POLE3 heterodimer and
CC possesses ATP-dependent nucleosome-remodeling activity (By similarity).
CC Within the complex, the heterodimer with POLE3 interacts with
CC SMARCA5/SNF2H; the interaction is direct and enhances nucleosome
CC sliding activity by the SMARCA5/SNF2H and BAZ1A/ACF1 interaction (By
CC similarity). Within the complex, the heterodimer with POLE3 interacts
CC with BAZ1A/ACF1; the interactions are direct (By similarity).
CC {ECO:0000250|UniProtKB:Q9NRG0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
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DR EMBL; AF230805; AAF67145.1; -; mRNA.
DR EMBL; AK010812; BAB27197.1; -; mRNA.
DR EMBL; BC016593; AAH16593.1; -; mRNA.
DR EMBL; BC061043; AAH61043.1; -; mRNA.
DR CCDS; CCDS27516.1; -.
DR RefSeq; NP_444298.1; NM_053068.3.
DR AlphaFoldDB; Q9JKP8; -.
DR SMR; Q9JKP8; -.
DR BioGRID; 220245; 1.
DR ComplexPortal; CPX-858; CHRAC chromatin remodeling complex.
DR IntAct; Q9JKP8; 2.
DR MINT; Q9JKP8; -.
DR STRING; 10090.ENSMUSP00000087197; -.
DR iPTMnet; Q9JKP8; -.
DR PhosphoSitePlus; Q9JKP8; -.
DR EPD; Q9JKP8; -.
DR jPOST; Q9JKP8; -.
DR MaxQB; Q9JKP8; -.
DR PaxDb; Q9JKP8; -.
DR PeptideAtlas; Q9JKP8; -.
DR PRIDE; Q9JKP8; -.
DR ProteomicsDB; 279073; -.
DR Antibodypedia; 27623; 192 antibodies from 29 providers.
DR DNASU; 93696; -.
DR Ensembl; ENSMUST00000089765; ENSMUSP00000087197; ENSMUSG00000068391.
DR GeneID; 93696; -.
DR KEGG; mmu:93696; -.
DR UCSC; uc007wbq.1; mouse.
DR CTD; 54108; -.
DR MGI; MGI:2135796; Chrac1.
DR VEuPathDB; HostDB:ENSMUSG00000068391; -.
DR eggNOG; KOG1657; Eukaryota.
DR GeneTree; ENSGT00510000048543; -.
DR InParanoid; Q9JKP8; -.
DR OMA; YNNGSGK; -.
DR OrthoDB; 1622159at2759; -.
DR PhylomeDB; Q9JKP8; -.
DR TreeFam; TF350392; -.
DR BioGRID-ORCS; 93696; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Chrac1; mouse.
DR PRO; PR:Q9JKP8; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9JKP8; protein.
DR Bgee; ENSMUSG00000068391; Expressed in saccule of membranous labyrinth and 262 other tissues.
DR ExpressionAtlas; Q9JKP8; baseline and differential.
DR Genevisible; Q9JKP8; MM.
DR GO; GO:0008623; C:CHRAC; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0006334; P:nucleosome assembly; ISO:MGI.
DR GO; GO:0006275; P:regulation of DNA replication; ISO:MGI.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR009072; Histone-fold.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; DNA-binding; DNA-directed DNA polymerase;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NRG0"
FT CHAIN 2..129
FT /note="Chromatin accessibility complex protein 1"
FT /id="PRO_0000089657"
FT REGION 109..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 104..120
FT /evidence="ECO:0000255"
FT COMPBIAS 113..129
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRG0"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRG0"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
SQ SEQUENCE 129 AA; 14127 MW; CDF843A5D96D5520 CRC64;
MADAAVGKEK CGDQRLVSLP LSRIRVIMKS SPEVSSINQE ALVLTAKATE LFVQYLATCS
YRHGSGKAKK ALTYSDLAST AEDSETLQFL ADILPKKILA SKYLKMLKEK REEEEDNEDD
GSDLGEALA
