H10_MOUSE
ID H10_MOUSE Reviewed; 194 AA.
AC P10922; Q3UKC0;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Histone H1.0;
DE AltName: Full=Histone H1';
DE AltName: Full=Histone H1(0);
DE AltName: Full=MyD196;
DE Contains:
DE RecName: Full=Histone H1.0, N-terminally processed;
GN Name=H1-0; Synonyms=H1f0, H1fv;
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].
RX PubMed=2846273; DOI=10.1002/j.1460-2075.1988.tb03163.x;
RA Alonso A., Breuer B., Bouterfa H., Doenecke D.;
RT "Early increase in histone H1(0) mRNA during differentiation of F9 cells to
RT parietal endoderm.";
RL EMBO J. 7:3003-3008(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=7891682; DOI=10.1128/mcb.15.4.1889;
RA Dong Y., Liu D., Skoultchi A.I.;
RT "An upstream control region required for inducible transcription of the
RT mouse H1(zero) histone gene during terminal differentiation.";
RL Mol. Cell. Biol. 15:1889-1900(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Blastocyst, Placenta, and Spinal ganglion;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
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 2-42.
RX PubMed=1690380;
RA Lord K.A., Hoffman-Liebermann B., Liebermann D.A.;
RT "Complexity of the immediate early response of myeloid cells to terminal
RT differentiation and growth arrest includes ICAM-1, Jun-B and histone
RT variants.";
RL Oncogene 5:387-396(1990).
CC -!- FUNCTION: Histones H1 are necessary for the condensation of nucleosome
CC chains into higher-order structures. The histones H1.0 are found in
CC cells that are in terminal stages of differentiation or that have low
CC rates of cell division.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- PTM: ADP-ribosylated on Ser-104 in response to DNA damage.
CC {ECO:0000250|UniProtKB:P07305}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; X13171; CAA31569.1; -; mRNA.
DR EMBL; U18295; AAA69911.1; -; Genomic_DNA.
DR EMBL; AK051213; BAC34559.1; -; mRNA.
DR EMBL; AK077473; BAC36817.1; -; mRNA.
DR EMBL; AK145675; BAE26583.1; -; mRNA.
DR EMBL; AK146077; BAE26881.1; -; mRNA.
DR EMBL; BC003830; AAH03830.1; -; mRNA.
DR EMBL; BC011493; AAH11493.1; -; mRNA.
DR EMBL; BC110361; AAI10362.1; -; mRNA.
DR CCDS; CCDS56990.1; -.
DR PIR; I49150; I49150.
DR RefSeq; NP_032223.2; NM_008197.3.
DR AlphaFoldDB; P10922; -.
DR SMR; P10922; -.
DR BioGRID; 200145; 11.
DR IntAct; P10922; 9.
DR MINT; P10922; -.
DR STRING; 10090.ENSMUSP00000137309; -.
DR iPTMnet; P10922; -.
DR PhosphoSitePlus; P10922; -.
DR EPD; P10922; -.
DR jPOST; P10922; -.
DR MaxQB; P10922; -.
DR PaxDb; P10922; -.
DR PeptideAtlas; P10922; -.
DR PRIDE; P10922; -.
DR ProteomicsDB; 269665; -.
DR TopDownProteomics; P10922; -.
DR ABCD; P10922; 2 sequenced antibodies.
DR Antibodypedia; 211; 741 antibodies from 34 providers.
DR DNASU; 14958; -.
DR Ensembl; ENSMUST00000180086; ENSMUSP00000137309; ENSMUSG00000096210.
DR GeneID; 14958; -.
DR KEGG; mmu:14958; -.
DR UCSC; uc007wsd.1; mouse.
DR CTD; 14958; -.
DR MGI; MGI:95893; H1f0.
DR VEuPathDB; HostDB:ENSMUSG00000096210; -.
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00810000125570; -.
DR HOGENOM; CLU_052897_1_1_1; -.
DR InParanoid; P10922; -.
DR OMA; HPAYSDM; -.
DR OrthoDB; 1565299at2759; -.
DR PhylomeDB; P10922; -.
DR TreeFam; TF313664; -.
DR Reactome; R-MMU-140342; Apoptosis induced DNA fragmentation.
DR Reactome; R-MMU-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR BioGRID-ORCS; 14958; 3 hits in 74 CRISPR screens.
DR ChiTaRS; H1f0; mouse.
DR PRO; PR:P10922; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P10922; protein.
DR Bgee; ENSMUSG00000096210; Expressed in medial ganglionic eminence and 260 other tissues.
DR Genevisible; P10922; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; ISO:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IMP:CAFA.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IMP:CAFA.
DR GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0030261; P:chromosome condensation; IBA:GO_Central.
DR GO; GO:0031507; P:heterochromatin assembly; ISO:MGI.
DR GO; GO:0045910; P:negative regulation of DNA recombination; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; ISO:MGI.
DR CDD; cd00073; H15; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005819; H1/H5.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00538; Linker_histone; 1.
DR PRINTS; PR00624; HISTONEH5.
DR SMART; SM00526; H15; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51504; H15; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ADP-ribosylation; Chromosome; Citrullination; DNA-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..194
FT /note="Histone H1.0"
FT /id="PRO_0000423208"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P07305"
FT CHAIN 2..194
FT /note="Histone H1.0, N-terminally processed"
FT /id="PRO_0000195913"
FT DOMAIN 24..97
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..194
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P07305"
FT MOD_RES 2
FT /note="N-acetylthreonine; in Histone H1.0, N-terminally
FT processed"
FT /evidence="ECO:0000250|UniProtKB:P07305"
FT MOD_RES 42
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P43275"
FT MOD_RES 104
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P07305"
FT CONFLICT 65
FT /note="D -> N (in Ref. 1; CAA31569)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="A -> G (in Ref. 1; CAA31569)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 194 AA; 20861 MW; 41EF06627E2AC81C CRC64;
MTENSTSAPA AKPKRAKASK KSTDHPKYSD MIVAAIQAEK NRAGSSRQSI QKYIKSHYKV
GENADSQIKL SIKRLVTTGV LKQTKGVGAS GSFRLAKGDE PKRSVAFKKT KKEVKKVATP
KKAAKPKKAA SKAPSKKPKA TPVKKAKKKP AATPKKAKKP KVVKVKPVKA SKPKKAKTVK
PKAKSSAKRA SKKK
