H13_MOUSE
ID H13_MOUSE Reviewed; 221 AA.
AC P43277; Q8C6M4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Histone H1.3;
DE AltName: Full=H1 VAR.4;
DE AltName: Full=H1d;
GN Name=H1-3 {ECO:0000250|UniProtKB:P16402};
GN Synonyms=H1f3 {ECO:0000312|MGI:MGI:107502},
GN Hist1h1d {ECO:0000312|MGI:MGI:107502};
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 [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8589518; DOI=10.1007/bf00356166;
RA Drabent B., Franke K., Bode C., Kosciessa U., Bouterfa H., Hameister H.,
RA Doenecke D.;
RT "Isolation of two murine H1 histone genes and chromosomal mapping of the H1
RT gene complement.";
RL Mamm. Genome 6:505-511(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=8858344; DOI=10.1101/gr.6.8.688;
RA Wang Z.-F., Krasikov T., Frey M.R., Wang J., Matera A.G., Marzluff W.F.;
RT "Characterization of the mouse histone gene cluster on chromosome 13: 45
RT histone genes in three patches spread over 1Mb.";
RL Genome Res. 6:688-701(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12408966; DOI=10.1006/geno.2002.6850;
RA Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT "The human and mouse replication-dependent histone genes.";
RL Genomics 80:487-498(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Ovary;
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 [5]
RP PHOSPHORYLATION.
RX PubMed=8639656; DOI=10.1021/bi951914e;
RA Talasz H., Helliger W., Puschendorf B., Lindner H.;
RT "In vivo phosphorylation of histone H1 variants during the cell cycle.";
RL Biochemistry 35:1761-1767(1996).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=12808097; DOI=10.1128/mcb.23.13.4559-4572.2003;
RA Fan Y., Nikitina T., Morin-Kensicki E.M., Zhao J., Magnuson T.R.,
RA Woodcock C.L., Skoultchi A.I.;
RT "H1 linker histones are essential for mouse development and affect
RT nucleosome spacing in vivo.";
RL Mol. Cell. Biol. 23:4559-4572(2003).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT THR-18, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND LYS-17, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [9]
RP CITRULLINATION AT ARG-55.
RX PubMed=24463520; DOI=10.1038/nature12942;
RA Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT "Citrullination regulates pluripotency and histone H1 binding to
RT chromatin.";
RL Nature 507:104-108(2014).
RN [10]
RP HYDROXYBUTYRYLATION AT LYS-33; LYS-35; LYS-53; LYS-65; LYS-86; LYS-91;
RP LYS-107 AND LYS-141.
RX PubMed=27105115; DOI=10.1016/j.molcel.2016.03.036;
RA Xie Z., Zhang D., Chung D., Tang Z., Huang H., Dai L., Qi S., Li J.,
RA Colak G., Chen Y., Xia C., Peng C., Ruan H., Kirkey M., Wang D.,
RA Jensen L.M., Kwon O.K., Lee S., Pletcher S.D., Tan M., Lombard D.B.,
RA White K.P., Zhao H., Li J., Roeder R.G., Yang X., Zhao Y.;
RT "Metabolic regulation of gene expression by histone lysine beta-
RT hydroxybutyrylation.";
RL Mol. Cell 62:194-206(2016).
CC -!- FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes
CC forming the macromolecular structure known as the chromatin fiber.
CC Histones H1 are necessary for the condensation of nucleosome chains
CC into higher-order structured fibers. Acts also as a regulator of
CC individual gene transcription through chromatin remodeling, nucleosome
CC spacing and DNA methylation (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:12808097}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes in
CC euchromatin. {ECO:0000250}.
CC -!- DOMAIN: The C-terminal domain is required for high-affinity binding to
CC chromatin. {ECO:0000250}.
CC -!- PTM: H1 histones are progressively phosphorylated during the cell
CC cycle, becoming maximally phosphorylated during late G2 phase and M
CC phase, and being dephosphorylated sharply thereafter.
CC {ECO:0000250|UniProtKB:P43275}.
CC -!- PTM: Hydroxybutyrylation of histones is induced by starvation.
CC {ECO:0000269|PubMed:27105115}.
CC -!- PTM: Citrullination at Arg-55 (H1R54ci) by PADI4 takes place within the
CC DNA-binding site of H1 and results in its displacement from chromatin
CC and global chromatin decondensation, thereby promoting pluripotency and
CC stem cell maintenance. {ECO:0000269|PubMed:24463520}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Triple-deficient mice (H1-
CC 2, H1-3 and H1-4) die by midgestation with a broad range of defects.
CC These embryos have about 50% of the normal ratio of H1 to nucleosomes,
CC demonstrating that critical levels of total H1 histones are essential
CC for mouse embryogenesis. {ECO:0000269|PubMed:12808097}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; Z38128; CAA86288.1; -; Genomic_DNA.
DR EMBL; U62923; AAB05799.1; -; Genomic_DNA.
DR EMBL; AY158906; AAO06217.1; -; Genomic_DNA.
DR EMBL; AK054269; BAC35711.1; -; mRNA.
DR CCDS; CCDS26346.1; -.
DR PIR; B35245; B35245.
DR PIR; S49482; S49482.
DR RefSeq; NP_663759.3; NM_145713.4.
DR AlphaFoldDB; P43277; -.
DR SMR; P43277; -.
DR BioGRID; 200144; 7.
DR IntAct; P43277; 6.
DR MINT; P43277; -.
DR STRING; 10090.ENSMUSP00000044395; -.
DR iPTMnet; P43277; -.
DR PhosphoSitePlus; P43277; -.
DR EPD; P43277; -.
DR jPOST; P43277; -.
DR PaxDb; P43277; -.
DR PeptideAtlas; P43277; -.
DR PRIDE; P43277; -.
DR ProteomicsDB; 271373; -.
DR TopDownProteomics; P43277; -.
DR Antibodypedia; 58672; 139 antibodies from 16 providers.
DR DNASU; 14957; -.
DR Ensembl; ENSMUST00000045301; ENSMUSP00000044395; ENSMUSG00000052565.
DR GeneID; 14957; -.
DR KEGG; mmu:14957; -.
DR UCSC; uc007pub.3; mouse.
DR CTD; 14957; -.
DR MGI; MGI:107502; H1f3.
DR VEuPathDB; HostDB:ENSMUSG00000052565; -.
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00940000155501; -.
DR HOGENOM; CLU_052897_7_0_1; -.
DR InParanoid; P43277; -.
DR OMA; DHEVAPA; -.
DR OrthoDB; 1565299at2759; -.
DR PhylomeDB; P43277; -.
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; 14957; 7 hits in 74 CRISPR screens.
DR PRO; PR:P43277; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P43277; protein.
DR Bgee; ENSMUSG00000052565; Expressed in cerebellar layer and 87 other tissues.
DR ExpressionAtlas; P43277; baseline and differential.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
DR GO; GO:0030527; F:structural constituent of chromatin; IMP:MGI.
DR GO; GO:0006325; P:chromatin organization; IMP:MGI.
DR GO; GO:0030261; P:chromosome condensation; IBA:GO_Central.
DR GO; GO:0098532; P:histone H3-K27 trimethylation; IGI:MGI.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IGI:MGI.
DR GO; GO:0045910; P:negative regulation of DNA recombination; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP: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 1: Evidence at protein level;
KW Acetylation; Chromosome; Citrullination; DNA-binding; Hydroxylation;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:23806337"
FT CHAIN 2..221
FT /note="Histone H1.3"
FT /id="PRO_0000195916"
FT DOMAIN 37..110
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..221
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16402"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 18
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 33
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 35
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 53
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 55
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 65
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 86
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 91
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 105
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:A7MAZ5"
FT MOD_RES 107
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 141
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:27105115"
FT CONFLICT 57
FT /note="G -> C (in Ref. 4; BAC35711)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 221 AA; 22100 MW; 19D888981281E55C CRC64;
MSETAPAAPA APAPVEKTPV KKKAKKTGAA AGKRKASGPP VSELITKAVA ASKERSGVSL
AALKKALAAA GYDVEKNNSR IKLGLKSLVS KGTLVQTKGT GASGSFKLNK KAASGEAKPK
AKKAGAAKAK KPAGAAKKPK KATGAATPKK TAKKTPKKAK KPAAAAGAKK VSKSPKKVKA
AKPKKAAKSP AKAKAPKAKA SKPKASKPKA TKAKKAAPRK K
