ID   H15_MOUSE               Reviewed;         223 AA.
AC   P43276; Q9CRM8;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 182.
DE   RecName: Full=Histone H1.5;
DE   AltName: Full=H1 VAR.5;
DE   AltName: Full=H1b;
GN   Name=H1-5; Synonyms=H1f5, Hist1h1b;
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=Blood;
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=10.1016/s0888-7543(02)96850-3;
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] OF 1-220.
RC   STRAIN=C57BL/6J; TISSUE=Embryonic kidney;
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   INTERACTION WITH MSX1.
RX   PubMed=16600910; DOI=10.1101/gad.1392006;
RA   Lee H., Quinn J.C., Prasanth K.V., Swiss V.A., Economides K.D.,
RA   Camacho M.M., Spector D.L., Abate-Shen C.;
RT   "PIAS1 confers DNA-binding specificity on the Msx1 homeoprotein.";
RL   Genes Dev. 20:784-794(2006).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
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).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-17; LYS-46 AND LYS-75,
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-34, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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-54.
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).
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   -!- SUBUNIT: Interacts with MSX1. {ECO:0000269|PubMed:16600910}.
CC   -!- INTERACTION:
CC       P43276; P13297: Msx1; NbExp=3; IntAct=EBI-903960, EBI-903969;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P16401}.
CC       Chromosome {ECO:0000250|UniProtKB:P16401}. Note=Mainly localizes with
CC       heterochromatin (By similarity). Associates with actively transcribed
CC       chromatin and not heterochromatin (By similarity).
CC       {ECO:0000250|UniProtKB:P16401}.
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:P16401}.
CC   -!- PTM: Citrullination at Arg-54 (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   -!- PTM: Hydroxybutyrylation of histones is induced by starvation.
CC       {ECO:0000250|UniProtKB:P43277}.
CC   -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00837}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z46227; CAA86299.1; -; Genomic_DNA.
DR   EMBL; U62922; AAB05798.1; -; Genomic_DNA.
DR   EMBL; AY158904; AAO06215.1; -; Genomic_DNA.
DR   EMBL; AK020117; BAB32001.1; -; mRNA.
DR   CCDS; CCDS26295.1; -.
DR   PIR; A35245; A35245.
DR   PIR; S49492; S49492.
DR   RefSeq; NP_064418.1; NM_020034.2.
DR   AlphaFoldDB; P43276; -.
DR   SMR; P43276; -.
DR   BioGRID; 208131; 19.
DR   IntAct; P43276; 5.
DR   MINT; P43276; -.
DR   STRING; 10090.ENSMUSP00000079356; -.
DR   GlyGen; P43276; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P43276; -.
DR   PhosphoSitePlus; P43276; -.
DR   EPD; P43276; -.
DR   jPOST; P43276; -.
DR   PaxDb; 10090-ENSMUSP00000079356; -.
DR   PeptideAtlas; P43276; -.
DR   ProteomicsDB; 269705; -.
DR   Pumba; P43276; -.
DR   Antibodypedia; 54587; 252 antibodies from 22 providers.
DR   DNASU; 56702; -.
DR   Ensembl; ENSMUST00000080511.3; ENSMUSP00000079356.3; ENSMUSG00000058773.3.
DR   GeneID; 56702; -.
DR   KEGG; mmu:56702; -.
DR   UCSC; uc007pri.2; mouse.
DR   AGR; MGI:1861461; -.
DR   CTD; 56702; -.
DR   MGI; MGI:1861461; H1f5.
DR   VEuPathDB; HostDB:ENSMUSG00000058773; -.
DR   eggNOG; KOG4012; Eukaryota.
DR   GeneTree; ENSGT00940000162950; -.
DR   HOGENOM; CLU_052897_7_0_1; -.
DR   InParanoid; P43276; -.
DR   OMA; THPSWID; -.
DR   OrthoDB; 5362469at2759; -.
DR   PhylomeDB; P43276; -.
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; 56702; 5 hits in 80 CRISPR screens.
DR   PRO; PR:P43276; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; P43276; Protein.
DR   Bgee; ENSMUSG00000058773; Expressed in uterus and 88 other cell types or tissues.
DR   GO; GO:0000785; C:chromatin; ISO:MGI.
DR   GO; GO:0005694; C:chromosome; ISO:MGI.
DR   GO; GO:0000792; C:heterochromatin; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
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:0042826; F:histone deacetylase binding; ISO:MGI.
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:0006325; P:chromatin organization; ISO:MGI.
DR   GO; GO:0030261; P:chromosome condensation; IBA:GO_Central.
DR   GO; GO:0071169; P:establishment of protein localization to chromatin; ISO:MGI.
DR   GO; GO:0007517; P:muscle organ development; IPI: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; ISO:MGI.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR   CDD; cd00073; H15; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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   PANTHER; PTHR11467; HISTONE H1; 1.
DR   PANTHER; PTHR11467:SF24; HISTONE H1.5; 1.
DR   Pfam; PF00538; Linker_histone; 1.
DR   PRINTS; PR00624; HISTONEH5.
DR   SMART; SM00526; H15; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51504; H15; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosome; Citrullination; DNA-binding; Hydroxylation;
KW   Methylation; 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..223
FT                   /note="Histone H1.5"
FT                   /id="PRO_0000195918"
FT   DOMAIN          36..109
FT                   /note="H15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          91..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..223
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:P16401"
FT   MOD_RES         17
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355"
FT   MOD_RES         27
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P16401"
FT   MOD_RES         34
FT                   /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P43277"
FT   MOD_RES         34
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         36
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         46
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         52
FT                   /note="N6-(beta-hydroxybutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P43277"
FT   MOD_RES         54
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000269|PubMed:24463520"
FT   MOD_RES         64
FT                   /note="N6-(beta-hydroxybutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P43277"
FT   MOD_RES         75
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         85
FT                   /note="N6-(beta-hydroxybutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P43277"
FT   MOD_RES         90
FT                   /note="N6-(beta-hydroxybutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P43277"
FT   MOD_RES         106
FT                   /note="N6-(beta-hydroxybutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P43277"
FT   MOD_RES         135
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P16401"
FT   MOD_RES         152
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P16401"
FT   MOD_RES         165
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P16401"
FT   MOD_RES         170
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16401"
FT   MOD_RES         186
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16401"
FT   CONFLICT        61
FT                   /note="A -> T (in Ref. 3; BAB32001)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        120
FT                   /note="A -> V (in Ref. 3; BAB32001)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        137
FT                   /note="K -> N (in Ref. 3; BAB32001)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        195
FT                   /note="S -> F (in Ref. 3; BAB32001)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   223 AA;  22576 MW;  B9C26AC31C2716B6 CRC64;
     MSETAPAETA APAPVEKSPA KKKTTKKAGA AKRKATGPPV SELITKAVSA SKERGGVSLP
     ALKKALAAGG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG ASGSFKLNKK AASGEAKPKA
     KKTGAAKAKK PAGATPKKPK KTAGAKKTVK KTPKKAKKPA AAGVKKVAKS PKKAKAAAKP
     KKAAKSPAKP KAVKSKASKP KVTKPKTAKP KAAKAKKAVS KKK
//