H11_HUMAN
ID H11_HUMAN Reviewed; 215 AA.
AC Q02539; Q3MJ34;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Histone H1.1;
DE AltName: Full=Histone H1a;
GN Name=H1-1 {ECO:0000312|HGNC:HGNC:4715}; Synonyms=H1F1, HIST1H1A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=2759094;
RA Eick S., Nicolai M., Mumberg D., Doenecke D.;
RT "Human H1 histones: conserved and varied sequence elements in two H1
RT subtype genes.";
RL Eur. J. Cell Biol. 49:110-115(1989).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 NOMENCLATURE.
RX PubMed=8003976; DOI=10.1002/pro.5560030406;
RA Parseghian M.H., Henschen A.H., Krieglstein K.G., Hamkalo B.A.;
RT "A proposal for a coherent mammalian histone H1 nomenclature correlated
RT with amino acid sequences.";
RL Protein Sci. 3:575-587(1994).
RN [6]
RP DOMAIN, AND MUTAGENESIS OF THR-152 AND SER-183.
RX PubMed=14985337; DOI=10.1074/jbc.m400070200;
RA Hendzel M.J., Lever M.A., Crawford E., Th'ng J.P.;
RT "The C-terminal domain is the primary determinant of histone H1 binding to
RT chromatin in vivo.";
RL J. Biol. Chem. 279:20028-20034(2004).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15911621; DOI=10.1074/jbc.m501627200;
RA Th'ng J.P., Sung R., Ye M., Hendzel M.J.;
RT "H1 family histones in the nucleus. Control of binding and localization by
RT the C-terminal domain.";
RL J. Biol. Chem. 280:27809-27814(2005).
RN [8]
RP INTERACTION WITH DFFB.
RX PubMed=19882353; DOI=10.1007/s10495-009-0418-7;
RA Ninios Y.P., Sekeri-Pataryas K.E., Sourlingas T.G.;
RT "Histone H1 subtype preferences of DFF40 and possible nuclear localization
RT of DFF40/45 in normal and trichostatin A-treated NB4 leukemic cells.";
RL Apoptosis 15:128-138(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
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 DFFB. {ECO:0000269|PubMed:19882353}.
CC -!- INTERACTION:
CC Q02539; Q8IUE6: H2AC21; NbExp=2; IntAct=EBI-932603, EBI-1642157;
CC Q02539; O94811: TPPP; NbExp=2; IntAct=EBI-932603, EBI-3927802;
CC Q02539; Q57V41: SIR2rp1; Xeno; NbExp=2; IntAct=EBI-932603, EBI-7579996;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837,
CC ECO:0000269|PubMed:15911621}. Chromosome {ECO:0000255|PROSITE-
CC ProRule:PRU00837, ECO:0000269|PubMed:15911621}. Note=Mainly localizes
CC in euchromatin.
CC -!- DOMAIN: The C-terminal domain is required for high-affinity binding to
CC chromatin. {ECO:0000269|PubMed:14985337}.
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: Citrullination at Arg-57 (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:0000250|UniProtKB:P43275}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; X57130; CAA40409.1; -; Genomic_DNA.
DR EMBL; AF531299; AAN06699.1; -; Genomic_DNA.
DR EMBL; U91328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069492; AAH69492.1; -; mRNA.
DR EMBL; BC101593; AAI01594.1; -; mRNA.
DR EMBL; BC112140; AAI12141.1; -; mRNA.
DR CCDS; CCDS4569.1; -.
DR PIR; S26363; S26363.
DR RefSeq; NP_005316.1; NM_005325.3.
DR AlphaFoldDB; Q02539; -.
DR SMR; Q02539; -.
DR BioGRID; 109275; 461.
DR CORUM; Q02539; -.
DR IntAct; Q02539; 211.
DR MINT; Q02539; -.
DR STRING; 9606.ENSP00000244573; -.
DR CarbonylDB; Q02539; -.
DR GlyGen; Q02539; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q02539; -.
DR PhosphoSitePlus; Q02539; -.
DR SwissPalm; Q02539; -.
DR BioMuta; HIST1H1A; -.
DR DMDM; 18202479; -.
DR EPD; Q02539; -.
DR jPOST; Q02539; -.
DR MassIVE; Q02539; -.
DR MaxQB; Q02539; -.
DR PaxDb; Q02539; -.
DR PeptideAtlas; Q02539; -.
DR PRIDE; Q02539; -.
DR ProteomicsDB; 58107; -.
DR Antibodypedia; 25489; 356 antibodies from 23 providers.
DR DNASU; 3024; -.
DR Ensembl; ENST00000244573.5; ENSP00000244573.4; ENSG00000124610.5.
DR GeneID; 3024; -.
DR KEGG; hsa:3024; -.
DR MANE-Select; ENST00000244573.5; ENSP00000244573.4; NM_005325.4; NP_005316.1.
DR UCSC; uc003nfo.4; human.
DR CTD; 3024; -.
DR DisGeNET; 3024; -.
DR GeneCards; H1-1; -.
DR HGNC; HGNC:4715; H1-1.
DR HPA; ENSG00000124610; Not detected.
DR MIM; 142709; gene.
DR neXtProt; NX_Q02539; -.
DR OpenTargets; ENSG00000124610; -.
DR VEuPathDB; HostDB:ENSG00000124610; -.
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00940000163269; -.
DR HOGENOM; CLU_052897_7_0_1; -.
DR InParanoid; Q02539; -.
DR OMA; QFKIAKF; -.
DR OrthoDB; 1565299at2759; -.
DR PhylomeDB; Q02539; -.
DR TreeFam; TF313664; -.
DR PathwayCommons; Q02539; -.
DR Reactome; R-HSA-140342; Apoptosis induced DNA fragmentation.
DR Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR SignaLink; Q02539; -.
DR SIGNOR; Q02539; -.
DR BioGRID-ORCS; 3024; 21 hits in 1077 CRISPR screens.
DR GeneWiki; HIST1H1A; -.
DR GenomeRNAi; 3024; -.
DR Pharos; Q02539; Tbio.
DR PRO; PR:Q02539; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q02539; protein.
DR Bgee; ENSG00000124610; Expressed in oocyte and 33 other tissues.
DR Genevisible; Q02539; HS.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; IEA:Ensembl.
DR GO; GO:0031490; F:chromatin DNA binding; IMP:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
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:0045910; P:negative regulation of DNA recombination; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IBA:GO_Central.
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:0000250|UniProtKB:P43275"
FT CHAIN 2..215
FT /note="Histone H1.1"
FT /id="PRO_0000195905"
FT DOMAIN 39..112
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..215
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P43275"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A3K5"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A3K5"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P43275"
FT MOD_RES 37
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A3K5"
FT MOD_RES 55
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 57
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P43275"
FT MOD_RES 67
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 78
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P43275"
FT MOD_RES 88
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 93
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 93
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43275"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:G3N131"
FT MOD_RES 109
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 125
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P43275"
FT MOD_RES 204
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P43275"
FT VARIANT 99
FT /note="T -> I (in dbSNP:rs417751)"
FT /id="VAR_049301"
FT VARIANT 115
FT /note="S -> F (in dbSNP:rs34541321)"
FT /id="VAR_049302"
FT VARIANT 140
FT /note="K -> R (in dbSNP:rs16891235)"
FT /id="VAR_049303"
FT MUTAGEN 152
FT /note="T->E: Significant destabilization of binding to
FT chromatin."
FT /evidence="ECO:0000269|PubMed:14985337"
FT MUTAGEN 183
FT /note="S->E: Significant destabilization of binding to
FT chromatin."
FT /evidence="ECO:0000269|PubMed:14985337"
SQ SEQUENCE 215 AA; 21842 MW; 854B03622D78774A CRC64;
MSETVPPAPA ASAAPEKPLA GKKAKKPAKA AAASKKKPAG PSVSELIVQA ASSSKERGGV
SLAALKKALA AAGYDVEKNN SRIKLGIKSL VSKGTLVQTK GTGASGSFKL NKKASSVETK
PGASKVATKT KATGASKKLK KATGASKKSV KTPKKAKKPA ATRKSSKNPK KPKTVKPKKV
AKSPAKAKAV KPKAAKARVT KPKTAKPKKA APKKK
