H11_BOVIN
ID H11_BOVIN Reviewed; 218 AA.
AC G3N131;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Histone H1.1;
DE AltName: Full=Histone H1a;
GN Name=H1-1 {ECO:0000250|UniProtKB:Q02539}; Synonyms=HIST1H1A;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP PHOSPHORYLATION AT SER-107.
RX PubMed=3134256; DOI=10.1016/0014-5793(88)81296-1;
RA Jakes S., Hastings T.G., Reimann E.M., Schlender K.K.;
RT "Identification of the phosphoserine residue in histone H1 phosphorylated
RT by protein kinase C.";
RL FEBS Lett. 234:31-34(1988).
RN [3]
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).
CC -!- FUNCTION: H1 histones bind to linker DNA between nucleosomes forming
CC the macromolecular structure known as the chromatin fiber. H1 histones
CC are necessary for the condensation of nucleosome chains into higher-
CC order structured fibers. Acts also as a regulator of individual gene
CC transcription through chromatin remodeling (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DFFB. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837}.
CC Chromosome {ECO:0000255|PROSITE-ProRule:PRU00837}. Note=Mainly
CC localizes in 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: 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; DAAA02055502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_010816821.1; XM_010818519.2.
DR RefSeq; XP_010823721.1; XM_010825419.2.
DR AlphaFoldDB; G3N131; -.
DR SMR; G3N131; -.
DR BioGRID; 545757; 4.
DR STRING; 9913.ENSBTAP00000055553; -.
DR iPTMnet; G3N131; -.
DR PaxDb; G3N131; -.
DR PRIDE; G3N131; -.
DR GeneID; 618164; -.
DR KEGG; bta:618164; -.
DR CTD; 3024; -.
DR eggNOG; KOG4012; Eukaryota.
DR HOGENOM; CLU_052897_7_0_1; -.
DR InParanoid; G3N131; -.
DR OrthoDB; 1565299at2759; -.
DR TreeFam; TF313664; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; 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: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..218
FT /note="Histone H1.1"
FT /id="PRO_0000419133"
FT DOMAIN 39..112
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 116..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..218
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; by PKC"
FT /evidence="ECO:0000269|PubMed:3134256"
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 206
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P43275"
SQ SEQUENCE 218 AA; 22100 MW; 81014DD34AA6E4A4 CRC64;
MSEVALPAPA ASTSPEKPSA GKKAKKPAKA AAAAKKKPAG PSVSELIVQA VSSSKERSGV
SLAALKKALA AAGYDVEKNN SRIKLGLKSL VGKGTLVQTK GTGASGSFKL NKKVASVDAK
PTATKVATKT KVTSASKKPK KASGAAAAKK SVKTPKKARK SVLTKKSSKS PKKPKAVKPK
KVAKSPAKAK AVKPKGAKVK VTKPKTAAKP KKAAPKKK
