H13_BOVIN
ID H13_BOVIN Reviewed; 221 AA.
AC A7MAZ5;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Histone H1.3;
GN Name=H1-3 {ECO:0000250|UniProtKB:P16402};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION AT SER-105.
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).
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, nucleosome spacing and DNA
CC methylation (By similarity). {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-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:0000250|UniProtKB:P43277}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; DAAA02055497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC151257; AAI51258.1; -; mRNA.
DR RefSeq; NP_001094536.1; NM_001101066.1.
DR AlphaFoldDB; A7MAZ5; -.
DR SMR; A7MAZ5; -.
DR STRING; 9913.ENSBTAP00000051256; -.
DR iPTMnet; A7MAZ5; -.
DR PaxDb; A7MAZ5; -.
DR PRIDE; A7MAZ5; -.
DR GeneID; 509275; -.
DR KEGG; bta:509275; -.
DR CTD; 3007; -.
DR eggNOG; KOG4012; Eukaryota.
DR HOGENOM; CLU_052897_7_0_1; -.
DR InParanoid; A7MAZ5; -.
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 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:P16402"
FT CHAIN 2..221
FT /note="Histone H1.3"
FT /id="PRO_0000419136"
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 87..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..104
FT /note="Polar residues"
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:0000250|UniProtKB:P16402"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16402"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 18
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16402"
FT MOD_RES 35
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 53
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 55
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 65
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 86
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 91
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 105
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:3134256"
FT MOD_RES 107
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
SQ SEQUENCE 221 AA; 22154 MW; 5EE0DA1416332D1D CRC64;
MSETAPVAPA APAPAEKTPV KKKAKKSGVA AGKRKASGPP VSELITKAVA ASKERSGVSL
AALKKALAAA GYDVEKNNSR IKLGLKSLVS KGTLVQTKGT GASGSFKLNK KAATGEAKPK
GKKAGAAKPK KAAGAAKKPK KSTGAATPKK AAKKTPKKVK KPAAAAGTKK VAKSPKKAKA
AKPKKPTKSP AKAKAPKPKA AKPKAAKPKA TKAKKAVSKK K
