H14_RABIT
ID H14_RABIT Reviewed; 219 AA.
AC P02252; G1T7E4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Histone H1.4;
GN Name=H1-4 {ECO:0000250|UniProtKB:P10412};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke;
RG The Genome Sequencing Platform;
RA Di Palma F., Heiman D., Young S., Gnerre S., Johnson J., Lander E.S.,
RA Lindblad-Toh K.;
RT "Genome Sequence of Oryctolagus cuniculus (European rabbit).";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-71, ACETYLATION AT SER-2, AND PHOSPHORYLATION AT
RP SER-36.
RX PubMed=5167020; DOI=10.1016/s0021-9258(19)45870-5;
RA Rall S.C., Cole R.D.;
RT "Amino acid sequence and sequence variability of the amino-terminal regions
RT of lysine-rich histones.";
RL J. Biol. Chem. 246:7175-7190(1971).
RN [3]
RP PROTEIN SEQUENCE OF 3-72.
RX PubMed=5547708; DOI=10.1016/s0021-9258(18)62397-x;
RA Langan T.A., Rall S.C., Cole R.D.;
RT "Variation in primary structure at a phosphorylation site in lysine-rich
RT histones.";
RL J. Biol. Chem. 246:1942-1944(1971).
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 -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes in
CC heterochromatin. {ECO:0000250}.
CC -!- DOMAIN: The C-terminal domain is required for high-affinity binding to
CC chromatin.
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: Acetylated at Lys-26. Deacetylated at Lys-26 by SIRT1.
CC {ECO:0000250|UniProtKB:P10412}.
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:0000250|UniProtKB:P43274}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; AAGW02052081; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A02579; A02579.
DR AlphaFoldDB; P02252; -.
DR SMR; P02252; -.
DR STRING; 9986.ENSOCUP00000012414; -.
DR iPTMnet; P02252; -.
DR eggNOG; KOG4012; Eukaryota.
DR HOGENOM; CLU_052897_7_0_1; -.
DR InParanoid; P02252; -.
DR OMA; PPWVDMI; -.
DR TreeFam; TF313664; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
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; Direct protein sequencing;
KW DNA-binding; Hydroxylation; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:5167020"
FT CHAIN 2..219
FT /note="Histone H1.4"
FT /id="PRO_0000195922"
FT DOMAIN 36..109
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..219
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:5167020"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15865"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P43274"
FT MOD_RES 18
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10412"
FT MOD_RES 26
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10412"
FT MOD_RES 26
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10412"
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:0000250|UniProtKB:P43274"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:5167020"
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:0000250|UniProtKB:P43274"
FT MOD_RES 64
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
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 146
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10412"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10412"
FT CONFLICT 4
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 8..9
FT /note="AP -> ET (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 16..17
FT /note="EK -> KSPA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 23..25
FT /note="KAR -> ARKK (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 219 AA; 21897 MW; 08DB0876BD4BC162 CRC64;
MSETAPAAPA APAPAEKTPV KKKARKSAGA AKRKASGPPV SELITKAVAA SKERSGVSLA
ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG ASGSFKLNKK AAAGEAKPKP
KKAGAAKPKK PAGAAKKPKK ATGAATPKKG AKKTPKKAKK PAAAAGAKKA KSPKKAKAAK
PKKAPKSPAK AKAVKPKAAK PKAAKPKTAK PKKAPAKKK
