H14_RAT
ID H14_RAT Reviewed; 219 AA.
AC P15865;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Histone H1.4;
DE AltName: Full=H1d;
GN Name=H1-4 {ECO:0000250|UniProtKB:P10412};
GN Synonyms=H1f4 {ECO:0000312|RGD:2776};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=8439560; DOI=10.1016/0167-4781(93)90293-m;
RA Drabent B., Kunz C., Doenecke D.;
RT "A rat histone H2B pseudogene is closely associated with the histone H1d
RT gene.";
RL Biochim. Biophys. Acta 1172:193-196(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2373370; DOI=10.1016/0378-1119(90)90015-j;
RA Cole K.D., Kandala J.C., Kremer E., Kistler W.S.;
RT "Isolation of a genomic clone encoding the rat histone variant, H1d.";
RL Gene 89:265-269(1990).
RN [3]
RP PROTEIN SEQUENCE OF 2-17; 34-46 AND 55-75, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Pheochromocytoma;
RA Bienvenut W.V., von Kriegsheim A.F., Kolch W.;
RL Submitted (AUG-2006) to UniProtKB.
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-18, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 euchromatin. {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 -!- PTM: ADP-ribosylated on Ser-150 in response to DNA damage.
CC {ECO:0000250|UniProtKB:P10412}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; X67320; CAA47734.1; -; Genomic_DNA.
DR EMBL; M31229; AAA41327.1; -; Genomic_DNA.
DR PIR; JH0159; JH0159.
DR RefSeq; NP_579819.1; NM_133285.1.
DR AlphaFoldDB; P15865; -.
DR SMR; P15865; -.
DR BioGRID; 251423; 4.
DR IntAct; P15865; 3.
DR STRING; 10116.ENSRNOP00000066786; -.
DR iPTMnet; P15865; -.
DR PhosphoSitePlus; P15865; -.
DR jPOST; P15865; -.
DR PaxDb; P15865; -.
DR PRIDE; P15865; -.
DR Ensembl; ENSRNOT00000072564; ENSRNOP00000066786; ENSRNOG00000047459.
DR GeneID; 201097; -.
DR KEGG; rno:201097; -.
DR CTD; 50709; -.
DR RGD; 2776; H1f4.
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00940000155501; -.
DR HOGENOM; CLU_052897_7_0_1; -.
DR InParanoid; P15865; -.
DR OMA; PPWVDMI; -.
DR OrthoDB; 1565299at2759; -.
DR PRO; PR:P15865; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000047459; Expressed in spleen and 16 other tissues.
DR Genevisible; P15865; RN.
DR GO; GO:0000785; C:chromatin; TAS:RGD.
DR GO; GO:0000792; C:heterochromatin; ISO:RGD.
DR GO; GO:0000786; C:nucleosome; IDA:CAFA.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0043531; F:ADP binding; IDA:CAFA.
DR GO; GO:0016208; F:AMP binding; IDA:CAFA.
DR GO; GO:0005524; F:ATP binding; IDA:CAFA.
DR GO; GO:0005509; F:calcium ion binding; IDA:CAFA.
DR GO; GO:0031490; F:chromatin DNA binding; ISO:RGD.
DR GO; GO:0032564; F:dATP binding; IDA:CAFA.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:CAFA.
DR GO; GO:0005525; F:GTP binding; IDA:CAFA.
DR GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IDA:CAFA.
DR GO; GO:0030527; F:structural constituent of chromatin; ISO:RGD.
DR GO; GO:0006325; P:chromatin organization; ISO:RGD.
DR GO; GO:0030261; P:chromosome condensation; IBA:GO_Central.
DR GO; GO:0098532; P:histone H3-K27 trimethylation; ISO:RGD.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; ISO:RGD.
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:RGD.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
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; ADP-ribosylation; Chromosome; Citrullination;
KW Direct protein sequencing; DNA-binding; Hydroxylation; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 2..219
FT /note="Histone H1.4"
FT /id="PRO_0000195924"
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 92..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|Ref.3"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P43274"
FT MOD_RES 18
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0000250|UniProtKB:P43274"
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 150
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P10412"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10412"
FT CONFLICT 163..164
FT /note="Missing (in Ref. 2; AAA41327)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 219 AA; 21987 MW; 8977726B816119CC CRC64;
MSETAPAAPA APAPAEKTPI KKKARKAAGG AKRKASGPPV SELITKAVAA SKERSGVSLA
ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG ASGSFKLNKK AASGEAKPKA
KKAGAAKAKK PAGAAKKPKK ATGTATPKKS TKKTPKKAKK PAAAAGAKKA KSPKKAKATK
AKKAPKSPAK ARAVKPKAAK PKTSKPKAAK PKKTAAKKK
