H10_RAT
ID H10_RAT Reviewed; 194 AA.
AC P43278;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Histone H1.0;
DE AltName: Full=Histone H1';
DE AltName: Full=Histone H1(0);
DE Contains:
DE RecName: Full=Histone H1.0, N-terminally processed;
GN Name=H1-0; Synonyms=H1f0;
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 [MRNA].
RA Suau P., Monsalves C., Martinez P., Vidal J.M., Ponte I.;
RL Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-194.
RC STRAIN=Sprague-Dawley;
RX PubMed=8479926; DOI=10.1093/nar/21.7.1674;
RA Castiglia D., Gristina R., Scaturro M., di Liegro I.;
RT "Cloning and analysis of cDNA for rat histone H1(0).";
RL Nucleic Acids Res. 21:1674-1674(1993).
CC -!- FUNCTION: Histones H1 are necessary for the condensation of nucleosome
CC chains into higher-order structures. The histones H1.0 are found in
CC cells that are in terminal stages of differentiation or that have low
CC rates of cell division.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- PTM: ADP-ribosylated on Ser-104 in response to DNA damage.
CC {ECO:0000250|UniProtKB:P07305}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; X72624; CAA51199.1; -; mRNA.
DR EMBL; BC061842; AAH61842.1; -; mRNA.
DR EMBL; X70685; CAA50020.1; -; mRNA.
DR PIR; S47348; S47348.
DR RefSeq; NP_036710.1; NM_012578.2.
DR AlphaFoldDB; P43278; -.
DR SMR; P43278; -.
DR BioGRID; 246602; 1.
DR STRING; 10116.ENSRNOP00000053053; -.
DR iPTMnet; P43278; -.
DR PhosphoSitePlus; P43278; -.
DR jPOST; P43278; -.
DR PaxDb; P43278; -.
DR PRIDE; P43278; -.
DR Ensembl; ENSRNOT00000112015; ENSRNOP00000093399; ENSRNOG00000063732.
DR GeneID; 24437; -.
DR KEGG; rno:24437; -.
DR UCSC; RGD:2777; rat.
DR CTD; 14958; -.
DR RGD; 2777; H1f0.
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00810000125570; -.
DR InParanoid; P43278; -.
DR OrthoDB; 1565299at2759; -.
DR PhylomeDB; P43278; -.
DR TreeFam; TF313664; -.
DR Reactome; R-RNO-140342; Apoptosis induced DNA fragmentation.
DR Reactome; R-RNO-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR PRO; PR:P43278; -.
DR Proteomes; UP000002494; Chromosome 7.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0000791; C:euchromatin; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0017053; C:transcription repressor complex; ISO:RGD.
DR GO; GO:0031490; F:chromatin DNA binding; ISO:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:RGD.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; ISO:RGD.
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:0031507; P:heterochromatin assembly; ISO:RGD.
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:2000679; P:positive regulation of transcription regulatory region DNA binding; 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 2: Evidence at transcript level;
KW Acetylation; ADP-ribosylation; Chromosome; Citrullination; DNA-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..194
FT /note="Histone H1.0"
FT /id="PRO_0000423210"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P07305"
FT CHAIN 2..194
FT /note="Histone H1.0, N-terminally processed"
FT /id="PRO_0000195923"
FT DOMAIN 24..97
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..194
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P07305"
FT MOD_RES 2
FT /note="N-acetylthreonine; in Histone H1.0, N-terminally
FT processed"
FT /evidence="ECO:0000250|UniProtKB:P07305"
FT MOD_RES 42
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P43275"
FT MOD_RES 104
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P07305"
SQ SEQUENCE 194 AA; 20885 MW; 352B696568B95171 CRC64;
MTENSTSTPA AKPKRAKAAK KSTDHPKYSD MIVAAIQAEK NRAGSSRQSI QKYIKSHYKV
GENADSQIKL SIKRLVTTGV LKQTKGVGAS GSFRLAKGDE PKRSVAFKKT KKEVKKVATP
KKAAKPKKAA SKAPSKKPKA TPVKKAKKKP AATPKKAKKP KIVKVKPVKA SKPKKAKPVK
PKAKSSAKRA SKKK
