H12_BOVIN
ID H12_BOVIN Reviewed; 213 AA.
AC P02253; A3KN02;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Histone H1.2;
DE AltName: Full=CTL-1;
GN Name=H1-2 {ECO:0000250|UniProtKB:P16403};
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=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-105.
RX PubMed=7204387; DOI=10.1016/s0021-9258(19)69718-8;
RA Liao L.W., Cole R.D.;
RT "The amino acid sequence of residues 1-104 of CTL-1, a bovine H1 histone.";
RL J. Biol. Chem. 256:3024-3029(1981).
RN [4]
RP AMINO-ACID COMPOSITION OF TRYPTIC PEPTIDES.
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 [5]
RP PHOSPHORYLATION AT SER-104.
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 [6]
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: 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 -!- INTERACTION:
CC P02253; Q57V41: SIR2rp1; Xeno; NbExp=7; IntAct=EBI-7580031, EBI-7579996;
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. {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. {ECO:0000250}.
CC -!- PTM: Crotonylation (Kcr) is specifically present in male germ cells and
CC marks testis-specific genes in post-meiotic cells, including X-linked
CC genes that escape sex chromosome inactivation in haploid cells.
CC Crotonylation marks active promoters and enhancers and confers
CC resistance to transcriptional repressors. It is also associated with
CC post-meiotically activated genes on autosomes.
CC {ECO:0000250|UniProtKB:P15864}.
CC -!- PTM: ADP-ribosylated on Ser-188 in response to DNA damage.
CC {ECO:0000250|UniProtKB:P16403}.
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:P15864}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; DAAA02055500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC133454; AAI33455.1; -; mRNA.
DR PIR; A92316; HSBO11.
DR RefSeq; NP_001076894.1; NM_001083425.1.
DR AlphaFoldDB; P02253; -.
DR SMR; P02253; -.
DR BioGRID; 170598; 4.
DR IntAct; P02253; 1.
DR MINT; P02253; -.
DR STRING; 9913.ENSBTAP00000015499; -.
DR iPTMnet; P02253; -.
DR PaxDb; P02253; -.
DR PeptideAtlas; P02253; -.
DR PRIDE; P02253; -.
DR GeneID; 513971; -.
DR KEGG; bta:513971; -.
DR CTD; 3006; -.
DR eggNOG; KOG4012; Eukaryota.
DR HOGENOM; CLU_052897_7_0_1; -.
DR InParanoid; P02253; -.
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; 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|PubMed:7204387"
FT CHAIN 2..213
FT /note="Histone H1.2"
FT /id="PRO_0000195903"
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 95..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..190
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..213
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine; partial"
FT /evidence="ECO:0000250|UniProtKB:P16403"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16403"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 23
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 26
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 27
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 34
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 34
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P16403"
FT MOD_RES 34
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P16403"
FT MOD_RES 46
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 52
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 52
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 54
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 63
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 64
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 64
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 64
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P16403"
FT MOD_RES 75
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 81
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 85
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 85
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 85
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P16403"
FT MOD_RES 90
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 90
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 90
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P16403"
FT MOD_RES 97
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 97
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P16403"
FT MOD_RES 97
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 104
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:3134256"
FT MOD_RES 106
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 110
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 117
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 121
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 129
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 136
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 146
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16403"
FT MOD_RES 148
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 159
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 159
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P16403"
FT MOD_RES 168
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P15864"
FT MOD_RES 168
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P16403"
FT MOD_RES 187
FT /note="N6-methyllysine; by EHMT1 and EHMT2"
FT /evidence="ECO:0000250|UniProtKB:P16403"
FT MOD_RES 188
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P16403"
SQ SEQUENCE 213 AA; 21356 MW; B5D69F890B6FB5DD CRC64;
MSETAPAAPA AAPPAEKTPV KKKAAKKPAG ARRKASGPPV SELITKAVAA SKERSGVSLA
ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG ASGSFKLNKK AATGEAKPKA
KKAGAAKPKK AAGAAKKTKK ATGAATPKKT AKKTPKKAKK PAAAAVTKKV AKSPKKAKAA
KPKKAAKSAA KAVKPKAAKP KVAKPKKAAP KKK
