H12_CAEEL
ID H12_CAEEL Reviewed; 191 AA.
AC P15796; O18649; Q8IU03; Q8MXR7;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Histone H1.2;
DE AltName: Full=Histone H1-like protein 2;
GN Name=hil-2; ORFNames=Y73B6BL.9;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM A).
RC STRAIN=Bristol N2, and him-8;
RX PubMed=11245572; DOI=10.1242/dev.128.7.1069;
RA Jedrusik M.A., Schulze E.;
RT "A single histone H1 isoform (H1.1) is essential for chromatin silencing
RT and germline development in Caenorhabditis elegans.";
RL Development 128:1069-1080(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP PROTEIN SEQUENCE OF 2-191 (ISOFORM A), AND ACETYLATION AT SER-2.
RC STRAIN=Bristol N2;
RX PubMed=2407235; DOI=10.1042/bj2650739;
RA Vanfleteren J.R., van Bun S.M., de Baere I., van Beeumen J.J.;
RT "The primary structure of a minor isoform (H1.2) of histone H1 from the
RT nematode Caenorhabditis elegans.";
RL Biochem. J. 265:739-746(1990).
CC -!- FUNCTION: Histones H1 are necessary for the condensation of nucleosome
CC chains into higher-order structures.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=P15796-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P15796-2; Sequence=VSP_011759;
CC -!- MISCELLANEOUS: H1.2 is a minor form.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF017812; AAB70559.1; -; Genomic_DNA.
DR EMBL; AF017811; AAB70666.1; -; mRNA.
DR EMBL; FO081731; CCD74158.2; -; Genomic_DNA.
DR EMBL; FO081731; CCD74159.2; -; Genomic_DNA.
DR PIR; T42232; T42232.
DR RefSeq; NP_741417.4; NM_171356.5.
DR RefSeq; NP_741418.2; NM_171909.5. [P15796-2]
DR AlphaFoldDB; P15796; -.
DR SMR; P15796; -.
DR BioGRID; 42511; 2.
DR STRING; 6239.Y73B6BL.9a; -.
DR iPTMnet; P15796; -.
DR EPD; P15796; -.
DR PaxDb; P15796; -.
DR PeptideAtlas; P15796; -.
DR PRIDE; P15796; -.
DR EnsemblMetazoa; Y73B6BL.9a.1; Y73B6BL.9a.1; WBGene00001853. [P15796-1]
DR EnsemblMetazoa; Y73B6BL.9b.1; Y73B6BL.9b.1; WBGene00001853. [P15796-2]
DR GeneID; 177390; -.
DR UCSC; Y73B6BL.9b; c. elegans. [P15796-1]
DR CTD; 177390; -.
DR WormBase; Y73B6BL.9a; CE47059; WBGene00001853; hil-2. [P15796-1]
DR WormBase; Y73B6BL.9b; CE46839; WBGene00001853; hil-2. [P15796-2]
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00970000195980; -.
DR HOGENOM; CLU_052897_1_1_1; -.
DR InParanoid; P15796; -.
DR OrthoDB; 1565299at2759; -.
DR PRO; PR:P15796; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001853; Expressed in embryo and 4 other tissues.
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; Alternative splicing; Chromosome; Direct protein sequencing;
KW DNA-binding; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..191
FT /note="Histone H1.2"
FT /id="PRO_0000195982"
FT DOMAIN 37..113
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..181
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000305|PubMed:2407235"
FT VAR_SEQ 49..116
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_011759"
FT CONFLICT 28
FT /note="K -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 31..32
FT /note="KA -> SS (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 45..51
FT /note="VTAAISS -> IKEAIKQ (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="K -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="A -> P (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 191 AA; 19779 MW; 927F7C2BD4C70864 CRC64;
MSDVTVAETP AVKTPTKAPK APKSKTTKEP KAKVAAAHPP FINMVTAAIS SLKERKGSSK
IAILKYITAN YKVGDQLTKI NSRLRAALNK GVASKALVQS VGNGASGRFR VAEKAAATKK
PVAKKPVAKK AATGEKKAKK TTVAKKTGDK VKKAKSPKKI AKPAAKKVAK SPAKKAAPKK
APAKKAAAPK A
