H18_HUMAN
ID H18_HUMAN Reviewed; 346 AA.
AC Q8IZA3; Q86WT7;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Histone H1.8 {ECO:0000305};
DE AltName: Full=Histone H1oo;
DE AltName: Full=Oocyte-specific histone H1;
DE AltName: Full=Oocyte-specific linker histone H1;
DE Short=osH1;
GN Name=H1-8 {ECO:0000312|HGNC:HGNC:18463};
GN Synonyms=H1FOO {ECO:0000312|HGNC:HGNC:18463}, H1OO, OSH1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=12711322; DOI=10.1016/s0006-291x(03)00610-7;
RA Tanaka Y., Kato S., Tanaka M., Kuji N., Yoshimura Y.;
RT "Structure and expression of the human oocyte-specific histone H1 gene
RT elucidated by direct RT-nested PCR of a single oocyte.";
RL Biochem. Biophys. Res. Commun. 304:351-357(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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).
CC -!- FUNCTION: May play a key role in the control of gene expression during
CC oogenesis and early embryogenesis, presumably through the perturbation
CC of chromatin structure. Essential for meiotic maturation of germinal
CC vesicle-stage oocytes. The somatic type linker histone H1c is rapidly
CC replaced by H1oo in a donor nucleus transplanted into an oocyte. The
CC greater mobility of H1oo as compared to H1c may contribute to this
CC rapid replacement and increased instability of the embryonic chromatin
CC structure. The rapid replacement of H1c with H1oo may play an important
CC role in nuclear remodeling (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00837}. Chromosome
CC {ECO:0000255|PROSITE-ProRule:PRU00837}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IZA3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IZA3-2; Sequence=VSP_034592;
CC -!- TISSUE SPECIFICITY: Oocyte-specific. {ECO:0000269|PubMed:12711322}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; AY158091; AAN46899.1; -; mRNA.
DR EMBL; CH471052; EAW79242.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79243.1; -; Genomic_DNA.
DR EMBL; BC047943; AAH47943.1; -; mRNA.
DR CCDS; CCDS3064.1; -. [Q8IZA3-1]
DR CCDS; CCDS77815.1; -. [Q8IZA3-2]
DR RefSeq; NP_001295191.1; NM_001308262.1. [Q8IZA3-2]
DR RefSeq; NP_722575.1; NM_153833.2. [Q8IZA3-1]
DR RefSeq; XP_016861222.1; XM_017005733.1. [Q8IZA3-2]
DR AlphaFoldDB; Q8IZA3; -.
DR SMR; Q8IZA3; -.
DR BioGRID; 126315; 187.
DR IntAct; Q8IZA3; 1.
DR STRING; 9606.ENSP00000319799; -.
DR iPTMnet; Q8IZA3; -.
DR PhosphoSitePlus; Q8IZA3; -.
DR BioMuta; H1FOO; -.
DR DMDM; 74762503; -.
DR EPD; Q8IZA3; -.
DR jPOST; Q8IZA3; -.
DR PaxDb; Q8IZA3; -.
DR PeptideAtlas; Q8IZA3; -.
DR PRIDE; Q8IZA3; -.
DR ProteomicsDB; 71310; -. [Q8IZA3-1]
DR ProteomicsDB; 71311; -. [Q8IZA3-2]
DR Antibodypedia; 33282; 183 antibodies from 26 providers.
DR DNASU; 132243; -.
DR Ensembl; ENST00000324382.7; ENSP00000319799.2; ENSG00000178804.8. [Q8IZA3-1]
DR Ensembl; ENST00000503977.1; ENSP00000422964.1; ENSG00000178804.8. [Q8IZA3-2]
DR GeneID; 132243; -.
DR KEGG; hsa:132243; -.
DR MANE-Select; ENST00000324382.7; ENSP00000319799.2; NM_153833.3; NP_722575.1.
DR UCSC; uc003emu.3; human. [Q8IZA3-1]
DR CTD; 132243; -.
DR DisGeNET; 132243; -.
DR GeneCards; H1-8; -.
DR HGNC; HGNC:18463; H1-8.
DR HPA; ENSG00000178804; Tissue enriched (testis).
DR neXtProt; NX_Q8IZA3; -.
DR VEuPathDB; HostDB:ENSG00000178804; -.
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00940000160900; -.
DR HOGENOM; CLU_070976_0_0_1; -.
DR InParanoid; Q8IZA3; -.
DR OMA; KMGPPMA; -.
DR OrthoDB; 1342218at2759; -.
DR PhylomeDB; Q8IZA3; -.
DR TreeFam; TF333386; -.
DR PathwayCommons; Q8IZA3; -.
DR SignaLink; Q8IZA3; -.
DR BioGRID-ORCS; 132243; 15 hits in 1069 CRISPR screens.
DR GeneWiki; H1FOO; -.
DR GenomeRNAi; 132243; -.
DR Pharos; Q8IZA3; Tbio.
DR PRO; PR:Q8IZA3; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8IZA3; protein.
DR Bgee; ENSG00000178804; Expressed in oocyte and 22 other tissues.
DR Genevisible; Q8IZA3; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; ISS:CAFA.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0031492; F:nucleosomal DNA binding; ISS:CAFA.
DR GO; GO:0030527; F:structural constituent of chromatin; ISS:CAFA.
DR GO; GO:0030261; P:chromosome condensation; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
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:0040029; P:regulation of gene expression, epigenetic; ISS:CAFA.
DR CDD; cd00073; H15; 1.
DR Gene3D; 1.10.10.10; -; 1.
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 SMART; SM00526; H15; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51504; H15; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chromosome; Cytoplasm; DNA-binding; Meiosis; Nucleus;
KW Reference proteome.
FT CHAIN 1..346
FT /note="Histone H1.8"
FT /id="PRO_0000343412"
FT DOMAIN 51..129
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 164..179
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..139
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034592"
FT VARIANT 296
FT /note="N -> S (in dbSNP:rs59415528)"
FT /id="VAR_061208"
SQ SEQUENCE 346 AA; 35813 MW; 666964009BE6F4AC CRC64;
MAPGSVTSDI SPSSTSTAGS SRSPESEKPG PSHGGVPPGG PSHSSLPVGR RHPPVLRMVL
EALQAGEQRR GTSVAAIKLY ILHKYPTVDV LRFKYLLKQA LATGMRRGLL ARPLNSKARG
ATGSFKLVPK HKKKIQPRKM APATAPRRAG EAKGKGPKKP SEAKEDPPNV GKVKKAAKRP
AKVQKPPPKP GAATEKARKQ GGAAKDTRAQ SGEARKVPPK PDKAMRAPSS AGGLSRKAKA
KGSRSSQGDA EAYRKTKAES KSSKPTASKV KNGAASPTKK KVVAKAKAPK AGQGPNTKAA
APAKGSGSKV VPAHLSRKTE APKGPRKAGL PIKASSSKVS SQRAEA
