H1T_HUMAN
ID H1T_HUMAN Reviewed; 207 AA.
AC P22492; Q6ISI1; Q8IUE8;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Histone H1t;
DE AltName: Full=Testicular H1 histone;
GN Name=H1-6 {ECO:0000312|HGNC:HGNC:4720};
GN Synonyms=H1FT, H1T, HIST1H1T {ECO:0000312|HGNC:HGNC:4720};
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND VARIANT LEU-14.
RX PubMed=1889752; DOI=10.1016/0378-1119(91)90284-i;
RA Drabent B., Kardalinou E., Doenecke D.;
RT "Structure and expression of the human gene encoding testicular H1 histone
RT (H1t).";
RL Gene 103:263-268(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND VARIANT LYS-178.
RX PubMed=8175896; DOI=10.1002/jcb.240540210;
RA Koppel D.A., Wolfe S.A., Fogelfeld L., Grimes S.R.;
RT "Primate testicular histone H1t genes are highly conserved and the human
RT H1t gene is located on chromosome 6.";
RL J. Cell. Biochem. 54:219-230(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12408966; DOI=10.1006/geno.2002.6850;
RA Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT "The human and mouse replication-dependent histone genes.";
RL Genomics 80:487-498(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP FUNCTION.
RX PubMed=26757249; DOI=10.1021/acs.biochem.5b01126;
RA Machida S., Hayashida R., Takaku M., Fukuto A., Sun J., Kinomura A.,
RA Tashiro S., Kurumizaka H.;
RT "Relaxed chromatin formation and weak suppression of homologous pairing by
RT the testis-specific linker histone H1T.";
RL Biochemistry 55:637-646(2016).
CC -!- FUNCTION: Testis-specific histone H1 that forms less compacted
CC chromatin compared to other H1 histone subtypes (PubMed:26757249).
CC Formation of more relaxed chromatin may be required to promote
CC chromatin architecture required for proper chromosome regulation during
CC meiosis, such as homologous recombination (PubMed:26757249). Histones
CC H1 act as linkers that bind to nucleosomes and compact polynucleosomes
CC into a higher-order chromatin configuration (Probable).
CC {ECO:0000269|PubMed:26757249, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:1889752,
CC ECO:0000269|PubMed:8175896}.
CC -!- DEVELOPMENTAL STAGE: This histone is a testis-specific H1 variant that
CC appears during meiosis in spermatogenesis.
CC {ECO:0000269|PubMed:8175896}.
CC -!- PTM: Phosphorylated in early spermatids.
CC {ECO:0000250|UniProtKB:P06349}.
CC -!- PTM: Citrullination at Arg-58 (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:P43275}.
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; M60094; AAA35944.1; -; Genomic_DNA.
DR EMBL; M97755; AAA19936.1; -; Genomic_DNA.
DR EMBL; AF531301; AAN06701.1; -; Genomic_DNA.
DR EMBL; BC069517; AAH69517.2; -; mRNA.
DR CCDS; CCDS34349.1; -.
DR PIR; JH0550; JH0550.
DR RefSeq; NP_005314.2; NM_005323.3.
DR AlphaFoldDB; P22492; -.
DR SMR; P22492; -.
DR BioGRID; 109265; 207.
DR IntAct; P22492; 137.
DR MINT; P22492; -.
DR STRING; 9606.ENSP00000341214; -.
DR iPTMnet; P22492; -.
DR PhosphoSitePlus; P22492; -.
DR SwissPalm; P22492; -.
DR BioMuta; HIST1H1T; -.
DR DMDM; 34395930; -.
DR EPD; P22492; -.
DR jPOST; P22492; -.
DR MassIVE; P22492; -.
DR MaxQB; P22492; -.
DR PaxDb; P22492; -.
DR PeptideAtlas; P22492; -.
DR PRIDE; P22492; -.
DR ProteomicsDB; 53996; -.
DR Antibodypedia; 25536; 53 antibodies from 22 providers.
DR DNASU; 3010; -.
DR Ensembl; ENST00000338379.6; ENSP00000341214.5; ENSG00000187475.6.
DR GeneID; 3010; -.
DR KEGG; hsa:3010; -.
DR MANE-Select; ENST00000338379.6; ENSP00000341214.5; NM_005323.4; NP_005314.2.
DR UCSC; uc003ngj.4; human.
DR CTD; 3010; -.
DR DisGeNET; 3010; -.
DR GeneCards; H1-6; -.
DR HGNC; HGNC:4720; H1-6.
DR HPA; ENSG00000187475; Group enriched (brain, choroid plexus, testis).
DR MIM; 142712; gene.
DR neXtProt; NX_P22492; -.
DR OpenTargets; ENSG00000187475; -.
DR VEuPathDB; HostDB:ENSG00000187475; -.
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00940000163525; -.
DR HOGENOM; CLU_052897_7_0_1; -.
DR InParanoid; P22492; -.
DR OMA; QHHKANI; -.
DR OrthoDB; 1565299at2759; -.
DR PhylomeDB; P22492; -.
DR TreeFam; TF313664; -.
DR PathwayCommons; P22492; -.
DR SignaLink; P22492; -.
DR BioGRID-ORCS; 3010; 7 hits in 1074 CRISPR screens.
DR GeneWiki; HIST1H1T; -.
DR GenomeRNAi; 3010; -.
DR Pharos; P22492; Tdark.
DR PRO; PR:P22492; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P22492; protein.
DR Bgee; ENSG00000187475; Expressed in monocyte and 45 other tissues.
DR Genevisible; P22492; HS.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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 GO; GO:0007283; P:spermatogenesis; IBA:GO_Central.
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 Chromosome; Citrullination; Developmental protein; Differentiation;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Spermatogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..207
FT /note="Histone H1t"
FT /id="PRO_0000195910"
FT DOMAIN 40..113
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..132
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..175
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 56
FT /note="Important for nucleosome binding properties"
FT /evidence="ECO:0000250|UniProtKB:P06349"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07133"
FT MOD_RES 58
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P43275"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07133"
FT MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07133"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07133"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07133"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06349"
FT VARIANT 14
FT /note="V -> L (in dbSNP:rs198844)"
FT /evidence="ECO:0000269|PubMed:1889752"
FT /id="VAR_049310"
FT VARIANT 52
FT /note="L -> F (in dbSNP:rs2051542)"
FT /id="VAR_049311"
FT VARIANT 178
FT /note="Q -> K (in dbSNP:rs198845)"
FT /evidence="ECO:0000269|PubMed:8175896"
FT /id="VAR_049312"
SQ SEQUENCE 207 AA; 22019 MW; 9CF27B275DA29B48 CRC64;
MSETVPAASA SAGVAAMEKL PTKKRGRKPA GLISASRKVP NLSVSKLITE ALSVSQERVG
MSLVALKKAL AAAGYDVEKN NSRIKLSLKS LVNKGILVQT RGTGASGSFK LSKKVIPKST
RSKAKKSVSA KTKKLVLSRD SKSPKTAKTN KRAKKPRATT PKTVRSGRKA KGAKGKQQQK
SPVKARASKS KLTQHHEVNV RKATSKK
