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   13-SEP-2023, entry version 182.
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=10.1016/s0888-7543(02)96850-3;
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}.
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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; 213.
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   ProteomicsDB; 53996; -.
DR   Antibodypedia; 25536; 73 antibodies from 23 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   AGR; HGNC:4720; -.
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; 5362469at2759; -.
DR   PhylomeDB; P22492; -.
DR   TreeFam; TF313664; -.
DR   PathwayCommons; P22492; -.
DR   SignaLink; P22492; -.
DR   BioGRID-ORCS; 3010; 7 hits in 1148 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; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; Winged helix' DNA-binding domain; 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
//