HILS1_MOUSE
ID HILS1_MOUSE Reviewed; 170 AA.
AC Q9QYL0;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Spermatid-specific linker histone H1-like protein {ECO:0000305};
DE AltName: Full=TISP64;
GN Name=Hils1 {ECO:0000312|MGI:MGI:2136691};
GN Synonyms=H1-9p {ECO:0000250|UniProtKB:P60008};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6 X 129; TISSUE=Testis;
RX PubMed=12920187; DOI=10.1073/pnas.1837812100;
RA Yan W., Ma L., Burns K.H., Matzuk M.M.;
RT "HILS1 is a spermatid-specific linker histone H1-like protein implicated in
RT chromatin remodeling during mammalian spermiogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10546-10551(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DNA-BINDING, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=14636221; DOI=10.1046/j.0105-6263.2003.00449.x;
RA Iguchi N., Tanaka H., Yomogida K., Nishimune Y.;
RT "Isolation and characterization of a novel cDNA encoding a DNA-binding
RT protein (Hils1) specifically expressed in testicular haploid germ cells.";
RL Int. J. Androl. 26:354-365(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: DNA-binding protein that may be implicated in chromatin
CC remodeling and/or transcriptional regulation during spermiogenesis, the
CC process of spermatid maturation into spermatozoa.
CC {ECO:0000269|PubMed:12920187, ECO:0000269|PubMed:14636221}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12920187,
CC ECO:0000269|PubMed:14636221}. Chromosome {ECO:0000269|PubMed:12920187,
CC ECO:0000269|PubMed:14636221}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in the testis by haploid germ
CC cells (at protein level). {ECO:0000269|PubMed:12920187,
CC ECO:0000269|PubMed:14636221}.
CC -!- DEVELOPMENTAL STAGE: Expression initiated at step 9 of spermatid
CC development and peaked between steps 10-13. Expression decreased
CC abruptly at step 14 and was undetectable after step 15.
CC {ECO:0000269|PubMed:14636221}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000305}.
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DR EMBL; AY286319; AAQ23051.1; -; mRNA.
DR EMBL; AB022320; BAA82785.1; -; mRNA.
DR EMBL; AB045724; BAB97206.1; -; mRNA.
DR EMBL; AK005718; BAB24203.1; -; mRNA.
DR EMBL; BC061119; AAH61119.1; -; mRNA.
DR CCDS; CCDS25267.1; -.
DR RefSeq; NP_061262.1; NM_018792.2.
DR AlphaFoldDB; Q9QYL0; -.
DR SMR; Q9QYL0; -.
DR STRING; 10090.ENSMUSP00000039866; -.
DR iPTMnet; Q9QYL0; -.
DR PhosphoSitePlus; Q9QYL0; -.
DR PaxDb; Q9QYL0; -.
DR PRIDE; Q9QYL0; -.
DR ProteomicsDB; 273343; -.
DR DNASU; 54388; -.
DR Ensembl; ENSMUST00000038928; ENSMUSP00000039866; ENSMUSG00000038994.
DR GeneID; 54388; -.
DR KEGG; mmu:54388; -.
DR UCSC; uc007kzq.1; mouse.
DR CTD; 54388; -.
DR MGI; MGI:2136691; Hils1.
DR VEuPathDB; HostDB:ENSMUSG00000038994; -.
DR eggNOG; ENOG502SVZZ; Eukaryota.
DR GeneTree; ENSGT00730000111487; -.
DR HOGENOM; CLU_105276_0_0_1; -.
DR InParanoid; Q9QYL0; -.
DR OMA; NMTRNAW; -.
DR OrthoDB; 1372071at2759; -.
DR PhylomeDB; Q9QYL0; -.
DR TreeFam; TF337069; -.
DR BioGRID-ORCS; 54388; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q9QYL0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9QYL0; protein.
DR Bgee; ENSMUSG00000038994; Expressed in seminiferous tubule of testis and 30 other tissues.
DR ExpressionAtlas; Q9QYL0; baseline and differential.
DR Genevisible; Q9QYL0; MM.
DR GO; GO:0001673; C:male germ cell nucleus; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0003676; F:nucleic acid binding; ISO:MGI.
DR GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
DR GO; GO:0030261; P:chromosome condensation; ISO:MGI.
DR GO; GO:0007281; P:germ cell development; ISO:MGI.
DR GO; GO:0031507; P:heterochromatin assembly; ISO:MGI.
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; ISO:MGI.
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 SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; Developmental protein; Differentiation;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Spermatogenesis;
KW Transcription; Transcription regulation.
FT CHAIN 1..170
FT /note="Spermatid-specific linker histone H1-like protein"
FT /id="PRO_0000196015"
FT DOMAIN 34..108
FT /note="H15"
FT REGION 118..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZZW6"
SQ SEQUENCE 170 AA; 19203 MW; 8968F3E639B63A2E CRC64;
MAQMVAGDQD AGTLWVPSQS ESQTESDIST QSLRKPTMSY VILKTLADKR VHNCVSLATL
KKAVSITGYN MTHNTWRFKR VLQNLLDKGM IMHVTCCKGA SGSLCLCKER ALKSNHRAKR
CQDRQKSQKP QKPGQRESEP CQLLLSSKKK NDQLFKGVRR VAKGNRHCHY
