H1_DROME
ID H1_DROME Reviewed; 256 AA.
AC P02255; Q4ABD3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Histone H1;
GN Name=His1;
GN and
GN Name=His1:CG31617; ORFNames=CG31617;
GN and
GN Name=His1:CG33804; ORFNames=CG33804;
GN and
GN Name=His1:CG33810; ORFNames=CG33810;
GN and
GN Name=His1:CG33813; ORFNames=CG33813;
GN and
GN Name=His1:CG33816; ORFNames=CG33816;
GN and
GN Name=His1:CG33819; ORFNames=CG33819;
GN and
GN Name=His1:CG33822; ORFNames=CG33822;
GN and
GN Name=His1:CG33825; ORFNames=CG33825;
GN and
GN Name=His1:CG33828; ORFNames=CG33828;
GN and
GN Name=His1:CG33831; ORFNames=CG33831;
GN and
GN Name=His1:CG33837; ORFNames=CG33837;
GN and
GN Name=His1:CG33840; ORFNames=CG33840;
GN and
GN Name=His1:CG33843; ORFNames=CG33843;
GN and
GN Name=His1:CG33846; ORFNames=CG33846;
GN and
GN Name=His1:CG33849; ORFNames=CG33849;
GN and
GN Name=His1:CG33852; ORFNames=CG33852;
GN and
GN Name=His1:CG33864; ORFNames=CG33864;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS1).
RX PubMed=3090518; DOI=10.1093/nar/14.13.5563;
RA Murphy T.J., Blumenfeld M.;
RT "Nucleotide sequence of a Drosophila melanogaster H1 histone gene.";
RL Nucleic Acids Res. 14:5563-5563(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS1).
RC STRAIN=AK-194;
RX PubMed=2536150; DOI=10.1093/nar/17.1.225;
RA Matsuo Y., Yamazaki T.;
RT "tRNA derived insertion element in histone gene repeating unit of
RT Drosophila melanogaster.";
RL Nucleic Acids Res. 17:225-238(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HIS1:CG31617; HIS1:CG31617;
RP HIS1:CG33804; HIS1:CG33810; HIS1:CG33813; HIS1:CG33816; HIS1:CG33819;
RP HIS1:CG33822; HIS1:CG33825; HIS1:CG33828; HIS1:CG33831; HIS1:CG33837;
RP HIS1:CG33840; HIS1:CG33843; HIS1:CG33846; HIS1:CG33849; HIS1:CG33852 AND
RP HIS1:CG33864).
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-47 AND 63-215 (HIS1).
RA Goldberg M.L.;
RL Thesis (1979), University of Stanford, United States.
RN [6]
RP PROTEIN SEQUENCE OF 22-117; 125-172 AND 185-231 (HIS1).
RX PubMed=1899487; DOI=10.1126/science.1899487;
RA Croston G.E., Kerrigan L.A., Lira L.M., Marshak D.R., Kadonaga J.T.;
RT "Sequence-specific antirepression of histone H1-mediated inhibition of
RT basal RNA polymerase II transcription.";
RL Science 251:643-649(1991).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11 (HIS1).
RX PubMed=1311255; DOI=10.1002/j.1460-2075.1992.tb05103.x;
RA Kas E., Laemmli U.K.;
RT "In vivo topoisomerase II cleavage of the Drosophila histone and satellite
RT III repeats: DNA sequence and structural characteristics.";
RL EMBO J. 11:705-716(1992).
RN [8]
RP PHOSPHORYLATION.
RX PubMed=16230526; DOI=10.1101/gad.1348905;
RA Ivanovska I., Khandan T., Ito T., Orr-Weaver T.L.;
RT "A histone code in meiosis: the histone kinase, NHK-1, is required for
RT proper chromosomal architecture in Drosophila oocytes.";
RL Genes Dev. 19:2571-2582(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
CC -!- FUNCTION: Histones H1 are necessary for the condensation of nucleosome
CC chains into higher-order structures.
CC -!- INTERACTION:
CC P02255; P05205: Su(var)205; NbExp=2; IntAct=EBI-151629, EBI-155532;
CC P02255; P45975: Su(var)3-9; NbExp=4; IntAct=EBI-151629, EBI-110378;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- PTM: Phosphorylated in oocytes during prophase I of meiosis.
CC {ECO:0000269|PubMed:16230526, ECO:0000269|PubMed:17372656}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; X04073; CAA27716.1; -; Genomic_DNA.
DR EMBL; X14215; CAA32433.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN11123.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66482.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66491.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66495.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66500.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66505.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66510.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66515.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66520.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66525.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66535.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66540.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66545.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66555.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66550.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66560.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66580.1; -; Genomic_DNA.
DR EMBL; X60225; CAA42786.1; -; Genomic_DNA.
DR PIR; A02585; HSFF1.
DR PIR; S07371; S07371.
DR RefSeq; NP_001027286.1; NM_001032115.2.
DR RefSeq; NP_001027295.1; NM_001032124.2.
DR RefSeq; NP_001027299.1; NM_001032128.2.
DR RefSeq; NP_001027304.1; NM_001032133.2.
DR RefSeq; NP_001027309.1; NM_001032138.2.
DR RefSeq; NP_001027314.1; NM_001032143.2.
DR RefSeq; NP_001027319.1; NM_001032148.2.
DR RefSeq; NP_001027324.1; NM_001032153.2.
DR RefSeq; NP_001027329.1; NM_001032158.2.
DR RefSeq; NP_001027339.1; NM_001032168.2.
DR RefSeq; NP_001027344.1; NM_001032173.2.
DR RefSeq; NP_001027349.1; NM_001032178.2.
DR RefSeq; NP_001027354.1; NM_001032183.2.
DR RefSeq; NP_001027359.1; NM_001032188.2.
DR RefSeq; NP_001027364.1; NM_001032193.2.
DR RefSeq; NP_001027384.1; NM_001032213.2.
DR RefSeq; NP_724341.1; NM_165380.4.
DR AlphaFoldDB; P02255; -.
DR SMR; P02255; -.
DR BioGRID; 534006; 1.
DR BioGRID; 534312; 20.
DR BioGRID; 77145; 7.
DR DIP; DIP-61415N; -.
DR IntAct; P02255; 13.
DR STRING; 7227.FBpp0085248; -.
DR iPTMnet; P02255; -.
DR PaxDb; P02255; -.
DR ABCD; P02255; 2 sequenced antibodies.
DR DNASU; 318854; -.
DR EnsemblMetazoa; FBtr0085892; FBpp0085248; FBgn0051617.
DR EnsemblMetazoa; FBtr0091808; FBpp0091052; FBgn0053804.
DR EnsemblMetazoa; FBtr0091814; FBpp0091057; FBgn0053810.
DR EnsemblMetazoa; FBtr0091817; FBpp0091059; FBgn0053813.
DR EnsemblMetazoa; FBtr0091820; FBpp0091062; FBgn0053816.
DR EnsemblMetazoa; FBtr0091823; FBpp0091065; FBgn0053819.
DR EnsemblMetazoa; FBtr0091826; FBpp0091068; FBgn0053822.
DR EnsemblMetazoa; FBtr0091829; FBpp0091071; FBgn0053825.
DR EnsemblMetazoa; FBtr0091832; FBpp0091074; FBgn0053828.
DR EnsemblMetazoa; FBtr0091835; FBpp0091077; FBgn0053831.
DR EnsemblMetazoa; FBtr0091841; FBpp0091083; FBgn0053837.
DR EnsemblMetazoa; FBtr0091844; FBpp0091086; FBgn0053840.
DR EnsemblMetazoa; FBtr0091847; FBpp0091089; FBgn0053843.
DR EnsemblMetazoa; FBtr0091850; FBpp0091092; FBgn0053846.
DR EnsemblMetazoa; FBtr0091853; FBpp0091095; FBgn0053849.
DR EnsemblMetazoa; FBtr0091856; FBpp0091098; FBgn0053852.
DR EnsemblMetazoa; FBtr0091868; FBpp0091110; FBgn0053864.
DR GeneID; 318854; -.
DR GeneID; 3771803; -.
DR GeneID; 3771816; -.
DR GeneID; 3771818; -.
DR GeneID; 3771838; -.
DR GeneID; 3771879; -.
DR GeneID; 3771910; -.
DR GeneID; 3771912; -.
DR GeneID; 3771981; -.
DR GeneID; 3772004; -.
DR GeneID; 3772075; -.
DR GeneID; 3772077; -.
DR GeneID; 3772225; -.
DR GeneID; 3772409; -.
DR GeneID; 3772665; -.
DR GeneID; 3772702; -.
DR GeneID; 3772715; -.
DR KEGG; dme:Dmel_CG31617; -.
DR KEGG; dme:Dmel_CG33804; -.
DR KEGG; dme:Dmel_CG33810; -.
DR KEGG; dme:Dmel_CG33813; -.
DR KEGG; dme:Dmel_CG33816; -.
DR KEGG; dme:Dmel_CG33819; -.
DR KEGG; dme:Dmel_CG33822; -.
DR KEGG; dme:Dmel_CG33825; -.
DR KEGG; dme:Dmel_CG33828; -.
DR KEGG; dme:Dmel_CG33831; -.
DR KEGG; dme:Dmel_CG33837; -.
DR KEGG; dme:Dmel_CG33840; -.
DR KEGG; dme:Dmel_CG33843; -.
DR KEGG; dme:Dmel_CG33846; -.
DR KEGG; dme:Dmel_CG33849; -.
DR KEGG; dme:Dmel_CG33852; -.
DR KEGG; dme:Dmel_CG33864; -.
DR UCSC; CG31617-RA; d. melanogaster.
DR CTD; 318854; -.
DR CTD; 3771803; -.
DR CTD; 3771816; -.
DR CTD; 3771818; -.
DR CTD; 3771838; -.
DR CTD; 3771879; -.
DR CTD; 3771910; -.
DR CTD; 3771912; -.
DR CTD; 3771981; -.
DR CTD; 3772004; -.
DR CTD; 3772075; -.
DR CTD; 3772077; -.
DR CTD; 3772225; -.
DR CTD; 3772409; -.
DR CTD; 3772665; -.
DR CTD; 3772702; -.
DR CTD; 3772715; -.
DR FlyBase; FBgn0001195; His1.
DR FlyBase; FBgn0051617; His1:CG31617.
DR FlyBase; FBgn0053804; His1:CG33804.
DR FlyBase; FBgn0053810; His1:CG33810.
DR FlyBase; FBgn0053813; His1:CG33813.
DR FlyBase; FBgn0053816; His1:CG33816.
DR FlyBase; FBgn0053819; His1:CG33819.
DR FlyBase; FBgn0053822; His1:CG33822.
DR FlyBase; FBgn0053825; His1:CG33825.
DR FlyBase; FBgn0053828; His1:CG33828.
DR FlyBase; FBgn0053831; His1:CG33831.
DR FlyBase; FBgn0053837; His1:CG33837.
DR FlyBase; FBgn0053840; His1:CG33840.
DR FlyBase; FBgn0053843; His1:CG33843.
DR FlyBase; FBgn0053846; His1:CG33846.
DR FlyBase; FBgn0053849; His1:CG33849.
DR FlyBase; FBgn0053852; His1:CG33852.
DR FlyBase; FBgn0053864; His1:CG33864.
DR VEuPathDB; VectorBase:FBgn0051617; -.
DR VEuPathDB; VectorBase:FBgn0053804; -.
DR VEuPathDB; VectorBase:FBgn0053810; -.
DR VEuPathDB; VectorBase:FBgn0053813; -.
DR VEuPathDB; VectorBase:FBgn0053816; -.
DR VEuPathDB; VectorBase:FBgn0053819; -.
DR VEuPathDB; VectorBase:FBgn0053822; -.
DR VEuPathDB; VectorBase:FBgn0053825; -.
DR VEuPathDB; VectorBase:FBgn0053828; -.
DR VEuPathDB; VectorBase:FBgn0053831; -.
DR VEuPathDB; VectorBase:FBgn0053837; -.
DR VEuPathDB; VectorBase:FBgn0053840; -.
DR VEuPathDB; VectorBase:FBgn0053843; -.
DR VEuPathDB; VectorBase:FBgn0053846; -.
DR VEuPathDB; VectorBase:FBgn0053849; -.
DR VEuPathDB; VectorBase:FBgn0053852; -.
DR VEuPathDB; VectorBase:FBgn0053864; -.
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00940000164370; -.
DR HOGENOM; CLU_052897_1_0_1; -.
DR InParanoid; P02255; -.
DR OMA; GASHPPY; -.
DR OrthoDB; 1565299at2759; -.
DR PhylomeDB; P02255; -.
DR Reactome; R-DME-140342; Apoptosis induced DNA fragmentation.
DR SignaLink; P02255; -.
DR PRO; PR:P02255; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0051617; Expressed in midgut and 13 other tissues.
DR Genevisible; P02255; DM.
DR GO; GO:0000785; C:chromatin; ISS:FlyBase.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; ISS:FlyBase.
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:0051276; P:chromosome organization; IMP:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0045910; P:negative regulation of DNA recombination; IBA:GO_Central.
DR GO; GO:0031057; P:negative regulation of histone modification; IDA:FlyBase.
DR GO; GO:0010526; P:negative regulation of transposition, RNA-mediated; IMP:FlyBase.
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 Chromosome; Direct protein sequencing; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..256
FT /note="Histone H1"
FT /id="PRO_0000195961"
FT DOMAIN 45..119
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
SQ SEQUENCE 256 AA; 26359 MW; 5314DA250A7D0B23 CRC64;
MSDSAVATSA SPVAAPPATV EKKVVQKKAS GSAGTKAKKA SATPSHPPTQ QMVDASIKNL
KERGGSSLLA IKKYITATYK CDAQKLAPFI KKYLKSAVVN GKLIQTKGKG ASGSFKLSAS
AKKEKDPKAK SKVLSAEKKV QSKKVASKKI GVSSKKTAVG AADKKPKAKK AVATKKTAEN
KKTEKAKAKD AKKTGIIKSK PAATKAKVTA AKPKAVVAKA SKAKPAVSAK PKKTVKKASV
SATAKKPKAK TTAAKK
