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Histone H1

 H1_DROME                Reviewed;         256 AA.
P02255; Q4ABD3;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
16-JAN-2019, entry version 158.
RecName: Full=Histone H1;
Name=His1;
and
Name=His1:CG31617; ORFNames=CG31617;
and
Name=His1:CG33804; ORFNames=CG33804;
and
Name=His1:CG33810; ORFNames=CG33810;
and
Name=His1:CG33813; ORFNames=CG33813;
and
Name=His1:CG33816; ORFNames=CG33816;
and
Name=His1:CG33819; ORFNames=CG33819;
and
Name=His1:CG33822; ORFNames=CG33822;
and
Name=His1:CG33825; ORFNames=CG33825;
and
Name=His1:CG33828; ORFNames=CG33828;
and
Name=His1:CG33831; ORFNames=CG33831;
and
Name=His1:CG33837; ORFNames=CG33837;
and
Name=His1:CG33840; ORFNames=CG33840;
and
Name=His1:CG33843; ORFNames=CG33843;
and
Name=His1:CG33846; ORFNames=CG33846;
and
Name=His1:CG33849; ORFNames=CG33849;
and
Name=His1:CG33852; ORFNames=CG33852;
and
Name=His1:CG33864; ORFNames=CG33864;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS1).
PubMed=3090518; DOI=10.1093/nar/14.13.5563;
Murphy T.J., Blumenfeld M.;
"Nucleotide sequence of a Drosophila melanogaster H1 histone gene.";
Nucleic Acids Res. 14:5563-5563(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS1).
STRAIN=AK-194;
PubMed=2536150; DOI=10.1093/nar/17.1.225;
Matsuo Y., Yamazaki T.;
"tRNA derived insertion element in histone gene repeating unit of
Drosophila melanogaster.";
Nucleic Acids Res. 17:225-238(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HIS1:CG31617;
HIS1:CG31617; HIS1:CG33804; HIS1:CG33810; HIS1:CG33813; HIS1:CG33816;
HIS1:CG33819; HIS1:CG33822; HIS1:CG33825; HIS1:CG33828; HIS1:CG33831;
HIS1:CG33837; HIS1:CG33840; HIS1:CG33843; HIS1:CG33846; HIS1:CG33849;
HIS1:CG33852 AND HIS1:CG33864).
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-47 AND 63-215 (HIS1).
Goldberg M.L.;
Thesis (1979), University of Stanford, United States.
[6]
PROTEIN SEQUENCE OF 22-117; 125-172 AND 185-231 (HIS1).
PubMed=1899487; DOI=10.1126/science.1899487;
Croston G.E., Kerrigan L.A., Lira L.M., Marshak D.R., Kadonaga J.T.;
"Sequence-specific antirepression of histone H1-mediated inhibition of
basal RNA polymerase II transcription.";
Science 251:643-649(1991).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11 (HIS1).
PubMed=1311255;
Kas E., Laemmli U.K.;
"In vivo topoisomerase II cleavage of the Drosophila histone and
satellite III repeats: DNA sequence and structural characteristics.";
EMBO J. 11:705-716(1992).
[8]
PHOSPHORYLATION.
PubMed=16230526; DOI=10.1101/gad.1348905;
Ivanovska I., Khandan T., Ito T., Orr-Weaver T.L.;
"A histone code in meiosis: the histone kinase, NHK-1, is required for
proper chromosomal architecture in Drosophila oocytes.";
Genes Dev. 19:2571-2582(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=17372656; DOI=10.1039/b617545g;
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,
Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
"An integrated chemical, mass spectrometric and computational strategy
for (quantitative) phosphoproteomics: application to Drosophila
melanogaster Kc167 cells.";
Mol. Biosyst. 3:275-286(2007).
-!- FUNCTION: Histones H1 are necessary for the condensation of
nucleosome chains into higher-order structures.
-!- INTERACTION:
P05205:Su(var)205; NbExp=2; IntAct=EBI-151629, EBI-155532;
P45975:Su(var)3-9; NbExp=4; IntAct=EBI-151629, EBI-110378;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
-!- PTM: Phosphorylated in oocytes during prophase I of meiosis.
{ECO:0000269|PubMed:16230526, ECO:0000269|PubMed:17372656}.
-!- SIMILARITY: Belongs to the histone H1/H5 family.
{ECO:0000255|PROSITE-ProRule:PRU00837}.
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EMBL; X04073; CAA27716.1; -; Genomic_DNA.
EMBL; X14215; CAA32433.1; -; Genomic_DNA.
EMBL; AE014134; AAN11123.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66482.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66491.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66495.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66500.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66505.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66510.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66515.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66520.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66525.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66535.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66540.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66545.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66555.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66550.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66560.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66580.1; -; Genomic_DNA.
EMBL; X60225; CAA42786.1; -; Genomic_DNA.
PIR; A02585; HSFF1.
PIR; S07371; S07371.
RefSeq; NP_001027286.1; NM_001032115.2.
RefSeq; NP_001027295.1; NM_001032124.2.
RefSeq; NP_001027299.1; NM_001032128.2.
RefSeq; NP_001027304.1; NM_001032133.2.
RefSeq; NP_001027309.1; NM_001032138.2.
RefSeq; NP_001027314.1; NM_001032143.2.
RefSeq; NP_001027319.1; NM_001032148.2.
RefSeq; NP_001027324.1; NM_001032153.2.
RefSeq; NP_001027329.1; NM_001032158.2.
RefSeq; NP_001027339.1; NM_001032168.2.
RefSeq; NP_001027344.1; NM_001032173.2.
RefSeq; NP_001027349.1; NM_001032178.2.
RefSeq; NP_001027354.1; NM_001032183.2.
RefSeq; NP_001027359.1; NM_001032188.2.
RefSeq; NP_001027364.1; NM_001032193.2.
RefSeq; NP_001027384.1; NM_001032213.2.
RefSeq; NP_724341.1; NM_165380.4.
ProteinModelPortal; P02255; -.
SMR; P02255; -.
BioGrid; 534006; 1.
BioGrid; 534312; 20.
BioGrid; 77145; 7.
DIP; DIP-61415N; -.
IntAct; P02255; 13.
STRING; 7227.FBpp0091110; -.
iPTMnet; P02255; -.
PaxDb; P02255; -.
PRIDE; P02255; -.
EnsemblMetazoa; FBtr0085892; FBpp0085248; FBgn0051617.
EnsemblMetazoa; FBtr0091808; FBpp0091052; FBgn0053804.
EnsemblMetazoa; FBtr0091814; FBpp0091057; FBgn0053810.
EnsemblMetazoa; FBtr0091817; FBpp0091059; FBgn0053813.
EnsemblMetazoa; FBtr0091820; FBpp0091062; FBgn0053816.
EnsemblMetazoa; FBtr0091823; FBpp0091065; FBgn0053819.
EnsemblMetazoa; FBtr0091826; FBpp0091068; FBgn0053822.
EnsemblMetazoa; FBtr0091829; FBpp0091071; FBgn0053825.
EnsemblMetazoa; FBtr0091832; FBpp0091074; FBgn0053828.
EnsemblMetazoa; FBtr0091835; FBpp0091077; FBgn0053831.
EnsemblMetazoa; FBtr0091841; FBpp0091083; FBgn0053837.
EnsemblMetazoa; FBtr0091844; FBpp0091086; FBgn0053840.
EnsemblMetazoa; FBtr0091847; FBpp0091089; FBgn0053843.
EnsemblMetazoa; FBtr0091850; FBpp0091092; FBgn0053846.
EnsemblMetazoa; FBtr0091853; FBpp0091095; FBgn0053849.
EnsemblMetazoa; FBtr0091856; FBpp0091098; FBgn0053852.
EnsemblMetazoa; FBtr0091868; FBpp0091110; FBgn0053864.
GeneID; 318854; -.
GeneID; 3771803; -.
GeneID; 3771816; -.
GeneID; 3771818; -.
GeneID; 3771838; -.
GeneID; 3771879; -.
GeneID; 3771910; -.
GeneID; 3771912; -.
GeneID; 3771981; -.
GeneID; 3772004; -.
GeneID; 3772075; -.
GeneID; 3772077; -.
GeneID; 3772225; -.
GeneID; 3772409; -.
GeneID; 3772665; -.
GeneID; 3772702; -.
GeneID; 3772715; -.
KEGG; dme:Dmel_CG31617; -.
KEGG; dme:Dmel_CG33804; -.
KEGG; dme:Dmel_CG33810; -.
KEGG; dme:Dmel_CG33813; -.
KEGG; dme:Dmel_CG33816; -.
KEGG; dme:Dmel_CG33819; -.
KEGG; dme:Dmel_CG33822; -.
KEGG; dme:Dmel_CG33825; -.
KEGG; dme:Dmel_CG33828; -.
KEGG; dme:Dmel_CG33831; -.
KEGG; dme:Dmel_CG33837; -.
KEGG; dme:Dmel_CG33840; -.
KEGG; dme:Dmel_CG33843; -.
KEGG; dme:Dmel_CG33846; -.
KEGG; dme:Dmel_CG33849; -.
KEGG; dme:Dmel_CG33852; -.
KEGG; dme:Dmel_CG33864; -.
UCSC; CG31617-RA; d. melanogaster.
CTD; 318854; -.
CTD; 3771803; -.
CTD; 3771816; -.
CTD; 3771818; -.
CTD; 3771838; -.
CTD; 3771879; -.
CTD; 3771910; -.
CTD; 3771912; -.
CTD; 3771981; -.
CTD; 3772004; -.
CTD; 3772075; -.
CTD; 3772077; -.
CTD; 3772225; -.
CTD; 3772409; -.
CTD; 3772665; -.
CTD; 3772702; -.
CTD; 3772715; -.
FlyBase; FBgn0001195; His1.
FlyBase; FBgn0051617; His1:CG31617.
FlyBase; FBgn0053804; His1:CG33804.
FlyBase; FBgn0053810; His1:CG33810.
FlyBase; FBgn0053813; His1:CG33813.
FlyBase; FBgn0053816; His1:CG33816.
FlyBase; FBgn0053819; His1:CG33819.
FlyBase; FBgn0053822; His1:CG33822.
FlyBase; FBgn0053825; His1:CG33825.
FlyBase; FBgn0053828; His1:CG33828.
FlyBase; FBgn0053831; His1:CG33831.
FlyBase; FBgn0053837; His1:CG33837.
FlyBase; FBgn0053840; His1:CG33840.
FlyBase; FBgn0053843; His1:CG33843.
FlyBase; FBgn0053846; His1:CG33846.
FlyBase; FBgn0053849; His1:CG33849.
FlyBase; FBgn0053852; His1:CG33852.
FlyBase; FBgn0053864; His1:CG33864.
eggNOG; ENOG410J0ZG; Eukaryota.
eggNOG; ENOG41120CT; LUCA.
GeneTree; ENSGT00940000164370; -.
InParanoid; P02255; -.
KO; K11275; -.
OMA; KPRSHPP; -.
OrthoDB; 1565299at2759; -.
PhylomeDB; P02255; -.
Reactome; R-DME-211227; Activation of DNA fragmentation factor.
PRO; PR:P02255; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0051617; Expressed in 3 organ(s), highest expression level in adult organism.
Genevisible; P02255; DM.
GO; GO:0000790; C:nuclear chromatin; ISS:FlyBase.
GO; GO:0000786; C:nucleosome; IEA:InterPro.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0031490; F:chromatin DNA binding; ISS:FlyBase.
GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
GO; GO:0006342; P:chromatin silencing; IMP:FlyBase.
GO; GO:0030261; P:chromosome condensation; IBA:GO_Central.
GO; GO:0051276; P:chromosome organization; IMP:FlyBase.
GO; GO:0031936; P:negative regulation of chromatin silencing; IBA:GO_Central.
GO; GO:0045910; P:negative regulation of DNA recombination; IBA:GO_Central.
GO; GO:0031057; P:negative regulation of histone modification; IDA:FlyBase.
GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
GO; GO:0016584; P:nucleosome positioning; IBA:GO_Central.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
CDD; cd00073; H15; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR005818; Histone_H1/H5_H15.
InterPro; IPR005819; Histone_H5.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00538; Linker_histone; 1.
PRINTS; PR00624; HISTONEH5.
SMART; SM00526; H15; 1.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS51504; H15; 1.
1: Evidence at protein level;
Chromosome; Complete proteome; Direct protein sequencing; DNA-binding;
Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 256 Histone H1.
/FTId=PRO_0000195961.
DOMAIN 45 119 H15. {ECO:0000255|PROSITE-
ProRule:PRU00837}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000269|PubMed:17372656}.
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


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