Full text data of HIST1H1B
HIST1H1B
(H1F5)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Histone H1.5 (Histone H1a; Histone H1b; Histone H1s-3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Histone H1.5 (Histone H1a; Histone H1b; Histone H1s-3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P16401
ID H15_HUMAN Reviewed; 226 AA.
AC P16401; Q14529; Q3MJ42;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Histone H1.5;
DE AltName: Full=Histone H1a;
DE AltName: Full=Histone H1b;
DE AltName: Full=Histone H1s-3;
GN Name=HIST1H1B; Synonyms=H1F5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=9031620; DOI=10.1016/S0378-1119(96)00582-3;
RA Albig W., Meergans T., Doenecke D.;
RT "Characterization of the H1.5 gene completes the set of human H1
RT subtype genes.";
RL Gene 184:141-148(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-226.
RC TISSUE=Spleen;
RX PubMed=2613692;
RA Ohe Y., Hayashi H., Iwai K.;
RT "Human spleen histone H1. Isolation and amino acid sequences of three
RT minor variants, H1a, H1c, and H1d.";
RL J. Biochem. 106:844-857(1989).
RN [6]
RP PROTEIN SEQUENCE OF 2-17; 37-49; 58-78 AND 89-100, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=10997781; DOI=10.1023/A:1009262819961;
RA Parseghian M.H., Newcomb R.L., Winokur S.T., Hamkalo B.A.;
RT "The distribution of somatic H1 subtypes is non-random on active vs.
RT inactive chromatin: distribution in human fetal fibroblasts.";
RL Chromosome Res. 8:405-424(2000).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=11746507; DOI=10.1002/jcb.1224;
RA Parseghian M.H., Newcomb R.L., Hamkalo B.A.;
RT "Distribution of somatic H1 subtypes is non-random on active vs.
RT inactive chromatin II: distribution in human adult fibroblasts.";
RL J. Cell. Biochem. 83:643-659(2001).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=15911621; DOI=10.1074/jbc.M501627200;
RA Th'ng J.P., Sung R., Ye M., Hendzel M.J.;
RT "H1 family histones in the nucleus. Control of binding and
RT localization by the C-terminal domain.";
RL J. Biol. Chem. 280:27809-27814(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11; SER-18 AND THR-39,
RP AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION AT THR-11 BY GSK3B.
RX PubMed=19136008; DOI=10.1016/j.jmb.2008.12.047;
RA Happel N., Stoldt S., Schmidt B., Doenecke D.;
RT "M phase-specific phosphorylation of histone H1.5 at threonine 10 by
RT GSK-3.";
RL J. Mol. Biol. 386:339-350(2009).
RN [14]
RP METHYLATION AT LYS-27.
RX PubMed=19552482; DOI=10.1021/pr9000652;
RA Lu A., Zougman A., Pudelko M., Bebenek M., Ziolkowski P., Mann M.,
RA Wisniewski J.R.;
RT "Mapping of lysine monomethylation of linker histones in human breast
RT and its cancer.";
RL J. Proteome Res. 8:4207-4215(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-168, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-18 AND THR-138, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-2; SER-18 AND THR-138, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [21]
RP VARIANT [LARGE SCALE ANALYSIS] ASP-86.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Histone H1 protein binds to linker DNA between
CC nucleosomes forming the macromolecular structure known as the
CC chromatin fiber. Histones H1 are necessary for the condensation of
CC nucleosome chains into higher-order structured fibers. Acts also
CC as a regulator of individual gene transcription through chromatin
CC remodeling, nucleosome spacing and DNA methylation (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=According to
CC PubMed:15911621 more commonly found in heterochromatin. According
CC to PubMed:10997781 associates with actively transcribed chromatin
CC and not heterochromatin.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in the majority of the
CC cell lines tested and in testis.
CC -!- DOMAIN: The C-terminal domain is required for high-affinity
CC binding to chromatin (By similarity).
CC -!- PTM: H1 histones are progressively phosphorylated during the cell
CC cycle, becoming maximally phosphorylated during late G2 phase and
CC M phase, and being dephosphorylated sharply thereafter (By
CC similarity). Phosphorylated at Thr-11 by GSK3B during mitosis in
CC prometaphase and dephosphorylated in telophase.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family.
CC -!- SIMILARITY: Contains 1 H15 (linker histone H1/H5 globular) domain.
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DR EMBL; X83509; CAA58498.1; -; Genomic_DNA.
DR EMBL; AF531304; AAN06704.1; -; Genomic_DNA.
DR EMBL; Z98744; CAB11421.1; -; Genomic_DNA.
DR EMBL; BC069101; AAH69101.1; -; mRNA.
DR EMBL; BC101581; AAI01582.1; -; mRNA.
DR EMBL; BC101583; AAI01584.1; -; mRNA.
DR PIR; S51660; S51660.
DR RefSeq; NP_005313.1; NM_005322.2.
DR UniGene; Hs.131956; -.
DR PDB; 2FE2; Model; -; A=2-226.
DR PDB; 2RHI; X-ray; 1.66 A; B=23-27.
DR PDBsum; 2FE2; -.
DR PDBsum; 2RHI; -.
DR ProteinModelPortal; P16401; -.
DR SMR; P16401; 40-112.
DR IntAct; P16401; 4.
DR MINT; MINT-3008567; -.
DR STRING; 9606.ENSP00000330074; -.
DR PhosphoSite; P16401; -.
DR DMDM; 19856407; -.
DR PaxDb; P16401; -.
DR PeptideAtlas; P16401; -.
DR PRIDE; P16401; -.
DR DNASU; 3009; -.
DR Ensembl; ENST00000331442; ENSP00000330074; ENSG00000184357.
DR GeneID; 3009; -.
DR KEGG; hsa:3009; -.
DR UCSC; uc003njx.3; human.
DR CTD; 3009; -.
DR GeneCards; GC06M027835; -.
DR HGNC; HGNC:4719; HIST1H1B.
DR HPA; CAB012241; -.
DR MIM; 142711; gene.
DR neXtProt; NX_P16401; -.
DR PharmGKB; PA29097; -.
DR eggNOG; NOG258621; -.
DR HOGENOM; HOG000251627; -.
DR HOVERGEN; HBG009035; -.
DR InParanoid; P16401; -.
DR KO; K11275; -.
DR OMA; TRVAKAK; -.
DR OrthoDB; EOG74TX2T; -.
DR Reactome; REACT_578; Apoptosis.
DR EvolutionaryTrace; P16401; -.
DR GeneWiki; HIST1H1B; -.
DR GenomeRNAi; 3009; -.
DR NextBio; 11932; -.
DR PRO; PR:P16401; -.
DR Bgee; P16401; -.
DR CleanEx; HS_HIST1H1B; -.
DR Genevestigator; P16401; -.
DR GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
DR GO; GO:0000786; C:nucleosome; NAS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; NAS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR005819; Histone_H5.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF00538; Linker_histone; 1.
DR PRINTS; PR00624; HISTONEH5.
DR SMART; SM00526; H15; 1.
DR PROSITE; PS51504; H15; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; Complete proteome;
KW Direct protein sequencing; DNA-binding; Methylation; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 226 Histone H1.5.
FT /FTId=PRO_0000195909.
FT DOMAIN 39 112 H15.
FT MOD_RES 2 2 N-acetylserine; partial.
FT MOD_RES 2 2 Phosphoserine.
FT MOD_RES 11 11 Phosphothreonine; by GSK3.
FT MOD_RES 18 18 Phosphoserine.
FT MOD_RES 27 27 N6-methyllysine.
FT MOD_RES 39 39 Phosphothreonine.
FT MOD_RES 138 138 Phosphothreonine.
FT MOD_RES 168 168 N6-acetyllysine.
FT MOD_RES 173 173 Phosphoserine.
FT VARIANT 86 86 G -> D (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036204.
FT VARIANT 144 144 K -> R (in dbSNP:rs11970638).
FT /FTId=VAR_049308.
FT VARIANT 211 211 A -> T (in dbSNP:rs34144478).
FT /FTId=VAR_049309.
FT CONFLICT 216 218 Missing (in Ref. 5; AA sequence).
SQ SEQUENCE 226 AA; 22580 MW; 0BA1402101766FDF CRC64;
MSETAPAETA TPAPVEKSPA KKKATKKAAG AGAAKRKATG PPVSELITKA VAASKERNGL
SLAALKKALA AGGYDVEKNN SRIKLGLKSL VSKGTLVQTK GTGASGSFKL NKKAASGEAK
PKAKKAGAAK AKKPAGATPK KAKKAAGAKK AVKKTPKKAK KPAAAGVKKV AKSPKKAKAA
AKPKKATKSP AKPKAVKPKA AKPKAAKPKA AKPKAAKAKK AAAKKK
//
ID H15_HUMAN Reviewed; 226 AA.
AC P16401; Q14529; Q3MJ42;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Histone H1.5;
DE AltName: Full=Histone H1a;
DE AltName: Full=Histone H1b;
DE AltName: Full=Histone H1s-3;
GN Name=HIST1H1B; Synonyms=H1F5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=9031620; DOI=10.1016/S0378-1119(96)00582-3;
RA Albig W., Meergans T., Doenecke D.;
RT "Characterization of the H1.5 gene completes the set of human H1
RT subtype genes.";
RL Gene 184:141-148(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-226.
RC TISSUE=Spleen;
RX PubMed=2613692;
RA Ohe Y., Hayashi H., Iwai K.;
RT "Human spleen histone H1. Isolation and amino acid sequences of three
RT minor variants, H1a, H1c, and H1d.";
RL J. Biochem. 106:844-857(1989).
RN [6]
RP PROTEIN SEQUENCE OF 2-17; 37-49; 58-78 AND 89-100, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=10997781; DOI=10.1023/A:1009262819961;
RA Parseghian M.H., Newcomb R.L., Winokur S.T., Hamkalo B.A.;
RT "The distribution of somatic H1 subtypes is non-random on active vs.
RT inactive chromatin: distribution in human fetal fibroblasts.";
RL Chromosome Res. 8:405-424(2000).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=11746507; DOI=10.1002/jcb.1224;
RA Parseghian M.H., Newcomb R.L., Hamkalo B.A.;
RT "Distribution of somatic H1 subtypes is non-random on active vs.
RT inactive chromatin II: distribution in human adult fibroblasts.";
RL J. Cell. Biochem. 83:643-659(2001).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=15911621; DOI=10.1074/jbc.M501627200;
RA Th'ng J.P., Sung R., Ye M., Hendzel M.J.;
RT "H1 family histones in the nucleus. Control of binding and
RT localization by the C-terminal domain.";
RL J. Biol. Chem. 280:27809-27814(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11; SER-18 AND THR-39,
RP AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION AT THR-11 BY GSK3B.
RX PubMed=19136008; DOI=10.1016/j.jmb.2008.12.047;
RA Happel N., Stoldt S., Schmidt B., Doenecke D.;
RT "M phase-specific phosphorylation of histone H1.5 at threonine 10 by
RT GSK-3.";
RL J. Mol. Biol. 386:339-350(2009).
RN [14]
RP METHYLATION AT LYS-27.
RX PubMed=19552482; DOI=10.1021/pr9000652;
RA Lu A., Zougman A., Pudelko M., Bebenek M., Ziolkowski P., Mann M.,
RA Wisniewski J.R.;
RT "Mapping of lysine monomethylation of linker histones in human breast
RT and its cancer.";
RL J. Proteome Res. 8:4207-4215(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-168, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-18 AND THR-138, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-2; SER-18 AND THR-138, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [21]
RP VARIANT [LARGE SCALE ANALYSIS] ASP-86.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Histone H1 protein binds to linker DNA between
CC nucleosomes forming the macromolecular structure known as the
CC chromatin fiber. Histones H1 are necessary for the condensation of
CC nucleosome chains into higher-order structured fibers. Acts also
CC as a regulator of individual gene transcription through chromatin
CC remodeling, nucleosome spacing and DNA methylation (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=According to
CC PubMed:15911621 more commonly found in heterochromatin. According
CC to PubMed:10997781 associates with actively transcribed chromatin
CC and not heterochromatin.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in the majority of the
CC cell lines tested and in testis.
CC -!- DOMAIN: The C-terminal domain is required for high-affinity
CC binding to chromatin (By similarity).
CC -!- PTM: H1 histones are progressively phosphorylated during the cell
CC cycle, becoming maximally phosphorylated during late G2 phase and
CC M phase, and being dephosphorylated sharply thereafter (By
CC similarity). Phosphorylated at Thr-11 by GSK3B during mitosis in
CC prometaphase and dephosphorylated in telophase.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family.
CC -!- SIMILARITY: Contains 1 H15 (linker histone H1/H5 globular) domain.
CC -----------------------------------------------------------------------
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DR EMBL; X83509; CAA58498.1; -; Genomic_DNA.
DR EMBL; AF531304; AAN06704.1; -; Genomic_DNA.
DR EMBL; Z98744; CAB11421.1; -; Genomic_DNA.
DR EMBL; BC069101; AAH69101.1; -; mRNA.
DR EMBL; BC101581; AAI01582.1; -; mRNA.
DR EMBL; BC101583; AAI01584.1; -; mRNA.
DR PIR; S51660; S51660.
DR RefSeq; NP_005313.1; NM_005322.2.
DR UniGene; Hs.131956; -.
DR PDB; 2FE2; Model; -; A=2-226.
DR PDB; 2RHI; X-ray; 1.66 A; B=23-27.
DR PDBsum; 2FE2; -.
DR PDBsum; 2RHI; -.
DR ProteinModelPortal; P16401; -.
DR SMR; P16401; 40-112.
DR IntAct; P16401; 4.
DR MINT; MINT-3008567; -.
DR STRING; 9606.ENSP00000330074; -.
DR PhosphoSite; P16401; -.
DR DMDM; 19856407; -.
DR PaxDb; P16401; -.
DR PeptideAtlas; P16401; -.
DR PRIDE; P16401; -.
DR DNASU; 3009; -.
DR Ensembl; ENST00000331442; ENSP00000330074; ENSG00000184357.
DR GeneID; 3009; -.
DR KEGG; hsa:3009; -.
DR UCSC; uc003njx.3; human.
DR CTD; 3009; -.
DR GeneCards; GC06M027835; -.
DR HGNC; HGNC:4719; HIST1H1B.
DR HPA; CAB012241; -.
DR MIM; 142711; gene.
DR neXtProt; NX_P16401; -.
DR PharmGKB; PA29097; -.
DR eggNOG; NOG258621; -.
DR HOGENOM; HOG000251627; -.
DR HOVERGEN; HBG009035; -.
DR InParanoid; P16401; -.
DR KO; K11275; -.
DR OMA; TRVAKAK; -.
DR OrthoDB; EOG74TX2T; -.
DR Reactome; REACT_578; Apoptosis.
DR EvolutionaryTrace; P16401; -.
DR GeneWiki; HIST1H1B; -.
DR GenomeRNAi; 3009; -.
DR NextBio; 11932; -.
DR PRO; PR:P16401; -.
DR Bgee; P16401; -.
DR CleanEx; HS_HIST1H1B; -.
DR Genevestigator; P16401; -.
DR GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
DR GO; GO:0000786; C:nucleosome; NAS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; NAS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR005819; Histone_H5.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF00538; Linker_histone; 1.
DR PRINTS; PR00624; HISTONEH5.
DR SMART; SM00526; H15; 1.
DR PROSITE; PS51504; H15; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; Complete proteome;
KW Direct protein sequencing; DNA-binding; Methylation; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 226 Histone H1.5.
FT /FTId=PRO_0000195909.
FT DOMAIN 39 112 H15.
FT MOD_RES 2 2 N-acetylserine; partial.
FT MOD_RES 2 2 Phosphoserine.
FT MOD_RES 11 11 Phosphothreonine; by GSK3.
FT MOD_RES 18 18 Phosphoserine.
FT MOD_RES 27 27 N6-methyllysine.
FT MOD_RES 39 39 Phosphothreonine.
FT MOD_RES 138 138 Phosphothreonine.
FT MOD_RES 168 168 N6-acetyllysine.
FT MOD_RES 173 173 Phosphoserine.
FT VARIANT 86 86 G -> D (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036204.
FT VARIANT 144 144 K -> R (in dbSNP:rs11970638).
FT /FTId=VAR_049308.
FT VARIANT 211 211 A -> T (in dbSNP:rs34144478).
FT /FTId=VAR_049309.
FT CONFLICT 216 218 Missing (in Ref. 5; AA sequence).
SQ SEQUENCE 226 AA; 22580 MW; 0BA1402101766FDF CRC64;
MSETAPAETA TPAPVEKSPA KKKATKKAAG AGAAKRKATG PPVSELITKA VAASKERNGL
SLAALKKALA AGGYDVEKNN SRIKLGLKSL VSKGTLVQTK GTGASGSFKL NKKAASGEAK
PKAKKAGAAK AKKPAGATPK KAKKAAGAKK AVKKTPKKAK KPAAAGVKKV AKSPKKAKAA
AKPKKATKSP AKPKAVKPKA AKPKAAKPKA AKPKAAKAKK AAAKKK
//
MIM
142711
*RECORD*
*FIELD* NO
142711
*FIELD* TI
*142711 HISTONE GENE CLUSTER 1, H1 HISTONE FAMILY, MEMBER B; HIST1H1B
;;HISTONE GENE CLUSTER 1, H1B;;
read moreHIST1 CLUSTER, H1B;;
H1B;;
H1.5;;
H1 HISTONE FAMILY, MEMBER 5, FORMERLY; H1F5, FORMERLY
*FIELD* TX
For background information on histones, histone gene clusters, and the
H1 histone family, see HIST1H1A (142709).
CLONING
Albig et al. (1997) isolated the gene for H1.5 histone.
GENE FUNCTION
By investigating MSX1 (142983) function in repression of myogenic gene
expression, Lee et al. (2004) identified a physical interaction between
MSX1 and H1B. Lee et al. (2004) found that MSX1 and H1B bind to a key
regulatory element of MYOD (159970), a central regulator of skeletal
muscle differentiation, where they induce repressed chromatin. Moreover,
MSX1 and H1B cooperated to inhibit muscle differentiation in cell
culture and in Xenopus animal caps. Lee et al. (2004) concluded that
their findings defined a theretofore unknown function for linker
histones in gene-specific transcriptional regulation.
See HIST1H1A (142709) for additional functional information on H1
histones.
MAPPING
By PCR analysis of chromosomal DNA from a panel of human/rodent somatic
cell hybrids, Albig et al. (1993) found that 6 human H1 histone genes,
including H1.5, are located on chromosome 6. By fluorescence in situ
hybridization with human metaphase chromosomes and PCR analysis of
somatic cell hybrid DNAs carrying only fragments of chromosome 6, they
demonstrated that the histone genes are clustered in the 6p22.2-p21.1
region.
Albig et al. (1997) showed that there are 2 clusters of histone genes on
chromosome 6p. The H1.5 gene is located in the second cluster, about 2
Mb centromeric of the major cluster. In a contig of the histone
gene-containing cosmids from this region, Albig and Doenecke (1997)
found 1 H1 gene (H1.5), 5 H2A genes, 4 H2B genes, 1 H2B pseudogene, 3 H3
genes, 3 H4 genes, and 1 H4 pseudogene. The cluster extends about 80 kb
with a nonordered arrangement of the histone genes. The dinucleotide
repeat polymorphic marker D6S105 was localized at the telomeric end of
this histone gene cluster. Almost all human histone genes isolated to
that time had been localized within the 2 clusters on 6p or in a small
group of histone genes on chromosome 1.
By genomic sequence analysis, Marzluff et al. (2002) determined that the
histone gene cluster on chromosome 6p22-p21, which they called histone
gene cluster-1 (HIST1), contains 55 histone genes, including HIST1H1B.
*FIELD* RF
1. Albig, W.; Doenecke, D.: The human histone gene cluster at the
D6S105 locus. Hum. Genet. 101: 284-294, 1997.
2. Albig, W.; Drabent, B.; Kunz, J.; Kalff-Suske, M.; Grzeschik, K.-H.;
Doenecke, D.: All known human H1 histone genes except the H1(0) gene
are clustered on chromosome 6. Genomics 16: 649-654, 1993.
3. Albig, W.; Meergans, T.; Doenecke, D.: Characterization of the
H1.5 gene completes the set of human H1 subtype genes. Gene 184:
141-148, 1997.
4. Lee, H.; Habas, R.; Abate-Shen, C.: Msx1 cooperates with histone
H1b for inhibition of transcription and myogenesis. Science 304:
1675-1678, 2004.
5. Marzluff, W. F.; Gongidi, P.; Woods, K. R.; Jin, J.; Maltais, L.
J.: The human and mouse replication-dependent histone genes. Genomics 80:
487-498, 2002.
*FIELD* CN
Matthew B. Gross - updated: 06/24/2010
Ada Hamosh - updated: 2/27/2008
Ada Hamosh - updated: 6/22/2004
Ada Hamosh - updated: 6/7/2001
Rebekah S. Rasooly - updated: 7/28/1998
Rebekah S. Rasooly - updated: 7/8/1998
Victor A. McKusick - updated: 2/12/1998
*FIELD* CD
Victor A. McKusick: 6/28/1993
*FIELD* ED
mgross: 06/24/2010
mgross: 5/26/2010
carol: 2/27/2008
alopez: 6/24/2004
terry: 6/22/2004
tkritzer: 3/31/2003
cwells: 6/12/2001
cwells: 6/11/2001
terry: 6/7/2001
carol: 3/4/1999
alopez: 7/28/1998
alopez: 7/14/1998
alopez: 7/10/1998
alopez: 7/8/1998
alopez: 2/12/1998
carol: 6/28/1993
*RECORD*
*FIELD* NO
142711
*FIELD* TI
*142711 HISTONE GENE CLUSTER 1, H1 HISTONE FAMILY, MEMBER B; HIST1H1B
;;HISTONE GENE CLUSTER 1, H1B;;
read moreHIST1 CLUSTER, H1B;;
H1B;;
H1.5;;
H1 HISTONE FAMILY, MEMBER 5, FORMERLY; H1F5, FORMERLY
*FIELD* TX
For background information on histones, histone gene clusters, and the
H1 histone family, see HIST1H1A (142709).
CLONING
Albig et al. (1997) isolated the gene for H1.5 histone.
GENE FUNCTION
By investigating MSX1 (142983) function in repression of myogenic gene
expression, Lee et al. (2004) identified a physical interaction between
MSX1 and H1B. Lee et al. (2004) found that MSX1 and H1B bind to a key
regulatory element of MYOD (159970), a central regulator of skeletal
muscle differentiation, where they induce repressed chromatin. Moreover,
MSX1 and H1B cooperated to inhibit muscle differentiation in cell
culture and in Xenopus animal caps. Lee et al. (2004) concluded that
their findings defined a theretofore unknown function for linker
histones in gene-specific transcriptional regulation.
See HIST1H1A (142709) for additional functional information on H1
histones.
MAPPING
By PCR analysis of chromosomal DNA from a panel of human/rodent somatic
cell hybrids, Albig et al. (1993) found that 6 human H1 histone genes,
including H1.5, are located on chromosome 6. By fluorescence in situ
hybridization with human metaphase chromosomes and PCR analysis of
somatic cell hybrid DNAs carrying only fragments of chromosome 6, they
demonstrated that the histone genes are clustered in the 6p22.2-p21.1
region.
Albig et al. (1997) showed that there are 2 clusters of histone genes on
chromosome 6p. The H1.5 gene is located in the second cluster, about 2
Mb centromeric of the major cluster. In a contig of the histone
gene-containing cosmids from this region, Albig and Doenecke (1997)
found 1 H1 gene (H1.5), 5 H2A genes, 4 H2B genes, 1 H2B pseudogene, 3 H3
genes, 3 H4 genes, and 1 H4 pseudogene. The cluster extends about 80 kb
with a nonordered arrangement of the histone genes. The dinucleotide
repeat polymorphic marker D6S105 was localized at the telomeric end of
this histone gene cluster. Almost all human histone genes isolated to
that time had been localized within the 2 clusters on 6p or in a small
group of histone genes on chromosome 1.
By genomic sequence analysis, Marzluff et al. (2002) determined that the
histone gene cluster on chromosome 6p22-p21, which they called histone
gene cluster-1 (HIST1), contains 55 histone genes, including HIST1H1B.
*FIELD* RF
1. Albig, W.; Doenecke, D.: The human histone gene cluster at the
D6S105 locus. Hum. Genet. 101: 284-294, 1997.
2. Albig, W.; Drabent, B.; Kunz, J.; Kalff-Suske, M.; Grzeschik, K.-H.;
Doenecke, D.: All known human H1 histone genes except the H1(0) gene
are clustered on chromosome 6. Genomics 16: 649-654, 1993.
3. Albig, W.; Meergans, T.; Doenecke, D.: Characterization of the
H1.5 gene completes the set of human H1 subtype genes. Gene 184:
141-148, 1997.
4. Lee, H.; Habas, R.; Abate-Shen, C.: Msx1 cooperates with histone
H1b for inhibition of transcription and myogenesis. Science 304:
1675-1678, 2004.
5. Marzluff, W. F.; Gongidi, P.; Woods, K. R.; Jin, J.; Maltais, L.
J.: The human and mouse replication-dependent histone genes. Genomics 80:
487-498, 2002.
*FIELD* CN
Matthew B. Gross - updated: 06/24/2010
Ada Hamosh - updated: 2/27/2008
Ada Hamosh - updated: 6/22/2004
Ada Hamosh - updated: 6/7/2001
Rebekah S. Rasooly - updated: 7/28/1998
Rebekah S. Rasooly - updated: 7/8/1998
Victor A. McKusick - updated: 2/12/1998
*FIELD* CD
Victor A. McKusick: 6/28/1993
*FIELD* ED
mgross: 06/24/2010
mgross: 5/26/2010
carol: 2/27/2008
alopez: 6/24/2004
terry: 6/22/2004
tkritzer: 3/31/2003
cwells: 6/12/2001
cwells: 6/11/2001
terry: 6/7/2001
carol: 3/4/1999
alopez: 7/28/1998
alopez: 7/14/1998
alopez: 7/10/1998
alopez: 7/8/1998
alopez: 2/12/1998
carol: 6/28/1993