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UniProtKB/Swiss-Prot entry P62805


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name H4_HUMAN
Primary accession number P62805
Secondary accession numbers A2VCL0 P02304 P02305 Q6DRA9 Q6FGB8 Q6NWP7
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 66)
Name and origin of the protein
Protein name Histone H4
Synonyms None
Gene names
Name: HIST1H4A
Synonyms: H4/A, H4FA
and
Name: HIST1H4B
Synonyms: H4/I, H4FI
and
Name: HIST1H4C
Synonyms: H4/G, H4FG
and
Name: HIST1H4D
Synonyms: H4/B, H4FB
and
Name: HIST1H4E
Synonyms: H4/J, H4FJ
and
Name: HIST1H4F
Synonyms: H4/C, H4FC
and
Name: HIST1H4H
Synonyms: H4/H, H4FH
and
Name: HIST1H4I
Synonyms: H4/M, H4FM
and
Name: HIST1H4J
Synonyms: H4/E, H4FE
and
Name: HIST1H4K
Synonyms: H4/D, H4FD
and
Name: HIST1H4L
Synonyms: H4/K, H4FK
and
Name: HIST2H4A
Synonyms: H4/N, H4F2, H4FN, HIST2H4
and
Name: HIST2H4B
Synonyms: H4/O, H4FO
and
Name: HIST4H4
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1093/nar/11.20.7069; PubMed=6314274 [NCBI, ExPASy, EBI, Israel, Japan]
Sierra F., Stein G., Stein J.;
"Structure and in vitro transcription of a human H4 histone gene.";
Nucleic Acids Res. 11:7069-7086(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3035717 [NCBI, ExPASy, EBI, Israel, Japan]
Pauli U., Chrysogelos S., Stein G., Stein J., Nick H.;
"Protein-DNA interactions in vivo upstream of a cell cycle-regulated human H4 histone gene.";
Science 236:1308-1311(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
DOI=10.1016/0888-7543(91)90183-F; PubMed=1916825 [NCBI, ExPASy, EBI, Israel, Japan]
Albig W., Kardalinou E., Drabent B., Zimmer A., Doenecke D.;
"Isolation and characterization of two human H1 histone genes within clusters of core histone genes.";
Genomics 10:940-948(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7626218 [NCBI, ExPASy, EBI, Israel, Japan]
Drabent B., Kardalinou E., Bode C., Doenecke D.;
"Association of histone H4 genes with the mammalian testis-specific H1t histone gene.";
DNA Cell Biol. 14:591-597(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/S0378-1119(96)00582-3; PubMed=9031620 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1007/s004390050630; PubMed=9439656 [NCBI, ExPASy, EBI, Israel, Japan]
Albig W., Doenecke D.;
"The human histone gene cluster at the D6S105 locus.";
Hum. Genet. 101:284-294(1997).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1006/geno.1996.4592; PubMed=9119399 [NCBI, ExPASy, EBI, Israel, Japan]
Albig W., Kioschis P., Poustka A., Meergans K., Doenecke D.;
"Human histone gene organization: nonregular arrangement within a large cluster.";
Genomics 40:314-322(1997).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H4A; HIST1H4B; HIST1H4C; HIST1H4D; HIST1H4E; HIST1H4F; HIST1H4H; HIST1H4I; HIST1H4J; HIST1H4K; HIST1H4L; HIST2H4A AND HIST4H4).
DOI=10.1016/S0888-7543(02)96850-3; PubMed=12408966 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8988030 [NCBI, ExPASy, EBI, Israel, Japan]
Akasaka T., Miura I., Takahashi N., Akasaka H., Yonetani N., Ohno H., Fukuhara S., Okuma M.;
"A recurring translocation, t(3;6)(q27;p21), in non-Hodgkin's lymphoma results in replacement of the 5' regulatory region of BCL6 with a novel H4 histone gene.";
Cancer Res. 57:7-12(1997).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/j.gene.2004.07.036; PubMed=15527963 [NCBI, ExPASy, EBI, Israel, Japan]
Braastad C.D., Hovhannisyan H., van Wijnen A.J., Stein J.L., Stein G.S.;
"Functional characterization of a human histone gene cluster duplication.";
Gene 342:35-40(2004).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (HIST1H4F; HIST1H4H AND HIST2H4A).
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HIST1H4A; HIST1H4B; HIST1H4C; HIST1H4D; HIST1H4E; HIST1H4F; HIST1H4H; HIST1H4I; HIST1H4J; HIST1H4K AND HIST1H4L).
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow, Brain, Eye, Lung, Pancreas, Placenta, and Prostate;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[15]
PROTEIN SEQUENCE OF 25-36; 47-56; 61-78 AND 81-93, AND MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (MAR-2005) to UniProtKB.
[16]
ACETYLATION AT LYS-6; LYS-9; LYS-13 AND LYS-17.
PubMed=7664735 [NCBI, ExPASy, EBI, Israel, Japan]
O'Neill L.P., Turner B.M.;
"Histone H4 acetylation distinguishes coding regions of the human genome from heterochromatin in a differentiation-dependent but transcription-independent manner.";
EMBO J. 14:3946-3957(1995).
[17]
DNA-BINDING REGION.
DOI=10.1038/331365a0; PubMed=3340182 [NCBI, ExPASy, EBI, Israel, Japan]
Ebralidse K.K., Grachev S.A., Mirzabekov A.D.;
"A highly basic histone H4 domain bound to the sharply bent region of nucleosomal DNA.";
Nature 331:365-367(1988).
[18]
ACETYLATION AT LYS-6; LYS-9; LYS-13 AND LYS-17.
DOI=10.1016/0014-5793(89)80947-0; PubMed=2474456 [NCBI, ExPASy, EBI, Israel, Japan]
Turner B.M., O'Neill L.P., Allan I.M.;
"Histone H4 acetylation in human cells. Frequency of acetylation at different sites defined by immunolabeling with site-specific antibodies.";
FEBS Lett. 253:141-145(1989).
[19]
METHYLATION AT ARG-4.
DOI=10.1016/S0960-9822(01)00294-9; PubMed=11448779 [NCBI, ExPASy, EBI, Israel, Japan]
Strahl B.D., Briggs S.D., Brame C.J., Caldwell J.A., Koh S.S., Ma H., Cook R.G., Shabanowitz J., Hunt D.F., Stallcup M.R., Allis C.D.;
"Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1.";
Curr. Biol. 11:996-1000(2001).
[20]
METHYLATION AT ARG-4.
DOI=10.1126/science.1060781; PubMed=11387442 [NCBI, ExPASy, EBI, Israel, Japan]
Wang H., Huang Z.-Q., Xia L., Feng Q., Erdjument-Bromage H., Strahl B.D., Briggs S.D., Allis C.D., Wong J., Tempst P., Zhang Y.;
"Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor.";
Science 293:853-857(2001).
[21]
METHYLATION AT LYS-21.
DOI=10.1016/S1097-2765(02)00548-8; PubMed=12086618 [NCBI, ExPASy, EBI, Israel, Japan]
Nishioka K., Rice J.C., Sarma K., Erdjument-Bromage H., Werner J., Wang Y., Chuikov S., Valenzuela P., Tempst P., Steward R., Lis J.T., Allis C.D., Reinberg D.;
"PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin.";
Mol. Cell 9:1201-1213(2002).
[22]
SUMOYLATION.
DOI=10.1073/pnas.1735528100; PubMed=14578449 [NCBI, ExPASy, EBI, Israel, Japan]
Shiio Y., Eisenman R.N.;
"Histone sumoylation is associated with transcriptional repression.";
Proc. Natl. Acad. Sci. U.S.A. 100:13225-13230(2003).
[23]
METHYLATION [LARGE SCALE ANALYSIS] AT LYS-21, AND MASS SPECTROMETRY.
DOI=10.1038/nmeth715; PubMed=15782174 [NCBI, ExPASy, EBI, Israel, Japan]
Ong S.E., Mittler G., Mann M.;
"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC.";
Nat. Methods 1:119-126(2004).
[24]
CITRULLINATION AT ARG-4, AND METHYLATION AT ARG-4.
DOI=10.1126/science.1101400; PubMed=15345777 [NCBI, ExPASy, EBI, Israel, Japan]
Wang Y., Wysocka J., Sayegh J., Lee Y.-H., Perlin J.R., Leonelli L., Sonbuchner L.S., McDonald C.H., Cook R.G., Dou Y., Roeder R.G., Clarke S., Stallcup M.R., Allis C.D., Coonrod S.A.;
"Human PAD4 regulates histone arginine methylation levels via demethylimination.";
Science 306:279-283(2004).
[25]
METHYLATION AT LYS-21.
DOI=10.1074/jbc.M501691200; PubMed=15964846 [NCBI, ExPASy, EBI, Israel, Japan]
Yin Y., Liu C., Tsai S.N., Zhou B., Ngai S.M., Zhu G.;
"SET8 recognizes the sequence RHRK20VLRDN within the N terminus of histone H4 and mono-methylates lysine 20.";
J. Biol. Chem. 280:30025-30031(2005).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[27]
UBIQUITINATION.
DOI=10.1016/j.molcel.2006.03.035; PubMed=16678110 [NCBI, ExPASy, EBI, Israel, Japan]
Wang H., Zhai L., Xu J., Joo H.-Y., Jackson S., Erdjument-Bromage H., Tempst P., Xiong Y., Zhang Y.;
"Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage.";
Mol. Cell 22:383-394(2006).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9; LYS-13 AND LYS-17, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan]
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.";
Mol. Cell 23:607-618(2006).
[29]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9 AND LYS-13, METHYLATION AT LYS-21, PHOSPHORYLATION AT SER-2, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M500288-MCP200; PubMed=16319397 [NCBI, ExPASy, EBI, Israel, Japan]
Bonenfant D., Coulot M., Towbin H., Schindler P., van Oostrum J.;
"Characterization of histones H2A and H2B variants and their post-translational modifications by mass spectrometry.";
Mol. Cell. Proteomics 5:541-552(2006).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASS SPECTROMETRY.
TISSUE=Pituitary;
DOI=10.1007/s11102-006-8916-x; PubMed=16807684 [NCBI, ExPASy, EBI, Israel, Japan]
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
"Phosphoproteomic analysis of the human pituitary.";
Pituitary 9:109-120(2006).
[31]
ACETYLATION AT SER-2; LYS-13 AND LYS-17, PHOSPHORYLATION AT SER-2, AND METHYLATION AT LYS-21.
DOI=10.1128/MCB.01517-07; PubMed=17967882 [NCBI, ExPASy, EBI, Israel, Japan]
Pesavento J.J., Yang H., Kelleher N.L., Mizzen C.A.;
"Certain and progressive methylation of histone H4 at lysine 20 during the cell cycle.";
Mol. Cell. Biol. 28:468-486(2008).
[32]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1093/nar/gki663; PubMed=15951514 [NCBI, ExPASy, EBI, Israel, Japan]
Tsunaka Y., Kajimura N., Tate S., Morikawa K.;
"Alteration of the nucleosomal DNA path in the crystal structure of a human nucleosome core particle.";
Nucleic Acids Res. 33:3424-3434(2005).
[33]
VARIANT [LARGE SCALE ANALYSIS] GLN-64.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
  • FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
  • SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.
  • INTERACTION:
    Q9Y468:L3MBTL; NbExp=2; IntAct=EBI-302023, EBI-1265089;
    Q9SU94:PRMT1.1 (xeno); NbExp=1; IntAct=EBI-302023, EBI-1382731;
    O82210:PRMT1.2 (xeno); NbExp=1; IntAct=EBI-302023, EBI-1382526;
    Q9NQR1:SETD8; NbExp=4; IntAct=EBI-302023, EBI-1268946;
  • SUBCELLULAR LOCATION: Nucleus.
  • PTM: Acetylation at Lys-6, Lys-9, Lys-13 and Lys-17 occurs in coding regions of the genome but not in heterochromatin.
  • PTM: Citrullination at Arg-4 by PADI4 impairs methylation.
  • PTM: Monomethylation at Arg-4 by PRMT1 favors acetylation at Lys-9 and Lys-13. Demethylation is performed by JMJD6.
  • PTM: Monomethylated, dimethylated or trimethylated at Lys-21. Monomethylation is performed by SET8. Trimethylation is performed by SUV420H1 and SUV420H2 and induces gene silencing.
  • PTM: Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins.
  • PTM: Sumoylated, which is associated with transcriptional repression.
  • SIMILARITY: Belongs to the histone H4 family.
  • SEQUENCE CAUTION:
    • Sequence=AAI28106.1; Type=Frameshift; Positions=3;
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X00038; CAA24918.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M16707; AAA52652.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M60749; AAA63188.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X60481; CAA43011.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X60482; CAA43012.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X60483; CAA43013.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X60484; CAA43014.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X60486; CAA43016.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X60487; CAA43017.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X67081; CAA47464.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z80787; CAB02549.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X83548; CAA58538.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525682; AAM83108.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY128653; AAN01438.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY128654; AAN01439.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY128655; AAN01440.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY128656; AAN01441.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY128657; AAN01442.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY128658; AAN01443.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY128659; AAN01444.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY128661; AAN01446.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY128662; AAN01447.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY128663; AAN01448.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY128664; AAN01449.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY128665; AAN01450.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB000905; BAA19208.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY648850; AAT68253.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR542169; CAG46966.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR542172; CAG46969.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR542180; CAG46977.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR542187; CAG46984.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR542189; CAG46986.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL021807; CAA16946.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL021917; CAC69642.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL031777; CAC03414.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL031777; CAC03418.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049822; CAC03426.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049822; CAC03427.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL353759; CAC04128.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z98744; CAD24074.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL591493; CAI12560.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL591493; CAI12567.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471087; EAW55509.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471087; EAW55510.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471087; EAW55538.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471087; EAW55549.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471087; EAW55555.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471094; EAW96325.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471081; EAX03086.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471081; EAX03111.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471081; EAX03112.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471081; EAX03121.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010926; AAH10926.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012587; AAH12587.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC016336; AAH16336.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC017361; AAH17361.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC020884; AAH20884.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC054014; AAH54014.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC066248; AAH66248.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC066249; AAH66249.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC066250; AAH66250.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC067495; AAH67495.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC067496; AAH67496.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC067497; AAH67497.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069288; AAH69288.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069392; AAH69392.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069467; AAH69467.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC050615; AAH50615.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069654; AAH69654.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC075806; AAH75806.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC093763; AAH93763.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC093765; AAH93765.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC093969; AAH93969.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC108260; AAI08261.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC111093; AAI11094.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC111434; AAI11435.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC112193; AAI12194.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC120939; AAI20940.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC128104; AAI28105.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC128105; AAI28106.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC130558; AAI30559.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC130560; AAI30561.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC143045; AAI43046.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D40335; HSHU4.
RefSeq NP_001029249.1; -.
NP_003486.1; -.
NP_003529.1; -.
NP_003530.1; -.
NP_003531.1; -.
NP_003532.1; -.
NP_003533.1; -.
NP_003534.1; -.
NP_003535.1; -.
NP_003536.1; -.
NP_003537.1; -.
NP_003539.1; -.
NP_068803.1; -.
NP_778224.1; -.
UniGene Hs.143080
3D structure databases
PDB
2CV5; X-ray; 2.50 A; B/F=1-103.[ExPASy / RCSB / EBI]
2RNY; NMR; -; B=14-28.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2CV5; -.
2RNY; -.
ModBase P62805.
Protein-protein interaction databases
IntAct P62805; -.
PTM databases
PhosphoSite P62805; -.
Enzyme and pathway databases
Reactome REACT_7970; Telomere Maintenance.
2D gel databases
SWISS-2DPAGE P62805; -.
Aarhus/Ghent-2DPAGE 53; NEPHGE.
Organism-specific databases
H-InvDB HIX0001001; -.
HIX0003499; -.
HIX0005643; -.
HIX0005658; -.
HIX0019648; -.
HIX0021127; -.
HIX0025222; -.
HIX0032918; -.
HIX0032931; -.
HIX0032933; -.
HIX0032934; -.
HIX0033000; -.
HIX0033460; -.
HIX0056766; -.
HGNC HGNC:4781; HIST1H4A.
HGNC:4789; HIST1H4B.
HGNC:4787; HIST1H4C.
HGNC:4782; HIST1H4D.
HGNC:4790; HIST1H4E.
HGNC:4783; HIST1H4F.
HGNC:4788; HIST1H4H.
HGNC:4793; HIST1H4I.
HGNC:4785; HIST1H4J.
HGNC:4784; HIST1H4K.
HGNC:4791; HIST1H4L.
HGNC:4794; HIST2H4A.
HGNC:29607; HIST2H4B.
HGNC:20510; HIST4H4.
GeneLynx HIST1H4A; Homo sapiens.
GenAtlas HIST1H4A.
HPA CAB011503; -.
MIM 142750; gene. [NCBI / EBI]
602822; gene. [NCBI / EBI]
602823; gene. [NCBI / EBI]
602824; gene. [NCBI / EBI]
602825; gene. [NCBI / EBI]
602826; gene. [NCBI / EBI]
602827; gene. [NCBI / EBI]
602828; gene. [NCBI / EBI]
602829; gene. [NCBI / EBI]
602830; gene. [NCBI / EBI]
602831; gene. [NCBI / EBI]
602833; gene. [NCBI / EBI]
PharmGKB PA29156; -.
GeneCards P62805.
Gene expression databases
ArrayExpres