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P62805 (H4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H4
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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length103 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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 structure

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.

Subcellular location

Nucleus. Chromosome.

Post-translational modification

Acetylation at Lys-6 (H4K5ac), Lys-9 (H4K8ac), Lys-13 (H4K12ac) and Lys-17 (H4K16ac) occurs in coding regions of the genome but not in heterochromatin. Ref.16 Ref.18 Ref.30 Ref.32

Citrullination at Arg-4 (H4R3ci) by PADI4 impairs methylation.

Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac) and Lys-13 (H4K12ac). Demethylation is performed by JMJD6. Symmetric dimethylation on Arg-4 (H4R3me2s) by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage. Ref.16 Ref.18 Ref.30 Ref.32

Monomethylated, dimethylated or trimethylated at Lys-21 (H4K20me1, H4K20me2, H4K20me3). Monomethylation is performed by SET8. Trimethylation is performed by SUV420H1 and SUV420H2 and induces gene silencing. Ref.19 Ref.20 Ref.22 Ref.24 Ref.25 Ref.30

Phosphorylated by PAK2 at Ser-48 (H4S47ph). This phosphorylation increases the association of H3.3-H4 with the histone chaperone HIRA, thus promoting nucleosome assembly of H3.3-H4 and inhibiting nucleosome assembly of H3.1-H4. Ref.30 Ref.38

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. Monoubiquitinated at Lys-92 of histone H4 (H4K91ub1) in response to DNA damage. The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post-translational modifications such as H4 Lys-21 methylation (H4K20me). Ref.28 Ref.32

Sumoylated, which is associated with transcriptional repression. Ref.23

Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. Ref.37

Involvement in disease

Chromosomal aberrations involving HISTONE H4 is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;6)(q27;p21), with BCL6.

Sequence similarities

Belongs to the histone H4 family.

Sequence caution

The sequence AAI28106.1 differs from that shown. Reason: Frameshift at position 3.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 103102Histone H4
PRO_0000158320

Regions

DNA binding17 – 215 Ref.17

Amino acid modifications

Modified residue21N-acetylserine Ref.30
Modified residue21Phosphoserine Ref.30
Modified residue41Asymmetric dimethylarginine; by PRMT1; alternate Ref.19 Ref.20 Ref.24
Modified residue41Citrulline; alternate
Modified residue41Omega-N-methylarginine; by PRMT1; alternate Ref.19 Ref.20 Ref.24
Modified residue41Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate By similarity
Modified residue61N6-acetyllysine; alternate Ref.16 Ref.18 Ref.34
Modified residue61N6-crotonyl-L-lysine; alternate Ref.37
Modified residue91N6-acetyllysine; alternate Ref.16 Ref.18 Ref.34
Modified residue91N6-crotonyl-L-lysine; alternate Ref.37
Modified residue131N6-acetyllysine; alternate Ref.16 Ref.18 Ref.30 Ref.34
Modified residue131N6-crotonyl-L-lysine; alternate Ref.37
Modified residue171N6-acetyllysine; alternate Ref.16 Ref.18 Ref.30 Ref.34
Modified residue171N6-crotonyl-L-lysine; alternate By similarity
Modified residue211N6,N6,N6-trimethyllysine; alternate Ref.22 Ref.25 Ref.30
Modified residue211N6,N6-dimethyllysine; alternate Ref.22 Ref.25 Ref.30
Modified residue211N6-methyllysine; alternate Ref.22 Ref.25 Ref.30
Modified residue321N6-acetyllysine Ref.34
Modified residue481Phosphoserine; by PAK2 Ref.27 Ref.31 Ref.33 Ref.35 Ref.38 Ref.39
Modified residue521Phosphotyrosine Ref.26 Ref.35
Modified residue891Phosphotyrosine By similarity
Modified residue921N6-acetyllysine; alternate Ref.32
Modified residue921N6-succinyllysine; alternate By similarity
Cross-link92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.32

Natural variations

Natural variant641E → Q in a breast cancer sample; somatic mutation. Ref.41
VAR_036206

Experimental info

Sequence conflict711V → A in AAH67496. Ref.14
Sequence conflict771A → P in CAG46986. Ref.11

Secondary structure

.................... 103
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62805 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A9E5DFD3F8B97598

FASTA10311,367
        10         20         30         40         50         60 
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK 

        70         80         90        100 
VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG 

« Hide

References

« Hide 'large scale' references
[1]"Structure and in vitro transcription of a human H4 histone gene."
Sierra F., Stein G., Stein J.
Nucleic Acids Res. 11:7069-7086(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Protein-DNA interactions in vivo upstream of a cell cycle-regulated human H4 histone gene."
Pauli U., Chrysogelos S., Stein G., Stein J., Nick H.
Science 236:1308-1311(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Isolation and characterization of two human H1 histone genes within clusters of core histone genes."
Albig W., Kardalinou E., Drabent B., Zimmer A., Doenecke D.
Genomics 10:940-948(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[4]"Association of histone H4 genes with the mammalian testis-specific H1t histone gene."
Drabent B., Kardalinou E., Bode C., Doenecke D.
DNA Cell Biol. 14:591-597(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Characterization of the H1.5 gene completes the set of human H1 subtype genes."
Albig W., Meergans T., Doenecke D.
Gene 184:141-148(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"The human histone gene cluster at the D6S105 locus."
Albig W., Doenecke D.
Hum. Genet. 101:284-294(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"Human histone gene organization: nonregular arrangement within a large cluster."
Albig W., Kioschis P., Poustka A., Meergans K., Doenecke D.
Genomics 40:314-322(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"The human and mouse replication-dependent histone genes."
Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.
Genomics 80:487-498(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H4A; HIST1H4B; HIST1H4C; HIST1H4D; HIST1H4E; HIST1H4F; HIST1H4H; HIST1H4I; HIST1H4J; HIST1H4K; HIST1H4L; HIST2H4A AND HIST4H4).
[9]"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."
Akasaka T., Miura I., Takahashi N., Akasaka H., Yonetani N., Ohno H., Fukuhara S., Okuma M.
Cancer Res. 57:7-12(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[10]"Functional characterization of a human histone gene cluster duplication."
Braastad C.D., Hovhannisyan H., van Wijnen A.J., Stein J.L., Stein G.S.
Gene 342:35-40(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[11]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
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.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (HIST1H4F; HIST1H4H AND HIST2H4A).
[12]"The DNA sequence and analysis of human chromosome 6."
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. expand/collapse author list , 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.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HIST1H4A; HIST1H4B; HIST1H4C; HIST1H4D; HIST1H4E; HIST1H4F; HIST1H4H; HIST1H4I; HIST1H4J; HIST1H4K AND HIST1H4L).
[13]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cerebellum, Eye and Placenta.
[15]Bienvenut W.V.
Submitted (MAR-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 25-36; 47-56; 61-78 AND 81-93, MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[16]"Histone H4 acetylation distinguishes coding regions of the human genome from heterochromatin in a differentiation-dependent but transcription-independent manner."
O'Neill L.P., Turner B.M.
EMBO J. 14:3946-3957(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-6; LYS-9; LYS-13 AND LYS-17.
[17]"A highly basic histone H4 domain bound to the sharply bent region of nucleosomal DNA."
Ebralidse K.K., Grachev S.A., Mirzabekov A.D.
Nature 331:365-367(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING REGION.
[18]"Histone H4 acetylation in human cells. Frequency of acetylation at different sites defined by immunolabeling with site-specific antibodies."
Turner B.M., O'Neill L.P., Allan I.M.
FEBS Lett. 253:141-145(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-6; LYS-9; LYS-13 AND LYS-17.
[19]"Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1."
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.
Curr. Biol. 11:996-1000(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT ARG-4.
[20]"Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor."
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.
Science 293:853-857(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT ARG-4.
[21]"Characterization of t(3;6)(q27;p21) breakpoints in B-cell non-Hodgkin's lymphoma and construction of the histone H4/BCL6 fusion gene, leading to altered expression of Bcl-6."
Kurata M., Maesako Y., Ueda C., Nishikori M., Akasaka T., Uchiyama T., Ohno H.
Cancer Res. 62:6224-6230(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN B-CELL NON-HODGKIN LYMPHOMA, CHROMOSOMAL TRANSLOCATION WITH BCL6.
[22]"PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin."
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.
Mol. Cell 9:1201-1213(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-21.
[23]"Histone sumoylation is associated with transcriptional repression."
Shiio Y., Eisenman R.N.
Proc. Natl. Acad. Sci. U.S.A. 100:13225-13230(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION.
[24]"Human PAD4 regulates histone arginine methylation levels via demethylimination."
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.
Science 306:279-283(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION AT ARG-4, METHYLATION AT ARG-4.
[25]"SET8 recognizes the sequence RHRK20VLRDN within the N terminus of histone H4 and mono-methylates lysine 20."
Yin Y., Liu C., Tsai S.N., Zhou B., Ngai S.M., Zhu G.
J. Biol. Chem. 280:30025-30031(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-21.
[26]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage."
Wang H., Zhai L., Xu J., Joo H.-Y., Jackson S., Erdjument-Bromage H., Tempst P., Xiong Y., Zhang Y.
Mol. Cell 22:383-394(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[29]"Structural basis for histone N-terminal recognition by human peptidylarginine deiminase 4."
Arita K., Shimizu T., Hashimoto H., Hidaka Y., Yamada M., Sato M.
Proc. Natl. Acad. Sci. U.S.A. 103:5291-5296(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION AT ARG-4.
[30]"Certain and progressive methylation of histone H4 at lysine 20 during the cell cycle."
Pesavento J.J., Yang H., Kelleher N.L., Mizzen C.A.
Mol. Cell. Biol. 28:468-486(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT SER-2; LYS-13 AND LYS-17, PHOSPHORYLATION AT SER-2, METHYLATION AT LYS-21.
[31]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[32]"BBAP monoubiquitylates histone H4 at lysine 91 and selectively modulates the DNA damage response."
Yan Q., Dutt S., Xu R., Graves K., Juszczynski P., Manis J.P., Shipp M.A.
Mol. Cell 36:110-120(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-92, UBIQUITINATION AT LYS-92.
[33]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[34]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9; LYS-13; LYS-17 AND LYS-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND TYR-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[36]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[37]"Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification."
Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T., Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.
Cell 146:1016-1028(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: CROTONYLATION AT LYS-6; LYS-9 AND LYS-13.
[38]"Phosphorylation of H4 Ser 47 promotes HIRA-mediated nucleosome assembly."
Kang B., Pu M., Hu G., Wen W., Dong Z., Zhao K., Stillman B., Zhang Z.
Genes Dev. 25:1359-1364(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-48.
[39]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[40]"Alteration of the nucleosomal DNA path in the crystal structure of a human nucleosome core particle."
Tsunaka Y., Kajimura N., Tate S., Morikawa K.
Nucleic Acids Res. 33:3424-3434(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[41]"The consensus coding sequences of human breast and colorectal cancers."
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. expand/collapse author list , 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.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-64.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00038 Genomic DNA. Translation: CAA24918.1. Sequence problems.
M16707 Genomic DNA. Translation: AAA52652.1.
M60749 Genomic DNA. Translation: AAA63188.1.
X60481 Genomic DNA. Translation: CAA43011.1.
X60482 Genomic DNA. Translation: CAA43012.1.
X60483 Genomic DNA. Translation: CAA43013.1.
X60484 Genomic DNA. Translation: CAA43014.1.
X60486 Genomic DNA. Translation: CAA43016.1.
X60487 Genomic DNA. Translation: CAA43017.1.
X67081 Genomic DNA. Translation: CAA47464.1.
Z80787 Genomic DNA. Translation: CAB02549.1.
X83548 Genomic DNA. Translation: CAA58538.1.
AF525682 Genomic DNA. Translation: AAM83108.1.
AY128653 Genomic DNA. Translation: AAN01438.1.
AY128654 Genomic DNA. Translation: AAN01439.1.
AY128655 Genomic DNA. Translation: AAN01440.1.
AY128656 Genomic DNA. Translation: AAN01441.1.
AY128657 Genomic DNA. Translation: AAN01442.1.
AY128658 Genomic DNA. Translation: AAN01443.1.
AY128659 Genomic DNA. Translation: AAN01444.1.
AY128661 Genomic DNA. Translation: AAN01446.1.
AY128662 Genomic DNA. Translation: AAN01447.1.
AY128663 Genomic DNA. Translation: AAN01448.1.
AY128664 Genomic DNA. Translation: AAN01449.1.
AY128665 Genomic DNA. Translation: AAN01450.1.
AB000905 Genomic DNA. Translation: BAA19208.1.
AY648850 Genomic DNA. Translation: AAT68253.1.
CR542169 mRNA. Translation: CAG46966.1.
CR542172 mRNA. Translation: CAG46969.1.
CR542180 mRNA. Translation: CAG46977.1.
CR542187 mRNA. Translation: CAG46984.1.
CR542189 mRNA. Translation: CAG46986.1.
AL021807 Genomic DNA. Translation: CAA16946.1.
AL021917 Genomic DNA. Translation: CAC69642.1.
AL031777 Genomic DNA. Translation: CAC03414.1.
AL031777 Genomic DNA. Translation: CAC03418.1.
AL049822 Genomic DNA. Translation: CAC03426.1.
AL049822 Genomic DNA. Translation: CAC03427.1.
AL353759 Genomic DNA. Translation: CAC04128.1.
Z98744 Genomic DNA. Translation: CAD24074.1.
AL591493 Genomic DNA. Translation: CAI12560.1.
AL591493 Genomic DNA. Translation: CAI12567.1.
CH471087 Genomic DNA. Translation: EAW55509.1.
CH471087 Genomic DNA. Translation: EAW55510.1.
CH471087 Genomic DNA. Translation: EAW55538.1.
CH471087 Genomic DNA. Translation: EAW55549.1.
CH471087 Genomic DNA. Translation: EAW55555.1.
CH471094 Genomic DNA. Translation: EAW96325.1.
CH471081 Genomic DNA. Translation: EAX03086.1.
CH471081 Genomic DNA. Translation: EAX03111.1.
CH471081 Genomic DNA. Translation: EAX03112.1.
CH471081 Genomic DNA. Translation: EAX03121.1.
BC017361 mRNA. Translation: AAH17361.1.
BC054014 mRNA. Translation: AAH54014.1.
BC066248 mRNA. Translation: AAH66248.1.
BC066249 mRNA. Translation: AAH66249.1.
BC066250 mRNA. Translation: AAH66250.1.
BC067495 mRNA. Translation: AAH67495.1.
BC067496 mRNA. Translation: AAH67496.1.
BC067497 mRNA. Translation: AAH67497.1.
BC069288 mRNA. Translation: AAH69288.1.
BC069392 mRNA. Translation: AAH69392.1.
BC069467 mRNA. Translation: AAH69467.1.
BC069654 mRNA. Translation: AAH69654.1.
BC093763 mRNA. Translation: AAH93763.1.
BC093765 mRNA. Translation: AAH93765.1.
BC093969 mRNA. Translation: AAH93969.1.
BC111093 mRNA. Translation: AAI11094.1.
BC111434 mRNA. Translation: AAI11435.1.
BC112193 mRNA. Translation: AAI12194.1.
BC120939 mRNA. Translation: AAI20940.1.
BC128104 mRNA. Translation: AAI28105.1.
BC128105 mRNA. Translation: AAI28106.1. Frameshift.
BC130558 mRNA. Translation: AAI30559.1.
BC130560 mRNA. Translation: AAI30561.1.
BC143045 mRNA. Translation: AAI43046.1.
PIRHSHU4. D40335.
RefSeqNP_001029249.1. NM_001034077.4.
NP_003486.1. NM_003495.2.
NP_003529.1. NM_003538.3.
NP_003530.1. NM_003539.3.
NP_003531.1. NM_003540.3.
NP_003532.1. NM_003541.2.
NP_003533.1. NM_003542.3.
NP_003534.1. NM_003543.3.
NP_003535.1. NM_003544.2.
NP_003536.1. NM_003545.3.
NP_003537.1. NM_003546.2.
NP_003539.1. NM_003548.2.
NP_068803.1. NM_021968.3.
NP_778224.1. NM_175054.2.
XP_005245367.1. XM_005245310.1.
XP_005245368.1. XM_005245311.1.
XP_005245369.1. XM_005245312.1.
XP_005245579.1. XM_005245522.1.
XP_005245580.1. XM_005245523.1.
XP_005245581.1. XM_005245524.1.
XP_005249493.1. XM_005249436.1.
XP_005249501.1. XM_005249444.1.
XP_005253358.1. XM_005253301.1.
XP_005277467.1. XM_005277410.1.
XP_005277468.1. XM_005277411.1.
XP_005277469.1. XM_005277412.1.
XP_005277485.1. XM_005277428.1.
XP_005277486.1. XM_005277429.1.
XP_005277487.1. XM_005277430.1.
UniGeneHs.143080.
Hs.247816.
Hs.248172.
Hs.248178.
Hs.248179.
Hs.278483.
Hs.46423.
Hs.528055.
Hs.533295.
Hs.55468.
Hs.591790.
Hs.655235.
Hs.662174.
Hs.706635.
Hs.745457.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BQZX-ray1.50B/F18-26[»]
2CV5X-ray2.50B/F1-103[»]
2KWNNMR-B10-24[»]
2KWONMR-B2-21[»]
2LVMNMR-B15-28[»]
2QQSX-ray2.82C/D17-26[»]
2RNYNMR-B14-28[»]
2RS9NMR-A2-11[»]
3A6NX-ray2.70B/F1-103[»]
3AFAX-ray2.50B/F1-103[»]
3AN2X-ray3.60B/F1-103[»]
3AV1X-ray2.50B/F1-103[»]
3AV2X-ray2.80B/F1-103[»]
3AYWX-ray2.90B/F1-103[»]
3AZEX-ray3.00B/F1-103[»]
3AZFX-ray2.70B/F1-103[»]
3AZGX-ray2.40B/F1-103[»]
3AZHX-ray3.49B/F1-103[»]
3AZIX-ray2.70B/F1-103[»]
3AZJX-ray2.89B/F1-103[»]
3AZKX-ray3.20B/F1-103[»]
3AZLX-ray2.70B/F1-103[»]
3AZMX-ray2.89B/F1-103[»]
3AZNX-ray3.00B/F1-103[»]
3CFSX-ray2.40E28-42[»]
3CFVX-ray2.60E/F25-42[»]
3F9WX-ray1.60E/F/G/H16-25[»]
3F9XX-ray1.25E/F/G/H16-25[»]
3F9YX-ray1.50E/F16-25[»]
3F9ZX-ray1.60E/F/G/H16-25[»]
3NQJX-ray2.10B21-103[»]
3NQUX-ray2.50B1-103[»]
3O36X-ray1.70D/E15-20[»]
3QZSX-ray1.80C/D13-22[»]
3QZTX-ray1.50B13-22[»]
3QZVX-ray2.00C8-18[»]
3R45X-ray2.60B1-103[»]
3UVWX-ray1.37B2-12[»]
3UVXX-ray1.91B12-22[»]
3UVYX-ray2.02B16-26[»]
3UW9X-ray2.30E/F8-18[»]
3W96X-ray3.00B/F1-103[»]
3W97X-ray3.20B/F1-103[»]
3W98X-ray3.42B/F1-103[»]
3W99X-ray3.00B/F17-103[»]
3WA9X-ray3.07B/F1-103[»]
3WAAX-ray3.20B/F1-103[»]
4GQBX-ray2.06C2-22[»]
4H9NX-ray1.95B2-103[»]
4H9OX-ray2.05B2-103[»]
4H9PX-ray2.20B2-103[»]
4H9QX-ray1.95B2-103[»]
4H9RX-ray2.20B2-103[»]
4H9SX-ray2.60C/D21-103[»]
4HGAX-ray2.80C1-103[»]
ProteinModelPortalP62805.
SMRP62805. Positions 21-102.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113899. 21 interactions.
113955. 147 interactions.
113956. 17 interactions.
113957. 29 interactions.
113958. 16 interactions.
113959. 17 interactions.
113960. 16 interactions.
113961. 17 interactions.
113962. 17 interactions.
113963. 18 interactions.
113964. 16 interactions.
113966. 41 interactions.
125732. 85 interactions.
299853. 17 interactions.
DIPDIP-33079N.
IntActP62805. 92 interactions.
MINTMINT-276350.
STRING9606.ENSP00000289352.

Chemistry

ChEMBLCHEMBL5876.

PTM databases

PhosphoSiteP62805.

2D gel databases

SWISS-2DPAGEP62805.

Proteomic databases

PaxDbP62805.
PeptideAtlasP62805.
PRIDEP62805.

Protocols and materials databases

DNASU8294.
8360.
8362.
8363.
8364.
8365.
8366.
8367.
8368.
8370.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000289352; ENSP00000289352; ENSG00000158406.
ENST00000340756; ENSP00000343282; ENSG00000188987.
ENST00000354348; ENSP00000346316; ENSG00000198339.
ENST00000355057; ENSP00000347168; ENSG00000197238.
ENST00000355981; ENSP00000348258; ENSG00000198558.
ENST00000357549; ENSP00000350159; ENSG00000197914.
ENST00000358064; ENSP00000350767; ENSG00000197837.
ENST00000359907; ENSP00000352980; ENSG00000196176.
ENST00000360441; ENSP00000353624; ENSG00000198518.
ENST00000369157; ENSP00000358153; ENSG00000182217.
ENST00000369165; ENSP00000358162; ENSG00000183941.
ENST00000377364; ENSP00000366581; ENSG00000124529.
ENST00000377727; ENSP00000366956; ENSG00000158406.
ENST00000377745; ENSP00000366974; ENSG00000198327.
ENST00000377803; ENSP00000367034; ENSG00000197061.
ENST00000392932; ENSP00000376663; ENSG00000182217.
ENST00000392933; ENSP00000376664; ENSG00000182217.
ENST00000392938; ENSP00000376668; ENSG00000183941.
ENST00000392939; ENSP00000376669; ENSG00000183941.
ENST00000539745; ENSP00000443017; ENSG00000197837.
ENST00000610125; ENSP00000476824; ENSG00000183941.
GeneID121504.
554313.
8294.
8359.
8360.
8361.
8362.
8363.
8364.
8365.
8366.
8367.
8368.
8370.
KEGGhsa:121504.
hsa:554313.
hsa:8294.
hsa:8359.
hsa:8360.
hsa:8361.
hsa:8362.
hsa:8363.
hsa:8364.
hsa:8365.
hsa:8366.
hsa:8367.
hsa:8368.
hsa:8370.
UCSCuc001ess.3. human.

Organism-specific databases

CTD121504.
554313.
8294.
8359.
8360.
8361.
8362.
8363.
8364.
8365.
8366.
8367.
8368.
8370.
GeneCardsGC01M149830.
GC01P149804.
GC06M026027.
GC06M026188.
GC06M026281.
GC06M027798.
GC06M027917.
GC06P026021.
GC06P026104.
GC06P026204.
GC06P026240.
GC06P027107.
GC06P027791.
GC12M014920.
HGNCHGNC: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.
HPACAB011503.
CAB021887.
CAB037279.
HPA042201.
MIM142750. gene.
602822. gene.
602823. gene.
602824. gene.
602825. gene.
602826. gene.
602827. gene.
602828. gene.
602829. gene.
602830. gene.
602831. gene.
602833. gene.
615069. gene.
neXtProtNX_P62805.
PharmGKBPA29169.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2036.
HOGENOMHOG000234654.
HOVERGENHBG051878.
InParanoidP62805.
KOK11254.
OMAYEEVRVV.
OrthoDBEOG77T174.
PhylomeDBP62805.

Enzyme and pathway databases

ReactomeREACT_111183. Meiosis.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_172623. Chromatin organization.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressP62805.
BgeeP62805.
CleanExHS_HIST1H4A.
HS_HIST1H4B.
HS_HIST1H4C.
HS_HIST1H4D.
HS_HIST1H4E.
HS_HIST1H4F.
HS_HIST1H4H.
HS_HIST1H4I.
HS_HIST1H4L.
HS_HIST2H4A.
HS_HIST2H4B.
HS_HIST4H4.
GenevestigatorP62805.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR001951. Histone_H4.
IPR019809. Histone_H4_CS.
[Graphical view]
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00623. HISTONEH4.
SMARTSM00417. H4. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS00047. HISTONE_H4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP62805.
GeneWikiHIST1H4A.
HIST1H4B.
HIST1H4C.
HIST1H4D.
HIST1H4E.
HIST1H4F.
HIST1H4H.
HIST1H4I.
HIST1H4J.
HIST1H4K.
HIST1H4L.
HIST2H4A.
HIST4H4.
NextBio31093.
PROP62805.
SOURCESearch...

Entry information

Entry nameH4_HUMAN
AccessionPrimary (citable) accession number: P62805
Secondary accession number(s): A2VCL0 expand/collapse secondary AC list , P02304, P02305, Q6DRA9, Q6FGB8, Q6NWP7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM