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UniProtKB/Swiss-Prot entry P62806


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

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Entry information
Entry name H4_MOUSE
Primary accession number P62806
Secondary accession numbers A0AUM5 A4FUP8 A4QMY0 P02304 P02305 Q0VDL9 Q2M2Q5 Q5T006 Q6PDS7 Q811M0 Q9D0C9 Q9D6Q8
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 62)
Name and origin of the protein
Protein name Histone H4
Synonyms None
Gene names
Name: Hist1h4a
and
Name: Hist1h4b
Synonyms: H4-53
and
Name: Hist1h4c
Synonyms: H4-12
and
Name: Hist1h4d
and
Name: Hist1h4f
and
Name: Hist1h4h
and
Name: Hist1h4i
and
Name: Hist1h4j
and
Name: Hist1h4k
and
Name: Hist1h4m
and
Name: Hist2h4a
Synonyms: Hist2h4
and
Name: Hist4h4
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0022-2836(81)90426-5; PubMed=6276563 [NCBI, ExPASy, EBI, Israel, Japan]
Seiler-Tuyns A., Birnstiel M.L.;
"Structure and expression in L-cells of a cloned H4 histone gene of the mouse.";
J. Mol. Biol. 151:607-625(1981).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H4B AND HIST1H4C).
DOI=10.1093/nar/17.2.795; PubMed=2915930 [NCBI, ExPASy, EBI, Israel, Japan]
Meier V.S., Boehni R., Schuemperli D.;
"Nucleotide sequence of two mouse histone H4 genes.";
Nucleic Acids Res. 17:795-795(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H4A).
STRAIN=C57BL/6;
PubMed=8858344 [NCBI, ExPASy, EBI, Israel, Japan]
Wang Z.-F., Krasikov T., Frey M.R., Wang J., Matera A.G., Marzluff W.F.;
"Characterization of the mouse histone gene cluster on chromosome 13: 45 histone genes in three patches spread over 1Mb.";
Genome Res. 6:688-701(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv;
Franke K., Drabent B., Doenecke D.;
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H4A; HIST1H4B; HIST1H4C; HIST1H4D; HIST1H4F; HIST1H44; HIST1H4I; HIST1H4J; HIST1H4K; HIST1H4M; 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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Egg, Pancreas, and Tongue;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
The mouse genome sequencing consortium;
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Brain, Embryo, Eye, Heart, Mammary gland, and Testis;
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).
[9]
METHYLATION AT LYS-21.
DOI=10.1101/gad.300704; PubMed=15145825 [NCBI, ExPASy, EBI, Israel, Japan]
Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G., Reinberg D., Jenuwein T.;
"A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin.";
Genes Dev. 18:1251-1262(2004).
[10]
PHOSPHORYLATION AT SER-2.
DOI=10.1101/gad.1457006; PubMed=16980586 [NCBI, ExPASy, EBI, Israel, Japan]
Krishnamoorthy T., Chen X., Govin J., Cheung W.L., Dorsey J., Schindler K., Winter E., Allis C.D., Guacci V., Khochbin S., Fuller M.T., Berger S.L.;
"Phosphorylation of histone H4 Ser1 regulates sporulation in yeast and is conserved in fly and mouse spermatogenesis.";
Genes Dev. 20:2580-2592(2006).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9; LYS-13 AND LYS-17, AND MASS SPECTROMETRY.
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).
[12]
METHYLATION AT ARG-4.
DOI=10.1038/ncb1413; PubMed=16699504 [NCBI, ExPASy, EBI, Israel, Japan]
Ancelin K., Lange U.C., Hajkova P., Schneider R., Bannister A.J., Kouzarides T., Surani M.A.;
"Blimp1 associates with Prmt5 and directs histone arginine methylation in mouse germ cells.";
Nat. Cell Biol. 8:623-630(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52, AND MASS SPECTROMETRY.
TISSUE=Mast cell;
PubMed=17947660 [NCBI, ExPASy, EBI, Israel, Japan]
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling.";
J. Immunol. 179:5864-5876(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52 AND TYR-89, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1021/pr0701254; PubMed=18034455 [NCBI, ExPASy, EBI, Israel, Japan]
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASS SPECTROMETRY.
TISSUE=Brain;
Lubec G., Kang S.;
Submitted (APR-2007) to UniProtKB.
[16]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH H2A-Z; H2B AND H3.
DOI=10.1038/81971; PubMed=11101893 [NCBI, ExPASy, EBI, Israel, Japan]
Suto R.K., Clarkson M.J., Tremethick D.J., Luger K.;
"Crystal structure of a nucleosome core particle containing the variant histone H2A.Z.";
Nat. Struct. Biol. 7:1121-1124(2000).
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.
  • SUBCELLULAR LOCATION: Nucleus (By similarity).
  • PTM: Acetylation at Lys-6, Lys-9, Lys-13 and Lys-17 occurs in coding regions of the genome but not in heterochromatin (By similarity).
  • 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: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.
  • 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 (By similarity).
  • PTM: Sumoylated, which is associated with transcriptional repression (By similarity).
  • SIMILARITY: Belongs to the histone H4 family.
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
V00753; CAA24130.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13235; CAA31621.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13236; CAA31622.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U62672; AAB04766.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y12290; CAA72967.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY158956; AAO06266.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY158957; AAO06267.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY158958; AAO06268.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY158959; AAO06269.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY158960; AAO06270.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY158961; AAO06271.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY158962; AAO06272.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY158963; AAO06273.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY158964; AAO06274.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY158965; AAO06275.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY158966; AAO06276.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY158967; AAO06277.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK007642; BAB25157.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK010085; BAB26692.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK011560; BAB27698.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK139521; BAE24047.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL589651; CAI24108.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL589651; CAI24109.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590388; CAI25838.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590388; CAI25839.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590614; CAI26128.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC028550; AAH28550.3; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC052219; AAH52219.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC057955; AAH57955.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC058529; AAH58529.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC087952; AAH87952.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC092144; AAH92144.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC115446; AAI15447.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC115447; AAI15448.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC115451; AAI15452.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC115448; AAI15449.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC115449; AAI15450.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC115450; AAI15451.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC117010; AAI17011.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC117012; AAI17013.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC111813; AAI11814.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC119241; AAI19242.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC119243; AAI19244.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC119611; AAI19612.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC119612; AAI19613.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC125598; AAI25599.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC125600; AAI25601.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC132186; AAI32187.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC132212; AAI32213.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC139809; AAI39810.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC152397; AAI52398.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S03426; S03426.
S03427; S03427.
RefSeq NP_291074.1; -.
NP_694813.1; -.
NP_783583.1; -.
NP_783585.1; -.
NP_783586.1; -.
NP_783587.1; -.
NP_783588.1; -.
NP_835499.1; -.
NP_835500.1; -.
NP_835515.1; -.
NP_835582.1; -.
NP_835583.1; -.
XP_001476113.1; -.
UniGene Mm.144300
3D structure databases
PDB
1F66; X-ray; 2.60 A; B/F=1-103.[ExPASy / RCSB / EBI]
1U35; X-ray; 3.00 A; B/F=1-103.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1F66; -.
1U35; -.
ModBase P62806.
PTM databases
PhosphoSite P62806; -.
Organism-specific databases
MGI MGI:2448419; Hist1h4a.
MGI:2448420; Hist1h4b.
MGI:2448421; Hist1h4c.
MGI:2448423; Hist1h4d.
MGI:2448425; Hist1h4f.
MGI:2448427; Hist1h4h.
MGI:2448432; Hist1h4i.
MGI:2448436; Hist1h4j.
MGI:2448439; Hist1h4k.
MGI:2448441; Hist1h4m.
MGI:2140113; Hist2h4.
MGI:2448443; Hist4h4.
GeneLynx Hist1h4a; Mus musculus.
Gene expression databases
ArrayExpress P62806; -.
CleanEx MM_HIST1H4A; -.
MM_HIST1H4B; -.
MM_HIST1H4C; -.
MM_HIST1H4D; -.
MM_HIST1H4F; -.
MM_HIST1H4H; -.
MM_HIST1H4I; -.
MM_HIST1H4J; -.
MM_HIST1H4K; -.
MM_HIST1H4M; -.
MM_HIST2H4; -.
MM_HIST4H4; -.
GermOnline ENSMUSG00000060093; Mus musculus.
ENSMUSG00000060639; Mus musculus.
ENSMUSG00000060678; Mus musculus.
ENSMUSG00000060832; Mus musculus.
ENSMUSG00000060981; Mus musculus.
ENSMUSG00000061482; Mus musculus.
ENSMUSG00000064288; Mus musculus.
ENSMUSG00000068851; Mus musculus.
ENSMUSG00000069266; Mus musculus.
ENSMUSG00000069274; Mus musculus.
ENSMUSG00000069305; Mus musculus.
ENSMUSG00000069306; Mus musculus.
Family and domain databases
InterPro IPR007125; Histone_core_D.
IPR001951; Histone_H4.
Graphical view of domain structure.
PANTHER PTHR10484; Histone_H4; 1.
Pfam PF00125; Histone; 1.
Pfam graphical view of domain structure.
PRINTS PR00623; HISTONEH4.
ProDom PD001827; Histone_H4; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00417; H4; 1.
SMART graphical view of domain structure.
PROSITE PS00047; HISTONE_H4; 1.
BLOCKS P62806.
Genome annotation databases
Ensembl ENSMUSG00000060093; Mus musculus. [Contig view]
ENSMUSG00000060639; Mus musculus. [Contig view]
ENSMUSG00000060678; Mus musculus. [Contig view]
ENSMUSG00000060832; Mus musculus. [Contig view]
ENSMUSG00000060981; Mus musculus. [Contig view]
ENSMUSG00000061482; Mus musculus. [Contig view]
ENSMUSG00000064288; Mus musculus. [Contig view]
ENSMUSG00000067455; Mus musculus. [Contig view]
ENSMUSG00000068851; Mus musculus. [Contig view]
ENSMUSG00000069266; Mus musculus. [Contig view]
ENSMUSG00000069274; Mus musculus. [Contig view]
ENSMUSG00000069305; Mus musculus. [Contig view]
ENSMUSG00000069306; Mus musculus. [Contig view]
GeneID 100041230; -.
319155; -.
319156; -.
319157; -.
319158; -.
319159; -.
319160; -.
319161; -.
320332; -.
326619; -.
326620; -.
69386; -.
97122; -.
KEGG mmu:100041230; -.
mmu:319155; -.
mmu:319156; -.
mmu:319157; -.
mmu:319158; -.
mmu:319159; -.
mmu:319160; -.
mmu:319161; -.
mmu:320332; -.
mmu:326619; -.
mmu:326620; -.
mmu:69386; -.
mmu:97122; -.
Phylogenomic databases
HOGENOM P62806; -.
HOVERGEN P62806; -.
Other
SOURCE Hist1h4a; Mus musculus.
ProtoNet P62806.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Chromosomal protein; Citrullination; DNA-binding; Methylation; Nucleosome core; Nucleus; Phosphoprotein; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   103  102     Histone H4. PRO_0000158329
DNA_BIND   17    21  5      
MOD_RES   2     2        N-acetylserine (By similarity). 
MOD_RES   2     2        Phosphoserine. 
MOD_RES   4     4        Citrulline; alternate (By similarity). 
MOD_RES   4     4        Omega-N-methylarginine; by PRMT1; alternate (By similarity). 
MOD_RES   4     4        Symmetric dimethylarginine; by PRMT5; alternate. 
MOD_RES   6     6        N6-acetyllysine. 
MOD_RES   9     9        N6-acetyllysine. 
MOD_RES   13    13        N6-acetyllysine. 
MOD_RES   17    17        N6-acetyllysine. 
MOD_RES   21    21        N6,N6,N6-trimethyllysine; alternate. 
MOD_RES   21    21        N6,N6-dimethyllysine; alternate (By similarity). 
MOD_RES   21    21        N6-methyllysine; alternate (By similarity). 
MOD_RES   48    48        Phosphoserine. 
MOD_RES   52    52        Phosphotyrosine. 
MOD_RES   89    89        Phosphotyrosine. 
CONFLICT   34    34        A -> V (in Ref. 6; BAB26692). 
CONFLICT   80    80        K -> E (in Ref. 6; BAB27698). 
CONFLICT   90    90        A -> R (in Ref. 2; CAA31622). 
HELIX   26    29  4      
HELIX   32    41  10      
HELIX   51    76  26      
STRAND   80    82  3      
HELIX   84    93  10      
STRAND   98   101  4      
Sequence information
Length: 103 AA [This is the length of the unprocessed precursor] Molecular weight: 11367 Da [This is the MW of the unprocessed precursor] CRC64: A9E5DFD3F8B97598 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK 

        70         80         90        100 
VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG 

P62806 in FASTA format

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