Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Histone H4  

UniProtKB / Swiss-Prot ID :  H4_MOUSE

Gene Name (Synonyms) : 
Hist1h4a
Hist1h4b, H4-53
Hist1h4c, H4-12
Hist1h4d
Hist1h4f
Hist1h4h
Hist1h4i
Hist1h4j
Hist1h4k
Hist1h4m
Hist2h4a, Hist2h4
Hist4h4  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Nucleus (By similarity). Chromosome (By similarity). 

Protein 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. 

Protein Sequence MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDA...
Predicted Secondary Structure CCCCCCCCCHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2Phosphoserine.---MSGRGK
---CCCCCC
36.88UniProtKB
Link-
4Asymmetric dimethylarginine; by PRMT1;alternate.-MSGRGKGG
-CCCCCCCC
36.02UniProtKB
Link-
4N2,N2-dimethylarginine-MSGRGKGG
-CCCCCCCC
36.02Phosphositeplus
Link-
4Symmetric dimethylarginine; by PRMT5 andPRMT7; alternate.-MSGRGKGG
-CCCCCCCC
36.02UniProtKB
Link-
6N6-acetyllysineSGRGKGGKG
CCCCCCCCH
64.23Phosphositeplus
Link-
6N6-acetyllysineSGRGKGGKG
CCCCCCCCH
64.23SysPTM
Link-
6N6-acetyllysine.SGRGKGGKG
CCCCCCCCH
64.23UniProtKB
Link-
9N6-acetyllysineGKGGKGLGK
CCCCCHHHH
60.68Phosphositeplus
Link-
9N6-acetyllysineGKGGKGLGK
CCCCCHHHH
60.68SysPTM
Link-
9N6-acetyllysine.GKGGKGLGK
CCCCCHHHH
60.68UniProtKB
Link-
13N6-acetyllysineKGLGKGGAK
CHHHHHHHH
60.25Phosphositeplus
Link-
13N6-acetyllysineKGLGKGGAK
CHHHHHHHH
60.25SysPTM
Link-
13N6-acetyllysine.KGLGKGGAK
CHHHHHHHH
60.25UniProtKB
Link-
17N6,N6,N6-trimethyllysineKGGAKRHRK
HHHHHHHHH
52.60Phosphositeplus
Link-
17N6-acetyllysineKGGAKRHRK
HHHHHHHHH
52.60Phosphositeplus
Link-
17N6-acetyllysineKGGAKRHRK
HHHHHHHHH
52.60SysPTM
Link-
17N6-acetyllysine.KGGAKRHRK
HHHHHHHHH
52.60UniProtKB
Link-
21N6,N6,N6-trimethyllysineKRHRKVLRD
HHHHHHHHH
39.22Phosphositeplus
Link-
21N6,N6,N6-trimethyllysine; alternate.KRHRKVLRD
HHHHHHHHH
39.22UniProtKB
Link-
21N6,N6-dimethyllysineKRHRKVLRD
HHHHHHHHH
39.22Phosphositeplus
Link-
21N6-acetyllysineKRHRKVLRD
HHHHHHHHH
39.22Phosphositeplus
Link-
21N6-methyllysineKRHRKVLRD
HHHHHHHHH
39.22Phosphositeplus
Link-
245-methylarginineRKVLRDNIQ
HHHHHHHHH
37.61Phosphositeplus
Link
24N2,N2-dimethylarginineRKVLRDNIQ
HHHHHHHHH
37.61Phosphositeplus
Link
32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QGITKPAIR
HCCCHHHHH
30.45Phosphositeplus
Link
365-methylarginineKPAIRRLAR
HHHHHHHHH
29.66Phosphositeplus
Link
48PhosphoserineVKRISGLIY
HHHHHHHHH
31.42Phosphositeplus
Link
48PhosphoserineVKRISGLIY
HHHHHHHHH
31.42SysPTM
Link
52PhosphotyrosineSGLIYEETR
HHHHHHHHH
16.86Phosphositeplus
Link
52PhosphotyrosineSGLIYEETR
HHHHHHHHH
16.86SysPTM
Link
52Phosphotyrosine.SGLIYEETR
HHHHHHHHH
16.86UniProtKB
Link
78Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TEHAKRKTV
CCCHHHHHH
57.23Phosphositeplus
Link
81PhosphothreonineAKRKTVTAM
HHHHHHHHH
27.41Phosphositeplus
Link
89PhosphotyrosineMDVVYALKR
HHHHHHHHH
13.18Phosphositeplus
Link
89Phosphotyrosine.MDVVYALKR
HHHHHHHHH
13.18UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
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.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9; LYS-13 AND LYS-17,AND MASS SPECTROMETRY.
Methylation
ReferencePubMed
"Blimp1 associates with Prmt5 and directs histone arginine methylationin mouse germ cells.";
Ancelin K., Lange U.C., Hajkova P., Schneider R., Bannister A.J.,Kouzarides T., Surani M.A.;
Nat. Cell Biol. 8:623-630(2006).
Cited for: METHYLATION AT ARG-4.
"A silencing pathway to induce H3-K9 and H4-K20 trimethylation atconstitutive heterochromatin.";
Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G.,Reinberg D., Jenuwein T.;
Genes Dev. 18:1251-1262(2004).
Cited for: METHYLATION AT LYS-21.
Phosphorylation
ReferencePubMed
"Phosphorylation of histone H4 Ser1 regulates sporulation in yeast andis conserved in fly and mouse spermatogenesis.";
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.;
Genes Dev. 20:2580-2592(2006).
Cited for: PHOSPHORYLATION AT SER-2.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52, AND MASSSPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52 AND TYR-89, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures