H4_XENLA - dbPTM
H4_XENLA - PTM Information in dbPTM
Basic Information of Protein
UniProt ID H4_XENLA
UniProt AC P62799
Protein Name Histone H4
Gene Name
Organism Xenopus laevis (African clawed frog).
Sequence Length 103
Subcellular Localization Nucleus. Chromosome.
Protein Description 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 MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSGRGKGGK
------CCCCCCCCC
36.88-
2Acetylation------MSGRGKGGK
------CCCCCCCCC
36.88-
4Citrullination----MSGRGKGGKGL
----CCCCCCCCCCC
36.02-
4Methylation----MSGRGKGGKGL
----CCCCCCCCCCC
36.02-
6Glutarylation--MSGRGKGGKGLGK
--CCCCCCCCCCCCC
64.23-
6Acetylation--MSGRGKGGKGLGK
--CCCCCCCCCCCCC
64.23-
6Other--MSGRGKGGKGLGK
--CCCCCCCCCCCCC
64.23-
6Butyrylation--MSGRGKGGKGLGK
--CCCCCCCCCCCCC
64.23-
6Lactoylation--MSGRGKGGKGLGK
--CCCCCCCCCCCCC
64.23-
9PropionylationSGRGKGGKGLGKGGA
CCCCCCCCCCCCCHH
60.68-
9AcetylationSGRGKGGKGLGKGGA
CCCCCCCCCCCCCHH
60.68-
9LactoylationSGRGKGGKGLGKGGA
CCCCCCCCCCCCCHH
60.68-
9OtherSGRGKGGKGLGKGGA
CCCCCCCCCCCCCHH
60.68-
9ButyrylationSGRGKGGKGLGKGGA
CCCCCCCCCCCCCHH
60.68-
13GlutarylationKGGKGLGKGGAKRHR
CCCCCCCCCHHHHHH
60.25-
13LactoylationKGGKGLGKGGAKRHR
CCCCCCCCCHHHHHH
60.25-
13MethylationKGGKGLGKGGAKRHR
CCCCCCCCCHHHHHH
60.25-
13ButyrylationKGGKGLGKGGAKRHR
CCCCCCCCCHHHHHH
60.25-
13OtherKGGKGLGKGGAKRHR
CCCCCCCCCHHHHHH
60.25-
13AcetylationKGGKGLGKGGAKRHR
CCCCCCCCCHHHHHH
60.25-
17OtherGLGKGGAKRHRKVLR
CCCCCHHHHHHHHHH
52.60-
17LactoylationGLGKGGAKRHRKVLR
CCCCCHHHHHHHHHH
52.60-
17PropionylationGLGKGGAKRHRKVLR
CCCCCHHHHHHHHHH
52.60-
17AcetylationGLGKGGAKRHRKVLR
CCCCCHHHHHHHHHH
52.60-
17ButyrylationGLGKGGAKRHRKVLR
CCCCCHHHHHHHHHH
52.60-
21MethylationGGAKRHRKVLRDNIQ
CHHHHHHHHHHHHCC
39.22-
32PropionylationDNIQGITKPAIRRLA
HHCCCCCHHHHHHHH
30.45-
32OtherDNIQGITKPAIRRLA
HHCCCCCHHHHHHHH
30.45-
32GlutarylationDNIQGITKPAIRRLA
HHCCCCCHHHHHHHH
30.45-
32SuccinylationDNIQGITKPAIRRLA
HHCCCCCHHHHHHHH
30.45-
32LactoylationDNIQGITKPAIRRLA
HHCCCCCHHHHHHHH
30.45-
32ButyrylationDNIQGITKPAIRRLA
HHCCCCCHHHHHHHH
30.45-
32AcetylationDNIQGITKPAIRRLA
HHCCCCCHHHHHHHH
30.45-
45OtherLARRGGVKRISGLIY
HHHCCCCCEEECCCH
47.49-
45ButyrylationLARRGGVKRISGLIY
HHHCCCCCEEECCCH
47.49-
45PropionylationLARRGGVKRISGLIY
HHHCCCCCEEECCCH
47.49-
48PhosphorylationRGGVKRISGLIYEET
CCCCCEEECCCHHHH
31.42-
52PhosphorylationKRISGLIYEETRGVL
CEEECCCHHHHHHHH
16.86-
60OtherEETRGVLKVFLENVI
HHHHHHHHHHHHHHH
28.65-
60AcetylationEETRGVLKVFLENVI
HHHHHHHHHHHHHHH
28.65-
60GlutarylationEETRGVLKVFLENVI
HHHHHHHHHHHHHHH
28.65-
78ButyrylationVTYTEHAKRKTVTAM
HHCCHHHCCCEECHH
57.23-
78OtherVTYTEHAKRKTVTAM
HHCCHHHCCCEECHH
57.23-
78LactoylationVTYTEHAKRKTVTAM
HHCCHHHCCCEECHH
57.23-
78GlutarylationVTYTEHAKRKTVTAM
HHCCHHHCCCEECHH
57.23-
78SuccinylationVTYTEHAKRKTVTAM
HHCCHHHCCCEECHH
57.23-
78PropionylationVTYTEHAKRKTVTAM
HHCCHHHCCCEECHH
57.23-
80PropionylationYTEHAKRKTVTAMDV
CCHHHCCCEECHHHH
46.79-
80AcetylationYTEHAKRKTVTAMDV
CCHHHCCCEECHHHH
46.79-
80OtherYTEHAKRKTVTAMDV
CCHHHCCCEECHHHH
46.79-
80ButyrylationYTEHAKRKTVTAMDV
CCHHHCCCEECHHHH
46.79-
80GlutarylationYTEHAKRKTVTAMDV
CCHHHCCCEECHHHH
46.79-
89PhosphorylationVTAMDVVYALKRQGR
ECHHHHHHHHHHCCC
13.18-
92AcetylationMDVVYALKRQGRTLY
HHHHHHHHHCCCCEE
34.21-
92SuccinylationMDVVYALKRQGRTLY
HHHHHHHHHCCCCEE
34.21-
92PropionylationMDVVYALKRQGRTLY
HHHHHHHHHCCCCEE
34.21-
92OtherMDVVYALKRQGRTLY
HHHHHHHHHCCCCEE
34.21-
92LactoylationMDVVYALKRQGRTLY
HHHHHHHHHCCCCEE
34.21-
92GlutarylationMDVVYALKRQGRTLY
HHHHHHHHHCCCCEE
34.21-
92ButyrylationMDVVYALKRQGRTLY
HHHHHHHHHCCCCEE
34.21-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
48SPhosphorylationKinasePAK2-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of H4_XENLA !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of H4_XENLA !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H4_XENLAhist1h4aphysical
23178455

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of H4_XENLA

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Related Literatures of Post-Translational Modification

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