H331_CAEEL - dbPTM
H331_CAEEL - PTM Information in dbPTM
Basic Information of Protein
UniProt ID H331_CAEEL
UniProt AC Q10453
Protein Name Histone H3.3 type 1
Gene Name his-71
Organism Caenorhabditis elegans.
Sequence Length 136
Subcellular Localization Nucleus. Chromosome.
Protein Description Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. 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 MARTKQTARKSTGGKAPRKQLATKAARKSAPTTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
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
5Acetylation---MARTKQTARKST
---CCCCCHHHHHCC
39.85-
5Methylation---MARTKQTARKST
---CCCCCHHHHHCC
39.85-
5"N6,N6,N6-trimethyllysine"---MARTKQTARKST
---CCCCCHHHHHCC
39.85-
10MethylationRTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.32-
10AcetylationRTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.32-
10"N6,N6,N6-trimethyllysine"RTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.32-
11PhosphorylationTKQTARKSTGGKAPR
CCHHHHHCCCCCCCH
27.0814702046
12PhosphorylationKQTARKSTGGKAPRK
CHHHHHCCCCCCCHH
53.6519530675
15AcetylationARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.47-
24AcetylationPRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.15-
28"N6,N6,N6-trimethyllysine"LATKAARKSAPTTGG
HHHHHHHHHCCCCCC
46.36-
28MethylationLATKAARKSAPTTGG
HHHHHHHHHCCCCCC
46.36-
29PhosphorylationATKAARKSAPTTGGV
HHHHHHHHCCCCCCC
33.65-
37"N6,N6,N6-trimethyllysine"APTTGGVKKPHRYRP
CCCCCCCCCCCCCCC
64.95-
37MethylationAPTTGGVKKPHRYRP
CCCCCCCCCCCCCCC
64.95-
58PhosphorylationEIRRYQKSTELLIRK
HHHHHHHCHHHHHHH
16.1619530675
59PhosphorylationIRRYQKSTELLIRKL
HHHHHHCHHHHHHHC
37.3719530675
80MethylationREIAQDFKTDLRFQS
HHHHHHHHHCHHHHH
49.79-

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

Oops, there are no upstream regulatory protein records of H331_CAEEL !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of H331_CAEEL !!

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 H331_CAEEL !!

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

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of H331_CAEEL

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Related Literatures of Post-Translational Modification

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