H33_RAT - dbPTM
H33_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID H33_RAT
UniProt AC P84245
Protein Name Histone H3.3
Gene Name H3f3b
Organism Rattus norvegicus (Rat).
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 MARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
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
3Asymmetric dimethylarginine-----MARTKQTARK
-----CCCCCHHHHH
40.95-
3Citrullination-----MARTKQTARK
-----CCCCCHHHHH
40.95-
3Methylation-----MARTKQTARK
-----CCCCCHHHHH
40.95-
4Phosphorylation----MARTKQTARKS
----CCCCCHHHHHC
20.2611498542
5Allysine---MARTKQTARKST
---CCCCCHHHHHCC
39.85-
5Acetylation---MARTKQTARKST
---CCCCCHHHHHCC
39.851001435
5Crotonylation---MARTKQTARKST
---CCCCCHHHHHCC
39.85-
5Deamination---MARTKQTARKST
---CCCCCHHHHHCC
39.85-
5Methylation---MARTKQTARKST
---CCCCCHHHHHCC
39.85-
5Other---MARTKQTARKST
---CCCCCHHHHHCC
39.85-
6Formation of an isopeptide bond--MARTKQTARKSTG
--CCCCCHHHHHCCC
39.5232273471
6Serotonylation--MARTKQTARKSTG
--CCCCCHHHHHCCC
39.52-
7Phosphorylation-MARTKQTARKSTGG
-CCCCCHHHHHCCCC
29.95-
9CitrullinationARTKQTARKSTGGKA
CCCCHHHHHCCCCCC
36.52-
9CitrullinationARTKQTARKSTGGKA
CCCCHHHHHCCCCCC
36.52-
9MethylationARTKQTARKSTGGKA
CCCCHHHHHCCCCCC
36.52-
10"N6,N6,N6-trimethyllysine"RTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.32-
10AcetylationRTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.3225786129
10CrotonylationRTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.32-
10LactoylationRTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.32-
10MethylationRTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.32-
10OtherRTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.32-
11ADP-ribosylationTKQTARKSTGGKAPR
CCHHHHHCCCCCCCH
27.08-
11PhosphorylationTKQTARKSTGGKAPR
CCHHHHHCCCCCCCH
27.0810911986
12PhosphorylationKQTARKSTGGKAPRK
CHHHHHCCCCCCCHH
53.6512560483
15AcetylationARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.4725786129
15GlutarylationARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.47-
15LactoylationARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.47-
15OtherARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.47-
15SuccinylationARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.47-
18Asymmetric dimethylarginineSTGGKAPRKQLATKA
CCCCCCCHHHHHHHH
44.18-
18CitrullinationSTGGKAPRKQLATKA
CCCCCCCHHHHHHHH
44.18-
18MethylationSTGGKAPRKQLATKA
CCCCCCCHHHHHHHH
44.18-
19N6-crotonyl-L-lysineTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.91-
19AcetylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.9125786129
19ButyrylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.91-
19CrotonylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.91-
19GlutarylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.91-
19LactoylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.91-
19MethylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.91-
19OtherTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.91-
24N6-crotonyl-L-lysinePRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.15-
24AcetylationPRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.1525786129
24ButyrylationPRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.15-
24CrotonylationPRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.15-
24GlutarylationPRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.15-
24LactoylationPRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.15-
24MethylationPRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.15-
24OtherPRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.15-
27CitrullinationQLATKAARKSAPSTG
HHHHHHHHHHCCCCC
38.02-
27CitrullinationQLATKAARKSAPSTG
HHHHHHHHHHCCCCC
38.02-
28"N6,N6,N6-trimethyllysine"LATKAARKSAPSTGG
HHHHHHHHHCCCCCC
46.36-
28AcetylationLATKAARKSAPSTGG
HHHHHHHHHCCCCCC
46.3625786129
28CrotonylationLATKAARKSAPSTGG
HHHHHHHHHCCCCCC
46.36-
28GlutarylationLATKAARKSAPSTGG
HHHHHHHHHCCCCCC
46.36-
28LactoylationLATKAARKSAPSTGG
HHHHHHHHHCCCCCC
46.36-
28MethylationLATKAARKSAPSTGG
HHHHHHHHHCCCCCC
46.36-
28OtherLATKAARKSAPSTGG
HHHHHHHHHCCCCCC
46.36-
29ADP-ribosylationATKAARKSAPSTGGV
HHHHHHHHCCCCCCC
39.60-
29PhosphorylationATKAARKSAPSTGGV
HHHHHHHHCCCCCCC
39.6028432305
32PhosphorylationAARKSAPSTGGVKKP
HHHHHCCCCCCCCCC
39.13-
37"N6,N6,N6-trimethyllysine"APSTGGVKKPHRYRP
CCCCCCCCCCCCCCC
64.95-
37AcetylationAPSTGGVKKPHRYRP
CCCCCCCCCCCCCCC
64.9519343714
37MethylationAPSTGGVKKPHRYRP
CCCCCCCCCCCCCCC
64.95-
37OtherAPSTGGVKKPHRYRP
CCCCCCCCCCCCCCC
64.95-
38AcetylationPSTGGVKKPHRYRPG
CCCCCCCCCCCCCCC
43.5825786129
38MethylationPSTGGVKKPHRYRPG
CCCCCCCCCCCCCCC
43.58-
42PhosphorylationGVKKPHRYRPGTVAL
CCCCCCCCCCCCHHH
20.37-
46PhosphorylationPHRYRPGTVALREIR
CCCCCCCCHHHHHHH
12.8023984901
57"N6,N6,N6-trimethyllysine"REIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
57AcetylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.8722902405
57CrotonylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
57GlutarylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
57LactoylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
57MethylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
57OtherREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
57SuccinylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
58PhosphorylationEIRRYQKSTELLIRK
HHHHHHHCHHHHHHH
16.1627097102
59PhosphorylationIRRYQKSTELLIRKL
HHHHHHCHHHHHHHC
37.3727097102
65MethylationSTELLIRKLPFQRLV
CHHHHHHHCCHHHHH
54.22-
65OtherSTELLIRKLPFQRLV
CHHHHHHHCCHHHHH
54.22-
65SuccinylationSTELLIRKLPFQRLV
CHHHHHHHCCHHHHH
54.2226843850
80"N6,N6,N6-trimethyllysine"REIAQDFKTDLRFQS
HHHHHHHHHCHHHHH
49.79-
80AcetylationREIAQDFKTDLRFQS
HHHHHHHHHCHHHHH
49.7922902405
80GlutarylationREIAQDFKTDLRFQS
HHHHHHHHHCHHHHH
49.79-
80LactoylationREIAQDFKTDLRFQS
HHHHHHHHHCHHHHH
49.79-
80MethylationREIAQDFKTDLRFQS
HHHHHHHHHCHHHHH
49.79-
80OtherREIAQDFKTDLRFQS
HHHHHHHHHCHHHHH
49.79-
80SuccinylationREIAQDFKTDLRFQS
HHHHHHHHHCHHHHH
49.79-
80UbiquitinationREIAQDFKTDLRFQS
HHHHHHHHHCHHHHH
49.79-
81PhosphorylationEIAQDFKTDLRFQSA
HHHHHHHHCHHHHHH
40.0129779826
87PhosphorylationKTDLRFQSAAIGALQ
HHCHHHHHHHHHHHH
19.5616641100
97PhosphorylationIGALQEASEAYLVGL
HHHHHHHHHHHHHHH
23.2317683130
108PhosphorylationLVGLFEDTNLCAIHA
HHHHHCCCCEEEEEE
23.93-
116AcetylationNLCAIHAKRVTIMPK
CEEEEEEEECEECHH
32.9925786129
116GlutarylationNLCAIHAKRVTIMPK
CEEEEEEEECEECHH
32.99-
123AcetylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.51-
123GlutarylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.51-
123MethylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.51-
123OtherKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.51-
123SuccinylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.51-

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
4TPhosphorylationKinaseHASPIN-Uniprot
7TPhosphorylationKinasePKC-Uniprot
11SPhosphorylationKinaseRPS6KA5A0A0G2K366
GPS
11SPhosphorylationKinaseAURKBO55099
GPS
11SPhosphorylationKinaseRPS6KA3D3Z8E0
GPS
11SPhosphorylationKinaseRPS6KA4D3ZSB7
GPS
11SPhosphorylationKinaseAURKCD4AD76
GPS
11SPhosphorylationKinasePKA-FAMILY-GPS
11SPhosphorylationKinaseALTERNATE-Uniprot
12TPhosphorylationKinaseDAPK3O88764
GPS
12TPhosphorylationKinasePKC-FAMILY-GPS
12TPhosphorylationKinasePKC-Uniprot
29SPhosphorylationKinaseMAPK8P49185
GPS
29SPhosphorylationKinaseMAPK9P49186
GPS
29SPhosphorylationKinaseALTERNATE-Uniprot
46TPhosphorylationKinaseDYRK1AQ63470
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
3RMethylation

-
4TPhosphorylation

-
5Kubiquitylation

-
5KAcetylation

-
5KMethylation

-
5KMethylation

-
5KMethylation

-
5KMethylation

-
5KPhosphorylation

-
5KMethylation

-
5KMethylation

-
7TPhosphorylation

-
7TMethylation

-
9RMethylation

-
9RMethylation

-
9RMethylation

-
9RCitrullination

-
9RAcetylation

-
10KPhosphorylation

-
10KPhosphorylation

-
10KPhosphorylation

-
10KMethylation

-
10KMethylation

-
10KPhosphorylation

-
10KAcetylation

-
10KAcetylation

-
10KAcetylation

-
10KAcetylation

-
10KMethylation

-
10KMethylation

-
10KMethylation

-
10KMethylation

-
11SAcetylation

12560483
11SAcetylation

12560483
11SAcetylation

12560483
11SMethylation

12560483
11SMethylation

12560483
11SPhosphorylation

12560483
11SPhosphorylation

12560483
11SPhosphorylation

12560483
11SPhosphorylation

12560483
11SPhosphorylation

12560483
11SPhosphorylation

12560483
11SPhosphorylation

12560483
12TPhosphorylation

12560483
12TMethylation

12560483
12TPhosphorylation

12560483
18RCitrullination

-
18RAcetylation

-
18RMethylation

-
18RMethylation

-
18RMethylation

-
19KMethylation

-
19KAcetylation

-
24KMethylation

-
24KAcetylation

-
28KMethylation

-
28KMethylation

-
29SPhosphorylation

-
32SPhosphorylation

-
37KMethylation

19343714
57KMethylation

-
80KSuccinylation

-
80Kubiquitylation

-
80KMethylation

-
80KMethylation

-
80KMethylation

-
120KMethylation

-
120Kubiquitylation

-
123KAcetylation

-
123KSuccinylation

-

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 H33_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H33_RATH3f3bphysical
22371606

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of H33_RAT

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Mass spectrometry-compatible silver staining of histones resolved onacetic acid-urea-Triton PAGE.";
Pramod K.S., Bharat K., Sanjay G.;
Proteomics 9:2589-2592(2009).
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, AND ACETYLATION AT LYS-37.
Phosphorylation
ReferencePubMed
"Novel mitosis-specific phosphorylation of histone H3 at Thr11mediated by Dlk/ZIP kinase.";
Preuss U., Landsberg G., Scheidtmann K.H.;
Nucleic Acids Res. 31:878-885(2003).
Cited for: PHOSPHORYLATION AT SER-11 AND THR-12.

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