H33_CHICK - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H33_CHICK
• UniProt AC: P84247
• Protein Name: Histone H3.3
• Gene Name: H3-IX
• Organism: Gallus gallus (Chicken).
• 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
3	Asymmetric dimethylarginine	-----MARTKQTARK -----CCCCCHHHHH	40.95	-
3	Methylation	-----MARTKQTARK -----CCCCCHHHHH	40.95	-
4	Phosphorylation	----MARTKQTARKS ----CCCCCHHHHHC	20.26	-
5	Methylation	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	-
5	Other	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	-
5	Allysine	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	-
5	Deamination	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	-
5	Acetylation	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	-
6	Serotonylation	--MARTKQTARKSTG --CCCCCHHHHHCCC	39.52	-
6	Formation of an isopeptide bond	--MARTKQTARKSTG --CCCCCHHHHHCCC	39.52	-
7	Phosphorylation	-MARTKQTARKSTGG -CCCCCHHHHHCCCC	29.95	-
10	Lactoylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	-
10	Other	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	-
10	Methylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	-
11	ADP-ribosylation	TKQTARKSTGGKAPR CCHHHHHCCCCCCCH	27.08	-
11	Phosphorylation	TKQTARKSTGGKAPR CCHHHHHCCCCCCCH	27.08	-
12	Phosphorylation	KQTARKSTGGKAPRK CHHHHHCCCCCCCHH	53.65	-
15	Other	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	-
15	Lactoylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	-
15	Glutarylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	-
15	Acetylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	-
18	Asymmetric dimethylarginine	STGGKAPRKQLATKA CCCCCCCHHHHHHHH	44.18	-
18	Methylation	STGGKAPRKQLATKA CCCCCCCHHHHHHHH	44.18	-
19	Methylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
19	Acetylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
19	Other	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
19	Lactoylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
19	Glutarylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
19	Butyrylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
24	Glutarylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
24	Lactoylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
24	Other	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
24	Acetylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
24	Butyrylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
28	Lactoylation	LATKAARKSAPSTGG HHHHHHHHHCCCCCC	46.36	-
28	Other	LATKAARKSAPSTGG HHHHHHHHHCCCCCC	46.36	-
28	Glutarylation	LATKAARKSAPSTGG HHHHHHHHHCCCCCC	46.36	-
28	Methylation	LATKAARKSAPSTGG HHHHHHHHHCCCCCC	46.36	-
28	Acetylation	LATKAARKSAPSTGG HHHHHHHHHCCCCCC	46.36	-
29	Phosphorylation	ATKAARKSAPSTGGV HHHHHHHHCCCCCCC	39.60	-
29	ADP-ribosylation	ATKAARKSAPSTGGV HHHHHHHHCCCCCCC	39.60	-
37	Acetylation	APSTGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	-
37	Other	APSTGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	-
37	Methylation	APSTGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	-
42	Phosphorylation	GVKKPHRYRPGTVAL CCCCCCCCCCCCHHH	20.37	-
57	Succinylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Other	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Lactoylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Glutarylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
58	Phosphorylation	EIRRYQKSTELLIRK HHHHHHHCHHHHHHH	16.16	-
65	Other	STELLIRKLPFQRLV CHHHHHHHCCHHHHH	54.22	-
65	Methylation	STELLIRKLPFQRLV CHHHHHHHCCHHHHH	54.22	-
80	Other	REIAQDFKTDLRFQS HHHHHHHHHCHHHHH	49.79	-
80	Succinylation	REIAQDFKTDLRFQS HHHHHHHHHCHHHHH	49.79	-
80	Glutarylation	REIAQDFKTDLRFQS HHHHHHHHHCHHHHH	49.79	-
80	Lactoylation	REIAQDFKTDLRFQS HHHHHHHHHCHHHHH	49.79	-
80	Methylation	REIAQDFKTDLRFQS HHHHHHHHHCHHHHH	49.79	-
81	Phosphorylation	EIAQDFKTDLRFQSA HHHHHHHHCHHHHHH	40.01	-
116	Glutarylation	NLCAIHAKRVTIMPK CEEEEEEEECEECHH	32.99	-
116	Acetylation	NLCAIHAKRVTIMPK CEEEEEEEECEECHH	32.99	-
123	Glutarylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	-
123	Other	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	-
123	Acetylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	-
123	Methylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	-
123	Succinylation	KRVTIMPKDIQLARR 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
4	T	Phosphorylation	Kinase	HASPIN	-	Uniprot
7	T	Phosphorylation	Kinase	PKC	-	Uniprot
11	S	Phosphorylation	Kinase	ALTERNATE	-	Uniprot
12	T	Phosphorylation	Kinase	PKC	-	Uniprot
29	S	Phosphorylation	Kinase	ALTERNATE	-	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	RAG1	P24271	PMID:22199232

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of H33_CHICK !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of H33_CHICK !!

Protein-Protein Interaction

Oops, there are no PPI records of H33_CHICK !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.