dbPTM

H32_XENLA - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H32_XENLA
UniProt AC	P84233
Protein Name	Histone H3.2
Gene Name
Organism	Xenopus laevis (African clawed frog).
Sequence Length	136
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	MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Methylation	-----MARTKQTARK -----CCCCCHHHHH	40.95	-
3	Citrullination	-----MARTKQTARK -----CCCCCHHHHH	40.95	-
4	Phosphorylation	----MARTKQTARKS ----CCCCCHHHHHC	20.26	-
5	Other	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	-
5	Acetylation	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	-
5	Methylation	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	12138181
5	Crotonylation	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	-
5	Deamination	---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	-
9	Methylation	ARTKQTARKSTGGKA CCCCHHHHHCCCCCC	36.52	-
9	Citrullination	ARTKQTARKSTGGKA CCCCHHHHHCCCCCC	36.52	-
10	Lactoylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	-
10	Crotonylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	-
10	Methylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	12138181
10	Acetylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	-
10	Other	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	-
11	Phosphorylation	TKQTARKSTGGKAPR CCHHHHHCCCCCCCH	27.08	-
11	ADP-ribosylation	TKQTARKSTGGKAPR CCHHHHHCCCCCCCH	27.08	-
12	Phosphorylation	KQTARKSTGGKAPRK CHHHHHCCCCCCCHH	53.65	-
15	Lactoylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	-
15	Acetylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	12138181
15	Other	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	-
15	Glutarylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	-
18	Citrullination	STGGKAPRKQLATKA CCCCCCCHHHHHHHH	44.18	-
18	Methylation	STGGKAPRKQLATKA CCCCCCCHHHHHHHH	44.18	12138181
19	Lactoylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
19	Other	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
19	Glutarylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
19	Methylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
19	Butyrylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
19	Crotonylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
19	Acetylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
24	Lactoylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
24	Acetylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
24	Crotonylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
24	Methylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
24	Other	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
24	Glutarylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
24	Butyrylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
27	Citrullination	QLATKAARKSAPATG HHHHHHHHHHCCCCC	38.02	-
28	Methylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	-
28	Other	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	-
28	Acetylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	-
28	Lactoylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	-
28	Glutarylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	-
28	Crotonylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	-
29	ADP-ribosylation	ATKAARKSAPATGGV HHHHHHHHCCCCCCC	33.65	-
29	Phosphorylation	ATKAARKSAPATGGV HHHHHHHHCCCCCCC	33.65	-
37	Acetylation	APATGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	-
37	Other	APATGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	-
37	Methylation	APATGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	-
38	Methylation	PATGGVKKPHRYRPG CCCCCCCCCCCCCCC	43.58	-
42	Phosphorylation	GVKKPHRYRPGTVAL CCCCCCCCCCCCHHH	20.37	-
57	Other	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Acetylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Methylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Succinylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Lactoylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Glutarylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Crotonylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
58	Phosphorylation	EIRRYQKSTELLIRK HHHHHHHCHHHHHHH	16.16	-
65	Methylation	STELLIRKLPFQRLV CHHHHHHHCCHHHHH	54.22	-
65	Other	STELLIRKLPFQRLV CHHHHHHHCCHHHHH	54.22	-
80	Succinylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	-
80	Lactoylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	-
80	Other	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	-
80	Methylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	-
80	Glutarylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	-
80	Acetylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	-
81	Phosphorylation	EIAQDFKTDLRFQSS HHHHHHCCCHHHCHH	40.01	-
87	Phosphorylation	KTDLRFQSSAVMALQ CCCHHHCHHHHHHHH	19.97	-
108	Phosphorylation	LVGLFEDTNLCAIHA HHHHHCCCCEEEEEE	23.93	-
111	S-palmitoylation	LFEDTNLCAIHAKRV HHCCCCEEEEEEEEC	3.47	-
116	Glutarylation	NLCAIHAKRVTIMPK CEEEEEEEECEECHH	32.99	-
116	Acetylation	NLCAIHAKRVTIMPK CEEEEEEEECEECHH	32.99	-
123	Other	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	-
123	Methylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	-
123	Glutarylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	-
123	Acetylation	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	Q91829	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of H32_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 H32_XENLA !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of H32_XENLA !!

Drug and Disease Associations

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

Regulatory Network of H32_XENLA

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Involvement of histone methylation and phosphorylation in regulationof transcription by thyroid hormone receptor."; Li J., Lin Q., Yoon H.-G., Huang Z.-Q., Strahl B.D., Allis C.D.,Wong J.; Mol. Cell. Biol. 22:5688-5697(2002). Cited for: METHYLATION AT LYS-5; LYS-10 AND ARG-18, PHOSPHORYLATION AT SER-11,AND ACETYLATION AT LYS-15.	12138181 [Abstract]
Methylation
Reference	PubMed
"Involvement of histone methylation and phosphorylation in regulationof transcription by thyroid hormone receptor."; Li J., Lin Q., Yoon H.-G., Huang Z.-Q., Strahl B.D., Allis C.D.,Wong J.; Mol. Cell. Biol. 22:5688-5697(2002). Cited for: METHYLATION AT LYS-5; LYS-10 AND ARG-18, PHOSPHORYLATION AT SER-11,AND ACETYLATION AT LYS-15.	12138181 [Abstract]