dbPTM

H2A4_CHICK - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H2A4_CHICK
UniProt AC	P02263
Protein Name	Histone H2A-IV
Gene Name
Organism	Gallus gallus (Chicken).
Sequence Length	129
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	MSGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTDSHKAKAK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSGRGKQGG ------CCCCCCCCH	36.88	-
2	Acetylation	------MSGRGKQGG ------CCCCCCCCH	36.88	667168
6	Other	--MSGRGKQGGKARA --CCCCCCCCHHHHH	44.39	-
6	Acetylation	--MSGRGKQGGKARA --CCCCCCCCHHHHH	44.39	12450536
10	Succinylation	GRGKQGGKARAKAKS CCCCCCHHHHHHHHH	41.34	-
10	Acetylation	GRGKQGGKARAKAKS CCCCCCHHHHHHHHH	41.34	12450536
10	Other	GRGKQGGKARAKAKS CCCCCCHHHHHHHHH	41.34	-
10	Lactoylation	GRGKQGGKARAKAKS CCCCCCHHHHHHHHH	41.34	-
37	Other	RVHRLLRKGNYAERV HHHHHHHCCCHHHHC	52.02	-
75	Other	GNAARDNKKTRIIPR CHHHHCCCCCCEEHH	60.87	-
76	Other	NAARDNKKTRIIPRH HHHHCCCCCCEEHHH	49.65	-
96	Succinylation	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	-
96	Glutarylation	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	-
96	Other	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	-
100	Glutarylation	ELNKLLGKVTIAQGG HHHHHHCCEEECCCC	35.85	-
105	Methylation	LGKVTIAQGGVLPNI HCCEEECCCCCCCCE	45.37	-
119	Other	IQAVLLPKKTDSHKA EEEEECCCCCCHHHH	69.17	-
119	Glutarylation	IQAVLLPKKTDSHKA EEEEECCCCCCHHHH	69.17	-
120	Glutarylation	QAVLLPKKTDSHKAK EEEECCCCCCHHHHC	56.47	-
120	Ubiquitination	QAVLLPKKTDSHKAK EEEECCCCCCHHHHC	56.47	2713375

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 H2A4_CHICK !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of H2A4_CHICK !!

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 H2A4_CHICK !!

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 H2A4_CHICK

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Primary structure of chicken erythrocyte histone H2A."; Laine B., Kmiecik D., Sautiere P., Biserte G.; Biochimie 60:147-150(1978). Cited for: PROTEIN SEQUENCE OF 2-129.	667168 [Abstract]
"Analysis of core histones by liquid chromatography-mass spectrometryand peptide mapping."; Zhang K., Tang H.; J. Chromatogr. B 783:173-179(2003). Cited for: PROTEIN SEQUENCE OF 5-12, ACETYLATION AT LYS-6 AND LYS-10, AND MASSSPECTROMETRY.	12450536 [Abstract]