H2AV_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H2AV_HUMAN
• UniProt AC: Q71UI9
• Protein Name: Histone H2A.V
• Gene Name: H2AFV
• Organism: Homo sapiens (Human).
• Sequence Length: 128
• Subcellular Localization: Nucleus. Chromosome.
• Protein Description: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division (By similarity)..
• Protein Sequence: MAGGKAGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTA

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
5	Ubiquitination	---MAGGKAGKDSGK ---CCCCCCCCCCHH	53.71	-
5	Acetylation	---MAGGKAGKDSGK ---CCCCCCCCCCHH	53.71	25825284
8	Acetylation	MAGGKAGKDSGKAKA CCCCCCCCCCHHHHH	54.29	21466224
8	Ubiquitination	MAGGKAGKDSGKAKA CCCCCCCCCCHHHHH	54.29	24816145
10	Phosphorylation	GGKAGKDSGKAKAKA CCCCCCCCHHHHHHH	45.75	29759185
12	Acetylation	KAGKDSGKAKAKAVS CCCCCCHHHHHHHHH	51.14	21466224
12	Lactoylation	KAGKDSGKAKAKAVS CCCCCCHHHHHHHHH	51.14	-
14	Acetylation	GKDSGKAKAKAVSRS CCCCHHHHHHHHHHH	54.64	21466224
14	Lactoylation	GKDSGKAKAKAVSRS CCCCHHHHHHHHHHH	54.64	-
16	Ubiquitination	DSGKAKAKAVSRSQR CCHHHHHHHHHHHHH	48.92	27667366
23	Methylation	KAVSRSQRAGLQFPV HHHHHHHHHCCCCCH	31.69	-
32	Methylation	GLQFPVGRIHRHLKT CCCCCHHHHHHHCCC	23.05	-
61	Phosphorylation	YSAAILEYLTAEVLE HHHHHHHHHHHHHHH	13.10	22817900
64	Ubiquitination	AILEYLTAEVLELAG HHHHHHHHHHHHHCC	11.42	21963094
75	Ubiquitination	ELAGNASKDLKVKRI HHCCCCCCCCCEEEE	65.75	-
76	Ubiquitination	LAGNASKDLKVKRIT HCCCCCCCCCEEEEC	49.58	21963094
78	Ubiquitination	GNASKDLKVKRITPR CCCCCCCCEEEECHH	56.71	21890473
78	Ubiquitination	GNASKDLKVKRITPR CCCCCCCCEEEECHH	56.71	23000965
83	Ubiquitination	DLKVKRITPRHLQLA CCCEEEECHHHHHHH	20.50	21890473
83	Ubiquitination	DLKVKRITPRHLQLA CCCEEEECHHHHHHH	20.50	23000965
84	Ubiquitination	LKVKRITPRHLQLAI CCEEEECHHHHHHHH	21.23	21890473
84	Ubiquitination	LKVKRITPRHLQLAI CCEEEECHHHHHHHH	21.23	23000965
88	Ubiquitination	RITPRHLQLAIRGDE EECHHHHHHHHCCCH	23.79	23000965
90	Ubiquitination	TPRHLQLAIRGDEEL CHHHHHHHHCCCHHH	4.04	21890473
90	Ubiquitination	TPRHLQLAIRGDEEL CHHHHHHHHCCCHHH	4.04	23000965
92	Methylation	RHLQLAIRGDEELDS HHHHHHHCCCHHHHH	40.68	-
95	Ubiquitination	QLAIRGDEELDSLIK HHHHCCCHHHHHHHH	64.38	23000965
95	Ubiquitination	QLAIRGDEELDSLIK HHHHCCCHHHHHHHH	64.38	21890473
96	Ubiquitination	LAIRGDEELDSLIKA HHHCCCHHHHHHHHH	63.72	21890473
96	Ubiquitination	LAIRGDEELDSLIKA HHHCCCHHHHHHHHH	63.72	23000965
99	Phosphorylation	RGDEELDSLIKATIA CCCHHHHHHHHHHHC	44.62	20873877
100	Ubiquitination	GDEELDSLIKATIAG CCHHHHHHHHHHHCC	4.68	23000965
102	Ubiquitination	EELDSLIKATIAGGG HHHHHHHHHHHCCCC	44.78	21906983
102	Acetylation	EELDSLIKATIAGGG HHHHHHHHHHHCCCC	44.78	-
104	Phosphorylation	LDSLIKATIAGGGVI HHHHHHHHHCCCCCH	13.32	24247654
116	Lactoylation	GVIPHIHKSLIGKKG CCHHHHHHHHCCCCC	46.48	-
116	Ubiquitination	GVIPHIHKSLIGKKG CCHHHHHHHHCCCCC	46.48	23000965
116	Acetylation	GVIPHIHKSLIGKKG CCHHHHHHHHCCCCC	46.48	72597301
116	Methylation	GVIPHIHKSLIGKKG CCHHHHHHHHCCCCC	46.48	-
117	Phosphorylation	VIPHIHKSLIGKKGQ CHHHHHHHHCCCCCC	15.85	24719451
121	Sumoylation	IHKSLIGKKGQQKTA HHHHHCCCCCCCCCC	46.89	-
121	Ubiquitination	IHKSLIGKKGQQKTA HHHHHCCCCCCCCCC	46.89	23000965
122	Ubiquitination	HKSLIGKKGQQKTA- HHHHCCCCCCCCCC-	57.66	23000965
126	Ubiquitination	IGKKGQQKTA----- CCCCCCCCCC-----	38.23	23000965

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of H2AV_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
5	K	Acetylation	Acetylated on Lys-5, Lys-8 and Lys-12 during interphase.	-
8	K	Acetylation	Acetylated on Lys-5, Lys-8 and Lys-12 during interphase.	-
12	K	Acetylation	Acetylated on Lys-5, Lys-8 and Lys-12 during interphase.	-
122	K	ubiquitylation	Monoubiquitination of Lys-122 gives a specific tag for epigenetic transcriptional repression.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of H2AV_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
TLS1_HUMAN	C9orf78	physical	22863883
FKBP9_HUMAN	FKBP9	physical	22863883
HERC4_HUMAN	HERC4	physical	22863883
HXK2_HUMAN	HK2	physical	22863883
NUBP2_HUMAN	NUBP2	physical	22863883
TRNT1_HUMAN	TRNT1	physical	22863883
XPP1_HUMAN	XPNPEP1	physical	22863883

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Acetylation

"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-8; LYS-12 AND LYS-14,AND MASS SPECTROMETRY.
PubMed: 16916647