H2AZ_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H2AZ_HUMAN
• UniProt AC: P0C0S5
• Protein Name: Histone H2A.Z
• Gene Name: H2AFZ
• 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..
• Protein Sequence: MAGGKAGKDSGKAKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV

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	Methylation	---MAGGKAGKDSGK ---CCCCCCCCCCCC	53.71	23324626
5	Lactylation	---MAGGKAGKDSGK ---CCCCCCCCCCCC	53.71	31645732
5	Acetylation	---MAGGKAGKDSGK ---CCCCCCCCCCCC	53.71	16319397
8	Acetylation	MAGGKAGKDSGKAKT CCCCCCCCCCCCCCC	54.29	16319397
8	Methylation	MAGGKAGKDSGKAKT CCCCCCCCCCCCCCC	54.29	23324626
8	Lactylation	MAGGKAGKDSGKAKT CCCCCCCCCCCCCCC	54.29	31645732
8	Ubiquitination	MAGGKAGKDSGKAKT CCCCCCCCCCCCCCC	54.29	24816145
12	Acetylation	KAGKDSGKAKTKAVS CCCCCCCCCCCHHCC	51.14	19608861
12	Lactoylation	KAGKDSGKAKTKAVS CCCCCCCCCCCHHCC	51.14	31645732
12	Lactylation	KAGKDSGKAKTKAVS CCCCCCCCCCCHHCC	51.14	31645732
14	Acetylation	GKDSGKAKTKAVSRS CCCCCCCCCHHCCHH	54.78	19608861
14	Lactoylation	GKDSGKAKTKAVSRS CCCCCCCCCHHCCHH	54.78	31645732
16	Acetylation	DSGKAKTKAVSRSQR CCCCCCCHHCCHHHH	46.19	26051181
16	Neddylation	DSGKAKTKAVSRSQR CCCCCCCHHCCHHHH	46.19	32015554
16	Ubiquitination	DSGKAKTKAVSRSQR CCCCCCCHHCCHHHH	46.19	25015289
23	Methylation	KAVSRSQRAGLQFPV HHCCHHHHHCCCCCH	31.69	-
32	Methylation	GLQFPVGRIHRHLKS CCCCCHHHHHHHHHH	23.05	-
43	O-linked_Glycosylation	HLKSRTTSHGRVGAT HHHHCCCCCCCHHHH	24.27	22121020
61	Phosphorylation	YSAAILEYLTAEVLE HHHHHHHHHHHHHHH	13.10	22817900
92	Methylation	RHLQLAIRGDEELDS HHHHHHHCCCHHHHH	40.68	-
99	Phosphorylation	RGDEELDSLIKATIA CCCHHHHHHHHHHHC	44.62	20873877
102	Acetylation	EELDSLIKATIAGGG HHHHHHHHHHHCCCC	44.78	25825284
102	Methylation	EELDSLIKATIAGGG HHHHHHHHHHHCCCC	44.78	-
102	Ubiquitination	EELDSLIKATIAGGG HHHHHHHHHHHCCCC	44.78	21906983
104	Phosphorylation	LDSLIKATIAGGGVI HHHHHHHHHCCCCCC	13.32	24247654
116	Methylation	GVIPHIHKSLIGKKG CCCHHHHHHHCCCCC	46.48	19608861
116	Lactoylation	GVIPHIHKSLIGKKG CCCHHHHHHHCCCCC	46.48	31645732
116	Acetylation	GVIPHIHKSLIGKKG CCCHHHHHHHCCCCC	46.48	25825284
116	Ubiquitination	GVIPHIHKSLIGKKG CCCHHHHHHHCCCCC	46.48	23000965
116	Malonylation	GVIPHIHKSLIGKKG CCCHHHHHHHCCCCC	46.48	26320211
117	Phosphorylation	VIPHIHKSLIGKKGQ CCHHHHHHHCCCCCC	15.85	24719451
121	Acetylation	IHKSLIGKKGQQKTV HHHHHCCCCCCCCCC	46.89	25953088
121	Ubiquitination	IHKSLIGKKGQQKTV HHHHHCCCCCCCCCC	46.89	23000965
121	Sumoylation	IHKSLIGKKGQQKTV HHHHHCCCCCCCCCC	46.89	-
122	Ubiquitination	HKSLIGKKGQQKTV- HHHHCCCCCCCCCC-	57.66	23000965
126	Ubiquitination	IGKKGQQKTV----- CCCCCCCCCC-----	43.28	23000965
126	Neddylation	IGKKGQQKTV----- CCCCCCCCCC-----	43.28	32015554

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
-	K	Ubiquitination	E3 ubiquitin ligase	PRC1	O43663	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	BMI1	P35226	PMID:17636032
-	K	Ubiquitination	E3 ubiquitin ligase	RNF2	Q99496	PMID:17636032
-	K	Ubiquitination	E3 ubiquitin ligase	BMI1#RNF2	P35226#Q99496	PMID:22199232

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; acetylation disappears at mitosis (By similarity).	16627869
5	K	Acetylation	Acetylated on Lys-5, Lys-8, Lys-12 and Lys-14 by KAT2A; KAT2A is recruited by the XPC complex in absence of DNA damage.	16627869
5	K	Methylation	Monomethylated on Lys-5 and Lys-8 by SETD6.	16627869
5	K	Methylation	SETD6 predominantly methylates Lys-8, lys-5 being a possible secondary site.	16627869
8	K	Acetylation	Acetylated on Lys-5, Lys-8 and Lys-12 during interphase; acetylation disappears at mitosis (By similarity).	16627869
8	K	Acetylation	Acetylated on Lys-5, Lys-8, Lys-12 and Lys-14 by KAT2A; KAT2A is recruited by the XPC complex in absence of DNA damage.	16627869
8	K	Methylation	Monomethylated on Lys-5 and Lys-8 by SETD6.	16627869
8	K	Methylation	SETD6 predominantly methylates Lys-8, lys-5 being a possible secondary site.	16627869
12	K	Acetylation	Acetylated on Lys-5, Lys-8 and Lys-12 during interphase; acetylation disappears at mitosis (By similarity).	11835281
12	K	Acetylation	Acetylated on Lys-5, Lys-8, Lys-12 and Lys-14 by KAT2A; KAT2A is recruited by the XPC complex in absence of DNA damage.	11835281
14	K	Acetylation	Acetylated on Lys-5, Lys-8, Lys-12 and Lys-14 by KAT2A; KAT2A is recruited by the XPC complex in absence of DNA damage.	19608861
122	K	ubiquitylation	Monoubiquitination of Lys-122 gives a specific tag for epigenetic transcriptional repression.	11835281

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of H2AZ_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
INCE_HUMAN	INCENP	physical	12660166
RUVB1_HUMAN	RUVBL1	physical	17721549
RUVB2_HUMAN	RUVBL2	physical	17721549
ACL6A_HUMAN	ACTL6A	physical	17721549
IN80C_HUMAN	INO80C	physical	17721549
CND2_HUMAN	NCAPH	physical	21633354
ZNHI1_HUMAN	ZNHIT1	physical	20473270
H4G_HUMAN	HIST1H4G	physical	22493515
H4_HUMAN	HIST1H4I	physical	22493515
TRRAP_HUMAN	TRRAP	physical	22467210
RUVB2_HUMAN	RUVBL2	physical	22467210
RUVB1_HUMAN	RUVBL1	physical	22467210
EP400_HUMAN	EP400	physical	22467210
ACL6A_HUMAN	ACTL6A	physical	22467210
SRCAP_HUMAN	SRCAP	physical	22467210
DMAP1_HUMAN	DMAP1	physical	22467210
EAF6_HUMAN	MEAF6	physical	22467210
KAT5_HUMAN	KAT5	physical	22467210
YETS4_HUMAN	YEATS4	physical	22467210
MO4L1_HUMAN	MORF4L1	physical	22467210
VPS72_HUMAN	VPS72	physical	22467210
ARP6_HUMAN	ACTR6	physical	22467210
EPC1_HUMAN	EPC1	physical	22467210
MRGBP_HUMAN	MRGBP	physical	22467210
ING3_HUMAN	ING3	physical	22467210
EZRI_HUMAN	EZR	physical	22863883
FUMH_HUMAN	FH	physical	22863883
NOL3_HUMAN	NOL3	physical	22863883
OGFD1_HUMAN	OGFOD1	physical	22863883
PSMD9_HUMAN	PSMD9	physical	22863883
PYGL_HUMAN	PYGL	physical	22863883
TRNT1_HUMAN	TRNT1	physical	22863883
BRD3_HUMAN	BRD3	physical	26344197

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

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-8; LYS-12 AND LYS-14,AND MASS SPECTROMETRY.
PubMed: 19608861

"Quantitative proteomic analysis of post-translational modificationsof human histones.";
Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M.,Finn P., Grauslund M., Hansen A.M., Jensen O.N.;
Mol. Cell. Proteomics 5:1314-1325(2006).
Cited for: ACETYLATION AT LYS-5; LYS-8 AND LYS-12, AND MASS SPECTROMETRY.
PubMed: 16627869

"Characterization of histones H2A and H2B variants and their post-translational modifications by mass spectrometry.";
Bonenfant D., Coulot M., Towbin H., Schindler P., van Oostrum J.;
Mol. Cell. Proteomics 5:541-552(2006).
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, AND ACETYLATION AT LYS-5 ANDLYS-8.
PubMed: 16319397

"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

Ubiquitylation

"Histone ubiquitination: a tagging tail unfolds?";
Jason L.J.M., Moore S.C., Lewis J.D., Lindsey G., Ausio J.;
Bioessays 24:166-174(2002).
Cited for: UBIQUITINATION AT LYS-122.
PubMed: 11835281