H2AW_HUMAN - dbPTM
H2AW_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID H2AW_HUMAN
UniProt AC Q9P0M6
Protein Name Core histone macro-H2A.2
Gene Name H2AFY2
Organism Homo sapiens (Human).
Sequence Length 372
Subcellular Localization Nucleus . Chromosome . Enriched in inactive X chromosome chromatin (PubMed:11331621, PubMed:11262398) and in senescence-associated heterochromatin (PubMed:15621527).
Protein Description Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. 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 stable X chromosome inactivation..
Protein Sequence MSGRSGKKKMSKLSRSARAGVIFPVGRLMRYLKKGTFKYRISVGAPVYMAAVIEYLAAEILELAGNAARDNKKARIAPRHILLAVANDEELNQLLKGVTIASGGVLPRIHPELLAKKRGTKGKSETILSPPPEKRGRKATSGKKGGKKSKAAKPRTSKKSKPKDSDKEGTSNSTSEDGPGDGFTILSSKSLVLGQKLSLTQSDISHIGSMRVEGIVHPTTAEIDLKEDIGKALEKAGGKEFLETVKELRKSQGPLEVAEAAVSQSSGLAAKFVIHCHIPQWGSDKCEEQLEETIKNCLSAAEDKKLKSVAFPPFPSGRNCFPKQTAAQVTLKAISAHFDDSSASSLKNVYFLLFDSESIGIYVQEMAKLDAK
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 Orthologous
Protein Cluster
2O-linked_Glycosylation------MSGRSGKKK
------CCCCCCHHH		42.8030379171
7Lactoylation-MSGRSGKKKMSKLS
-CCCCCCHHHHHHHH		50.93-
9LactoylationSGRSGKKKMSKLSRS
CCCCCHHHHHHHHHH		52.47-
12AcetylationSGKKKMSKLSRSARA
CCHHHHHHHHHHHHC		47.1619608861
27MethylationGVIFPVGRLMRYLKK
CEEEEHHHHHHHHHH		26.08-
31PhosphorylationPVGRLMRYLKKGTFK
EHHHHHHHHHHCCEE		14.65-
55PhosphorylationYMAAVIEYLAAEILE
HHHHHHHHHHHHHHH		7.19-
102PhosphorylationLKGVTIASGGVLPRI
HHCCEECCCCCCCCC		32.0324114839
116UbiquitinationIHPELLAKKRGTKGK
CCHHHHHHHCCCCCC		42.8621906983
117UbiquitinationHPELLAKKRGTKGKS
CHHHHHHHCCCCCCC		50.91-
120PhosphorylationLLAKKRGTKGKSETI
HHHHHCCCCCCCCCC		40.4329038488
123UbiquitinationKKRGTKGKSETILSP
HHCCCCCCCCCCCCC		46.8321906983
124PhosphorylationKRGTKGKSETILSPP
HCCCCCCCCCCCCCC		48.9526330541
126PhosphorylationGTKGKSETILSPPPE
CCCCCCCCCCCCCCH		34.0230266825
129PhosphorylationGKSETILSPPPEKRG
CCCCCCCCCCCHHCC		31.3530266825
140PhosphorylationEKRGRKATSGKKGGK
HHCCCCCCCCCCCCC		40.8420860994
160PhosphorylationKPRTSKKSKPKDSDK
CCCCCCCCCCCCCCC		58.91-
165PhosphorylationKKSKPKDSDKEGTSN
CCCCCCCCCCCCCCC		57.6228450419
170PhosphorylationKDSDKEGTSNSTSED
CCCCCCCCCCCCCCC		26.3128450419
171PhosphorylationDSDKEGTSNSTSEDG
CCCCCCCCCCCCCCC		39.3728450419
173PhosphorylationDKEGTSNSTSEDGPG
CCCCCCCCCCCCCCC		32.8326657352
174PhosphorylationKEGTSNSTSEDGPGD
CCCCCCCCCCCCCCC		40.1526657352
175PhosphorylationEGTSNSTSEDGPGDG
CCCCCCCCCCCCCCC		33.2528450419
190PhosphorylationFTILSSKSLVLGQKL
EEEEECCCEECCCCE		26.1727251275
198PhosphorylationLVLGQKLSLTQSDIS
EECCCCEECCHHHHH		36.0822817900
200PhosphorylationLGQKLSLTQSDISHI
CCCCEECCHHHHHHH		23.7422817900
205PhosphorylationSLTQSDISHIGSMRV
ECCHHHHHHHHCCEE		17.6520860994
239SumoylationALEKAGGKEFLETVK
HHHHCCCHHHHHHHH		44.3628112733
239UbiquitinationALEKAGGKEFLETVK
HHHHCCCHHHHHHHH		44.36-
246UbiquitinationKEFLETVKELRKSQG
HHHHHHHHHHHHCCC		59.4521906983
251PhosphorylationTVKELRKSQGPLEVA
HHHHHHHCCCCHHHH		33.6627050516
263PhosphorylationEVAEAAVSQSSGLAA
HHHHHHHHCCCCCHH		21.44-
266PhosphorylationEAAVSQSSGLAAKFV
HHHHHCCCCCHHHEE		30.13-
285AcetylationIPQWGSDKCEEQLEE
CCCCCCHHHHHHHHH		45.2925825284
304AcetylationCLSAAEDKKLKSVAF
HHHHHHHHCCCCCCC		52.0625825284
332UbiquitinationTAAQVTLKAISAHFD
CHHHHHHHHHHHCCC		34.0221906983
341PhosphorylationISAHFDDSSASSLKN
HHHCCCCCCCHHHCC		29.6427251275
342PhosphorylationSAHFDDSSASSLKNV
HHCCCCCCCHHHCCE		38.8825849741
362PhosphorylationDSESIGIYVQEMAKL
CHHHHEEHHHHHHHH		7.29-
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 H2AW_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of H2AW_HUMAN !!
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 H2AW_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WWP1_HUMANWWP1physical
21988832
H2AY_HUMANH2AFYphysical
28514442
TONSL_HUMANTONSLphysical
28514442
IPO9_HUMANIPO9physical
28514442
ZN189_HUMANZNF189physical
28514442
MMS22_HUMANMMS22Lphysical
28514442
SP16H_HUMANSUPT16Hphysical
28514442
CENPQ_HUMANCENPQphysical
28514442
NO40_HUMANZCCHC17physical
28514442
HEXI1_HUMANHEXIM1physical
28514442
CENPC_HUMANCENPCphysical
28514442
SPT2_HUMANSPTY2D1physical
28514442
PPM1G_HUMANPPM1Gphysical
28514442
CARF_HUMANCDKN2AIPphysical
28514442
BRX1_HUMANBRIX1physical
28514442
PUM3_HUMANKIAA0020physical
28514442
H2A2B_HUMANHIST2H2ABphysical
28514442
RL26L_HUMANRPL26L1physical
28514442
PARP2_HUMANPARP2physical
28514442
TRM1L_HUMANTRMT1Lphysical
28514442
REXO4_HUMANREXO4physical
28514442
RBM28_HUMANRBM28physical
28514442
RRP5_HUMANPDCD11physical
28514442
MCM2_HUMANMCM2physical
28514442
RL3_HUMANRPL3physical
28514442
NPA1P_HUMANURB1physical
28514442
TRI26_HUMANTRIM26physical
28514442
CCNT1_HUMANCCNT1physical
28514442
BBX_HUMANBBXphysical
28514442
CK057_HUMANC11orf57physical
28514442
PURB_HUMANPURBphysical
28514442
SSRP1_HUMANSSRP1physical
28514442
RFC1_HUMANRFC1physical
28514442
RPF2_HUMANRPF2physical
28514442
MBB1A_HUMANMYBBP1Aphysical
28514442
NOP2_HUMANNOP2physical
28514442
BMS1_HUMANBMS1physical
28514442
ZFP62_HUMANZFP62physical
28514442
RRS1_HUMANRRS1physical
28514442
RBM34_HUMANRBM34physical
28514442
NLE1_HUMANNLE1physical
28514442
MAK16_HUMANMAK16physical
28514442
GLYR1_HUMANGLYR1physical
28514442
NSA2_HUMANNSA2physical
28514442
RM34_HUMANMRPL34physical
28514442
NOC3L_HUMANNOC3Lphysical
28514442
URB2_HUMANURB2physical
28514442
CCNT2_HUMANCCNT2physical
28514442
DDX18_HUMANDDX18physical
28514442
PATZ1_HUMANPATZ1physical
28514442
CEBPZ_HUMANCEBPZphysical
28514442
RBM19_HUMANRBM19physical
28514442
RPF1_HUMANRPF1physical
28514442
MCM4_HUMANMCM4physical
28514442
RL7L_HUMANRPL7L1physical
28514442
RL37A_HUMANRPL37Aphysical
28514442
RLA0_HUMANRPLP0physical
28514442
TEX10_HUMANTEX10physical
28514442
DKC1_HUMANDKC1physical
28514442
DDX24_HUMANDDX24physical
28514442
RSBN1_HUMANRSBN1physical
28514442
DDX31_HUMANDDX31physical
28514442
RL4_HUMANRPL4physical
28514442
RS13_HUMANRPS13physical
28514442
DDX51_HUMANDDX51physical
28514442
PRP4B_HUMANPRPF4Bphysical
28514442
MRT4_HUMANMRTO4physical
28514442
EBP2_HUMANEBNA1BP2physical
28514442
RIOX2_HUMANMINAphysical
28514442
RL8_HUMANRPL8physical
28514442
DDX21_HUMANDDX21physical
28514442
RL7A_HUMANRPL7Aphysical
28514442
ZC3H8_HUMANZC3H8physical
28514442
RRP8_HUMANRRP8physical
28514442
DHX57_HUMANDHX57physical
28514442
RL15_HUMANRPL15physical
28514442
ZN770_HUMANZNF770physical
28514442
NOG1_HUMANGTPBP4physical
28514442
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.
Regulatory Network of H2AW_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-12, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND MASSSPECTROMETRY.

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