H2AY_HUMAN - dbPTM
H2AY_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID H2AY_HUMAN
UniProt AC O75367
Protein Name Core histone macro-H2A.1
Gene Name H2AFY
Organism Homo sapiens (Human).
Sequence Length 372
Subcellular Localization Nucleus . Chromosome . Enriched in inactive X chromosome chromatin and in senescence-associated heterochromatin.
Protein Description Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. [PubMed: 12718888]
Protein Sequence MSSRGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGKLEAIITPPPAKKAKSPSQKKPVSKKAGGKKGARKSKKKQGEVSKAASADSTTEGTPADGFTVLSTKSLFLGQKLNLIHSEISNLAGFEVEAIINPTNADIDLKDDLGNTLEKKGGKEFVEAVLELRKKNGPLEVAGAAVSAGHGLPAKFVIHCNSPVWGADKCEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYFVSTMSSSIKTVYFVLFDSESIGIYVQEMAKLDAN
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
7Acetylation-MSSRGGKKKSTKTS
-CCCCCCCCCCCCCC		60.917824983
7Lactoylation-MSSRGGKKKSTKTS
-CCCCCCCCCCCCCC		60.91-
9LactoylationSSRGGKKKSTKTSRS
CCCCCCCCCCCCCHH		67.83-
9UbiquitinationSSRGGKKKSTKTSRS
CCCCCCCCCCCCCHH		67.8324816145
10PhosphorylationSRGGKKKSTKTSRSA
CCCCCCCCCCCCHHH		43.9721406692
11PhosphorylationRGGKKKSTKTSRSAK
CCCCCCCCCCCHHHC		47.4221406692
12AcetylationGGKKKSTKTSRSAKA
CCCCCCCCCCHHHCC		52.157824993
12UbiquitinationGGKKKSTKTSRSAKA
CCCCCCCCCCHHHCC		52.1523503661
13PhosphorylationGKKKSTKTSRSAKAG
CCCCCCCCCHHHCCE		29.4821406692
14PhosphorylationKKKSTKTSRSAKAGV
CCCCCCCCHHHCCEE		26.2921406692
16PhosphorylationKSTKTSRSAKAGVIF
CCCCCCHHHCCEEEE		33.6121406692
182-HydroxyisobutyrylationTKTSRSAKAGVIFPV
CCCCHHHCCEEEEEH		47.09-
18AcetylationTKTSRSAKAGVIFPV
CCCCHHHCCEEEEEH		47.0920167786
18MethylationTKTSRSAKAGVIFPV
CCCCHHHCCEEEEEH		47.0916210244
18UbiquitinationTKTSRSAKAGVIFPV
CCCCHHHCCEEEEEH		47.0921906983
18 (in isoform 1)Ubiquitination-47.0921890473
18 (in isoform 2)Methylation-47.09-
18 (in isoform 2)Ubiquitination-47.0921890473
18 (in isoform 3)Methylation-47.09-
27MethylationGVIFPVGRMLRYIKK
EEEEEHHHHHHHHHH		22.61-
55PhosphorylationYMAAVLEYLTAEILE
HHHHHHHHHHHHHHH		12.75-
96UbiquitinationEELNQLLKGVTIASG
HHHHHHHHCCEECCC		60.99-
99PhosphorylationNQLLKGVTIASGGVL
HHHHHCCEECCCCCC		21.3528122231
102PhosphorylationLKGVTIASGGVLPNI
HHCCEECCCCCCCCC		32.0321712546
1162-HydroxyisobutyrylationIHPELLAKKRGSKGK
CCHHHHHHHCCCCCC		42.86-
116AcetylationIHPELLAKKRGSKGK
CCHHHHHHHCCCCCC		42.8625953088
116NeddylationIHPELLAKKRGSKGK
CCHHHHHHHCCCCCC		42.8632015554
116UbiquitinationIHPELLAKKRGSKGK
CCHHHHHHHCCCCCC		42.8623000965
116 (in isoform 1)Ubiquitination-42.8621890473
116 (in isoform 2)Ubiquitination-42.8621890473
116 (in isoform 3)Ubiquitination-42.8621890473
117UbiquitinationHPELLAKKRGSKGKL
CHHHHHHHCCCCCCE		57.2823000965
117 (in isoform 1)Ubiquitination-57.2821890473
117 (in isoform 2)Ubiquitination-57.2821890473
117 (in isoform 3)Ubiquitination-57.2821890473
120PhosphorylationLLAKKRGSKGKLEAI
HHHHHCCCCCCEEEE		42.1229214152
121UbiquitinationLAKKRGSKGKLEAII
HHHHCCCCCCEEEEE		63.9923000965
121 (in isoform 1)Ubiquitination-63.9921890473
121 (in isoform 2)Ubiquitination-63.9921890473
121 (in isoform 3)Ubiquitination-63.9921890473
123"N6,N6-dimethyllysine"KKRGSKGKLEAIITP
HHCCCCCCEEEEECC		47.06-
123AcetylationKKRGSKGKLEAIITP
HHCCCCCCEEEEECC		47.0623749302
123MethylationKKRGSKGKLEAIITP
HHCCCCCCEEEEECC		47.0616210244
123NeddylationKKRGSKGKLEAIITP
HHCCCCCCEEEEECC		47.0632015554
123SumoylationKKRGSKGKLEAIITP
HHCCCCCCEEEEECC		47.0628112733
123UbiquitinationKKRGSKGKLEAIITP
HHCCCCCCEEEEECC		47.0623000965
123 (in isoform 1)Ubiquitination-47.0621890473
123 (in isoform 2)Methylation-47.06-
123 (in isoform 2)Ubiquitination-47.0621890473
123 (in isoform 3)Methylation-47.06-
123 (in isoform 3)Ubiquitination-47.0621890473
129PhosphorylationGKLEAIITPPPAKKA
CCEEEEECCCCCCCC		24.5129255136
129 (in isoform 2)Phosphorylation-24.51-
129 (in isoform 3)Phosphorylation-24.51-
1342-HydroxyisobutyrylationIITPPPAKKAKSPSQ
EECCCCCCCCCCHHH		60.06-
134AcetylationIITPPPAKKAKSPSQ
EECCCCCCCCCCHHH		60.0625953088
134NeddylationIITPPPAKKAKSPSQ
EECCCCCCCCCCHHH		60.0632015554
134UbiquitinationIITPPPAKKAKSPSQ
EECCCCCCCCCCHHH		60.0633845483
135UbiquitinationITPPPAKKAKSPSQK
ECCCCCCCCCCHHHC		64.2525015289
138PhosphorylationPPAKKAKSPSQKKPV
CCCCCCCCHHHCCCC		34.3426055452
138 (in isoform 2)Phosphorylation-34.34-
138 (in isoform 3)Phosphorylation-34.34-
140PhosphorylationAKKAKSPSQKKPVSK
CCCCCCHHHCCCCCC		62.8224732914
140 (in isoform 2)Phosphorylation-62.82-
140 (in isoform 3)Phosphorylation-62.82-
142AcetylationKAKSPSQKKPVSKKA
CCCCHHHCCCCCCCC		64.4825953088
146PhosphorylationPSQKKPVSKKAGGKK
HHHCCCCCCCCCCCC		36.6524732914
153AcetylationSKKAGGKKGARKSKK
CCCCCCCCCCCHHHC		62.1619809309
158PhosphorylationGKKGARKSKKKQGEV
CCCCCCHHHCCCCCC		44.12-
159AcetylationKKGARKSKKKQGEVS
CCCCCHHHCCCCCCC		68.0019809319
160UbiquitinationKGARKSKKKQGEVSK
CCCCHHHCCCCCCCC		58.3723503661
161AcetylationGARKSKKKQGEVSKA
CCCHHHCCCCCCCCH		68.2425953088
161UbiquitinationGARKSKKKQGEVSKA
CCCHHHCCCCCCCCH		68.2423503661
166PhosphorylationKKKQGEVSKAASADS
HCCCCCCCCHHCCCC		16.5727422710
166UbiquitinationKKKQGEVSKAASADS
HCCCCCCCCHHCCCC		16.5721963094
167AcetylationKKQGEVSKAASADST
CCCCCCCCHHCCCCC		53.8225953088
167SumoylationKKQGEVSKAASADST
CCCCCCCCHHCCCCC		53.8228112733
167UbiquitinationKKQGEVSKAASADST
CCCCCCCCHHCCCCC		53.8221906983
167 (in isoform 1)Ubiquitination-53.8221890473
167 (in isoform 2)Ubiquitination-53.8221890473
169 (in isoform 3)Phosphorylation-14.6925849741
170O-linked_GlycosylationGEVSKAASADSTTEG
CCCCCHHCCCCCCCC		37.1532119511
170PhosphorylationGEVSKAASADSTTEG
CCCCCHHCCCCCCCC		37.1529255136
170 (in isoform 2)Phosphorylation-37.15-
172PhosphorylationVSKAASADSTTEGTP
CCCHHCCCCCCCCCC		43.9832142685
172 (in isoform 3)Phosphorylation-43.9825849741
173PhosphorylationSKAASADSTTEGTPA
CCHHCCCCCCCCCCC		36.6229255136
173 (in isoform 2)Phosphorylation-36.62-
173 (in isoform 3)Phosphorylation-36.6225849741
174PhosphorylationKAASADSTTEGTPAD
CHHCCCCCCCCCCCC		29.4329255136
174 (in isoform 2)Phosphorylation-29.43-
174 (in isoform 3)Phosphorylation-29.43-
175PhosphorylationAASADSTTEGTPADG
HHCCCCCCCCCCCCC		36.0529255136
175 (in isoform 2)Phosphorylation-36.05-
177 (in isoform 3)Phosphorylation-34.60-
178PhosphorylationADSTTEGTPADGFTV
CCCCCCCCCCCCEEE		14.7425159151
178 (in isoform 2)Phosphorylation-14.74-
184PhosphorylationGTPADGFTVLSTKSL
CCCCCCEEEEEEHHH		26.5123927012
187PhosphorylationADGFTVLSTKSLFLG
CCCEEEEEEHHHHHH		29.4723403867
188PhosphorylationDGFTVLSTKSLFLGQ
CCEEEEEEHHHHHHH		22.0823927012
188UbiquitinationDGFTVLSTKSLFLGQ
CCEEEEEEHHHHHHH		22.0823000965
188 (in isoform 3)Ubiquitination-22.0821890473
189AcetylationGFTVLSTKSLFLGQK
CEEEEEEHHHHHHHH		41.6126051181
189SumoylationGFTVLSTKSLFLGQK
CEEEEEEHHHHHHHH		41.6128112733
189UbiquitinationGFTVLSTKSLFLGQK
CEEEEEEHHHHHHHH		41.6123000965
189 (in isoform 1)Ubiquitination-41.6121890473
189 (in isoform 2)Ubiquitination-41.6121890473
190PhosphorylationFTVLSTKSLFLGQKL
EEEEEEHHHHHHHHH		25.1727499020
196UbiquitinationKSLFLGQKLNLIHSE
HHHHHHHHHHHHHHH		37.23-
234UbiquitinationDDLGNTLEKKGGKEF
CCHHHHHHHHCHHHH		51.1627667366
2352-HydroxyisobutyrylationDLGNTLEKKGGKEFV
CHHHHHHHHCHHHHH		60.89-
235UbiquitinationDLGNTLEKKGGKEFV
CHHHHHHHHCHHHHH		60.8921906983
235 (in isoform 1)Ubiquitination-60.8921890473
236MethylationLGNTLEKKGGKEFVE
HHHHHHHHCHHHHHH		64.6216210244
236UbiquitinationLGNTLEKKGGKEFVE
HHHHHHHHCHHHHHH		64.6232015554
236 (in isoform 2)Methylation-64.62-
238MethylationNTLEKKGGKEFVEAV
HHHHHHCHHHHHHHH		34.8916210244
238UbiquitinationNTLEKKGGKEFVEAV
HHHHHHCHHHHHHHH		34.8932015554
238 (in isoform 3)Methylation-34.89-
239"N6,N6-dimethyllysine"TLEKKGGKEFVEAVL
HHHHHCHHHHHHHHH		57.56-
239MethylationTLEKKGGKEFVEAVL
HHHHHCHHHHHHHHH		57.5616210244
239UbiquitinationTLEKKGGKEFVEAVL
HHHHHCHHHHHHHHH		57.5632015554
246UbiquitinationKEFVEAVLELRKKNG
HHHHHHHHHHHHHCC		7.0822817900
247UbiquitinationEFVEAVLELRKKNGP
HHHHHHHHHHHHCCC		39.6721890473
248UbiquitinationFVEAVLELRKKNGPL
HHHHHHHHHHHCCCC		9.4621890473
248 (in isoform 2)Ubiquitination-9.4621890473
249MethylationVEAVLELRKKNGPLE
HHHHHHHHHHCCCCE		38.23-
249UbiquitinationVEAVLELRKKNGPLE
HHHHHHHHHHCCCCE		38.2322817900
250UbiquitinationEAVLELRKKNGPLEV
HHHHHHHHHCCCCEE		64.3121890473
250 (in isoform 3)Ubiquitination-64.3121890473
251UbiquitinationAVLELRKKNGPLEVA
HHHHHHHHCCCCEEE		61.7822817900
251 (in isoform 1)Ubiquitination-61.7821890473
268UbiquitinationAVSAGHGLPAKFVIH
EECCCCCCCEEEEEE		2.8632015554
270UbiquitinationSAGHGLPAKFVIHCN
CCCCCCCEEEEEEEC		23.9832015554
271UbiquitinationAGHGLPAKFVIHCNS
CCCCCCEEEEEEECC		37.9232015554
278PhosphorylationKFVIHCNSPVWGADK
EEEEEECCCCCCHHH		26.6525159151
281UbiquitinationIHCNSPVWGADKCEE
EEECCCCCCHHHHHH		10.3125015289
282UbiquitinationHCNSPVWGADKCEEL
EECCCCCCHHHHHHH		24.9132015554
284UbiquitinationNSPVWGADKCEELLE
CCCCCCHHHHHHHHH		52.8032015554
285AcetylationSPVWGADKCEELLEK
CCCCCHHHHHHHHHH		42.9125825284
285MalonylationSPVWGADKCEELLEK
CCCCCHHHHHHHHHH		42.9126320211
285UbiquitinationSPVWGADKCEELLEK
CCCCCHHHHHHHHHH		42.9133845483
288UbiquitinationWGADKCEELLEKTVK
CCHHHHHHHHHHHHH		69.0323000965
289UbiquitinationGADKCEELLEKTVKN
CHHHHHHHHHHHHHH		3.3223000965
291UbiquitinationDKCEELLEKTVKNCL
HHHHHHHHHHHHHHH		60.3423000965
292AcetylationKCEELLEKTVKNCLA
HHHHHHHHHHHHHHH		59.6025825284
292UbiquitinationKCEELLEKTVKNCLA
HHHHHHHHHHHHHHH		59.6023000965
292 (in isoform 2)Ubiquitination-59.6021890473
294UbiquitinationEELLEKTVKNCLALA
HHHHHHHHHHHHHHC		6.5923000965
294 (in isoform 3)Ubiquitination-6.5921890473
295AcetylationELLEKTVKNCLALAD
HHHHHHHHHHHHHCC		47.3725953088
295UbiquitinationELLEKTVKNCLALAD
HHHHHHHHHHHHHCC		47.3723000965
295 (in isoform 1)Ubiquitination-47.3721890473
300UbiquitinationTVKNCLALADDKKLK
HHHHHHHHCCCCCCC		3.2822817900
301UbiquitinationVKNCLALADDKKLKS
HHHHHHHCCCCCCCC		19.8333845483
302UbiquitinationKNCLALADDKKLKSI
HHHHHHCCCCCCCCC		69.9422817900
303UbiquitinationNCLALADDKKLKSIA
HHHHHCCCCCCCCCC		44.3627667366
3042-HydroxyisobutyrylationCLALADDKKLKSIAF
HHHHCCCCCCCCCCC		61.63-
304AcetylationCLALADDKKLKSIAF
HHHHCCCCCCCCCCC		61.6323749302
304UbiquitinationCLALADDKKLKSIAF
HHHHCCCCCCCCCCC		61.6327667366
304 (in isoform 2)Ubiquitination-61.6321890473
305UbiquitinationLALADDKKLKSIAFP
HHHCCCCCCCCCCCC		69.0522817900
306UbiquitinationALADDKKLKSIAFPS
HHCCCCCCCCCCCCC		6.9227667366
306 (in isoform 3)Ubiquitination-6.9221890473
3072-HydroxyisobutyrylationLADDKKLKSIAFPSI
HCCCCCCCCCCCCCC		49.01-
307AcetylationLADDKKLKSIAFPSI
HCCCCCCCCCCCCCC		49.0126051181
307MalonylationLADDKKLKSIAFPSI
HCCCCCCCCCCCCCC		49.0126320211
307UbiquitinationLADDKKLKSIAFPSI
HCCCCCCCCCCCCCC		49.0127667366
307 (in isoform 1)Ubiquitination-49.0121890473
308PhosphorylationADDKKLKSIAFPSIG
CCCCCCCCCCCCCCC		29.5920860994
313PhosphorylationLKSIAFPSIGSGRNG
CCCCCCCCCCCCCCC		32.8820860994
316PhosphorylationIAFPSIGSGRNGFPK
CCCCCCCCCCCCCCH		32.6720860994
319UbiquitinationPSIGSGRNGFPKQTA
CCCCCCCCCCCHHHH		61.0421890473
320UbiquitinationSIGSGRNGFPKQTAA
CCCCCCCCCCHHHHH		38.5823000965
320 (in isoform 2)Ubiquitination-38.5821890473
322UbiquitinationGSGRNGFPKQTAAQL
CCCCCCCCHHHHHHH		29.2823000965
322 (in isoform 3)Ubiquitination-29.2821890473
323SumoylationSGRNGFPKQTAAQLI
CCCCCCCHHHHHHHH		59.0028112733
323UbiquitinationSGRNGFPKQTAAQLI
CCCCCCCHHHHHHHH		59.0023000965
323 (in isoform 1)Ubiquitination-59.0021890473
325PhosphorylationRNGFPKQTAAQLILK
CCCCCHHHHHHHHHH		30.04-
329UbiquitinationPKQTAAQLILKAISS
CHHHHHHHHHHHHHH		4.2029967540
331UbiquitinationQTAAQLILKAISSYF
HHHHHHHHHHHHHHH		4.1029967540
332UbiquitinationTAAQLILKAISSYFV
HHHHHHHHHHHHHHH		36.3629967540
362PhosphorylationDSESIGIYVQEMAKL
CHHHHEEEHHHHHHH		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
-KUbiquitinationE3 ubiquitin ligaseSPOPO43791
PMID:15897469
-KUbiquitinationE3 ubiquitin ligaseTRIM59Q8IWR1
PMID:31488827
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
116Kubiquitylation

16129414
117Kubiquitylation

16129414
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 H2AY_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XRCC5_HUMANXRCC5physical
17158748
HSP74_HUMANHSPA4physical
17158748
HDAC1_HUMANHDAC1physical
17158748
MEP50_HUMANWDR77physical
17158748
RCC1_HUMANRCC1physical
17158748
DEK_HUMANDEKphysical
17158748
RAN_HUMANRANphysical
17158748
PHF14_HUMANPHF14physical
17158748
PARP1_HUMANPARP1physical
17158748
TOP1_HUMANTOP1physical
17158748
PARP1_HUMANPARP1physical
17322296
HDAC1_HUMANHDAC1physical
16107708
HDAC1_HUMANHDAC1physical
17474147
HDAC2_HUMANHDAC2physical
17474147
ERBB2_HUMANERBB2physical
22589551
A4_HUMANAPPphysical
21832049
ERIC2_HUMANERICH2physical
25416956
PARP1_HUMANPARP1physical
25306110
PARP1_HUMANPARP1physical
25417162
ATRX_HUMANATRXphysical
25417162
MECP2_HUMANMECP2physical
25417162
CBX1_HUMANCBX1physical
25417162
H11_HUMANHIST1H1Aphysical
25417162
H2B1B_HUMANHIST1H2BBphysical
25417162
H31_HUMANHIST1H3Aphysical
25417162
PARP1_HUMANPARP1physical
23473667
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 H2AY_HUMAN

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Related Literatures of Post-Translational Modification
Methylation
ReferencePubMed
"Mapping post-translational modifications of the histone variantMacroH2A1 using tandem mass spectrometry.";
Chu F., Nusinow D.A., Chalkley R.J., Plath K., Panning B.,Burlingame A.L.;
Mol. Cell. Proteomics 5:194-203(2006).
Cited for: METHYLATION AT LYS-18 AND LYS-123, PHOSPHORYLATION AT THR-129, ANDMASS 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 THR-129; SER-170 ANDSER-173, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129; SER-170; SER-173AND THR-178, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129; SER-170; SER-173AND THR-174, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129, AND MASSSPECTROMETRY.
"Mapping post-translational modifications of the histone variantMacroH2A1 using tandem mass spectrometry.";
Chu F., Nusinow D.A., Chalkley R.J., Plath K., Panning B.,Burlingame A.L.;
Mol. Cell. Proteomics 5:194-203(2006).
Cited for: METHYLATION AT LYS-18 AND LYS-123, PHOSPHORYLATION AT THR-129, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129 AND THR-178, ANDMASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Histone variant macroH2A1.2 is mono-ubiquitinated at its histonedomain.";
Ogawa Y., Ono T., Wakata Y., Okawa K., Tagami H., Shibahara K.;
Biochem. Biophys. Res. Commun. 336:204-209(2005).
Cited for: UBIQUITINATION AT LYS-116 AND LYS-117, AND MASS SPECTROMETRY.

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