H2A1J_HUMAN - dbPTM
H2A1J_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID H2A1J_HUMAN
UniProt AC Q99878
Protein Name Histone H2A type 1-J
Gene Name HIST1H2AJ
Organism Homo sapiens (Human).
Sequence Length 128
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 MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTESHHKTK
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
2Phosphorylation------MSGRGKQGG
------CCCCCCCCC		36.8816319397
2Acetylation------MSGRGKQGG
------CCCCCCCCC		36.8815823041
4Citrullination----MSGRGKQGGKA
----CCCCCCCCCHH		41.66-
4Methylation----MSGRGKQGGKA
----CCCCCCCCCHH		41.66-
4Citrullination----MSGRGKQGGKA
----CCCCCCCCCHH		41.6615823041
6Methylation--MSGRGKQGGKARA
--CCCCCCCCCHHCH		44.39-
6Acetylation--MSGRGKQGGKARA
--CCCCCCCCCHHCH		44.39158671
6Other--MSGRGKQGGKARA
--CCCCCCCCCHHCH		44.3924681537
10AcetylationGRGKQGGKARAKAKT
CCCCCCCHHCHHHHH		41.34158673
10LactoylationGRGKQGGKARAKAKT
CCCCCCCHHCHHHHH		41.34-
10OtherGRGKQGGKARAKAKT
CCCCCCCHHCHHHHH		41.3427105115
10SuccinylationGRGKQGGKARAKAKT
CCCCCCCHHCHHHHH		41.3422389435
14AcetylationQGGKARAKAKTRSSR
CCCHHCHHHHHHHHC		44.8815612631
14UbiquitinationQGGKARAKAKTRSSR
CCCHHCHHHHHHHHC		44.8822980979
14OtherQGGKARAKAKTRSSR
CCCHHCHHHHHHHHC		44.8827105115
16UbiquitinationGKARAKAKTRSSRAG
CHHCHHHHHHHHCCC		43.7122980979
17PhosphorylationKARAKAKTRSSRAGL
HHCHHHHHHHHCCCC		40.4123882029
19PhosphorylationRAKAKTRSSRAGLQF
CHHHHHHHHCCCCCC		29.4323312004
20PhosphorylationAKAKTRSSRAGLQFP
HHHHHHHHCCCCCCC		23.9027966365
21MethylationKAKTRSSRAGLQFPV
HHHHHHHCCCCCCCH		33.64-
30MethylationGLQFPVGRVHRLLRK
CCCCCHHHHHHHHHC		22.69-
37N6-crotonyl-L-lysineRVHRLLRKGNYAERV
HHHHHHHCCCHHHHC		52.02-
37UbiquitinationRVHRLLRKGNYAERV
HHHHHHHCCCHHHHC		52.0227667366
37OtherRVHRLLRKGNYAERV
HHHHHHHCCCHHHHC		52.0227105115
37CrotonylationRVHRLLRKGNYAERV
HHHHHHHCCCHHHHC		52.0221925322
40PhosphorylationRLLRKGNYAERVGAG
HHHHCCCHHHHCCCC		20.6428152594
58PhosphorylationYLAAVLEYLTAEILE
HHHHHHHHHHHHHHH		12.75-
75OtherGNAARDNKKTRIIPR
CHHHHCCCCCCEEHH		60.8724681537
76OtherNAARDNKKTRIIPRH
HHHHCCCCCCEEHHH		49.6524681537
77PhosphorylationAARDNKKTRIIPRHL
HHHCCCCCCEEHHHH		28.8023882029
82MethylationKKTRIIPRHLQLAIR
CCCCEEHHHHHHHHC		32.51-
89MethylationRHLQLAIRNDEELNK
HHHHHHHCCHHHHHH		38.65-
96GlutarylationRNDEELNKLLGKVTI
CCHHHHHHHHCCEEE		58.6831542297
96OtherRNDEELNKLLGKVTI
CCHHHHHHHHCCEEE		58.6827105115
96UbiquitinationRNDEELNKLLGKVTI
CCHHHHHHHHCCEEE		58.6821890473
96AcetylationRNDEELNKLLGKVTI
CCHHHHHHHHCCEEE		58.6822389435
96NeddylationRNDEELNKLLGKVTI
CCHHHHHHHHCCEEE		58.6832015554
96SuccinylationRNDEELNKLLGKVTI
CCHHHHHHHHCCEEE		58.6822389435
96UbiquitinationRNDEELNKLLGKVTI
CCHHHHHHHHCCEEE		58.6823000965
100UbiquitinationELNKLLGKVTIAQGG
HHHHHHCCEEECCCC		35.8523000965
100GlutarylationELNKLLGKVTIAQGG
HHHHHHCCEEECCCC		35.8531542297
100AcetylationELNKLLGKVTIAQGG
HHHHHHCCEEECCCC		35.85158629
102PhosphorylationNKLLGKVTIAQGGVL
HHHHCCEEECCCCCC		17.6824732914
105MethylationLGKVTIAQGGVLPNI
HCCEEECCCCCCCCE		45.3724352239
119NeddylationIQAVLLPKKTESHHK
EEEEECCCCCCCCCC		72.7632015554
119AcetylationIQAVLLPKKTESHHK
EEEEECCCCCCCCCC		72.76158659
119N6-crotonyl-L-lysineIQAVLLPKKTESHHK
EEEEECCCCCCCCCC		72.76-
119SumoylationIQAVLLPKKTESHHK
EEEEECCCCCCCCCC		72.76-
119UbiquitinationIQAVLLPKKTESHHK
EEEEECCCCCCCCCC		72.7623000965
119GlutarylationIQAVLLPKKTESHHK
EEEEECCCCCCCCCC		72.7631542297
119OtherIQAVLLPKKTESHHK
EEEEECCCCCCCCCC		72.7627105115
119CrotonylationIQAVLLPKKTESHHK
EEEEECCCCCCCCCC		72.7621925322
120CrotonylationQAVLLPKKTESHHKT
EEEECCCCCCCCCCC		56.4321925322
120GlutarylationQAVLLPKKTESHHKT
EEEECCCCCCCCCCC		56.4331542297
120N6-crotonyl-L-lysineQAVLLPKKTESHHKT
EEEECCCCCCCCCCC		56.43-
120AcetylationQAVLLPKKTESHHKT
EEEECCCCCCCCCCC		56.43164059
120UbiquitinationQAVLLPKKTESHHKT
EEEECCCCCCCCCCC		56.4323000965
121PhosphorylationAVLLPKKTESHHKTK
EEECCCCCCCCCCCC		49.1722617229
123PhosphorylationLLPKKTESHHKTK--
ECCCCCCCCCCCC--		35.8022617229
126CrotonylationKKTESHHKTK-----
CCCCCCCCCC-----		53.2221925322
126GlutarylationKKTESHHKTK-----
CCCCCCCCCC-----		53.2231542297
126N6-crotonyl-L-lysineKKTESHHKTK-----
CCCCCCCCCC-----		53.22-
126UbiquitinationKKTESHHKTK-----
CCCCCCCCCC-----		53.2223000965
128UbiquitinationTESHHKTK-------
CCCCCCCC-------		64.25-
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
2SPhosphorylationKinaseRPS6KA5O75582
Uniprot
121TPhosphorylationKinaseDCAF1Q9Y4B6
Uniprot
-KUbiquitinationE3 ubiquitin ligaseBMI1P35226
PMID:16359901
-KUbiquitinationE3 ubiquitin ligaseBMI1#RNF2P35226#Q99496
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
2SAcetylation

15010469
2SPhosphorylation

15010469
2SPhosphorylation

15010469
2SPhosphorylation

15010469
4RMethylation

15823041
14Kubiquitylation

22980979
14Kubiquitylation

22980979
16Kubiquitylation

22980979
16Kubiquitylation

22980979
27KMethylation

15386022
27Kubiquitylation

15386022
63Kubiquitylation

15386022
105QMethylation

24352239
120Kubiquitylation

15386022
120Kubiquitylation

15386022
121TPhosphorylation

15078818
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 H2A1J_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of H2A1J_HUMAN !!
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 H2A1J_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Precise characterization of human histones in the H2A gene family bytop down mass spectrometry.";
Boyne M.T. II, Pesavento J.J., Mizzen C.A., Kelleher N.L.;
J. Proteome Res. 5:248-253(2006).
Cited for: MASS SPECTROMETRY, AND ACETYLATION AT SER-2.
"Deimination of histone H2A and H4 at arginine 3 in HL-60granulocytes.";
Hagiwara T., Hidaka Y., Yamada M.;
Biochemistry 44:5827-5834(2005).
Cited for: ACETYLATION AT SER-2, CITRULLINATION AT ARG-4, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 PHOSPHORYLATION AT SER-2.
"Phosphorylation of histone H2A inhibits transcription on chromatintemplates.";
Zhang Y., Griffin K., Mondal N., Parvin J.D.;
J. Biol. Chem. 279:21866-21872(2004).
Cited for: PHOSPHORYLATION AT SER-2, AND MUTAGENESIS OF SER-2.
Ubiquitylation
ReferencePubMed
"DNA damage triggers nucleotide excision repair-dependentmonoubiquitylation of histone H2A.";
Bergink S., Salomons F.A., Hoogstraten D., Groothuis T.A.M.,de Waard H., Wu J., Yuan L., Citterio E., Houtsmuller A.B.,Neefjes J., Hoeijmakers J.H.J., Vermeulen W., Dantuma N.P.;
Genes Dev. 20:1343-1352(2006).
Cited for: UBIQUITINATION AT LYS-120.
"Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox genesilencing.";
Cao R., Tsukada Y., Zhang Y.;
Mol. Cell 20:845-854(2005).
Cited for: UBIQUITINATION AT LYS-120.
"Role of histone H2A ubiquitination in Polycomb silencing.";
Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P.,Jones R.S., Zhang Y.;
Nature 431:873-878(2004).
Cited for: UBIQUITINATION AT LYS-120.

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