H2AJ_HUMAN - dbPTM
H2AJ_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID H2AJ_HUMAN
UniProt AC Q9BTM1
Protein Name Histone H2A.J
Gene Name H2AFJ
Organism Homo sapiens (Human).
Sequence Length 129
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 MSGRGKQGGKVRAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTESQKTKSK
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
36.8821406692
6Acetylation--MSGRGKQGGKVRA
--CCCCCCCCCCCCH
44.39158541
6Lactylation--MSGRGKQGGKVRA
--CCCCCCCCCCCCH
44.3931645732
6Ubiquitination--MSGRGKQGGKVRA
--CCCCCCCCCCCCH
44.39-
10UbiquitinationGRGKQGGKVRAKAKS
CCCCCCCCCCHHCCC
35.06-
10AcetylationGRGKQGGKVRAKAKS
CCCCCCCCCCHHCCC
35.0626051181
10LactylationGRGKQGGKVRAKAKS
CCCCCCCCCCHHCCC
35.0631645732
10LactoylationGRGKQGGKVRAKAKS
CCCCCCCCCCHHCCC
35.06-
17PhosphorylationKVRAKAKSRSSRAGL
CCCHHCCCCCCCCCC
42.1023882029
19PhosphorylationRAKAKSRSSRAGLQF
CHHCCCCCCCCCCCC
31.1330622161
20PhosphorylationAKAKSRSSRAGLQFP
HHCCCCCCCCCCCCC
25.6627966365
21MethylationKAKSRSSRAGLQFPV
HCCCCCCCCCCCCCH
33.64-
30MethylationGLQFPVGRVHRLLRK
CCCCCHHHHHHHHHC
22.69-
37 (in isoform 2)Ubiquitination-52.0221890473
37 (in isoform 1)Ubiquitination-52.0221890473
37UbiquitinationRVHRLLRKGNYAERV
HHHHHHHCCCHHHHC
52.0221906983
40PhosphorylationRLLRKGNYAERVGAG
HHHHCCCHHHHCCCC
20.6428152594
58PhosphorylationYLAAVLEYLTAEILE
HHHHHHHHHHHHHHH
12.75-
77PhosphorylationAARDNKKTRIIPRHL
HHHCCCCCCEEHHHH
28.8023882029
82MethylationKKTRIIPRHLQLAIR
CCCCEEHHHHHHHHC
32.51-
89MethylationRHLQLAIRNDEELNK
HHHHHHHCCHHHHHH
38.65-
96 (in isoform 1)Ubiquitination-58.6821890473
96 (in isoform 2)Ubiquitination-58.6821890473
96AcetylationRNDEELNKLLGKVTI
CCHHHHHHHHCCEEE
58.688395049
96UbiquitinationRNDEELNKLLGKVTI
CCHHHHHHHHCCEEE
58.6821906983
100 (in isoform 1)Ubiquitination-35.8521890473
100AcetylationELNKLLGKVTIAQGG
HHHHHHCCEEECCCC
35.8524471261
100UbiquitinationELNKLLGKVTIAQGG
HHHHHHCCEEECCCC
35.8521906983
102PhosphorylationNKLLGKVTIAQGGVL
HHHHCCEEECCCCCC
17.6820068231
105MethylationLGKVTIAQGGVLPNI
HCCEEECCCCCCCCE
45.37-
119AcetylationIQAVLLPKKTESQKT
EEEEECCCCCCCCCC
72.7623236377
119 (in isoform 1)Ubiquitination-72.7621890473
119SumoylationIQAVLLPKKTESQKT
EEEEECCCCCCCCCC
72.76-
119UbiquitinationIQAVLLPKKTESQKT
EEEEECCCCCCCCCC
72.7618781797
119SumoylationIQAVLLPKKTESQKT
EEEEECCCCCCCCCC
72.76-
120AcetylationQAVLLPKKTESQKTK
EEEECCCCCCCCCCC
56.4315177633
120UbiquitinationQAVLLPKKTESQKTK
EEEECCCCCCCCCCC
56.4321906983
121PhosphorylationAVLLPKKTESQKTKS
EEECCCCCCCCCCCC
47.1720068231
123PhosphorylationLLPKKTESQKTKSK-
ECCCCCCCCCCCCC-
42.0625849741
125UbiquitinationPKKTESQKTKSK---
CCCCCCCCCCCC---
68.17-

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
121TPhosphorylationKinaseDCAF1Q9Y4B6
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
2SAcetylation

-
2SPhosphorylation

-
2SPhosphorylation

-
2SPhosphorylation

-
63Kubiquitylation

-
105QMethylation

-
120Kubiquitylation

-
121TPhosphorylation

-

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 H2AJ_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of H2AJ_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 H2AJ_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-96, AND MASS SPECTROMETRY.

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