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 | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSGRGKQGG ------CCCCCCCCC | 36.88 | 21406692 | |
6 | Acetylation | --MSGRGKQGGKVRA --CCCCCCCCCCCCH | 44.39 | 158541 | |
6 | Lactylation | --MSGRGKQGGKVRA --CCCCCCCCCCCCH | 44.39 | 31645732 | |
6 | Ubiquitination | --MSGRGKQGGKVRA --CCCCCCCCCCCCH | 44.39 | - | |
10 | Ubiquitination | GRGKQGGKVRAKAKS CCCCCCCCCCHHCCC | 35.06 | - | |
10 | Acetylation | GRGKQGGKVRAKAKS CCCCCCCCCCHHCCC | 35.06 | 26051181 | |
10 | Lactylation | GRGKQGGKVRAKAKS CCCCCCCCCCHHCCC | 35.06 | 31645732 | |
10 | Lactoylation | GRGKQGGKVRAKAKS CCCCCCCCCCHHCCC | 35.06 | - | |
17 | Phosphorylation | KVRAKAKSRSSRAGL CCCHHCCCCCCCCCC | 42.10 | 23882029 | |
19 | Phosphorylation | RAKAKSRSSRAGLQF CHHCCCCCCCCCCCC | 31.13 | 30622161 | |
20 | Phosphorylation | AKAKSRSSRAGLQFP HHCCCCCCCCCCCCC | 25.66 | 27966365 | |
21 | Methylation | KAKSRSSRAGLQFPV HCCCCCCCCCCCCCH | 33.64 | - | |
30 | Methylation | GLQFPVGRVHRLLRK CCCCCHHHHHHHHHC | 22.69 | - | |
37 (in isoform 2) | Ubiquitination | - | 52.02 | 21890473 | |
37 (in isoform 1) | Ubiquitination | - | 52.02 | 21890473 | |
37 | Ubiquitination | RVHRLLRKGNYAERV HHHHHHHCCCHHHHC | 52.02 | 21906983 | |
40 | Phosphorylation | RLLRKGNYAERVGAG HHHHCCCHHHHCCCC | 20.64 | 28152594 | |
58 | Phosphorylation | YLAAVLEYLTAEILE HHHHHHHHHHHHHHH | 12.75 | - | |
77 | Phosphorylation | AARDNKKTRIIPRHL HHHCCCCCCEEHHHH | 28.80 | 23882029 | |
82 | Methylation | KKTRIIPRHLQLAIR CCCCEEHHHHHHHHC | 32.51 | - | |
89 | Methylation | RHLQLAIRNDEELNK HHHHHHHCCHHHHHH | 38.65 | - | |
96 (in isoform 1) | Ubiquitination | - | 58.68 | 21890473 | |
96 (in isoform 2) | Ubiquitination | - | 58.68 | 21890473 | |
96 | Acetylation | RNDEELNKLLGKVTI CCHHHHHHHHCCEEE | 58.68 | 8395049 | |
96 | Ubiquitination | RNDEELNKLLGKVTI CCHHHHHHHHCCEEE | 58.68 | 21906983 | |
100 (in isoform 1) | Ubiquitination | - | 35.85 | 21890473 | |
100 | Acetylation | ELNKLLGKVTIAQGG HHHHHHCCEEECCCC | 35.85 | 24471261 | |
100 | Ubiquitination | ELNKLLGKVTIAQGG HHHHHHCCEEECCCC | 35.85 | 21906983 | |
102 | Phosphorylation | NKLLGKVTIAQGGVL HHHHCCEEECCCCCC | 17.68 | 20068231 | |
105 | Methylation | LGKVTIAQGGVLPNI HCCEEECCCCCCCCE | 45.37 | - | |
119 | Acetylation | IQAVLLPKKTESQKT EEEEECCCCCCCCCC | 72.76 | 23236377 | |
119 (in isoform 1) | Ubiquitination | - | 72.76 | 21890473 | |
119 | Sumoylation | IQAVLLPKKTESQKT EEEEECCCCCCCCCC | 72.76 | - | |
119 | Ubiquitination | IQAVLLPKKTESQKT EEEEECCCCCCCCCC | 72.76 | 18781797 | |
119 | Sumoylation | IQAVLLPKKTESQKT EEEEECCCCCCCCCC | 72.76 | - | |
120 | Acetylation | QAVLLPKKTESQKTK EEEECCCCCCCCCCC | 56.43 | 15177633 | |
120 | Ubiquitination | QAVLLPKKTESQKTK EEEECCCCCCCCCCC | 56.43 | 21906983 | |
121 | Phosphorylation | AVLLPKKTESQKTKS EEECCCCCCCCCCCC | 47.17 | 20068231 | |
123 | Phosphorylation | LLPKKTESQKTKSK- ECCCCCCCCCCCCC- | 42.06 | 25849741 | |
125 | Ubiquitination | PKKTESQKTKSK--- CCCCCCCCCCCC--- | 68.17 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
121 | T | Phosphorylation | Kinase | DCAF1 | Q9Y4B6 | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
2 | S | Acetylation |
| - |
2 | S | Phosphorylation |
| - |
2 | S | Phosphorylation |
| - |
2 | S | Phosphorylation |
| - |
63 | K | ubiquitylation |
| - |
105 | Q | Methylation |
| - |
120 | K | ubiquitylation |
| - |
121 | T | Phosphorylation |
| - |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of H2AJ_HUMAN !! |
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. |
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Acetylation | |
Reference | PubMed |
"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. |