UniProt ID | HMGN4_HUMAN | |
---|---|---|
UniProt AC | O00479 | |
Protein Name | High mobility group nucleosome-binding domain-containing protein 4 | |
Gene Name | HMGN4 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 90 | |
Subcellular Localization | Nucleus. | |
Protein Description | ||
Protein Sequence | MPKRKAKGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPRPKKASAKKGEKLPKGRKGKADAGKDGNNPAKNRDASTLQSQKAEGTGDAK | |
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 |
---|---|---|---|---|---|
7 | Acetylation | -MPKRKAKGDAKGDK -CCCCCCCCCCCCCH | 61.43 | 7354851 | |
14 | Acetylation | KGDAKGDKAKVKDEP CCCCCCCHHHCCCCH | 59.79 | 7354859 | |
18 | Succinylation | KGDKAKVKDEPQRRS CCCHHHCCCCHHHHH | 56.52 | 23954790 | |
25 | Phosphorylation | KDEPQRRSARLSAKP CCCHHHHHHHHCCCC | 21.67 | 29496963 | |
29 | Phosphorylation | QRRSARLSAKPAPPK HHHHHHHCCCCCCCC | 28.79 | 25159151 | |
29 | ADP-ribosylation | QRRSARLSAKPAPPK HHHHHHHCCCCCCCC | 28.79 | 28190768 | |
31 | Acetylation | RSARLSAKPAPPKPE HHHHHCCCCCCCCCC | 38.03 | 23954790 | |
31 | Succinylation | RSARLSAKPAPPKPE HHHHHCCCCCCCCCC | 38.03 | 23954790 | |
31 | Ubiquitination | RSARLSAKPAPPKPE HHHHHCCCCCCCCCC | 38.03 | - | |
36 | Acetylation | SAKPAPPKPEPRPKK CCCCCCCCCCCCCCC | 62.04 | 26051181 | |
51 | Acetylation | ASAKKGEKLPKGRKG CCCCCCCCCCCCCCC | 77.94 | 25953088 | |
64 | Acetylation | KGKADAGKDGNNPAK CCCCCCCCCCCCHHH | 65.27 | 26051181 | |
71 | Ubiquitination | KDGNNPAKNRDASTL CCCCCHHHCCCHHHH | 54.49 | - | |
71 | Acetylation | KDGNNPAKNRDASTL CCCCCHHHCCCHHHH | 54.49 | 22361335 | |
76 | Phosphorylation | PAKNRDASTLQSQKA HHHCCCHHHHHHHHH | 33.66 | 21712546 | |
77 | Phosphorylation | AKNRDASTLQSQKAE HHCCCHHHHHHHHHC | 30.45 | 23663014 | |
80 | Phosphorylation | RDASTLQSQKAEGTG CCHHHHHHHHHCCCC | 36.44 | 23401153 | |
82 | Acetylation | ASTLQSQKAEGTGDA HHHHHHHHHCCCCCC | 54.36 | 19608861 | |
86 | Phosphorylation | QSQKAEGTGDAK--- HHHHHCCCCCCC--- | 24.32 | 23403867 | |
90 | Acetylation | AEGTGDAK------- HCCCCCCC------- | 66.66 | 61175 |
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 HMGN4_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HMGN4_HUMAN !! |
* 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 HMGN4_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of HMGN4_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-82, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"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 SER-80, AND MASSSPECTROMETRY. |