UniProt ID | HM20A_HUMAN | |
---|---|---|
UniProt AC | Q9NP66 | |
Protein Name | High mobility group protein 20A | |
Gene Name | HMG20A | |
Organism | Homo sapiens (Human). | |
Sequence Length | 347 | |
Subcellular Localization | Nucleus . | |
Protein Description | Plays a role in neuronal differentiation as chromatin-associated protein. Acts as inhibitor of HMG20B. Overcomes the repressive effects of the neuronal silencer REST and induces the activation of neuronal-specific genes. Involved in the recruitment of the histone methyltransferase KMT2A/MLL1 and consequent increased methylation of histone H3 lysine 4 (By similarity).. | |
Protein Sequence | MENLMTSSTLPPLFADEDGSKESNDLATTGLNHPEVPYSSGATSSTNNPEFVEDLSQGQLLQSESSNAAEGNEQRHEDEQRSKRGGWSKGRKRKKPLRDSNAPKSPLTGYVRFMNERREQLRAKRPEVPFPEITRMLGNEWSKLPPEEKQRYLDEADRDKERYMKELEQYQKTEAYKVFSRKTQDRQKGKSHRQDAARQATHDHEKETEVKERSVFDIPIFTEEFLNHSKAREAELRQLRKSNMEFEERNAALQKHVESMRTAVEKLEVDVIQERSRNTVLQQHLETLRQVLTSSFASMPLPGSGETPTVDTIDSYMNRLHSIILANPQDNENFIATVREVVNRLDR | |
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 |
---|---|---|---|---|---|
6 | Phosphorylation | --MENLMTSSTLPPL --CCCCCCCCCCCCC | 23.77 | - | |
7 | Phosphorylation | -MENLMTSSTLPPLF -CCCCCCCCCCCCCC | 13.83 | 28348404 | |
8 | Phosphorylation | MENLMTSSTLPPLFA CCCCCCCCCCCCCCC | 25.46 | 28348404 | |
9 | Phosphorylation | ENLMTSSTLPPLFAD CCCCCCCCCCCCCCC | 42.95 | 28348404 | |
20 | Phosphorylation | LFADEDGSKESNDLA CCCCCCCCCCCCCCC | 45.64 | 25159151 | |
100 | Phosphorylation | RKKPLRDSNAPKSPL CCCCCCCCCCCCCCC | 28.58 | 25159151 | |
105 | Phosphorylation | RDSNAPKSPLTGYVR CCCCCCCCCCHHHHH | 24.88 | 22167270 | |
108 | Phosphorylation | NAPKSPLTGYVRFMN CCCCCCCHHHHHHHH | 29.83 | 23927012 | |
110 | Phosphorylation | PKSPLTGYVRFMNER CCCCCHHHHHHHHHH | 5.34 | 23927012 | |
152 | Phosphorylation | PPEEKQRYLDEADRD CHHHHHHHHHHHHHH | 18.93 | 22817900 | |
163 | Phosphorylation | ADRDKERYMKELEQY HHHHHHHHHHHHHHH | 17.40 | 22817900 | |
165 | Ubiquitination | RDKERYMKELEQYQK HHHHHHHHHHHHHHH | 50.65 | - | |
170 | Phosphorylation | YMKELEQYQKTEAYK HHHHHHHHHHHHHHH | 11.55 | 22817900 | |
172 | Acetylation | KELEQYQKTEAYKVF HHHHHHHHHHHHHHH | 43.32 | 26051181 | |
172 | Ubiquitination | KELEQYQKTEAYKVF HHHHHHHHHHHHHHH | 43.32 | - | |
173 | Phosphorylation | ELEQYQKTEAYKVFS HHHHHHHHHHHHHHC | 15.43 | - | |
176 | Phosphorylation | QYQKTEAYKVFSRKT HHHHHHHHHHHCHHH | 11.06 | - | |
177 | Acetylation | YQKTEAYKVFSRKTQ HHHHHHHHHHCHHHH | 43.80 | 26051181 | |
177 | Ubiquitination | YQKTEAYKVFSRKTQ HHHHHHHHHHCHHHH | 43.80 | - | |
230 | Ubiquitination | EEFLNHSKAREAELR HHHHCHHHHHHHHHH | 43.86 | - | |
255 | Ubiquitination | ERNAALQKHVESMRT HHHHHHHHHHHHHHH | 50.93 | - | |
287 | Phosphorylation | VLQQHLETLRQVLTS HHHHHHHHHHHHHHH | 33.33 | - |
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 HM20A_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HM20A_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 HM20A_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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Phosphorylation | |
Reference | PubMed |
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND MASSSPECTROMETRY. | |
"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-105, AND MASSSPECTROMETRY. | |
"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 SER-105, AND MASSSPECTROMETRY. |