UniProt ID | SOX2_HUMAN | |
---|---|---|
UniProt AC | P48431 | |
Protein Name | Transcription factor SOX-2 | |
Gene Name | SOX2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 317 | |
Subcellular Localization | Nucleus. | |
Protein Description | Transcription factor that forms a trimeric complex with OCT4 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206 (By similarity). Critical for early embryogenesis and for embryonic stem cell pluripotency. May function as a switch in neuronal development. Downstream SRRT target that mediates the promotion of neural stem cell self-renewal (By similarity). Keeps neural cells undifferentiated by counteracting the activity of proneural proteins and suppresses neuronal differentiation (By similarity).. | |
Protein Sequence | MYNMMETELKPPGPQQTSGGGGGNSTAAAAGGNQKNSPDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKLLSETEKRPFIDEAKRLRALHMKEHPDYKYRPRRKTKTLMKKDKYTLPGGLLAPGGNSMASGVGVGAGLGAGVNQRMDSYAHMNGWSNGSYSMMQDQLGYPQHPGLNAHGAAQMQPMHRYDVSALQYNSMTSSQTYMNGSPTYSMSYSQQGTPGMALGSMGSVVKSEASSSPPVVTSSSHSRAPCQAGDLRDMISMYLPGAEVPEPAAPSRLHMSQHYQSGPVPGTAINGTLPLSHM | |
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 |
---|---|---|---|---|---|
18 | Phosphorylation | PPGPQQTSGGGGGNS CCCCCCCCCCCCCCC | 30.97 | 22210691 | |
25 | Phosphorylation | SGGGGGNSTAAAAGG CCCCCCCCHHHHCCC | 23.77 | 22210691 | |
26 | Phosphorylation | GGGGGNSTAAAAGGN CCCCCCCHHHHCCCC | 25.06 | 22210691 | |
37 | Phosphorylation | AGGNQKNSPDRVKRP CCCCCCCCHHHCCCH | 34.90 | 21406692 | |
52 | Phosphorylation | MNAFMVWSRGQRRKM HHHHHHCCHHHHHHH | 18.34 | 30631047 | |
69 | Phosphorylation | ENPKMHNSEISKRLG HCCCCCHHHHHHHHC | 22.94 | - | |
73 | Acetylation | MHNSEISKRLGAEWK CCHHHHHHHHCHHHH | 58.25 | 18585111 | |
118 | Phosphorylation | RPRRKTKTLMKKDKY CCCCCCCCCCCCCCC | 37.00 | - | |
121 | Ubiquitination | RKTKTLMKKDKYTLP CCCCCCCCCCCCCCC | 62.02 | - | |
125 | Phosphorylation | TLMKKDKYTLPGGLL CCCCCCCCCCCCCEE | 24.52 | 22474382 | |
126 | Phosphorylation | LMKKDKYTLPGGLLA CCCCCCCCCCCCEEC | 32.02 | 22474382 | |
138 | Phosphorylation | LLAPGGNSMASGVGV EECCCCCCCCCCCCC | 20.99 | 22474382 | |
245 | Sumoylation | GSMGSVVKSEASSSP CCHHHEEHHHHCCCC | 40.18 | - | |
245 | Sumoylation | GSMGSVVKSEASSSP CCHHHEEHHHHCCCC | 40.18 | - | |
246 | Phosphorylation | SMGSVVKSEASSSPP CHHHEEHHHHCCCCC | 27.13 | 19144917 | |
246 | O-linked_Glycosylation | SMGSVVKSEASSSPP CHHHEEHHHHCCCCC | 27.13 | 30620550 | |
249 | Phosphorylation | SVVKSEASSSPPVVT HEEHHHHCCCCCEEC | 27.57 | 30631047 | |
250 | Phosphorylation | VVKSEASSSPPVVTS EEHHHHCCCCCEECC | 54.64 | 22617229 | |
251 | Phosphorylation | VKSEASSSPPVVTSS EHHHHCCCCCEECCC | 30.63 | 22617229 | |
256 | O-linked_Glycosylation | SSSPPVVTSSSHSRA CCCCCEECCCCCCCC | 24.11 | 30620550 | |
256 | Phosphorylation | SSSPPVVTSSSHSRA CCCCCEECCCCCCCC | 24.11 | 21406692 | |
257 | Phosphorylation | SSPPVVTSSSHSRAP CCCCEECCCCCCCCC | 20.45 | 21406692 | |
258 | Phosphorylation | SPPVVTSSSHSRAPC CCCEECCCCCCCCCC | 23.78 | 21406692 | |
259 | Phosphorylation | PPVVTSSSHSRAPCQ CCEECCCCCCCCCCC | 25.83 | 21406692 | |
261 | Phosphorylation | VVTSSSHSRAPCQAG EECCCCCCCCCCCCC | 31.89 | 23312004 | |
277 | Phosphorylation | LRDMISMYLPGAEVP HHHHHHHCCCCCCCC | 11.71 | - |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SOX2_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 SOX2_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
206900 | Microphthalmia, syndromic, 3 (MCOPS3) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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