UniProt ID | FOXP3_MOUSE | |
---|---|---|
UniProt AC | Q99JB6 | |
Protein Name | Forkhead box protein P3 | |
Gene Name | Foxp3 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 429 | |
Subcellular Localization | Nucleus . Cytoplasm . Predominantly expressed in the cytoplasm in activated conventional T-cells whereas predominantly expressed in the nucleus in regulatory T-cells (Treg) (By similarity). The 41 kDa form derived by proteolytic processing is found e | |
Protein Description | Transcriptional regulator which is crucial for the development and inhibitory function of regulatory T-cells (Treg). Plays an essential role in maintaining homeostasis of the immune system by allowing the acquisition of full suppressive function and stability of the Treg lineage, and by directly modulating the expansion and function of conventional T-cells. Can act either as a transcriptional repressor or a transcriptional activator depending on its interactions with other transcription factors, histone acetylases and deacetylases. The suppressive activity of Treg involves the coordinate activation of many genes, including CTLA4 and TNFRSF18 by FOXP3 along with repression of genes encoding cytokines such as interleukin-2 (IL2) and interferon-gamma (IFNG). Inhibits cytokine production and T-cell effector function by repressing the activity of two key transcription factors, RELA and NFATC2. [PubMed: 15790681 Mediates transcriptional repression of IL2 via its association with histone acetylase KAT5 and histone deacetylase HDAC7 (By similarity Can activate the expression of TNFRSF18, IL2RA and CTLA4 and repress the expression of IL2 and IFNG via its association with transcription factor RUNX1] | |
Protein Sequence | MPNPRPAKPMAPSLALGPSPGVLPSWKTAPKGSELLGTRGSGGPFQGRDLRSGAHTSSSLNPLPPSQLQLPTVPLVMVAPSGARLGPSPHLQALLQDRPHFMHQLSTVDAHAQTPVLQVRPLDNPAMISLPPPSAATGVFSLKARPGLPPGINVASLEWVSREPALLCTFPRSGTPRKDSNLLAAPQGSYPLLANGVCKWPGCEKVFEEPEEFLKHCQADHLLDEKGKAQCLLQREVVQSLEQQLELEKEKLGAMQAHLAGKMALAKAPSVASMDKSSCCIVATSTQGSVLPAWSAPREAPDGGLFAVRRHLWGSHGNSSFPEFFHNMDYFKYHNMRPPFTYATLIRWAILEAPERQRTLNEIYHWFTRMFAYFRNHPATWKNAIRHNLSLHKCFVRVESEKGAVWTVDEFEFRKKRSQRPNKCSNPCP | |
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 |
---|---|---|---|---|---|
19 | Phosphorylation | PSLALGPSPGVLPSW CCCCCCCCCCCCCCC | 32.27 | 23853094 | |
27 | Ubiquitination | PGVLPSWKTAPKGSE CCCCCCCCCCCCCCC | 38.86 | - | |
31 | Acetylation | PSWKTAPKGSELLGT CCCCCCCCCCCCCCC | 73.02 | 22312127 | |
33 | O-linked_Glycosylation | WKTAPKGSELLGTRG CCCCCCCCCCCCCCC | 31.06 | 30664665 | |
33 | Phosphorylation | WKTAPKGSELLGTRG CCCCCCCCCCCCCCC | 31.06 | - | |
38 | O-linked_Glycosylation | KGSELLGTRGSGGPF CCCCCCCCCCCCCCC | 31.65 | 30664665 | |
41 | Phosphorylation | ELLGTRGSGGPFQGR CCCCCCCCCCCCCCC | 36.97 | - | |
57 | O-linked_Glycosylation | LRSGAHTSSSLNPLP CCCCCCCCCCCCCCC | 14.20 | 30664665 | |
58 | O-linked_Glycosylation | RSGAHTSSSLNPLPP CCCCCCCCCCCCCCH | 39.75 | 30664665 | |
59 | O-linked_Glycosylation | SGAHTSSSLNPLPPS CCCCCCCCCCCCCHH | 31.75 | 30664665 | |
72 | O-linked_Glycosylation | PSQLQLPTVPLVMVA HHHCCCCCCCEEEEC | 43.26 | 30664665 | |
175 | Phosphorylation | CTFPRSGTPRKDSNL EECCCCCCCCCCCCC | 22.59 | 23853094 | |
249 | Ubiquitination | EQQLELEKEKLGAMQ HHHHHHHHHHHHHHH | 73.16 | 23973222 | |
251 | Ubiquitination | QLELEKEKLGAMQAH HHHHHHHHHHHHHHH | 64.39 | 23973222 | |
262 | Ubiquitination | MQAHLAGKMALAKAP HHHHHHHHHHHHCCC | 18.52 | 23973222 | |
262 | Acetylation | MQAHLAGKMALAKAP HHHHHHHHHHHHCCC | 18.52 | 22312127 | |
267 | Ubiquitination | AGKMALAKAPSVASM HHHHHHHCCCCCHHC | 62.78 | 23973222 | |
267 | Acetylation | AGKMALAKAPSVASM HHHHHHHCCCCCHHC | 62.78 | 22312127 | |
270 | O-linked_Glycosylation | MALAKAPSVASMDKS HHHHCCCCCHHCCCC | 34.86 | 30664665 | |
273 | O-linked_Glycosylation | AKAPSVASMDKSSCC HCCCCCHHCCCCCCE | 25.92 | 30664665 | |
285 | O-linked_Glycosylation | SCCIVATSTQGSVLP CCEEEEECCCCCEEE | 14.70 | 30664665 | |
286 | O-linked_Glycosylation | CCIVATSTQGSVLPA CEEEEECCCCCEEEC | 32.37 | 30664665 | |
393 | Ubiquitination | RHNLSLHKCFVRVES HHHCEEEEEEEEEEC | 34.36 | 23973222 | |
418 | Phosphorylation | FEFRKKRSQRPNKCS HHHHHHHCCCCCCCC | 39.15 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
19 | S | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
19 | S | Phosphorylation | Kinase | CDK2 | P97377 | Uniprot |
33 | S | Phosphorylation | Kinase | PIM2 | Q9P1W9 | PSP |
41 | S | Phosphorylation | Kinase | PIM2 | Q9P1W9 | PSP |
175 | T | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
175 | T | Phosphorylation | Kinase | CDK2 | P97377 | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
418 | S | Phosphorylation |
| 23853094 |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of FOXP3_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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