UniProt ID | CITE2_HUMAN | |
---|---|---|
UniProt AC | Q99967 | |
Protein Name | Cbp/p300-interacting transactivator 2 | |
Gene Name | CITED2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 270 | |
Subcellular Localization | Nucleus . Colocalizes with EP300 in dot-like structures. | |
Protein Description | Transcriptional coactivator of the p300/CBP-mediated transcription complex. Acts as a bridge, linking TFAP2 transcription factors and the p300/CBP transcriptional coactivator complex in order to stimulate TFAP2-mediated transcriptional activation. Positively regulates TGF-beta signaling through its association with the SMAD/p300/CBP-mediated transcriptional coactivator complex. Stimulates the peroxisome proliferator-activated receptors PPARA transcriptional activity. Enhances estrogen-dependent transactivation mediated by estrogen receptors. Acts also as a transcriptional corepressor; interferes with the binding of the transcription factors HIF1A or STAT2 and the p300/CBP transcriptional coactivator complex. Participates in sex determination and early gonad development by stimulating transcription activation of SRY. Plays a role in controlling left-right patterning during embryogenesis; potentiates transcriptional activation of NODAL-mediated gene transcription in the left lateral plate mesoderm (LPM). Plays an essential role in differentiation of the adrenal cortex from the adrenogonadal primordium (AGP); stimulates WT1-mediated transcription activation thereby up-regulating the nuclear hormone receptor NR5A1 promoter activity. Associates with chromatin to the PITX2 P1 promoter region.. | |
Protein Sequence | MADHMMAMNHGRFPDGTNGLHHHPAHRMGMGQFPSPHHHQQQQPQHAFNALMGEHIHYGAGNMNATSGIRHAMGPGTVNGGHPPSALAPAARFNNSQFMGPPVASQGGSLPASMQLQKLNNQYFNHHPYPHNHYMPDLHPAAGHQMNGTNQHFRDCNPKHSGGSSTPGGSGGSSTPGGSGSSSGGGAGSSNSGGGSGSGNMPASVAHVPAAMLPPNVIDTDFIDEEVLMSLVIEMGLDRIKELPELWLGQNEFDFMTDFVCKQQPSRVSC | |
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 |
---|---|---|---|---|---|
12 | Methylation | MMAMNHGRFPDGTNG CCCCCCCCCCCCCCC | 32.16 | - | |
85 | Phosphorylation | VNGGHPPSALAPAAR CCCCCCHHHHCCCHH | 40.12 | - | |
166 | Phosphorylation | KHSGGSSTPGGSGGS CCCCCCCCCCCCCCC | 27.87 | - | |
175 | Phosphorylation | GGSGGSSTPGGSGSS CCCCCCCCCCCCCCC | 27.87 | - | |
266 | Phosphorylation | FVCKQQPSRVSC--- HHHCCCCCCCCC--- | 40.76 | 28102081 | |
269 | Phosphorylation | KQQPSRVSC------ CCCCCCCCC------ | 17.01 | 28102081 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CITE2_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 CITE2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
AP2A_HUMAN | TFAP2A | physical | 12586840 | |
AP2C_HUMAN | TFAP2C | physical | 12586840 | |
AP2A_HUMAN | TFAP2A | physical | 11744733 | |
AP2B_HUMAN | TFAP2B | physical | 11744733 | |
AP2C_HUMAN | TFAP2C | physical | 11744733 | |
EP300_HUMAN | EP300 | physical | 10593900 | |
TBP_HUMAN | TBP | physical | 10593900 | |
SMAD3_HUMAN | SMAD3 | physical | 16619037 | |
EP300_HUMAN | EP300 | physical | 12778114 | |
FBXL5_HUMAN | FBXL5 | physical | 25956243 | |
EP300_HUMAN | EP300 | physical | 25956243 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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