CITE2_HUMAN - dbPTM
CITE2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
12MethylationMMAMNHGRFPDGTNG
CCCCCCCCCCCCCCC
32.16-
85PhosphorylationVNGGHPPSALAPAAR
CCCCCCHHHHCCCHH
40.12-
166PhosphorylationKHSGGSSTPGGSGGS
CCCCCCCCCCCCCCC
27.87-
175PhosphorylationGGSGGSSTPGGSGSS
CCCCCCCCCCCCCCC
27.87-
266PhosphorylationFVCKQQPSRVSC---
HHHCCCCCCCCC---
40.7628102081
269PhosphorylationKQQPSRVSC------
CCCCCCCCC------
17.0128102081

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
85SPhosphorylationKinaseERK2P28482
PSP
166TPhosphorylationKinaseERK2P28482
PSP
175TPhosphorylationKinaseERK2P28482
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CITE2_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AP2A_HUMANTFAP2Aphysical
12586840
AP2C_HUMANTFAP2Cphysical
12586840
AP2A_HUMANTFAP2Aphysical
11744733
AP2B_HUMANTFAP2Bphysical
11744733
AP2C_HUMANTFAP2Cphysical
11744733
EP300_HUMANEP300physical
10593900
TBP_HUMANTBPphysical
10593900
SMAD3_HUMANSMAD3physical
16619037
EP300_HUMANEP300physical
12778114
FBXL5_HUMANFBXL5physical
25956243
EP300_HUMANEP300physical
25956243

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CITE2_HUMAN

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Related Literatures of Post-Translational Modification

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