FOXP3_HUMAN - dbPTM
FOXP3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FOXP3_HUMAN
UniProt AC Q9BZS1
Protein Name Forkhead box protein P3
Gene Name FOXP3
Organism Homo sapiens (Human).
Sequence Length 431
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). The 41 kDa form derived by proteolytic processing is found exclusively in th
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]
Protein Sequence MPNPRPGKPSAPSLALGPSPGASPSWRAAPKASDLLGARGPGGTFQGRDLRGGAHASSSSLNPMPPSQLQLPTLPLVMVAPSGARLGPLPHLQALLQDRPHFMHQLSTVDAHARTPVLQVHPLESPAMISLTPPTTATGVFSLKARPGLPPGINVASLEWVSREPALLCTFPNPSAPRKDSTLSAVPQSSYPLLANGVCKWPGCEKVFEEPEDFLKHCQADHLLDEKGRAQCLLQREMVQSLEQQLVLEKEKLSAMQAHLAGKMALTKASSVASSDKGSCCIVAAGSQGPVVPAWSGPREAPDSLFAVRRHLWGSHGNSTFPEFLHNMDYFKFHNMRPPFTYATLIRWAILEAPEKQRTLNEIYHWFTRMFAFFRNHPATWKNAIRHNLSLHKCFVRVESEKGAVWTVDELEFRKKRSQRPSRCSNPTPGP
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
10PhosphorylationNPRPGKPSAPSLALG
CCCCCCCCCCCCCCC
57.1922210691
19PhosphorylationPSLALGPSPGASPSW
CCCCCCCCCCCCCHH
33.8822210691
23PhosphorylationLGPSPGASPSWRAAP
CCCCCCCCCHHHCCC
25.9422210691
25PhosphorylationPSPGASPSWRAAPKA
CCCCCCCHHHCCCCH
27.0526091039
31AcetylationPSWRAAPKASDLLGA
CHHHCCCCHHHHCCC
56.6622312127
33PhosphorylationWRAAPKASDLLGARG
HHCCCCHHHHCCCCC
34.61-
44PhosphorylationGARGPGGTFQGRDLR
CCCCCCCCCCCCCCC
20.78-
107PhosphorylationPHFMHQLSTVDAHAR
CCHHHHHHHCCHHCC
21.5822210691
115PhosphorylationTVDAHARTPVLQVHP
HCCHHCCCCEEEEEC
20.6622210691
138PhosphorylationLTPPTTATGVFSLKA
ECCCCCCCEEEEEEE
31.6122210691
142PhosphorylationTTATGVFSLKARPGL
CCCCEEEEEEECCCC
26.93-
179AcetylationPNPSAPRKDSTLSAV
CCCCCCCCCCCCCCC
55.7863828001
227AcetylationADHLLDEKGRAQCLL
HHHHCCHHHHHHHHH
54.0563828003
250AcetylationEQQLVLEKEKLSAMQ
HHHHHHCHHHHHHHH
56.8663827999
252AcetylationQLVLEKEKLSAMQAH
HHHHCHHHHHHHHHH
59.8363828005
263AcetylationMQAHLAGKMALTKAS
HHHHHHHHHHHHHHH
18.5222312127
268AcetylationAGKMALTKASSVASS
HHHHHHHHHHHHCCC
47.3122312127
270PhosphorylationKMALTKASSVASSDK
HHHHHHHHHHCCCCC
27.23-
274PhosphorylationTKASSVASSDKGSCC
HHHHHHCCCCCCCEE
36.59-
275PhosphorylationKASSVASSDKGSCCI
HHHHHCCCCCCCEEE
33.34-
296PhosphorylationGPVVPAWSGPREAPD
CCEECCCCCCCCCCC
40.8124667141
342PhosphorylationNMRPPFTYATLIRWA
CCCCCCHHHHHHHHH
9.66-
356UbiquitinationAILEAPEKQRTLNEI
HHHHCHHHHCHHHHH
43.98-
393UbiquitinationRHNLSLHKCFVRVES
HHHCEEEEEEEEEEE
34.36-
418PhosphorylationLEFRKKRSQRPSRCS
HHHHHHHHCCCCCCC
39.1522678915
422PhosphorylationKKRSQRPSRCSNPTP
HHHHCCCCCCCCCCC
48.37-

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
19SPhosphorylationKinaseCDK2P24941
Uniprot
270SPhosphorylationKinaseGSK3BP49841
PSP
274SPhosphorylationKinaseGSK3BP49841
PSP
342YPhosphorylationKinaseLCKP06239
PSP
422SPhosphorylationKinasePIM1P11309
PSP
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:23973223

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
418SPhosphorylation

23396208
418SPhosphorylation

23396208

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 FOXP3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NFAC2_HUMANNFATC2physical
19564342
HDAC9_HUMANHDAC9physical
17360565
IKZF4_HUMANIKZF4physical
19696312
REL_HUMANRELphysical
21490927
KAT8_HUMANKAT8physical
22152480
HDAC1_HUMANHDAC1physical
21974802
H15_HUMANHIST1H1Bphysical
21654845
TF65_HUMANRELAphysical
15790681
NFAC1_HUMANNFATC1physical
15790681
RUNX1_HUMANRUNX1physical
17377532
GATA3_HUMANGATA3physical
23395819
IKZF3_HUMANIKZF3physical
20676092
CHIP_HUMANSTUB1physical
23973223
PR20E_HUMANPRR20Aphysical
25416956
PR20C_HUMANPRR20Aphysical
25416956
PR20D_HUMANPRR20Aphysical
25416956
PR20B_HUMANPRR20Aphysical
25416956
PR20A_HUMANPRR20Aphysical
25416956
SIVA_HUMANSIVA1physical
21955384
SIVA_HUMANSIVA1genetic
21955384
SIR1_HUMANSIRT1physical
19996091
FOXP1_HUMANFOXP1physical
25609649
HXD13_HUMANHOXD13physical
25609649
AKAP8_HUMANAKAP8physical
25609649
FOXP4_HUMANFOXP4physical
25609649
FUBP3_HUMANFUBP3physical
25609649
KAISO_HUMANZBTB33physical
25609649
ESRP2_HUMANESRP2physical
25609649
NU133_HUMANNUP133physical
25609649
NOVA1_HUMANNOVA1physical
25609649
SATB2_HUMANSATB2physical
25609649
CCAR2_HUMANCCAR2physical
25609649
RALY_HUMANRALYphysical
25609649
WRIP1_HUMANWRNIP1physical
25609649
ZBT34_HUMANZBTB34physical
25609649
ZBT37_HUMANZBTB37physical
25609649
ZFR_HUMANZFRphysical
25609649
DSRAD_HUMANADARphysical
25609649
ELP3_HUMANELP3physical
25609649
FOXP2_HUMANFOXP2physical
25609649
SMC2_HUMANSMC2physical
25609649
CDC27_HUMANCDC27physical
25609649
FEN1_HUMANFEN1physical
25609649
HXC13_HUMANHOXC13physical
25609649
NU107_HUMANNUP107physical
25609649
P4HA1_HUMANP4HA1physical
25609649
SATB1_HUMANSATB1physical
25609649
SUGP2_HUMANSUGP2physical
25609649
BEND3_HUMANBEND3physical
25609649
CENPB_HUMANCENPBphysical
25609649
HDAC2_HUMANHDAC2physical
25609649
HIPK1_HUMANHIPK1physical
25609649
NACC1_HUMANNACC1physical
25609649
NACC2_HUMANNACC2physical
25609649
NOVA2_HUMANNOVA2physical
25609649
NRF1_HUMANNRF1physical
25609649
NU160_HUMANNUP160physical
25609649
SMC3_HUMANSMC3physical
25609649
TFCP2_HUMANTFCP2physical
25609649
UBIP1_HUMANUBP1physical
25609649
ZN326_HUMANZNF326physical
25609649
UBP11_HUMANUSP11physical
25609649
ALBU_HUMANALBphysical
25609649
PSA5_HUMANPSMA5physical
25609649
PSB4_HUMANPSMB4physical
25609649
FOXP1_HUMANFOXP1physical
28514442
FOXP4_HUMANFOXP4physical
28514442
FOXP2_HUMANFOXP2physical
28514442
SMYD2_HUMANSMYD2physical
28514442
CDC23_HUMANCDC23physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FOXP3_HUMAN

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Related Literatures of Post-Translational Modification

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