GATA3_HUMAN - dbPTM
GATA3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GATA3_HUMAN
UniProt AC P23771
Protein Name Trans-acting T-cell-specific transcription factor GATA-3
Gene Name GATA3
Organism Homo sapiens (Human).
Sequence Length 443
Subcellular Localization Nucleus.
Protein Description Transcriptional activator which binds to the enhancer of the T-cell receptor alpha and delta genes. Binds to the consensus sequence 5'-AGATAG-3'. Required for the T-helper 2 (Th2) differentiation process following immune and inflammatory responses..
Protein Sequence MEVTADQPRWVSHHHPAVLNGQHPDTHHPGLSHSYMDAAQYPLPEEVDVLFNIDGQGNHVPPYYGNSVRATVQRYPPTHHGSQVCRPPLLHGSLPWLDGGKALGSHHTASPWNLSPFSKTSIHHGSPGPLSVYPPASSSSLSGGHASPHLFTFPPTPPKDVSPDPSLSTPGSAGSARQDEKECLKYQVPLPDSMKLESSHSRGSMTALGGASSSTHHPITTYPPYVPEYSSGLFPPSSLLGGSPTGFGCKSRPKARSSTGRECVNCGATSTPLWRRDGTGHYLCNACGLYHKMNGQNRPLIKPKRRLSAARRAGTSCANCQTTTTTLWRRNANGDPVCNACGLYYKLHNINRPLTMKKEGIQTRNRKMSSKSKKCKKVHDSLEDFPKNSSFNPAALSRHMSSLSHISPFSHSSHMLTTPTPMHPPSSLSFGPHHPSSMVTAMG
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
71PhosphorylationYGNSVRATVQRYPPT
CCCCHHHHHCCCCCC		13.4523532336
105PhosphorylationDGGKALGSHHTASPW
CCCCCCCCCCCCCCC		16.9723403867
108PhosphorylationKALGSHHTASPWNLS
CCCCCCCCCCCCCCC		24.3323403867
110PhosphorylationLGSHHTASPWNLSPF
CCCCCCCCCCCCCCC		31.4425849741
115PhosphorylationTASPWNLSPFSKTSI
CCCCCCCCCCCCCCC		22.2322617229
118PhosphorylationPWNLSPFSKTSIHHG
CCCCCCCCCCCCCCC		38.1125849741
156PhosphorylationHLFTFPPTPPKDVSP
CCEECCCCCCCCCCC		53.08-
162PhosphorylationPTPPKDVSPDPSLST
CCCCCCCCCCCCCCC		33.4523911959
166PhosphorylationKDVSPDPSLSTPGSA
CCCCCCCCCCCCCCC		42.1930576142
168PhosphorylationVSPDPSLSTPGSAGS
CCCCCCCCCCCCCCC		36.5725849741
169PhosphorylationSPDPSLSTPGSAGSA
CCCCCCCCCCCCCCC		36.6425849741
172PhosphorylationPSLSTPGSAGSARQD
CCCCCCCCCCCCCCC		30.5725849741
186PhosphorylationDEKECLKYQVPLPDS
CHHHHHHCCCCCCCC		11.20-
193PhosphorylationYQVPLPDSMKLESSH
CCCCCCCCCCCCCCC		18.8427251275
195UbiquitinationVPLPDSMKLESSHSR
CCCCCCCCCCCCCCC		53.7229967540
198PhosphorylationPDSMKLESSHSRGSM
CCCCCCCCCCCCCCC		43.7327251275
199PhosphorylationDSMKLESSHSRGSMT
CCCCCCCCCCCCCCE		18.9924719451
237PhosphorylationSSGLFPPSSLLGGSP
CCCCCCCHHHCCCCC		33.5827251275
238PhosphorylationSGLFPPSSLLGGSPT
CCCCCCHHHCCCCCC		33.1327251275
243PhosphorylationPSSLLGGSPTGFGCK
CHHHCCCCCCCCCCC		19.9328348404
245PhosphorylationSLLGGSPTGFGCKSR
HHCCCCCCCCCCCCC		47.0028348404
257 (in isoform 2)Phosphorylation-36.7928348404
258 (in isoform 2)Phosphorylation-29.3624719451
258PhosphorylationSRPKARSSTGRECVN
CCCCCCCCCCCCCCC		29.3624719451
259 (in isoform 2)Phosphorylation-41.3228348404
261DimethylationKARSSTGRECVNCGA
CCCCCCCCCCCCCCC		33.94-
261MethylationKARSSTGRECVNCGA
CCCCCCCCCCCCCCC		33.94-
271PhosphorylationVNCGATSTPLWRRDG
CCCCCCCCCCCCCCC		20.32-
282PhosphorylationRRDGTGHYLCNACGL
CCCCCCCHHHHHHHC		17.8117360941
290PhosphorylationLCNACGLYHKMNGQN
HHHHHHCHHHHCCCC		5.6717360941
292AcetylationNACGLYHKMNGQNRP
HHHHCHHHHCCCCCC		22.0966281
302AcetylationGQNRPLIKPKRRLSA
CCCCCCCCHHHHHHH		52.77-
304AcetylationNRPLIKPKRRLSAAR
CCCCCCHHHHHHHHH		45.1966277
308PhosphorylationIKPKRRLSAARRAGT
CCHHHHHHHHHHHCC		20.3316109788
344PhosphorylationVCNACGLYYKLHNIN
CHHHHHHHHHHHCCC		5.48-
346AcetylationNACGLYYKLHNINRP
HHHHHHHHHHCCCCC		29.7010970860
369PhosphorylationQTRNRKMSSKSKKCK
HHHHHHCCCCCHHHH		37.33-
371AcetylationRNRKMSSKSKKCKKV
HHHHCCCCCHHHHHH		60.0120167786
373AcetylationRKMSSKSKKCKKVHD
HHCCCCCHHHHHHHH		66.9630588895
374AcetylationKMSSKSKKCKKVHDS
HCCCCCHHHHHHHHC		59.3830588901
376AcetylationSSKSKKCKKVHDSLE
CCCCHHHHHHHHCHH		67.7130588907
377UbiquitinationSKSKKCKKVHDSLED
CCCHHHHHHHHCHHH		55.0329967540
378UbiquitinationKSKKCKKVHDSLEDF
CCHHHHHHHHCHHHC		3.5629967540
381PhosphorylationKCKKVHDSLEDFPKN
HHHHHHHCHHHCCCC		20.8425849741
382PhosphorylationCKKVHDSLEDFPKNS
HHHHHHCHHHCCCCC		10.2324719451
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
156TPhosphorylationKinaseCDK2P24941
PSP
308SPhosphorylationKinasePRKACAP17612
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GATA3_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 GATA3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBTN1_HUMANLMO1physical
9819382
RBTN2_HUMANLMO2physical
9819382
TAL1_HUMANTAL1physical
9819382
BMI1_HUMANBMI1physical
17114435
MDM2_HUMANMDM2physical
15975924
HDAC3_HUMANHDAC3physical
17075044
HDAC5_HUMANHDAC5physical
17075044
TBX21_HUMANTBX21physical
17075044
RARB_HUMANRARBphysical
20211142
HDAC4_HUMANHDAC4physical
16922677
MYB_HUMANMYBphysical
22039304
BRCA1_HUMANBRCA1physical
22120723
UBP21_HUMANUSP21physical
23395819
PSA3_HUMANPSMA3physical
25416956
FBXW7_HUMANFBXW7physical
24820417
WEE1_HUMANWEE1genetic
28319113
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
146255Hypoparathyroidism, sensorineural deafness, and renal disease (HDR)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GATA3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115 AND SER-162, ANDMASS SPECTROMETRY.

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