TADA3_HUMAN - dbPTM
TADA3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TADA3_HUMAN
UniProt AC O75528
Protein Name Transcriptional adapter 3
Gene Name TADA3
Organism Homo sapiens (Human).
Sequence Length 432
Subcellular Localization Nucleus .
Protein Description Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex. Also known as a coactivator for p53/TP53-dependent transcriptional activation. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4..
Protein Sequence MSELKDCPLQFHDFKSVDHLKVCPRYTAVLARSEDDGIGIEELDTLQLELETLLSSASRRLRVLEAETQILTDWQDKKGDRRFLKLGRDHELGAPPKHGKPKKQKLEGKAGHGPGPGPGRPKSKNLQPKIQEYEFTDDPIDVPRIPKNDAPNRFWASVEPYCADITSEEVRTLEELLKPPEDEAEHYKIPPLGKHYSQRWAQEDLLEEQKDGARAAAVADKKKGLMGPLTELDTKDVDALLKKSEAQHEQPEDGCPFGALTQRLLQALVEENIISPMEDSPIPDMSGKESGADGASTSPRNQNKPFSVPHTKSLESRIKEELIAQGLLESEDRPAEDSEDEVLAELRKRQAELKALSAHNRTKKHDLLRLAKEEVSRQELRQRVRMADNEVMDAFRKIMAARQKKRTPTKKEKDQAWKTLKERESILKLLDG
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
21SumoylationFKSVDHLKVCPRYTA
CCCCCCCEECCCCEE		38.07-
21AcetylationFKSVDHLKVCPRYTA
CCCCCCCEECCCCEE		38.0726051181
21SumoylationFKSVDHLKVCPRYTA
CCCCCCCEECCCCEE		38.0728112733
26PhosphorylationHLKVCPRYTAVLARS
CCEECCCCEEEEEEC		5.5618452278
26 (in isoform 2)Phosphorylation-5.56-
27 (in isoform 2)Phosphorylation-16.15-
27PhosphorylationLKVCPRYTAVLARSE
CEECCCCEEEEEECC		16.1518452278
33 (in isoform 2)Phosphorylation-39.51-
33PhosphorylationYTAVLARSEDDGIGI
CEEEEEECCCCCCCH		39.5118452278
85MethylationKGDRRFLKLGRDHEL
CCCHHHHHCCCCCCC		46.30115980241
103AcetylationPKHGKPKKQKLEGKA
CCCCCCCCCCCCCCC		62.2826051181
109AcetylationKKQKLEGKAGHGPGP
CCCCCCCCCCCCCCC		41.6525953088
122AcetylationGPGPGRPKSKNLQPK
CCCCCCCCCCCCCCC		73.1026051181
124AcetylationGPGRPKSKNLQPKIQ
CCCCCCCCCCCCCCE		68.7326051181
129UbiquitinationKSKNLQPKIQEYEFT
CCCCCCCCCEEEECC		44.02-
129SumoylationKSKNLQPKIQEYEFT
CCCCCCCCCEEEECC		44.0228112733
133PhosphorylationLQPKIQEYEFTDDPI
CCCCCEEEECCCCCC		10.4428796482
147UbiquitinationIDVPRIPKNDAPNRF
CCCCCCCCCCCCCCC		66.15-
147AcetylationIDVPRIPKNDAPNRF
CCCCCCCCCCCCCCC		66.15113666009
187PhosphorylationPEDEAEHYKIPPLGK
CHHHHHHCCCCCCCH		11.3428796482
194UbiquitinationYKIPPLGKHYSQRWA
CCCCCCCHHHHHHHH		47.23-
194AcetylationYKIPPLGKHYSQRWA
CCCCCCCHHHHHHHH		47.23113666007
210UbiquitinationEDLLEEQKDGARAAA
HHHHHHHHHHHHHHH		62.50-
222UbiquitinationAAAVADKKKGLMGPL
HHHHHCHHCCCCCCC		53.25-
222AcetylationAAAVADKKKGLMGPL
HHHHHCHHCCCCCCC		53.25113666005
223UbiquitinationAAVADKKKGLMGPLT
HHHHCHHCCCCCCCC		64.12-
243UbiquitinationDVDALLKKSEAQHEQ
HHHHHHHHHHHHHCC		54.20-
275PhosphorylationLVEENIISPMEDSPI
HHHCCCCCCCCCCCC		17.8820873877
280PhosphorylationIISPMEDSPIPDMSG
CCCCCCCCCCCCCCC		16.0630278072
286PhosphorylationDSPIPDMSGKESGAD
CCCCCCCCCCCCCCC		54.8420873877
290PhosphorylationPDMSGKESGADGAST
CCCCCCCCCCCCCCC		42.6523663014
296PhosphorylationESGADGASTSPRNQN
CCCCCCCCCCCCCCC		34.6429255136
297PhosphorylationSGADGASTSPRNQNK
CCCCCCCCCCCCCCC		42.0623401153
298PhosphorylationGADGASTSPRNQNKP
CCCCCCCCCCCCCCC		21.2629255136
298 (in isoform 2)Phosphorylation-21.26-
304AcetylationTSPRNQNKPFSVPHT
CCCCCCCCCCCCCCC		37.3626051181
307PhosphorylationRNQNKPFSVPHTKSL
CCCCCCCCCCCCHHH		43.1826074081
311PhosphorylationKPFSVPHTKSLESRI
CCCCCCCCHHHHHHH		19.0926074081
312AcetylationPFSVPHTKSLESRIK
CCCCCCCHHHHHHHH		50.43113666011
330PhosphorylationIAQGLLESEDRPAED
HHHCCHHCCCCCCCC		44.7824732914
338PhosphorylationEDRPAEDSEDEVLAE
CCCCCCCCHHHHHHH		38.1530266825
354UbiquitinationRKRQAELKALSAHNR
HHHHHHHHHHHCCCC		38.49-
354MethylationRKRQAELKALSAHNR
HHHHHHHHHHHCCCC		38.49115980233
372UbiquitinationHDLLRLAKEEVSRQE
HHHHHHHHHHHHHHH		60.03-
377MethylationLAKEEVSRQELRQRV
HHHHHHHHHHHHHHH		38.8924395461
381MethylationEVSRQELRQRVRMAD
HHHHHHHHHHHHHHH		22.8524395469
404AcetylationKIMAARQKKRTPTKK
HHHHHHHHCCCCCHH		38.377289879
410AcetylationQKKRTPTKKEKDQAW
HHCCCCCHHHHHHHH		61.207289889
418AcetylationKEKDQAWKTLKERES
HHHHHHHHHHHHHHH		47.1719608861
425PhosphorylationKTLKERESILKLLDG
HHHHHHHHHHHHHCC		39.1724719451
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

Oops, there are no upstream regulatory protein records of TADA3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TADA3_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 TADA3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SGF29_HUMANCCDC101physical
16189514
TAD2A_HUMANTADA2Aphysical
11707411
EP300_HUMANEP300physical
11707411
P53_HUMANTP53physical
11707411
EIF3J_HUMANEIF3Jphysical
16169070
HSP7C_HUMANHSPA8physical
16169070
RFX1_HUMANRFX1physical
16169070
SAP18_HUMANSAP18physical
16169070
RARA_HUMANRARAphysical
12235159
RXRA_HUMANRXRAphysical
12235159
ESR1_HUMANESR1physical
12034840
ANR12_HUMANANKRD12physical
18377363
KAT2B_HUMANKAT2Bphysical
18089809
KAT2A_HUMANKAT2Aphysical
18089809
EP300_HUMANEP300physical
18089809
ESR1_HUMANESR1physical
18089809
CTNB1_HUMANCTNNB1physical
18059173
P53_HUMANTP53physical
17452980
RARA_HUMANRARAphysical
20413580
ESR1_HUMANESR1physical
20413580
ANDR_HUMANARphysical
20413580
TRXR2_HUMANTXNRD2physical
20413580
NR1I2_HUMANNR1I2physical
20413580
PIAS4_HUMANPIAS4physical
15383276
ING5_HUMANING5physical
15383276
MAGH1_HUMANMAGEH1physical
15383276
TAF5L_HUMANTAF5Lphysical
22939629
KDM1A_HUMANKDM1Aphysical
23455924
P53_HUMANTP53physical
17272277
SGF29_HUMANCCDC101physical
25416956
HEXI2_HUMANHEXIM2physical
25416956
CSR2B_HUMANCSRP2BPphysical
26186194
YETS2_HUMANYEATS2physical
26186194
SP20H_HUMANSUPT20Hphysical
26186194
ZZZ3_HUMANZZZ3physical
26186194
HAUS1_HUMANHAUS1physical
26186194
TRRAP_HUMANTRRAPphysical
26186194
TAF10_HUMANTAF10physical
26186194
KAT2B_HUMANKAT2Bphysical
26186194
KAT2A_HUMANKAT2Aphysical
26186194
TADA1_HUMANTADA1physical
26186194
TAF9B_HUMANTAF9Bphysical
26186194
MCAF1_HUMANATF7IPphysical
26186194
TAF12_HUMANTAF12physical
26186194
NC2B_HUMANDR1physical
26186194
TAD2A_HUMANTADA2Aphysical
26186194
SPT20_HUMANSPATA20physical
26186194
HAUS4_HUMANHAUS4physical
26186194
TAF5L_HUMANTAF5Lphysical
26186194
SUPT3_HUMANSUPT3Hphysical
26186194
TAF6L_HUMANTAF6Lphysical
26186194
SPF27_HUMANBCAS2physical
26186194
ST65G_HUMANSUPT7Lphysical
26186194
SGF29_HUMANCCDC101physical
26344197
TAD2A_HUMANTADA2Aphysical
28514442
KAT2B_HUMANKAT2Bphysical
28514442
CSR2B_HUMANCSRP2BPphysical
28514442
YETS2_HUMANYEATS2physical
28514442
KAT2A_HUMANKAT2Aphysical
28514442
TADA1_HUMANTADA1physical
28514442
ZZZ3_HUMANZZZ3physical
28514442
TAF6L_HUMANTAF6Lphysical
28514442
SP20H_HUMANSUPT20Hphysical
28514442
TAF12_HUMANTAF12physical
28514442
ST65G_HUMANSUPT7Lphysical
28514442
TAF9B_HUMANTAF9Bphysical
28514442
TAF5L_HUMANTAF5Lphysical
28514442
SUPT3_HUMANSUPT3Hphysical
28514442
MCAF1_HUMANATF7IPphysical
28514442
TRRAP_HUMANTRRAPphysical
28514442
HAUS4_HUMANHAUS4physical
28514442
SPT20_HUMANSPATA20physical
28514442
HAUS1_HUMANHAUS1physical
28514442
TAF10_HUMANTAF10physical
28514442
NC2B_HUMANDR1physical
28514442
SPF27_HUMANBCAS2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TADA3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-418, AND MASS SPECTROMETRY.

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