TAF10_HUMAN - dbPTM
TAF10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAF10_HUMAN
UniProt AC Q12962
Protein Name Transcription initiation factor TFIID subunit 10
Gene Name TAF10
Organism Homo sapiens (Human).
Sequence Length 218
Subcellular Localization Nucleus .
Protein Description TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TIIFD is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors..
Protein Sequence MSCSGSGADPEAAPASAASAPGPAPPVSAPAALPSSTAAENKASPAGTAGGPGAGAAAGGTGPLAARAGEPAERRGAAPVSAGGAAPPEGAISNGVYVLPSAANGDVKPVVSSTPLVDFLMQLEDYTPTIPDAVTGYYLNRAGFEASDPRIIRLISLAAQKFISDIANDALQHCKMKGTASGSSRSKSKDRKYTLTMEDLTPALSEYGINVKKPHYFT
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
2Phosphorylation------MSCSGSGAD
------CCCCCCCCC		19.5928348404
2Acetylation------MSCSGSGAD
------CCCCCCCCC		19.5919413330
4Phosphorylation----MSCSGSGADPE
----CCCCCCCCCCC		28.7828348404
6Phosphorylation--MSCSGSGADPEAA
--CCCCCCCCCCCCC		17.9528348404
16PhosphorylationDPEAAPASAASAPGP
CCCCCCCHHHCCCCC		24.2528348404
19PhosphorylationAAPASAASAPGPAPP
CCCCHHHCCCCCCCC		34.4128348404
35PhosphorylationSAPAALPSSTAAENK
CCCCCCCCCHHHHHC		40.9728348404
36PhosphorylationAPAALPSSTAAENKA
CCCCCCCCHHHHHCC		21.8128348404
37PhosphorylationPAALPSSTAAENKAS
CCCCCCCHHHHHCCC		33.9428985074
44PhosphorylationTAAENKASPAGTAGG
HHHHHCCCCCCCCCC		19.5230266825
48PhosphorylationNKASPAGTAGGPGAG
HCCCCCCCCCCCCCC		25.0030266825
61PhosphorylationAGAAAGGTGPLAARA
CCCCCCCCCCCHHHC		34.4129396449
67MethylationGTGPLAARAGEPAER
CCCCCHHHCCCCHHH		37.20115918105
147PhosphorylationNRAGFEASDPRIIRL
HHCCCCCCCHHHHHH		40.7320068231
161UbiquitinationLISLAAQKFISDIAN
HHHHHHHHHHHHHHH		39.68-
175UbiquitinationNDALQHCKMKGTASG
HHHHHHHHHCCCCCC		41.3332015554
175AcetylationNDALQHCKMKGTASG
HHHHHHHHHCCCCCC		41.3325953088
177UbiquitinationALQHCKMKGTASGSS
HHHHHHHCCCCCCCC		38.31-
186PhosphorylationTASGSSRSKSKDRKY
CCCCCCCCCCCCCCE		43.14-
187AcetylationASGSSRSKSKDRKYT
CCCCCCCCCCCCCEE		61.497975571
189TrimethylationGSSRSKSKDRKYTLT
CCCCCCCCCCCEEEE		66.35-
189MethylationGSSRSKSKDRKYTLT
CCCCCCCCCCCEEEE		66.3525959397
189DeaminationGSSRSKSKDRKYTLT
CCCCCCCCCCCEEEE		66.3525959397
191MethylationSRSKSKDRKYTLTME
CCCCCCCCCEEEEHH		37.30-
201PhosphorylationTLTMEDLTPALSEYG
EEEHHHHHHHHHHHC		20.8829083192
205PhosphorylationEDLTPALSEYGINVK
HHHHHHHHHHCCCCC		30.7729083192
207PhosphorylationLTPALSEYGINVKKP
HHHHHHHHCCCCCCC		21.6729083192
212UbiquitinationSEYGINVKKPHYFT-
HHHCCCCCCCCCCC-		56.9829967540
216PhosphorylationINVKKPHYFT-----
CCCCCCCCCC-----		19.9027642862
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 TAF10_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
189KMethylation

15099517
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 TAF10_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TAF4_HUMANTAF4physical
17643375
TAF6L_HUMANTAF6Lphysical
17643375
TAF5L_HUMANTAF5Lphysical
17643375
TAF2_HUMANTAF2physical
17643375
SPTN1_HUMANSPTAN1physical
17643375
ST65G_HUMANSUPT7Lphysical
17643375
GOGA3_HUMANGOLGA3physical
17643375
TAF9_HUMANTAF9physical
17643375
ARHG1_HUMANARHGEF1physical
17643375
KAT2B_HUMANKAT2Bphysical
17643375
TRRAP_HUMANTRRAPphysical
17643375
SNPC4_HUMANSNAPC4physical
17643375
SK2L2_HUMANSKIV2L2physical
17643375
TAF1_HUMANTAF1physical
17643375
TAF9B_HUMANTAF9Bphysical
17643375
KAT2A_HUMANKAT2Aphysical
17643375
TF3C5_HUMANGTF3C5physical
17643375
PFKAL_HUMANPFKLphysical
17643375
DHX15_HUMANDHX15physical
17643375
TADA1_HUMANTADA1physical
17643375
TAF3_HUMANTAF3physical
17643375
HS90B_HUMANHSP90AB1physical
17643375
ELAV1_HUMANELAVL1physical
17643375
ARHGI_HUMANARHGEF18physical
17643375
ARHG2_HUMANARHGEF2physical
17643375
ERCC5_HUMANERCC5physical
17643375
TADA3_HUMANTADA3physical
17643375
SMRC1_HUMANSMARCC1physical
17643375
SP20H_HUMANSUPT20Hphysical
17643375
ANLN_HUMANANLNphysical
17643375
PRP31_HUMANPRPF31physical
17643375
SMCA4_HUMANSMARCA4physical
17643375
PCBP1_HUMANPCBP1physical
17643375
RPAB1_HUMANPOLR2Ephysical
17643375
MIPT3_HUMANTRAF3IP1physical
17643375
TAF7_HUMANTAF7physical
17643375
PF21A_HUMANPHF21Aphysical
17643375
MCM6_HUMANMCM6physical
17643375
SETD7_HUMANSETD7physical
15099517
TBP_HUMANTBPphysical
15099517
TAF7_HUMANTAF7physical
15099517
TAF6_HUMANTAF6physical
15099517
RPB1_HUMANPOLR2Aphysical
15099517
SP130_HUMANSAP130physical
17375202
KAT2A_HUMANKAT2Aphysical
17375202
TAF5_HUMANTAF5physical
17375202
TAF6_HUMANTAF6physical
17375202
ST65G_HUMANSUPT7Lphysical
17375202
TAF8_HUMANTAF8physical
17375202
SUPT3_HUMANSUPT3Hphysical
17375202
TAF5_HUMANTAF5physical
9603525
TAF7_HUMANTAF7physical
9603525
TBP_HUMANTBPphysical
9603525
TRRAP_HUMANTRRAPphysical
12601814
TAF2_HUMANTAF2physical
12601814
TAF4_HUMANTAF4physical
12601814
SF3B3_HUMANSF3B3physical
12601814
TAF5_HUMANTAF5physical
12601814
KAT2A_HUMANKAT2Aphysical
12601814
TAF6_HUMANTAF6physical
12601814
TAF6L_HUMANTAF6Lphysical
12601814
TAF5L_HUMANTAF5Lphysical
12601814
SPIT3_HUMANSPINT3physical
12601814
TAF9_HUMANTAF9physical
12601814
TAF12_HUMANTAF12physical
12601814
ERCC1_HUMANERCC1physical
22323595
TAF4_HUMANTAF4physical
22939629
TAF5_HUMANTAF5physical
22939629
TAF6_HUMANTAF6physical
22939629
TBP_HUMANTBPphysical
22939629
TAF7_HUMANTAF7physical
22939629
TAF13_HUMANTAF13physical
22939629
TAF9_HUMANTAF9physical
22939629
TAF3_HUMANTAF3physical
15870280
TAF8_HUMANTAF8physical
15870280
ST65G_HUMANSUPT7Lphysical
15870280
IMA1_HUMANKPNA2physical
15870280
IMB1_HUMANKPNB1physical
15870280
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 TAF10_HUMAN

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Related Literatures of Post-Translational Modification
Methylation
ReferencePubMed
"Structural basis for the methylation site specificity of SET7/9.";
Couture J.-F., Collazo E., Hauk G., Trievel R.C.;
Nat. Struct. Mol. Biol. 13:140-146(2006).
Cited for: MOTIF, AND METHYLATION AT LYS-189.
"Gene-specific modulation of TAF10 function by SET9-mediatedmethylation.";
Kouskouti A., Scheer E., Staub A., Tora L., Talianidis I.;
Mol. Cell 14:175-182(2004).
Cited for: METHYLATION AT LYS-189, AND MUTAGENESIS OF LYS-189.

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