TAF1D_HUMAN - dbPTM
TAF1D_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAF1D_HUMAN
UniProt AC Q9H5J8
Protein Name TATA box-binding protein-associated factor RNA polymerase I subunit D
Gene Name TAF1D
Organism Homo sapiens (Human).
Sequence Length 278
Subcellular Localization Nucleus .
Protein Description Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (preinitiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1/TIF-IB with the rDNA promoter. SL1/TIF-IB is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA. Formation of SL1/TIF-IB excludes the association of TBP with TFIID subunits..
Protein Sequence MDKSGIDSLDHVTSDAVELANRSDNSSDSSLFKTQCIPYSPKGEKRNPIRKFVRTPESVHASDSSSDSSFEPIPLTIKAIFERFKNRKKRYKKKKKRRYQPTGRPRGRPEGRRNPIYSLIDKKKQFRSRGSGFPFLESENEKNAPWRKILTFEQAVARGFFNYIEKLKYEHHLKESLKQMNVGEDLENEDFDSRRYKFLDDDGSISPIEESTAEDEDATHLEDNECDIKLAGDSFIVSSEFPVRLSVYLEEEDITEEAALSKKRATKAKNTGQRGLKM
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
4Phosphorylation----MDKSGIDSLDH
----CCCCCCCCCCC
36.4021406692
8PhosphorylationMDKSGIDSLDHVTSD
CCCCCCCCCCCCHHH
33.5021406692
13PhosphorylationIDSLDHVTSDAVELA
CCCCCCCHHHHHHHH
19.9221406692
14PhosphorylationDSLDHVTSDAVELAN
CCCCCCHHHHHHHHH
23.6021406692
23PhosphorylationAVELANRSDNSSDSS
HHHHHHCCCCCCCCC
40.7421815630
26PhosphorylationLANRSDNSSDSSLFK
HHHCCCCCCCCCCCC
40.2821815630
27PhosphorylationANRSDNSSDSSLFKT
HHCCCCCCCCCCCCC
48.0021815630
29PhosphorylationRSDNSSDSSLFKTQC
CCCCCCCCCCCCCCC
30.7821406692
30PhosphorylationSDNSSDSSLFKTQCI
CCCCCCCCCCCCCCC
42.7021406692
34PhosphorylationSDSSLFKTQCIPYSP
CCCCCCCCCCCCCCC
22.7226552605
39PhosphorylationFKTQCIPYSPKGEKR
CCCCCCCCCCCCCCC
20.0728450419
40PhosphorylationKTQCIPYSPKGEKRN
CCCCCCCCCCCCCCC
18.1219664994
55PhosphorylationPIRKFVRTPESVHAS
CCHHHCCCCCCCCCC
26.5523312004
58PhosphorylationKFVRTPESVHASDSS
HHCCCCCCCCCCCCC
22.0223312004
62PhosphorylationTPESVHASDSSSDSS
CCCCCCCCCCCCCCC
24.1323312004
64PhosphorylationESVHASDSSSDSSFE
CCCCCCCCCCCCCCC
29.2823312004
65PhosphorylationSVHASDSSSDSSFEP
CCCCCCCCCCCCCCC
43.0623312004
66PhosphorylationVHASDSSSDSSFEPI
CCCCCCCCCCCCCCC
45.5223312004
78UbiquitinationEPIPLTIKAIFERFK
CCCCCHHHHHHHHHH
30.14-
117PhosphorylationEGRRNPIYSLIDKKK
CCCCCCCHHHHHHHH
9.9327642862
128PhosphorylationDKKKQFRSRGSGFPF
HHHHHHHHCCCCCCC
42.1328555341
138PhosphorylationSGFPFLESENEKNAP
CCCCCCCCCCCCCCC
48.1230266825
142UbiquitinationFLESENEKNAPWRKI
CCCCCCCCCCCHHHH
70.73-
151PhosphorylationAPWRKILTFEQAVAR
CCHHHHHHHHHHHHH
28.71-
166UbiquitinationGFFNYIEKLKYEHHL
HHHHHHHHHCCHHHH
40.4921890473
178UbiquitinationHHLKESLKQMNVGED
HHHHHHHHCCCCCCC
57.70-
197UbiquitinationDFDSRRYKFLDDDGS
CCCCCCEEEECCCCC
37.32-
204PhosphorylationKFLDDDGSISPIEES
EEECCCCCCCCCCCC
27.2122617229
206PhosphorylationLDDDGSISPIEESTA
ECCCCCCCCCCCCCC
22.8625159151
211PhosphorylationSISPIEESTAEDEDA
CCCCCCCCCCCCCCC
21.8128450419
212PhosphorylationISPIEESTAEDEDAT
CCCCCCCCCCCCCCC
37.0328450419
219PhosphorylationTAEDEDATHLEDNEC
CCCCCCCCCCCCCCC
39.0426552605
234PhosphorylationDIKLAGDSFIVSSEF
CEEECCCEEEEECCC
18.8929255136
238PhosphorylationAGDSFIVSSEFPVRL
CCCEEEEECCCCEEE
21.2326074081
239PhosphorylationGDSFIVSSEFPVRLS
CCEEEEECCCCEEEE
32.1526074081

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 TAF1D_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TAF1D_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 TAF1D_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DPOLB_HUMANPOLBphysical
15520167
PTN_HUMANPTNphysical
16169070
HAP1_HUMANHAP1physical
16169070
CENPB_HUMANCENPBphysical
19615732
CSK21_HUMANCSNK2A1physical
19615732
CSK22_HUMANCSNK2A2physical
19615732
CSK2B_HUMANCSNK2Bphysical
19615732
IPO5_HUMANIPO5physical
19615732
TBP_HUMANTBPphysical
19615732
TAF1C_HUMANTAF1Cphysical
19615732
TAF1B_HUMANTAF1Bphysical
19615732
TAF1A_HUMANTAF1Aphysical
19615732
RPAC1_HUMANPOLR1Cphysical
19615732
PSME3_HUMANPSME3physical
19615732
RPA1_HUMANPOLR1Aphysical
19615732
RRP15_HUMANRRP15physical
19615732
RRN3_HUMANRRN3physical
19615732
SSF1_HUMANPPANphysical
19615732
RPA49_HUMANPOLR1Ephysical
19615732
RPA2_HUMANPOLR1Bphysical
19615732
RPA43_HUMANTWISTNBphysical
19615732
TAF1B_HUMANTAF1Bphysical
17318177
TAF1C_HUMANTAF1Cphysical
17318177
TAF1A_HUMANTAF1Aphysical
17318177
TBP_MOUSETbpphysical
17318177
UBF1_HUMANUBTFphysical
17318177
MIC60_HUMANIMMTphysical
21900206
CEP70_HUMANCEP70physical
21900206
RL36L_HUMANRPL36ALphysical
21900206
TIP_HUMANITFG1physical
21900206
HS90B_HUMANHSP90AB1physical
21900206
FEZ1_HUMANFEZ1physical
21900206
HAP1_HUMANHAP1physical
21900206
TYB4_HUMANTMSB4Xphysical
21900206
SNF5_HUMANSMARCB1physical
21900206
EZH2_HUMANEZH2physical
21900206
DDAH2_HUMANDDAH2physical
21900206
GANP_HUMANMCM3APphysical
21900206
FA20C_HUMANFAM20Cphysical
21900206
ING5_HUMANING5physical
21900206
UB2D1_HUMANUBE2D1physical
21900206
LRIF1_HUMANLRIF1physical
21900206
PTN_HUMANPTNphysical
21900206
FAF1_HUMANFAF1physical
21900206
NGEF_HUMANNGEFphysical
21900206
CEP70_HUMANCEP70physical
25416956
TAF1A_HUMANTAF1Aphysical
26186194
NPM_HUMANNPM1physical
26186194
TAF1C_HUMANTAF1Cphysical
26186194
TAF1A_HUMANTAF1Aphysical
28514442
TAF1C_HUMANTAF1Cphysical
28514442
NPM_HUMANNPM1physical
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 TAF1D_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-138 AND SER-234, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND MASSSPECTROMETRY.

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