TFDP2_HUMAN - dbPTM
TFDP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TFDP2_HUMAN
UniProt AC Q14188
Protein Name Transcription factor Dp-2
Gene Name TFDP2
Organism Homo sapiens (Human).
Sequence Length 446
Subcellular Localization Nucleus.
Protein Description Can stimulate E2F-dependent transcription. Binds DNA cooperatively with E2F family members through the E2 recognition site, 5'-TTTC[CG]CGC-3', found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The TFDP2:E2F complex functions in the control of cell-cycle progression from G1 to S phase. The E2F1:DP complex appears to mediate both cell proliferation and apoptosis. Blocks adipocyte differentiation by repressing CEBPA binding to its target gene promoters. [PubMed: 20176812]
Protein Sequence MTAKNVGLTSTNAEVRGFIDQNLSPTKGNISFVAFPVSNTNSPTKILPKTLGPINVNVGPQMIISTPQRLTSSGSVLIGSPYTPAPAMVTQTHIAEATGWVPGDRKRARKFIDSDFSESKRSKKGDKNGKGLRHFSMKVCEKVQRKGTTSYNEVADELVSEFTNSNNHLAADSAYDQKNIRRRVYDALNVLMAMNIISKEKKEIKWIGLPTNSAQECQNLEIEKQRRIERIKQKRAQLQELLLQQIAFKNLVQRNRQNEQQNQGPPALNSTIQLPFIIINTSRKTVIDCSISSDKFEYLFNFDNTFEIHDDIEVLKRMGMSFGLESGKCSLEDLKLAKSLVPKALEGYITDISTGPSWLNQGLLLNSTQSVSNLDLTTGATLPQSSVNQGLCLDAEVALATGQFLAPNSHQSSSAASHCSESRGETPCSFNDEDEEDDEEDSSSPE
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
2Acetylation------MTAKNVGLT
------CCCCCCCCC
46.4622814378
2Phosphorylation------MTAKNVGLT
------CCCCCCCCC
46.4624719451
4 (in isoform 2)Phosphorylation-42.8924043423
4 (in isoform 3)Phosphorylation-42.8924043423
5 (in isoform 2)Phosphorylation-30.5324043423
5 (in isoform 3)Phosphorylation-30.5324043423
9PhosphorylationTAKNVGLTSTNAEVR
CCCCCCCCCCCHHHH
27.8124719451
10PhosphorylationAKNVGLTSTNAEVRG
CCCCCCCCCCHHHHC
25.3824719451
10 (in isoform 2)Phosphorylation-25.3824043423
10 (in isoform 3)Phosphorylation-25.3824043423
11PhosphorylationKNVGLTSTNAEVRGF
CCCCCCCCCHHHHCC
32.9624719451
11UbiquitinationKNVGLTSTNAEVRGF
CCCCCCCCCHHHHCC
32.9624816145
11 (in isoform 2)Phosphorylation-32.9624043423
11 (in isoform 3)Phosphorylation-32.9624043423
12 (in isoform 2)Phosphorylation-33.5924043423
12 (in isoform 3)Phosphorylation-33.5924043423
14 (in isoform 2)Phosphorylation-34.5124043423
14 (in isoform 3)Phosphorylation-34.5124043423
19 (in isoform 2)Phosphorylation-6.2424043423
19 (in isoform 3)Phosphorylation-6.2424043423
21 (in isoform 2)Phosphorylation-48.2024043423
21 (in isoform 3)Phosphorylation-48.2024043423
22 (in isoform 2)Phosphorylation-38.4424043423
22 (in isoform 3)Phosphorylation-38.4424043423
23UbiquitinationRGFIDQNLSPTKGNI
HCCCCCCCCCCCCCE
5.5829967540
24PhosphorylationGFIDQNLSPTKGNIS
CCCCCCCCCCCCCEE
37.7619664994
26PhosphorylationIDQNLSPTKGNISFV
CCCCCCCCCCCEEEE
48.4830266825
27UbiquitinationDQNLSPTKGNISFVA
CCCCCCCCCCEEEEE
54.0324816145
29 (in isoform 2)Phosphorylation-28.4324043423
29 (in isoform 3)Phosphorylation-28.4324043423
31PhosphorylationSPTKGNISFVAFPVS
CCCCCCEEEEEEECC
20.0519690332
31 (in isoform 2)Phosphorylation-20.0524043423
31 (in isoform 3)Phosphorylation-20.0524043423
37 (in isoform 2)Phosphorylation-5.7924043423
37 (in isoform 3)Phosphorylation-5.7924043423
38PhosphorylationSFVAFPVSNTNSPTK
EEEEEECCCCCCCCE
37.8725159151
40PhosphorylationVAFPVSNTNSPTKIL
EEEECCCCCCCCEEC
29.5725159151
42PhosphorylationFPVSNTNSPTKILPK
EECCCCCCCCEECCC
31.7225159151
42 (in isoform 2)Phosphorylation-31.7224043423
42 (in isoform 3)Phosphorylation-31.7224043423
44PhosphorylationVSNTNSPTKILPKTL
CCCCCCCCEECCCCC
30.4525159151
45UbiquitinationSNTNSPTKILPKTLG
CCCCCCCEECCCCCC
45.7029967540
49UbiquitinationSPTKILPKTLGPINV
CCCEECCCCCCCCCC
53.5929967540
59UbiquitinationGPINVNVGPQMIIST
CCCCCCCCCCEEEEC
11.0829967540
63UbiquitinationVNVGPQMIISTPQRL
CCCCCCEEEECCCEE
1.5724816145
65PhosphorylationVGPQMIISTPQRLTS
CCCCEEEECCCEECC
24.1028348404
66PhosphorylationGPQMIISTPQRLTSS
CCCEEEECCCEECCC
17.0328348404
69UbiquitinationMIISTPQRLTSSGSV
EEEECCCEECCCCCE
40.9329967540
80PhosphorylationSGSVLIGSPYTPAPA
CCCEEECCCCCCCCC
14.03-
81UbiquitinationGSVLIGSPYTPAPAM
CCEEECCCCCCCCCE
31.6329967540
85UbiquitinationIGSPYTPAPAMVTQT
ECCCCCCCCCEEEEC
9.1829967540
88UbiquitinationPYTPAPAMVTQTHIA
CCCCCCCEEEECHHH
3.0529967540
92UbiquitinationAPAMVTQTHIAEATG
CCCEEEECHHHHHHC
13.0929967540
96UbiquitinationVTQTHIAEATGWVPG
EEECHHHHHHCCCCC
46.2724816145
102UbiquitinationAEATGWVPGDRKRAR
HHHHCCCCCCHHHHH
32.2424816145
108UbiquitinationVPGDRKRARKFIDSD
CCCCHHHHHHHHCCC
23.2729967540
110UbiquitinationGDRKRARKFIDSDFS
CCHHHHHHHHCCCCC
45.76-
113UbiquitinationKRARKFIDSDFSESK
HHHHHHHCCCCCHHH
45.3321890473
114PhosphorylationRARKFIDSDFSESKR
HHHHHHCCCCCHHHH
35.4227732954
114UbiquitinationRARKFIDSDFSESKR
HHHHHHCCCCCHHHH
35.4229967540
117PhosphorylationKFIDSDFSESKRSKK
HHHCCCCCHHHHCCC
46.0530576142
118UbiquitinationFIDSDFSESKRSKKG
HHCCCCCHHHHCCCC
61.3429967540
119PhosphorylationIDSDFSESKRSKKGD
HCCCCCHHHHCCCCC
31.9721815630
120UbiquitinationDSDFSESKRSKKGDK
CCCCCHHHHCCCCCC
57.5529967540
122PhosphorylationDFSESKRSKKGDKNG
CCCHHHHCCCCCCCC
42.327739537
124UbiquitinationSESKRSKKGDKNGKG
CHHHHCCCCCCCCCC
73.8524816145
127UbiquitinationKRSKKGDKNGKGLRH
HHCCCCCCCCCCHHH
76.0329967540
136PhosphorylationGKGLRHFSMKVCEKV
CCCHHHHHHHHHHHH
16.1524719451
136UbiquitinationGKGLRHFSMKVCEKV
CCCHHHHHHHHHHHH
16.1521890473
137UbiquitinationKGLRHFSMKVCEKVQ
CCHHHHHHHHHHHHH
3.5421890473
138UbiquitinationGLRHFSMKVCEKVQR
CHHHHHHHHHHHHHH
42.40-
142UbiquitinationFSMKVCEKVQRKGTT
HHHHHHHHHHHHCCC
38.2429967540
145UbiquitinationKVCEKVQRKGTTSYN
HHHHHHHHHCCCCHH
42.2129967540
146UbiquitinationVCEKVQRKGTTSYNE
HHHHHHHHCCCCHHH
43.4429967540
152UbiquitinationRKGTTSYNEVADELV
HHCCCCHHHHHHHHH
36.7121890473
162UbiquitinationADELVSEFTNSNNHL
HHHHHHHHHCCCCCC
6.4521890473
162UbiquitinationADELVSEFTNSNNHL
HHHHHHHHHCCCCCC
6.4521890473
162UbiquitinationADELVSEFTNSNNHL
HHHHHHHHHCCCCCC
6.4521890473
164UbiquitinationELVSEFTNSNNHLAA
HHHHHHHCCCCCCCC
48.3229967540
172 (in isoform 2)Ubiquitination-28.3521890473
173 (in isoform 3)Ubiquitination-24.8121890473
177UbiquitinationAADSAYDQKNIRRRV
CCCCHHHHHHHHHHH
28.1929967540
178UbiquitinationADSAYDQKNIRRRVY
CCCHHHHHHHHHHHH
51.98-
185PhosphorylationKNIRRRVYDALNVLM
HHHHHHHHHHHHHHH
8.1625072903
188UbiquitinationRRRVYDALNVLMAMN
HHHHHHHHHHHHHHH
4.1021890473
188 (in isoform 4)Ubiquitination-4.1021890473
189UbiquitinationRRVYDALNVLMAMNI
HHHHHHHHHHHHHHH
26.9621890473
189 (in isoform 5)Ubiquitination-26.9621890473
196UbiquitinationNVLMAMNIISKEKKE
HHHHHHHHHCCCCCC
2.1229967540
198PhosphorylationLMAMNIISKEKKEIK
HHHHHHHCCCCCCCE
30.8522817900
199UbiquitinationMAMNIISKEKKEIKW
HHHHHHCCCCCCCEE
64.2429967540
201UbiquitinationMNIISKEKKEIKWIG
HHHHCCCCCCCEEEE
60.48-
202UbiquitinationNIISKEKKEIKWIGL
HHHCCCCCCCEEEEC
66.8029967540
205UbiquitinationSKEKKEIKWIGLPTN
CCCCCCCEEEECCCC
33.5729967540
221UbiquitinationAQECQNLEIEKQRRI
HHHHHCHHHHHHHHH
57.5621890473
224UbiquitinationCQNLEIEKQRRIERI
HHCHHHHHHHHHHHH
55.5629967540
227UbiquitinationLEIEKQRRIERIKQK
HHHHHHHHHHHHHHH
32.4021890473
228UbiquitinationEIEKQRRIERIKQKR
HHHHHHHHHHHHHHH
4.5521890473
238UbiquitinationIKQKRAQLQELLLQQ
HHHHHHHHHHHHHHH
4.1129967540
241UbiquitinationKRAQLQELLLQQIAF
HHHHHHHHHHHHHHH
3.5929967540
249UbiquitinationLLQQIAFKNLVQRNR
HHHHHHHHHHHHHHH
40.1121890473
249 (in isoform 1)Ubiquitination-40.1121890473
250UbiquitinationLQQIAFKNLVQRNRQ
HHHHHHHHHHHHHHH
38.7021890473
270PhosphorylationQGPPALNSTIQLPFI
CCCCCCHHCEECCEE
27.9524043423
271PhosphorylationGPPALNSTIQLPFII
CCCCCHHCEECCEEE
16.2124043423
275UbiquitinationLNSTIQLPFIIINTS
CHHCEECCEEEEECC
11.3029967540
278UbiquitinationTIQLPFIIINTSRKT
CEECCEEEEECCCCE
1.7129967540
281PhosphorylationLPFIIINTSRKTVID
CCEEEEECCCCEEEE
21.3524043423
282PhosphorylationPFIIINTSRKTVIDC
CEEEEECCCCEEEEE
27.5624043423
307UbiquitinationFNFDNTFEIHDDIEV
EECCCCEEECCHHHH
37.0629967540
310UbiquitinationDNTFEIHDDIEVLKR
CCCEEECCHHHHHHH
65.3329967540
321PhosphorylationVLKRMGMSFGLESGK
HHHHHCCCCCCCCCC
15.5029083192
326PhosphorylationGMSFGLESGKCSLED
CCCCCCCCCCCCHHH
48.9029083192
328UbiquitinationSFGLESGKCSLEDLK
CCCCCCCCCCHHHHH
29.90-
330PhosphorylationGLESGKCSLEDLKLA
CCCCCCCCHHHHHHH
37.9829083192
335UbiquitinationKCSLEDLKLAKSLVP
CCCHHHHHHHHHHCH
59.7329967540
338UbiquitinationLEDLKLAKSLVPKAL
HHHHHHHHHHCHHHH
55.5529967540
426PhosphorylationCSESRGETPCSFNDE
CCCCCCCCCCCCCCC
32.2130177828
429PhosphorylationSRGETPCSFNDEDEE
CCCCCCCCCCCCCCC
28.4330177828
442PhosphorylationEEDDEEDSSSPE---
CCCCCCCCCCCC---
35.6828985074
443PhosphorylationEDDEEDSSSPE----
CCCCCCCCCCC----
63.3328985074
444PhosphorylationDDEEDSSSPE-----
CCCCCCCCCC-----
36.6830177828

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 TFDP2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
24SPhosphorylation

23186163

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 TFDP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
E2F6_HUMANE2F6physical
9704927
E2F1_HUMANE2F1physical
9704927
E2F4_HUMANE2F4physical
26186194
E2F5_HUMANE2F5physical
26186194
RB_HUMANRB1physical
26186194
E2F2_HUMANE2F2physical
26186194
E2F3_HUMANE2F3physical
26186194
E2F1_HUMANE2F1physical
26186194
E2F2_HUMANE2F2physical
28514442
E2F4_HUMANE2F4physical
28514442
E2F3_HUMANE2F3physical
28514442
E2F5_HUMANE2F5physical
28514442
E2F1_HUMANE2F1physical
28514442
RB_HUMANRB1physical
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 TFDP2_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-24, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND MASSSPECTROMETRY.

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