VGLL4_HUMAN - dbPTM
VGLL4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VGLL4_HUMAN
UniProt AC Q14135
Protein Name Transcription cofactor vestigial-like protein 4
Gene Name VGLL4
Organism Homo sapiens (Human).
Sequence Length 290
Subcellular Localization Nucleus.
Protein Description May act as a specific coactivator for the mammalian TEFs..
Protein Sequence METPLDVLSRAASLVHADDEKREAALRGEPRMQTLPVASALSSHRTGPPPISPSKRKFSMEPGDEDLDCDNDHVSKMSRIFNPHLNKTANGDCRRDPRERSRSPIERAVAPTMSLHGSHLYTSLPSLGLEQPLALTKNSLDASRPAGLSPTLTPGERQQNRPSVITCASAGARNCNLSHCPIAHSGCAAPGPASYRRPPSAATTCDPVVEEHFRRSLGKNYKEPEPAPNSVSITGSVDDHFAKALGDTWLQIKAAKDGASSSPESASRRGQPASPSAHMVSHSHSPSVVS
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
1Acetylation-------METPLDVL
-------CCCHHHHH
13.4422814378
13PhosphorylationDVLSRAASLVHADDE
HHHHHHHHHHCCCHH
29.9122985185
39PhosphorylationMQTLPVASALSSHRT
CCHHHHHHHHHHCCC
29.9424719451
42PhosphorylationLPVASALSSHRTGPP
HHHHHHHHHCCCCCC
24.6625159151
43PhosphorylationPVASALSSHRTGPPP
HHHHHHHHCCCCCCC
20.17-
46PhosphorylationSALSSHRTGPPPISP
HHHHHCCCCCCCCCH
48.9223898821
52PhosphorylationRTGPPPISPSKRKFS
CCCCCCCCHHHCCCC
28.9729255136
54PhosphorylationGPPPISPSKRKFSME
CCCCCCHHHCCCCCC
38.0030266825
58PhosphorylationISPSKRKFSMEPGDE
CCHHHCCCCCCCCCC
11.0418669648
59PhosphorylationSPSKRKFSMEPGDED
CHHHCCCCCCCCCCC
25.8523927012
60PhosphorylationPSKRKFSMEPGDEDL
HHHCCCCCCCCCCCC
8.96-
65PhosphorylationFSMEPGDEDLDCDND
CCCCCCCCCCCCCCC
67.40-
82UbiquitinationSKMSRIFNPHLNKTA
HHHHHHHCCCCCCCC
22.25-
88PhosphorylationFNPHLNKTANGDCRR
HCCCCCCCCCCCCCC
25.04-
93UbiquitinationNKTANGDCRRDPRER
CCCCCCCCCCCHHHH
3.99-
101PhosphorylationRRDPRERSRSPIERA
CCCHHHHCCCHHHHH
32.1525159151
103PhosphorylationDPRERSRSPIERAVA
CHHHHCCCHHHHHHH
31.3225159151
107PhosphorylationRSRSPIERAVAPTMS
HCCCHHHHHHHCCCE
34.77-
109PhosphorylationRSPIERAVAPTMSLH
CCHHHHHHHCCCEEC
9.09-
122PhosphorylationLHGSHLYTSLPSLGL
ECCCCHHHCCCCCCC
30.10-
123PhosphorylationHGSHLYTSLPSLGLE
CCCCHHHCCCCCCCC
25.4027251275
126PhosphorylationHLYTSLPSLGLEQPL
CHHHCCCCCCCCCCC
40.1228348404
139PhosphorylationPLALTKNSLDASRPA
CCCCCCCCCCCCCCC
29.2323403867
143PhosphorylationTKNSLDASRPAGLSP
CCCCCCCCCCCCCCC
38.1630266825
149PhosphorylationASRPAGLSPTLTPGE
CCCCCCCCCCCCCCC
18.2129255136
151PhosphorylationRPAGLSPTLTPGERQ
CCCCCCCCCCCCCCC
39.6323401153
153PhosphorylationAGLSPTLTPGERQQN
CCCCCCCCCCCCCCC
31.5530266825
155PhosphorylationLSPTLTPGERQQNRP
CCCCCCCCCCCCCCC
37.1718220336
157PhosphorylationPTLTPGERQQNRPSV
CCCCCCCCCCCCCCE
49.66-
159PhosphorylationLTPGERQQNRPSVIT
CCCCCCCCCCCCEEE
54.8718669648
163PhosphorylationERQQNRPSVITCASA
CCCCCCCCEEEECCC
23.9428555341
169PhosphorylationPSVITCASAGARNCN
CCEEEECCCCCCCCC
29.4028555341
200PhosphorylationASYRRPPSAATTCDP
HHHCCCCCCCCCCCH
32.9725849741
203PhosphorylationRRPPSAATTCDPVVE
CCCCCCCCCCCHHHH
27.8927794612
204PhosphorylationRPPSAATTCDPVVEE
CCCCCCCCCCHHHHH
15.3623312004
206PhosphorylationPSAATTCDPVVEEHF
CCCCCCCCHHHHHHH
36.62-
221PhosphorylationRRSLGKNYKEPEPAP
HHHCCCCCCCCCCCC
21.8822210691
230PhosphorylationEPEPAPNSVSITGSV
CCCCCCCCCEEEECC
19.0422210691
232PhosphorylationEPAPNSVSITGSVDD
CCCCCCCEEEECCCH
17.7928348404
234PhosphorylationAPNSVSITGSVDDHF
CCCCCEEEECCCHHH
18.8528348404
236PhosphorylationNSVSITGSVDDHFAK
CCCEEEECCCHHHHH
17.4528348404
260PhosphorylationKAAKDGASSSPESAS
HHCCCCCCCCHHHHH
36.5623663014
261PhosphorylationAAKDGASSSPESASR
HCCCCCCCCHHHHHH
49.7529255136
262PhosphorylationAKDGASSSPESASRR
CCCCCCCCHHHHHHC
30.1429255136
265PhosphorylationGASSSPESASRRGQP
CCCCCHHHHHHCCCC
34.6227794612
267PhosphorylationSSSPESASRRGQPAS
CCCHHHHHHCCCCCC
31.6125159151
268PhosphorylationSSPESASRRGQPASP
CCHHHHHHCCCCCCC
46.60-
274PhosphorylationSRRGQPASPSAHMVS
HHCCCCCCCCCCCCC
26.5229255136
276PhosphorylationRGQPASPSAHMVSHS
CCCCCCCCCCCCCCC
28.4529255136
280PhosphorylationASPSAHMVSHSHSPS
CCCCCCCCCCCCCCC
3.14-
281PhosphorylationSPSAHMVSHSHSPSV
CCCCCCCCCCCCCCC
16.2329255136
282PhosphorylationPSAHMVSHSHSPSVV
CCCCCCCCCCCCCCC
20.37-
283PhosphorylationSAHMVSHSHSPSVVS
CCCCCCCCCCCCCCC
20.3929255136
285PhosphorylationHMVSHSHSPSVVS--
CCCCCCCCCCCCC--
23.1423927012
287PhosphorylationVSHSHSPSVVS----
CCCCCCCCCCC----
37.8625159151
289PhosphorylationHSHSPSVVS------
CCCCCCCCC------
7.06-
290PhosphorylationSHSPSVVS-------
CCCCCCCC-------
32.1423927012
291PhosphorylationHSPSVVS--------
CCCCCCC--------
-
296PhosphorylationVS-------------
CC-------------
-

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 VGLL4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VGLL4_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 VGLL4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TEAD1_HUMANTEAD1physical
15140898
MEF2A_HUMANMEF2Aphysical
15140898
I2BP2_HUMANIRF2BP2physical
20702774
I2BP2_HUMANIRF2BP2physical
26186194
I2BP1_HUMANIRF2BP1physical
26186194
I2BPL_HUMANIRF2BPLphysical
26186194
TEAD1_HUMANTEAD1physical
26186194
TEAD4_HUMANTEAD4physical
26186194
TEAD3_HUMANTEAD3physical
26186194
UBP11_HUMANUSP11physical
26186194
UBP11_HUMANUSP11physical
28042509
I2BP1_HUMANIRF2BP1physical
28514442
TEAD4_HUMANTEAD4physical
28514442
TEAD3_HUMANTEAD3physical
28514442
I2BPL_HUMANIRF2BPLphysical
28514442
I2BP2_HUMANIRF2BP2physical
28514442
TEAD1_HUMANTEAD1physical
28514442
UBP11_HUMANUSP11physical
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 VGLL4_HUMAN

loading...

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-52 AND SER-290, 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-52, AND MASSSPECTROMETRY.
"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-52; SER-149 AND THR-153,AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND MASSSPECTROMETRY.

TOP