GPBL1_HUMAN - dbPTM
GPBL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPBL1_HUMAN
UniProt AC Q9HC44
Protein Name Vasculin-like protein 1
Gene Name GPBP1L1
Organism Homo sapiens (Human).
Sequence Length 474
Subcellular Localization Nucleus .
Protein Description Possible transcription factor..
Protein Sequence MAQHDFVPAWLNFSTPQSAKSPTATFEKHGEHLPRGEGRFGVSRRRHNSSDGFFNNGPLRTAGDSWHQPSLFRHDSVDSGVSKGAYAGITGNPSGWHSSSRGHDGMSQRSGGGTGNHRHWNGSFHSRKGCAFQEKPPMEIREEKKEDKVEKLQFEEEDFPSLNPEAGKQHQPCRPIGTPSGVWENPPSAKQPSKMLVIKKVSKEDPAAAFSAAFTSPGSHHANGNKLSSVVPSVYKNLVPKPVPPPSKPNAWKANRMEHKSGSLSSSRESAFTSPISVTKPVVLASGAALSSPKESPSSTTPPIEISSSRLTKLTRRTTDRKSEFLKTLKDDRNGDFSENRDCDKLEDLEDNSTPEPKENGEEGCHQNGLALPVVEEGEVLSHSLEAEHRLLKAMGWQEYPENDENCLPLTEDELKEFHMKTEQLRRNGFGKNGFLQSRSSSLFSPWRSTCKAEFEDSDTETSSSETSDDDAWK
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
14PhosphorylationVPAWLNFSTPQSAKS
CCEECCCCCCCCCCC
37.8028450419
15PhosphorylationPAWLNFSTPQSAKSP
CEECCCCCCCCCCCC
22.6228450419
18PhosphorylationLNFSTPQSAKSPTAT
CCCCCCCCCCCCCCC
38.5825106551
21PhosphorylationSTPQSAKSPTATFEK
CCCCCCCCCCCCHHH
27.4829255136
23PhosphorylationPQSAKSPTATFEKHG
CCCCCCCCCCHHHCC
45.4829255136
25PhosphorylationSAKSPTATFEKHGEH
CCCCCCCCHHHCCCC
34.5028450419
43PhosphorylationGEGRFGVSRRRHNSS
CCCCCCCCCCCCCCC
22.0522985185
49PhosphorylationVSRRRHNSSDGFFNN
CCCCCCCCCCCCCCC
24.5522167270
50PhosphorylationSRRRHNSSDGFFNNG
CCCCCCCCCCCCCCC
47.2527273156
61PhosphorylationFNNGPLRTAGDSWHQ
CCCCCCCCCCCCCCC
42.5523186163
65PhosphorylationPLRTAGDSWHQPSLF
CCCCCCCCCCCCCCC
26.0723186163
70PhosphorylationGDSWHQPSLFRHDSV
CCCCCCCCCCCCCCC
33.3023917254
76PhosphorylationPSLFRHDSVDSGVSK
CCCCCCCCCCCCCCC
23.0027273156
79PhosphorylationFRHDSVDSGVSKGAY
CCCCCCCCCCCCCCC
38.6529396449
82PhosphorylationDSVDSGVSKGAYAGI
CCCCCCCCCCCCEEC
28.9723403867
86PhosphorylationSGVSKGAYAGITGNP
CCCCCCCCEECCCCC
17.6527642862
90PhosphorylationKGAYAGITGNPSGWH
CCCCEECCCCCCCCC
29.95-
94PhosphorylationAGITGNPSGWHSSSR
EECCCCCCCCCCCCC
59.52-
98PhosphorylationGNPSGWHSSSRGHDG
CCCCCCCCCCCCCCC
24.4125159151
99PhosphorylationNPSGWHSSSRGHDGM
CCCCCCCCCCCCCCC
15.9227080861
100PhosphorylationPSGWHSSSRGHDGMS
CCCCCCCCCCCCCCC
45.3427080861
101MethylationSGWHSSSRGHDGMSQ
CCCCCCCCCCCCCCC
48.70-
109MethylationGHDGMSQRSGGGTGN
CCCCCCCCCCCCCCC
29.93-
123PhosphorylationNHRHWNGSFHSRKGC
CCCCCCCCCCCCCCC
19.3021406692
126PhosphorylationHWNGSFHSRKGCAFQ
CCCCCCCCCCCCCCC
33.4121406692
161PhosphorylationFEEEDFPSLNPEAGK
CCCCCCCCCCCCCCC
40.5527251275
193PhosphorylationPPSAKQPSKMLVIKK
CCCCCCCCCEEEEEE
28.3630576142
199MethylationPSKMLVIKKVSKEDP
CCCEEEEEECCCCCH
39.3823644510
200MethylationSKMLVIKKVSKEDPA
CCEEEEEECCCCCHH
40.3923644510
202PhosphorylationMLVIKKVSKEDPAAA
EEEEEECCCCCHHHH
38.9330108239
203AcetylationLVIKKVSKEDPAAAF
EEEEECCCCCHHHHH
69.957297989
203MethylationLVIKKVSKEDPAAAF
EEEEECCCCCHHHHH
69.9523644510
211PhosphorylationEDPAAAFSAAFTSPG
CCHHHHHHHHHCCCC
17.6021406692
215PhosphorylationAAFSAAFTSPGSHHA
HHHHHHHCCCCCCCC
29.3221406692
216PhosphorylationAFSAAFTSPGSHHAN
HHHHHHCCCCCCCCC
22.3225159151
219PhosphorylationAAFTSPGSHHANGNK
HHHCCCCCCCCCCCC
18.5821406692
228PhosphorylationHANGNKLSSVVPSVY
CCCCCCHHHCCCHHH
23.77-
229PhosphorylationANGNKLSSVVPSVYK
CCCCCHHHCCCHHHC
37.25-
233PhosphorylationKLSSVVPSVYKNLVP
CHHHCCCHHHCCCCC
26.8628555341
235PhosphorylationSSVVPSVYKNLVPKP
HHCCCHHHCCCCCCC
9.8628555341
248AcetylationKPVPPPSKPNAWKAN
CCCCCCCCCCCCHHH
48.3325953088
253MethylationPSKPNAWKANRMEHK
CCCCCCCHHHCCCCC
33.11-
265PhosphorylationEHKSGSLSSSRESAF
CCCCCCCCCCCHHHC
28.15-
270PhosphorylationSLSSSRESAFTSPIS
CCCCCCHHHCCCCCC
27.8028450419
273PhosphorylationSSRESAFTSPISVTK
CCCHHHCCCCCCCCC
33.0526657352
274PhosphorylationSRESAFTSPISVTKP
CCHHHCCCCCCCCCC
17.4925159151
277PhosphorylationSAFTSPISVTKPVVL
HHCCCCCCCCCCEEE
27.4128450419
279PhosphorylationFTSPISVTKPVVLAS
CCCCCCCCCCEEEEC
23.8828450419
286PhosphorylationTKPVVLASGAALSSP
CCCEEEECCCCCCCC
25.4622199227
291PhosphorylationLASGAALSSPKESPS
EECCCCCCCCCCCCC
39.6122199227
292PhosphorylationASGAALSSPKESPSS
ECCCCCCCCCCCCCC
40.6225159151
296PhosphorylationALSSPKESPSSTTPP
CCCCCCCCCCCCCCC
35.8929255136
298PhosphorylationSSPKESPSSTTPPIE
CCCCCCCCCCCCCEE
49.9830266825
299PhosphorylationSPKESPSSTTPPIEI
CCCCCCCCCCCCEEE
39.4226657352
300PhosphorylationPKESPSSTTPPIEIS
CCCCCCCCCCCEEEC
47.8930266825
301PhosphorylationKESPSSTTPPIEISS
CCCCCCCCCCEEECH
29.0830266825
307PhosphorylationTTPPIEISSSRLTKL
CCCCEEECHHHHHHH
14.9630266825
308PhosphorylationTPPIEISSSRLTKLT
CCCEEECHHHHHHHH
25.7430266825
309PhosphorylationPPIEISSSRLTKLTR
CCEEECHHHHHHHHH
25.2330266825
319PhosphorylationTKLTRRTTDRKSEFL
HHHHHHCCCCHHHHH
31.81-
353PhosphorylationLEDLEDNSTPEPKEN
HHHCCCCCCCCCCCC
58.6321815630
354PhosphorylationEDLEDNSTPEPKENG
HHCCCCCCCCCCCCC
37.6223401153
382PhosphorylationVEEGEVLSHSLEAEH
EECCCEECCCHHHHH
19.0623401153
384PhosphorylationEGEVLSHSLEAEHRL
CCCEECCCHHHHHHH
25.2425159151
400PhosphorylationKAMGWQEYPENDENC
HHCCCCCCCCCCCCC
10.76-
411PhosphorylationDENCLPLTEDELKEF
CCCCCCCCHHHHHHH
39.18-
438PhosphorylationGKNGFLQSRSSSLFS
CCCCCCCCCCCCCCC
35.9626546556
440PhosphorylationNGFLQSRSSSLFSPW
CCCCCCCCCCCCCCC
29.5328450419
441PhosphorylationGFLQSRSSSLFSPWR
CCCCCCCCCCCCCCH
29.9230576142
442PhosphorylationFLQSRSSSLFSPWRS
CCCCCCCCCCCCCHH
34.3828450419
445PhosphorylationSRSSSLFSPWRSTCK
CCCCCCCCCCHHHEE
28.9225159151

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 GPBL1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GPBL1_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 GPBL1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PKHF2_HUMANPLEKHF2physical
16189514
GATA_HUMANQRSL1physical
28514442
TAC2N_HUMANTC2Nphysical
28514442
PLCD3_HUMANPLCD3physical
28514442
KANL2_HUMANKANSL2physical
28514442
CNO11_HUMANCNOT11physical
28514442
AMPD2_HUMANAMPD2physical
28514442
ZBTB1_HUMANZBTB1physical
28514442
MCRS1_HUMANMCRS1physical
28514442
MAP2_HUMANMETAP2physical
28514442
PI42C_HUMANPIP4K2Cphysical
28514442
UTP6_HUMANUTP6physical
28514442
CNO10_HUMANCNOT10physical
28514442
CNOT2_HUMANCNOT2physical
28514442
PI42B_HUMANPIP4K2Bphysical
28514442
AP2A1_HUMANAP2A1physical
28514442
AP2A2_HUMANAP2A2physical
28514442
ECD_HUMANECDphysical
28514442
ACD11_HUMANACAD11physical
28514442
CNOT1_HUMANCNOT1physical
28514442
EIF3A_HUMANEIF3Aphysical
28514442
TSSC4_HUMANTSSC4physical
28514442
AP1B1_HUMANAP1B1physical
28514442
CNOT8_HUMANCNOT8physical
28514442
EIF3E_HUMANEIF3Ephysical
28514442
E41L5_HUMANEPB41L5physical
28514442
DCAF5_HUMANDCAF5physical
28514442
EIF3C_HUMANEIF3Cphysical
28514442
EIF3H_HUMANEIF3Hphysical
28514442
AP2S1_HUMANAP2S1physical
28514442
CNO6L_HUMANCNOT6Lphysical
28514442
PDD2L_HUMANPDCD2Lphysical
28514442
U520_HUMANSNRNP200physical
28514442
AP2M1_HUMANAP2M1physical
28514442
EIF3M_HUMANEIF3Mphysical
28514442
CNOT9_HUMANRQCD1physical
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 GPBL1_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-49, AND MASSSPECTROMETRY.
"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-49, AND MASSSPECTROMETRY.

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