VINEX_HUMAN - dbPTM
VINEX_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VINEX_HUMAN
UniProt AC O60504
Protein Name Vinexin
Gene Name SORBS3
Organism Homo sapiens (Human).
Sequence Length 671
Subcellular Localization Isoform Alpha: Cell junction. Cytoplasm, cytoskeleton. Localized at cell-extracellular matrix junctions (By similarity). Both isoforms were localized at focal adhesion and cell-cell adhesion sites..
Isoform Beta: Cell junction. Nucleus. Cytoplasm, c
Protein Description Vinexin alpha isoform promotes up-regulation of actin stress fiber formation. Vinexin beta isoform plays a role in cell spreading and enhances the activation of JNK/SAPK in response to EGF stimulation by using its third SH3 domain..
Protein Sequence MQGPPRSLRAGLSLDDFIPGHLQSHIGSSSRGTRVPVIRNGGSNTLNFQFHDPAPRTVCNGGYTPRRDASQHPDPAWYQTWPGPGSKPSASTKIPASQHTQNWSATWTKDSKRRDKRWVKYEGIGPVDESGMPIAPRSSVDRPRDWYRRMFQQIHRKMPDLQLDWTFEEPPRDPRHLGAQQRPAHRPGPATSSSGRSWDHSEELPRSTFNYRPGAFSTVLQPSNQVLRRREKVDNVWTEESWNQFLQELETGQRPKKPLVDDPGEKPSQPIEVLLERELAELSAELDKDLRAIETRLPSPKSSPAPRRAPEQRPPAGPASAWSSSYPHAPYLGSARSLSPHKMADGGSPFLGRRDFVYPSSTRDPSASNGGGSPARREEKKRKAARLKFDFQAQSPKELTLQKGDIVYIHKEVDKNWLEGEHHGRLGIFPANYVEVLPADEIPKPIKPPTYQVLEYGEAVAQYTFKGDLEVELSFRKGEHICLIRKVNENWYEGRITGTGRQGIFPASYVQVSREPRLRLCDDGPQLPTSPRLTAAARSARHPSSPSALRSPADPIDLGGQTSPRRTGFSFPTQEPRPQTQNLGTPGPALSHSRGPSHPLDLGTSSPNTSQIHWTPYRAMYQYRPQNEDELELREGDRVDVMQQCDDGWFVGVSRRTQKFGTFPGNYVAPV
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
2 (in isoform 2)Acetylation-73.4419369195
6 (in isoform 2)Phosphorylation-52.0025849741
13PhosphorylationRSLRAGLSLDDFIPG
CCCCCCCCHHHCCCC		28.9126657352
24PhosphorylationFIPGHLQSHIGSSSR
CCCCHHHHHCCCCCC		24.3523312004
28PhosphorylationHLQSHIGSSSRGTRV
HHHHHCCCCCCCCEE		25.2528857561
29PhosphorylationLQSHIGSSSRGTRVP
HHHHCCCCCCCCEEE		20.8828857561
30PhosphorylationQSHIGSSSRGTRVPV
HHHCCCCCCCCEEEE		36.1028857561
55UbiquitinationFQFHDPAPRTVCNGG
EEECCCCCCCCCCCC		37.5529967540
61UbiquitinationAPRTVCNGGYTPRRD
CCCCCCCCCCCCCCC		25.9229967540
64PhosphorylationTVCNGGYTPRRDASQ
CCCCCCCCCCCCCCC		17.3727251275
73UbiquitinationRRDASQHPDPAWYQT
CCCCCCCCCCCHHCC		41.4629967540
80PhosphorylationPDPAWYQTWPGPGSK
CCCCHHCCCCCCCCC		20.2428857561
97PhosphorylationASTKIPASQHTQNWS
CCCCCCHHHCCCCCE		19.6930576142
100PhosphorylationKIPASQHTQNWSATW
CCCHHHCCCCCEEEE		18.8930576142
104PhosphorylationSQHTQNWSATWTKDS
HHCCCCCEEEECCCC		24.3029514088
106PhosphorylationHTQNWSATWTKDSKR
CCCCCEEEECCCCCH		28.3129514088
108PhosphorylationQNWSATWTKDSKRRD
CCCEEEECCCCCHHC		22.1829514088
111PhosphorylationSATWTKDSKRRDKRW
EEEECCCCCHHCCCC		29.6228857561
112AcetylationATWTKDSKRRDKRWV
EEECCCCCHHCCCCE		62.687823933
116AcetylationKDSKRRDKRWVKYEG
CCCCHHCCCCEEEEC		46.477823941
188PhosphorylationQRPAHRPGPATSSSG
CCCCCCCCCCCCCCC		25.1632142685
191PhosphorylationAHRPGPATSSSGRSW
CCCCCCCCCCCCCCC		32.0723312004
192PhosphorylationHRPGPATSSSGRSWD
CCCCCCCCCCCCCCC		25.3123312004
192O-linked_GlycosylationHRPGPATSSSGRSWD
CCCCCCCCCCCCCCC		25.3130379171
193PhosphorylationRPGPATSSSGRSWDH
CCCCCCCCCCCCCCC		32.2423312004
194PhosphorylationPGPATSSSGRSWDHS
CCCCCCCCCCCCCCC		37.6823312004
197PhosphorylationATSSSGRSWDHSEEL
CCCCCCCCCCCCCCC		40.1428857561
201PhosphorylationSGRSWDHSEELPRST
CCCCCCCCCCCCCCC		30.2328857561
217PhosphorylationNYRPGAFSTVLQPSN
CCCCCCCHHHCCCCH		19.6417192257
218PhosphorylationYRPGAFSTVLQPSNQ
CCCCCCHHHCCCCHH		20.8417192257
221PhosphorylationGAFSTVLQPSNQVLR
CCCHHHCCCCHHHHH		34.7332645325
268PhosphorylationDDPGEKPSQPIEVLL
CCCCCCCCCCHHHHH		60.7120068231
283PhosphorylationERELAELSAELDKDL
HHHHHHHHHHHHHHH		15.9427251275
295PhosphorylationKDLRAIETRLPSPKS
HHHHHHHHCCCCCCC		31.2429514088
299PhosphorylationAIETRLPSPKSSPAP
HHHHCCCCCCCCCCC		49.9425159151
301UbiquitinationETRLPSPKSSPAPRR
HHCCCCCCCCCCCCC		68.8329967540
302PhosphorylationTRLPSPKSSPAPRRA
HCCCCCCCCCCCCCC		44.9630576142
303PhosphorylationRLPSPKSSPAPRRAP
CCCCCCCCCCCCCCC		31.0730576142
337PhosphorylationPYLGSARSLSPHKMA
CCCCCCCCCCCCCCC		32.6823836654
339PhosphorylationLGSARSLSPHKMADG
CCCCCCCCCCCCCCC		26.6327422710
348PhosphorylationHKMADGGSPFLGRRD
CCCCCCCCCCCCCCC		20.2929255136
358PhosphorylationLGRRDFVYPSSTRDP
CCCCCEECCCCCCCC		9.4423312004
360PhosphorylationRRDFVYPSSTRDPSA
CCCEECCCCCCCCCC		27.0123312004
361PhosphorylationRDFVYPSSTRDPSAS
CCEECCCCCCCCCCC		23.9823312004
362PhosphorylationDFVYPSSTRDPSASN
CEECCCCCCCCCCCC		43.3523312004
366PhosphorylationPSSTRDPSASNGGGS
CCCCCCCCCCCCCCC		48.9330266825
368PhosphorylationSTRDPSASNGGGSPA
CCCCCCCCCCCCCHH		40.1030266825
373PhosphorylationSASNGGGSPARREEK
CCCCCCCCHHHHHHH		20.7523401153
395PhosphorylationKFDFQAQSPKELTLQ
CCCCCCCCCCEEEEC		40.7419664994
397UbiquitinationDFQAQSPKELTLQKG
CCCCCCCCEEEECCC		71.2829967540
403UbiquitinationPKELTLQKGDIVYIH
CCEEEECCCCEEEEE		62.7629967540
408PhosphorylationLQKGDIVYIHKEVDK
ECCCCEEEEEEECCC		9.5327642862
415UbiquitinationYIHKEVDKNWLEGEH
EEEEECCCCCCCCCC		56.0229967540
477MalonylationEVELSFRKGEHICLI
EEEEEEECCCEEEEE		67.6426320211
497PhosphorylationNWYEGRITGTGRQGI
CEEECCCCCCCCCCC		27.5929978859
499PhosphorylationYEGRITGTGRQGIFP
EECCCCCCCCCCCCC		22.1229978859
508PhosphorylationRQGIFPASYVQVSRE
CCCCCCCHHEEECCC		26.5228152594
509PhosphorylationQGIFPASYVQVSREP
CCCCCCHHEEECCCC		9.3028152594
513PhosphorylationPASYVQVSREPRLRL
CCHHEEECCCCCEEE		17.5228152594
529PhosphorylationDDGPQLPTSPRLTAA
CCCCCCCCCHHHHHH		61.0129255136
530PhosphorylationDGPQLPTSPRLTAAA
CCCCCCCCHHHHHHH		13.1919664994
534PhosphorylationLPTSPRLTAAARSAR
CCCCHHHHHHHHHCC		18.6122199227
539PhosphorylationRLTAAARSARHPSSP
HHHHHHHHCCCCCCH		25.5723403867
544PhosphorylationARSARHPSSPSALRS
HHHCCCCCCHHHHCC		49.0829255136
545PhosphorylationRSARHPSSPSALRSP
HHCCCCCCHHHHCCC		27.5929255136
547PhosphorylationARHPSSPSALRSPAD
CCCCCCHHHHCCCCC		41.7130266825
551PhosphorylationSSPSALRSPADPIDL
CCHHHHCCCCCCCCC		25.8623927012
556PhosphorylationLRSPADPIDLGGQTS
HCCCCCCCCCCCCCC		7.6018669648
562PhosphorylationPIDLGGQTSPRRTGF
CCCCCCCCCCCCCCC		43.9323927012
563PhosphorylationIDLGGQTSPRRTGFS
CCCCCCCCCCCCCCC		14.4419664994
567PhosphorylationGQTSPRRTGFSFPTQ
CCCCCCCCCCCCCCC		43.8126074081
573PhosphorylationRTGFSFPTQEPRPQT
CCCCCCCCCCCCCCC		43.4828857561
580PhosphorylationTQEPRPQTQNLGTPG
CCCCCCCCCCCCCCC		23.3128857561
585PhosphorylationPQTQNLGTPGPALSH
CCCCCCCCCCCCCCC		28.3925159151
591PhosphorylationGTPGPALSHSRGPSH
CCCCCCCCCCCCCCC		22.8620068231
593PhosphorylationPGPALSHSRGPSHPL
CCCCCCCCCCCCCCC		35.2420068231
594MethylationGPALSHSRGPSHPLD
CCCCCCCCCCCCCCC		56.47115919841
597PhosphorylationLSHSRGPSHPLDLGT
CCCCCCCCCCCCCCC		40.3323927012
604PhosphorylationSHPLDLGTSSPNTSQ
CCCCCCCCCCCCCCC		33.0723927012
605PhosphorylationHPLDLGTSSPNTSQI
CCCCCCCCCCCCCCC		41.8422167270
606PhosphorylationPLDLGTSSPNTSQIH
CCCCCCCCCCCCCCC		23.2322167270
609PhosphorylationLGTSSPNTSQIHWTP
CCCCCCCCCCCCCCC		25.9523927012
610PhosphorylationGTSSPNTSQIHWTPY
CCCCCCCCCCCCCCC		33.5023927012
615PhosphorylationNTSQIHWTPYRAMYQ
CCCCCCCCCCCCCEE		9.0425159151
617PhosphorylationSQIHWTPYRAMYQYR
CCCCCCCCCCCEEEC		12.0223403867
620SulfoxidationHWTPYRAMYQYRPQN
CCCCCCCCEEECCCC		1.2630846556
621PhosphorylationWTPYRAMYQYRPQNE
CCCCCCCEEECCCCH		11.0426074081
623PhosphorylationPYRAMYQYRPQNEDE
CCCCCEEECCCCHHC		13.5326074081
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
188SPhosphorylationKinaseMAPK1P28482
GPS
188SPhosphorylationKinaseERK1P27361
PSP
530SPhosphorylationKinaseMAPK1P28482
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
530SPhosphorylation

16964243
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 VINEX_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBMX_HUMANRBMXphysical
16189514
SKT_HUMANKIAA1217physical
16189514
DMRTB_HUMANDMRTB1physical
16189514
ATL4_HUMANADAMTSL4physical
16189514
CPSF7_HUMANCPSF7physical
16189514
EFS_HUMANEFSphysical
16189514
DDX17_HUMANDDX17physical
16189514
MK01_HUMANMAPK1physical
15184391
DLG5_HUMANDLG5physical
12657639
CBL_HUMANCBLphysical
16923119
SRCN1_HUMANSRCIN1physical
18662323
WASL_HUMANWASLphysical
18662323
SYPH_HUMANSYPphysical
18662323
AKT1_HUMANAKT1physical
15784622
VINEX_HUMANSORBS3physical
25416956
HNRL1_HUMANHNRNPUL1physical
25416956
DIP2A_HUMANDIP2Aphysical
25416956
ZBT7B_HUMANZBTB7Bphysical
25416956
SPN90_HUMANNCKIPSDphysical
25416956
VP37C_HUMANVPS37Cphysical
25416956
TB22B_HUMANTBC1D22Bphysical
25416956
ZC4H2_HUMANZC4H2physical
25416956
PAK5_HUMANPAK7physical
25416956
SYVM_HUMANVARS2physical
25416956
SH24A_HUMANSH2D4Aphysical
25416956
VP37B_HUMANVPS37Bphysical
25416956
TRI41_HUMANTRIM41physical
25416956
SAXO1_HUMANFAM154Aphysical
25416956
CPNE2_HUMANCPNE2physical
25416956
PAK2_HUMANPAK2physical
21516116
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 VINEX_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-530 AND SER-563, ANDMASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348; SER-530 ANDSER-563, AND MASS SPECTROMETRY.
"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-530 AND SER-563, 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-395; SER-530; SER-545;SER-551 AND SER-563, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; THR-218; SER-395;SER-530; SER-545 AND SER-563, 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-563, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-529 AND SER-530, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348; SER-545 ANDSER-551, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530 AND SER-563, ANDMASS SPECTROMETRY.

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