VINEX_MOUSE - dbPTM
VINEX_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VINEX_MOUSE
UniProt AC Q9R1Z8
Protein Name Vinexin
Gene Name Sorbs3
Organism Mus musculus (Mouse).
Sequence Length 733
Subcellular Localization Cell junction, focal adhesion. Cell junction. Cytoplasm, cytoskeleton. Localized at focal adhesion sites, cell-cell junctions and cell-extracellular matrix junctions.
Protein Description Promotes up-regulation of actin stress fiber formation..
Protein Sequence MARILGVGRSSASSLNNKEDNESDVALLSPKDPNRVHTKEQLAHPASSNLDPSMQGLPAGLSLDDFIPGHLRTHIGSSSRGTRVPVIRNGGSNTLNFQFHDPAPRTVCNGCPPPRRDGSLNPDPAWYQTWPGPGSRPSMSPKPPASQHAQNWSATWTKDSKRQDKRWVKYEGIGPVDESGMPIAPRSSVDSPRDWYRRMFQQIHRKMPDLQLDWTLEDPPKVVSARASSAEPRHLGTLQRPASRPGTTETSSGRNWNHSEETSRNTFNYNFRPSSSGLHPPNQVPRHREKVENVWTEDSWNQFLHELETGHKPKKPLVDDPVEKPAQPIEVLLERELAKLSAELDKDLRAIETRLPSPKNSQAPRRPLEQPGLEQQPSARLSSAWRPNSPHAPYFSSSRPLSPHRMADGGGSPFLGRRDFVYPSSAREPSASERGSSPSRKEEKKRKAARLKFDFQAQSPKELSLQKGDIVYIHKEVDKNWLEGEHHGRLGIFPANYVEVLPADEIPKPIKPPTYQVLEYGDAVAQYTFKGDLEVELSFRKGERICLIRKVNEHWYEGRITGTGRQGIFPASYVQINREPRLRLCDDGPQLPASPNPTTTAHLSSHSHPSSIPVDPTDWGGRTSPRRSAFPFPITLQEPRSQTQSLNTPGPTLSHPRATSRPINLGPSSPNTEIHWTPYRAMYQYRPQNEDELELREGDRVDVMQQCDDGWFVGVSRRTQKFGTFPGNYVAPV
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
10PhosphorylationRILGVGRSSASSLNN
CEECCCCCCHHHHCC
25.0725293948
11PhosphorylationILGVGRSSASSLNNK
EECCCCCCHHHHCCC
30.7025293948
13PhosphorylationGVGRSSASSLNNKED
CCCCCCHHHHCCCCC
36.9925293948
14PhosphorylationVGRSSASSLNNKEDN
CCCCCHHHHCCCCCC
34.5325293948
29PhosphorylationESDVALLSPKDPNRV
CCCCEECCCCCCCCC
30.6525521595
129PhosphorylationPDPAWYQTWPGPGSR
CCCHHHHCCCCCCCC
20.2422817900
140PhosphorylationPGSRPSMSPKPPASQ
CCCCCCCCCCCCHHH
33.8221183079
191PhosphorylationAPRSSVDSPRDWYRR
CCCCCCCCHHHHHHH
21.4926643407
229PhosphorylationVVSARASSAEPRHLG
EEEEECCCCCCCCCC
35.3518779572
237PhosphorylationAEPRHLGTLQRPASR
CCCCCCCCCCCCCCC
26.5224719451
243PhosphorylationGTLQRPASRPGTTET
CCCCCCCCCCCCCCC
41.5129472430
247PhosphorylationRPASRPGTTETSSGR
CCCCCCCCCCCCCCC
24.9229472430
248PhosphorylationPASRPGTTETSSGRN
CCCCCCCCCCCCCCC
43.0929472430
250PhosphorylationSRPGTTETSSGRNWN
CCCCCCCCCCCCCCC
26.5429472430
353PhosphorylationKDLRAIETRLPSPKN
HHHHHHHHCCCCCCC
31.2423984901
357PhosphorylationAIETRLPSPKNSQAP
HHHHCCCCCCCCCCC
53.7718779572
378PhosphorylationPGLEQQPSARLSSAW
CCCCCCCCCCHHCCC
22.9829514104
382PhosphorylationQQPSARLSSAWRPNS
CCCCCCHHCCCCCCC
16.6826643407
383PhosphorylationQPSARLSSAWRPNSP
CCCCCHHCCCCCCCC
36.1226643407
389PhosphorylationSSAWRPNSPHAPYFS
HCCCCCCCCCCCCCC
22.2727742792
394PhosphorylationPNSPHAPYFSSSRPL
CCCCCCCCCCCCCCC
19.5126643407
396PhosphorylationSPHAPYFSSSRPLSP
CCCCCCCCCCCCCCC
22.8926160508
397PhosphorylationPHAPYFSSSRPLSPH
CCCCCCCCCCCCCCC
22.0726160508
398PhosphorylationHAPYFSSSRPLSPHR
CCCCCCCCCCCCCCC
36.4026160508
402PhosphorylationFSSSRPLSPHRMADG
CCCCCCCCCCCCCCC
22.7327742792
406OxidationRPLSPHRMADGGGSP
CCCCCCCCCCCCCCC
3.4717242355
412PhosphorylationRMADGGGSPFLGRRD
CCCCCCCCCCCCCCC
18.7625521595
425PhosphorylationRDFVYPSSAREPSAS
CCCCCCCCCCCCCHH
27.1725338131
436PhosphorylationPSASERGSSPSRKEE
CCHHHCCCCCCHHHH
45.3424719451
437PhosphorylationSASERGSSPSRKEEK
CHHHCCCCCCHHHHH
29.7130352176
439PhosphorylationSERGSSPSRKEEKKR
HHCCCCCCHHHHHHH
58.9123608596
459PhosphorylationKFDFQAQSPKELSLQ
CCCCCCCCCCHHCCC
40.7426824392
472PhosphorylationLQKGDIVYIHKEVDK
CCCCCEEEEEEECCC
9.5329514104
594PhosphorylationDGPQLPASPNPTTTA
CCCCCCCCCCCCCCC
24.2226824392
598PhosphorylationLPASPNPTTTAHLSS
CCCCCCCCCCCCCCC
43.3425777480
599PhosphorylationPASPNPTTTAHLSSH
CCCCCCCCCCCCCCC
24.2025777480
600PhosphorylationASPNPTTTAHLSSHS
CCCCCCCCCCCCCCC
17.9825777480
604PhosphorylationPTTTAHLSSHSHPSS
CCCCCCCCCCCCCCC
19.0125777480
605PhosphorylationTTTAHLSSHSHPSSI
CCCCCCCCCCCCCCC
35.0625777480
607PhosphorylationTAHLSSHSHPSSIPV
CCCCCCCCCCCCCCC
38.7621659605
610PhosphorylationLSSHSHPSSIPVDPT
CCCCCCCCCCCCCCC
35.1623649490
611PhosphorylationSSHSHPSSIPVDPTD
CCCCCCCCCCCCCCC
35.0523649490
617PhosphorylationSSIPVDPTDWGGRTS
CCCCCCCCCCCCCCC
39.6625777480
623PhosphorylationPTDWGGRTSPRRSAF
CCCCCCCCCCCCCCC
46.4823567750
624PhosphorylationTDWGGRTSPRRSAFP
CCCCCCCCCCCCCCC
18.3021183079
628PhosphorylationGRTSPRRSAFPFPIT
CCCCCCCCCCCCCEE
35.2322817900
641PhosphorylationITLQEPRSQTQSLNT
EECCCCHHHCCCCCC
48.5829472430
643PhosphorylationLQEPRSQTQSLNTPG
CCCCHHHCCCCCCCC
22.7529472430
645PhosphorylationEPRSQTQSLNTPGPT
CCHHHCCCCCCCCCC
27.2929472430
648PhosphorylationSQTQSLNTPGPTLSH
HHCCCCCCCCCCCCC
34.6122028470
652PhosphorylationSLNTPGPTLSHPRAT
CCCCCCCCCCCCCCC
46.9729472430
654PhosphorylationNTPGPTLSHPRATSR
CCCCCCCCCCCCCCC
33.6429472430
659PhosphorylationTLSHPRATSRPINLG
CCCCCCCCCCCCCCC
26.9226643407
660PhosphorylationLSHPRATSRPINLGP
CCCCCCCCCCCCCCC
34.7726643407
668PhosphorylationRPINLGPSSPNTEIH
CCCCCCCCCCCCCEE
57.5421659605
669PhosphorylationPINLGPSSPNTEIHW
CCCCCCCCCCCCEEC
25.8826824392
672PhosphorylationLGPSSPNTEIHWTPY
CCCCCCCCCEECCCC
39.4323737553
677PhosphorylationPNTEIHWTPYRAMYQ
CCCCEECCCCHHHEE
9.0423984901
679PhosphorylationTEIHWTPYRAMYQYR
CCEECCCCHHHEEEC
12.0225777480

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
127YPhosphorylationKinaseABL-FAMILY-GPS
594SPhosphorylationKinaseMK01P63085
PhosphoELM
648TPhosphorylationKinaseMAPK1P63085
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
594SPhosphorylation

15184391

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAF1_MOUSERaf1physical
15836771

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VINEX_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Extracellular signal-regulated kinase activated by epidermal growthfactor and cell adhesion interacts with and phosphorylates vinexin.";
Mitsushima M., Suwa A., Amachi T., Ueda K., Kioka N.;
J. Biol. Chem. 279:34570-34577(2004).
Cited for: PHOSPHORYLATION AT SER-594, INTERACTION WITH MAPK1/ERK2, ANDSUBCELLULAR LOCATION.

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