VINC_MOUSE - dbPTM
VINC_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VINC_MOUSE
UniProt AC Q64727
Protein Name Vinculin
Gene Name Vcl
Organism Mus musculus (Mouse).
Sequence Length 1066
Subcellular Localization Cell membrane
Peripheral membrane protein
Cytoplasmic side . Cell junction, adherens junction . Cell junction, focal adhesion . Cytoplasm, cytoskeleton . Cell membrane, sarcolemma
Peripheral membrane protein
Cytoplasmic side . Recruitment to
Protein Description Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion (By similarity)..
Protein Sequence MPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVAAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVQAAQMLQSDPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTVEKMSAEINEIIRVLQLTSWDEDAWASKDTEAMKRALASIDSKLNQAKGWLRDPNASPGDAGEQAIRQILDEAGKVGELCAGKERREILGTCKMLGQMTDQVADLRARGQGASPVAMQKAQQVSQGLDVLTAKVENAARKLEAMTNSKQSIAKKIDAAQNWLADPNGGPEGEEQIRGALAEARKIAELCDDPKERDDILRSLGEIAALTSKLGDLRRQGKGDSPEARALAKQVATALQNLQTKTNRAVANSRPAKAAVHLEGKIEQAQRWIDNPTVDDRGVGQAAIRGLVAEGHRLANVMMGPYRQDLLAKCDRVDQLTAQLADLAARGEGESPQARALASQLQDSLKDLKAQMQEAMTQEVSDVFSDTTTPIKLLAVAATAPPDAPNREEVFDERAANFENHSGRLGATAEKAAAVGTANKSTVEGIQASVKTARELTPQVISAARILLRNPGNQAAYEHFETMKNQWIDNVEKMTGLVDEAIDTKSLLDASEEAIKKDLDKCKVAMANIQPQMLVAGATSIARRANRILLVAKREVENSEDPKFREAVKAASDELSKTISPMVMDAKAVAGNISDPGLQKSFLDSGYRILGAVAKVREAFQPQEPDFPPPPPDLEQLRLTDELAPPKPPLPEGEVPPPRPPPPEEKDEEFPEQKAGEVINQPMMMAARQLHDEARKWSSKGNDIIAAAKRMALLMAEMSRLVRGGSGTKRALIQCAKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKILSTVKATMLGRTNISDEESEQATEMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLRWVRKTPWYQ
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
52PhosphorylationAAVQAAVSNLVRVGK
HHHHHHHHHHHHCCC
21.51-
59UbiquitinationSNLVRVGKETVQTTE
HHHHHCCCCCCCCCH
47.5622790023
71AcetylationTTEDQILKRDMPPAF
CCHHHHHHCCCCHHH
48.2422826441
80AcetylationDMPPAFIKVENACTK
CCCHHHHHHHHHHHH
36.7222826441
97PhosphorylationQAAQMLQSDPYSVPA
HHHHHHHCCCCCCCH
36.2727180971
100PhosphorylationQMLQSDPYSVPARDY
HHHHCCCCCCCHHHE
27.5627742792
101PhosphorylationMLQSDPYSVPARDYL
HHHCCCCCCCHHHEE
27.3227742792
170AcetylationNLGPGMTKMAKMIDE
CCCCCHHHHHHHHHH
28.1523806337
170MalonylationNLGPGMTKMAKMIDE
CCCCCHHHHHHHHHH
28.1526320211
170SuccinylationNLGPGMTKMAKMIDE
CCCCCHHHHHHHHHH
28.1523806337
173AcetylationPGMTKMAKMIDERQQ
CCHHHHHHHHHHHHH
32.6522826441
183PhosphorylationDERQQELTHQEHRVM
HHHHHHHCCCHHHHH
22.2929899451
197PhosphorylationMLVNSMNTVKELLPV
HHHHCHHHHHHHHHH
25.0629899451
216UbiquitinationMKIFVTTKNSKNQGI
HHHEEECCCCCCCCH
50.2722790023
219UbiquitinationFVTTKNSKNQGIEEA
EEECCCCCCCCHHHH
63.7822790023
228UbiquitinationQGIEEALKNRNFTVE
CCHHHHHHCCCCCHH
61.9922790023
251PhosphorylationIIRVLQLTSWDEDAW
HHHHHHCCCCCCCHH
18.1425195567
260PhosphorylationWDEDAWASKDTEAMK
CCCCHHHCCCHHHHH
21.9922817900
261UbiquitinationDEDAWASKDTEAMKR
CCCHHHCCCHHHHHH
62.0122790023
272PhosphorylationAMKRALASIDSKLNQ
HHHHHHHHHHHHHHH
27.9826824392
275PhosphorylationRALASIDSKLNQAKG
HHHHHHHHHHHHCCC
37.0525521595
276AcetylationALASIDSKLNQAKGW
HHHHHHHHHHHCCCC
47.9423806337
276SuccinylationALASIDSKLNQAKGW
HHHHHHHHHHHCCCC
47.9423806337
276UbiquitinationALASIDSKLNQAKGW
HHHHHHHHHHHCCCC
47.94-
281UbiquitinationDSKLNQAKGWLRDPN
HHHHHHCCCCCCCCC
40.6422790023
290PhosphorylationWLRDPNASPGDAGEQ
CCCCCCCCCCHHHHH
35.7424925903
308UbiquitinationQILDEAGKVGELCAG
HHHHHHCCHHHHHCC
54.8622790023
316AcetylationVGELCAGKERREILG
HHHHHCCHHHHHHHH
29.53134199
316MalonylationVGELCAGKERREILG
HHHHHCCHHHHHHHH
29.5326320211
324PhosphorylationERREILGTCKMLGQM
HHHHHHHHHHHHHCC
12.9017203969
326AcetylationREILGTCKMLGQMTD
HHHHHHHHHHHCCHH
36.6823236377
332PhosphorylationCKMLGQMTDQVADLR
HHHHHCCHHHHHHHH
18.5226643407
346PhosphorylationRARGQGASPVAMQKA
HHCCCCCCHHHHHHH
27.0825521595
352AcetylationASPVAMQKAQQVSQG
CCHHHHHHHHHHHHC
34.7722826441
357PhosphorylationMQKAQQVSQGLDVLT
HHHHHHHHHCHHHHH
17.7527180971
364PhosphorylationSQGLDVLTAKVENAA
HHCHHHHHHHHHHHH
25.0426824392
366AcetylationGLDVLTAKVENAARK
CHHHHHHHHHHHHHH
44.8622826441
366UbiquitinationGLDVLTAKVENAARK
CHHHHHHHHHHHHHH
44.8622790023
378PhosphorylationARKLEAMTNSKQSIA
HHHHHHHHCCHHHHH
43.3126824392
380PhosphorylationKLEAMTNSKQSIAKK
HHHHHHCCHHHHHHH
23.9426824392
381UbiquitinationLEAMTNSKQSIAKKI
HHHHHCCHHHHHHHH
50.5722790023
383PhosphorylationAMTNSKQSIAKKIDA
HHHCCHHHHHHHHHH
28.4026824392
387UbiquitinationSKQSIAKKIDAAQNW
CHHHHHHHHHHHHHH
36.4822790023
434PhosphorylationERDDILRSLGEIAAL
HHHHHHHHHHHHHHH
36.9625521595
442PhosphorylationLGEIAALTSKLGDLR
HHHHHHHHHHHHHHH
21.0626824392
443PhosphorylationGEIAALTSKLGDLRR
HHHHHHHHHHHHHHH
27.0827180971
444AcetylationEIAALTSKLGDLRRQ
HHHHHHHHHHHHHHC
51.7822826441
444UbiquitinationEIAALTSKLGDLRRQ
HHHHHHHHHHHHHHC
51.7822790023
456PhosphorylationRRQGKGDSPEARALA
HHCCCCCCHHHHHHH
33.0526824392
464UbiquitinationPEARALAKQVATALQ
HHHHHHHHHHHHHHH
46.2722790023
475PhosphorylationTALQNLQTKTNRAVA
HHHHHHHHHHHHHHH
42.9025338131
476UbiquitinationALQNLQTKTNRAVAN
HHHHHHHHHHHHHHH
30.7322790023
496AcetylationAAVHLEGKIEQAQRW
HHHHHCHHHHHHHHH
33.4223236377
537PhosphorylationANVMMGPYRQDLLAK
HCHHCCHHHHHHHHH
18.3825195567
545S-nitrosocysteineRQDLLAKCDRVDQLT
HHHHHHHCCHHHHHH
3.16-
545S-nitrosylationRQDLLAKCDRVDQLT
HHHHHHHCCHHHHHH
3.1620925432
566PhosphorylationAARGEGESPQARALA
HHCCCCCCHHHHHHH
32.9226824392
574PhosphorylationPQARALASQLQDSLK
HHHHHHHHHHHHHHH
32.0724899341
579PhosphorylationLASQLQDSLKDLKAQ
HHHHHHHHHHHHHHH
25.1026824392
581AcetylationSQLQDSLKDLKAQMQ
HHHHHHHHHHHHHHH
66.0423236377
581UbiquitinationSQLQDSLKDLKAQMQ
HHHHHHHHHHHHHHH
66.0422790023
584UbiquitinationQDSLKDLKAQMQEAM
HHHHHHHHHHHHHHH
46.8622790023
596PhosphorylationEAMTQEVSDVFSDTT
HHHHHHHHHHHCCCC
27.5725619855
600PhosphorylationQEVSDVFSDTTTPIK
HHHHHHHCCCCCCCH
33.6227087446
602PhosphorylationVSDVFSDTTTPIKLL
HHHHHCCCCCCCHHE
31.2225619855
603PhosphorylationSDVFSDTTTPIKLLA
HHHHCCCCCCCHHEH
35.2525619855
604PhosphorylationDVFSDTTTPIKLLAV
HHHCCCCCCCHHEHH
25.7127087446
614PhosphorylationKLLAVAATAPPDAPN
HHEHHHHCCCCCCCC
29.9325338131
637PhosphorylationAANFENHSGRLGATA
HHHCCCCCCCCCCHH
36.8726824392
643PhosphorylationHSGRLGATAEKAAAV
CCCCCCCHHHHHHHH
33.2829514104
646AcetylationRLGATAEKAAAVGTA
CCCCHHHHHHHHCCC
40.6423806337
646SuccinylationRLGATAEKAAAVGTA
CCCCHHHHHHHHCCC
40.6423806337
655UbiquitinationAAVGTANKSTVEGIQ
HHHCCCCHHHHHHHH
45.0722790023
656PhosphorylationAVGTANKSTVEGIQA
HHCCCCHHHHHHHHH
37.1826824392
664PhosphorylationTVEGIQASVKTAREL
HHHHHHHHHHHHHHH
14.0522871156
666UbiquitinationEGIQASVKTARELTP
HHHHHHHHHHHHHCH
33.6922790023
672PhosphorylationVKTARELTPQVISAA
HHHHHHHCHHHHHHH
13.61-
677PhosphorylationELTPQVISAARILLR
HHCHHHHHHHHHHHH
19.6126824392
692PhosphorylationNPGNQAAYEHFETMK
CCCCHHHHHHHHHHH
16.9826824392
697PhosphorylationAAYEHFETMKNQWID
HHHHHHHHHHHHHHH
32.2829472430
699AcetylationYEHFETMKNQWIDNV
HHHHHHHHHHHHHHH
54.1023236377
699UbiquitinationYEHFETMKNQWIDNV
HHHHHHHHHHHHHHH
54.1022790023
710PhosphorylationIDNVEKMTGLVDEAI
HHHHHHHHCCCCHHH
38.1325777480
719PhosphorylationLVDEAIDTKSLLDAS
CCCHHHCHHHHHHHC
19.2026239621
720UbiquitinationVDEAIDTKSLLDASE
CCHHHCHHHHHHHCH
35.0422790023
721PhosphorylationDEAIDTKSLLDASEE
CHHHCHHHHHHHCHH
35.9425521595
726PhosphorylationTKSLLDASEEAIKKD
HHHHHHHCHHHHHHH
35.3226824392
731AcetylationDASEEAIKKDLDKCK
HHCHHHHHHHHHHHC
47.4823236377
731UbiquitinationDASEEAIKKDLDKCK
HHCHHHHHHHHHHHC
47.4822790023
754PhosphorylationQMLVAGATSIARRAN
HHHHHCHHHHHHHHH
21.5426824392
755PhosphorylationMLVAGATSIARRANR
HHHHCHHHHHHHHHH
17.4530352176
768MalonylationNRILLVAKREVENSE
HHHEEEEEHHHCCCC
41.4326320211
774PhosphorylationAKREVENSEDPKFRE
EEHHHCCCCCHHHHH
29.8517203969
778AcetylationVENSEDPKFREAVKA
HCCCCCHHHHHHHHH
70.1822826441
778UbiquitinationVENSEDPKFREAVKA
HCCCCCHHHHHHHHH
70.1822790023
784AcetylationPKFREAVKAASDELS
HHHHHHHHHHHHHHH
45.337719587
784UbiquitinationPKFREAVKAASDELS
HHHHHHHHHHHHHHH
45.3322790023
787PhosphorylationREAVKAASDELSKTI
HHHHHHHHHHHHHCC
36.1626824392
792UbiquitinationAASDELSKTISPMVM
HHHHHHHHCCCHHHH
63.6022790023
793PhosphorylationASDELSKTISPMVMD
HHHHHHHCCCHHHHC
24.2623984901
795PhosphorylationDELSKTISPMVMDAK
HHHHHCCCHHHHCHH
16.5126824392
802AcetylationSPMVMDAKAVAGNIS
CHHHHCHHHHCCCCC
38.8523236377
802UbiquitinationSPMVMDAKAVAGNIS
CHHHHCHHHHCCCCC
38.8522790023
809PhosphorylationKAVAGNISDPGLQKS
HHHCCCCCCCHHHHH
41.5825521595
815AcetylationISDPGLQKSFLDSGY
CCCCHHHHHHHHHHH
48.4922826441
815UbiquitinationISDPGLQKSFLDSGY
CCCCHHHHHHHHHHH
48.4922790023
816PhosphorylationSDPGLQKSFLDSGYR
CCCHHHHHHHHHHHH
20.3426824392
820PhosphorylationLQKSFLDSGYRILGA
HHHHHHHHHHHHHHH
39.6126239621
822PhosphorylationKSFLDSGYRILGAVA
HHHHHHHHHHHHHHH
9.8325521595
830UbiquitinationRILGAVAKVREAFQP
HHHHHHHHHHHHHCC
34.9122790023
913PhosphorylationHDEARKWSSKGNDII
HHHHHHHHHCCHHHH
25.8022817900
915AcetylationEARKWSSKGNDIIAA
HHHHHHHCCHHHHHH
57.1022826441
915MalonylationEARKWSSKGNDIIAA
HHHHHHHCCHHHHHH
57.1026320211
915UbiquitinationEARKWSSKGNDIIAA
HHHHHHHCCHHHHHH
57.10-
924AcetylationNDIIAAAKRMALLMA
HHHHHHHHHHHHHHH
37.6722826441
924UbiquitinationNDIIAAAKRMALLMA
HHHHHHHHHHHHHHH
37.6722790023
941PhosphorylationSRLVRGGSGTKRALI
HHHHCCCCCHHHHHH
46.2229514104
952AcetylationRALIQCAKDIAKASD
HHHHHHHHHHHHCCH
58.2423806337
952MalonylationRALIQCAKDIAKASD
HHHHHHHHHHHHCCH
58.2426320211
956MalonylationQCAKDIAKASDEVTR
HHHHHHHHCCHHHHH
49.0826320211
956UbiquitinationQCAKDIAKASDEVTR
HHHHHHHHCCHHHHH
49.08-
990PhosphorylationQVCERIPTISTQLKI
HHHHHCCCHHHHHHH
25.7827180971
993PhosphorylationERIPTISTQLKILST
HHCCCHHHHHHHHHH
33.7926824392
996UbiquitinationPTISTQLKILSTVKA
CCHHHHHHHHHHHHH
31.6122790023
1002AcetylationLKILSTVKATMLGRT
HHHHHHHHHHHCCCC
37.9222826441
1002UbiquitinationLKILSTVKATMLGRT
HHHHHHHHHHHCCCC
37.9222790023
1033PhosphorylationNAQNLMQSVKETVRE
HHHHHHHHHHHHHHH
22.61-
1035UbiquitinationQNLMQSVKETVREAE
HHHHHHHHHHHHHHH
53.5722790023
1047AcetylationEAEAASIKIRTDAGF
HHHHHCCEEEECCCC
24.5222826441
1055PhosphorylationIRTDAGFTLRWVRKT
EEECCCCEEEEHHCC
17.9426824392
1065PhosphorylationWVRKTPWYQ------
EHHCCCCCC------
12.9220006947

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
1065YPhosphorylationKinaseSRC-TYPE TYR-KINASES-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VINC_MOUSE !!

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 VINC_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAVR1_MOUSERaver1physical
11724819

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290 AND SER-721, ANDMASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290 AND SER-721, ANDMASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-324 AND SER-774, ANDMASS SPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290, AND MASSSPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-822, AND MASSSPECTROMETRY.

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