VINC_RAT - dbPTM
VINC_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VINC_RAT
UniProt AC P85972
Protein Name Vinculin {ECO:0000250|UniProtKB:P18206}
Gene Name Vcl {ECO:0000250|UniProtKB:P18206}
Organism Rattus norvegicus (Rat).
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..
Protein Sequence MPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVAAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVQAAQMLQSDPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTVGKMSAEINEIIRVLQLTSWDEDAWASKDTEAMKRALASIDSKLNQAKGWLRDPNASPGDAGEQAIRQILDEAGKVGELCAGKERREILGTCKMLGQMTDQVADLRARGQGASPVAMQKAQQVSQGLDVLTAKVENAARKLEAMTNSKQSIAKKIDAAQNWLADPNGGPEGEEQIRGALAEARKIAELCDDPKERDDILRSLGEIAALTSKLGDLRRQGKGDSPEARALAKQVATALQNLQTKTNRAVANSRPAKAAVHLEGKIEQAQRWIDNPTVDDRGVGQAAIRGLVAEGHRLANVMMGPYRQDLLAKCDRVDQLAAQLADLAARGEGESPQARALASQLQDSLKDLKTQMQEAMTQEVSDVFSDTTTPIKLLAVAATAPPDAPNREEVFDERAANFENHSGRLGATAEKAAAVGAANKSTVEGIQASVKTARELTPQVISAARILLRNPGNQAAYEHFETMKNQWIDNVEKMTGLVDEAIDTKSLLDASEEAIKKDLDKCKVAMANIQPQMLVAGATSIARRANRILLVAKREVENSEDPKFREAVKAASDELSKTISPMVMDAKAVAGNISDPGLQKSFLDSGYRILGAVAKVREAFQPQEPDFPPPPPDLEQLRLTDELAPPKPPLPEGEVPPPRPPPPEEKDEEFPEQKAGEVINQPMMMAARQLHDEARKWSSKGNDIIAAAKRMALLMAEMSRLVRGGSGTKRALIQCAKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKILSTVKATMLGRTNISDEESEQATEMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLRWVRKTPWYQ
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
59AcetylationSNLVRVGKETVQTTE
HHHHHCCCCCCCCCH
47.5622902405
71AcetylationTTEDQILKRDMPPAF
CCHHHHHHCCCCHHH
48.2422902405
97PhosphorylationQAAQMLQSDPYSVPA
HHHHHHHCCCCCCCH
36.2724945867
100PhosphorylationQMLQSDPYSVPARDY
HHHHCCCCCCCHHHE
27.5624945867
101PhosphorylationMLQSDPYSVPARDYL
HHHCCCCCCCHHHEE
27.3224945867
107PhosphorylationYSVPARDYLIDGSRG
CCCCHHHEEEECCCC
10.45-
170AcetylationNLGPGMTKMAKMIDE
CCCCCHHHHHHHHHH
28.1522902405
173AcetylationPGMTKMAKMIDERQQ
CCHHHHHHHHHHHHH
32.6522902405
219UbiquitinationFVTTKNSKNQGIEEA
EEECCCCCCCCHHHH
63.78-
228AcetylationQGIEEALKNRNFTVG
CCHHHHHHCCCCCCH
61.9922902405
260PhosphorylationWDEDAWASKDTEAMK
CCCCHHHCCCHHHHH
21.9922673903
272PhosphorylationAMKRALASIDSKLNQ
HHHHHHHHHHHHHHH
27.9822108457
275PhosphorylationRALASIDSKLNQAKG
HHHHHHHHHHHHCCC
37.0522673903
276AcetylationALASIDSKLNQAKGW
HHHHHHHHHHHCCCC
47.9422902405
290PhosphorylationWLRDPNASPGDAGEQ
CCCCCCCCCCHHHHH
35.7423712012
346PhosphorylationRARGQGASPVAMQKA
HHCCCCCCHHHHHHH
27.0823712012
357PhosphorylationMQKAQQVSQGLDVLT
HHHHHHHHHCHHHHH
17.7522673903
364PhosphorylationSQGLDVLTAKVENAA
HHCHHHHHHHHHHHH
25.0425575281
366AcetylationGLDVLTAKVENAARK
CHHHHHHHHHHHHHH
44.8622902405
434PhosphorylationERDDILRSLGEIAAL
HHHHHHHHHHHHHHH
36.9629779826
442PhosphorylationLGEIAALTSKLGDLR
HHHHHHHHHHHHHHH
21.0628432305
443PhosphorylationGEIAALTSKLGDLRR
HHHHHHHHHHHHHHH
27.0828432305
444AcetylationEIAALTSKLGDLRRQ
HHHHHHHHHHHHHHC
51.7822902405
456PhosphorylationRRQGKGDSPEARALA
HHCCCCCCHHHHHHH
33.0529779826
496AcetylationAAVHLEGKIEQAQRW
HHHHHCHHHHHHHHH
33.4222902405
537PhosphorylationANVMMGPYRQDLLAK
HCHHCCHHHHHHHHH
18.38-
566PhosphorylationAARGEGESPQARALA
HHCCCCCCHHHHHHH
32.9228826663
574PhosphorylationPQARALASQLQDSLK
HHHHHHHHHHHHHHH
32.0722673903
579PhosphorylationLASQLQDSLKDLKTQ
HHHHHHHHHHHHHHH
25.1022673903
596PhosphorylationEAMTQEVSDVFSDTT
HHHHHHHHHHHCCCC
27.5724945867
600PhosphorylationQEVSDVFSDTTTPIK
HHHHHHHCCCCCCCH
33.6224945867
602PhosphorylationVSDVFSDTTTPIKLL
HHHHHCCCCCCCHHE
31.2224945867
603PhosphorylationSDVFSDTTTPIKLLA
HHHHCCCCCCCHHEH
35.2524945867
604PhosphorylationDVFSDTTTPIKLLAV
HHHCCCCCCCHHEHH
25.7124945867
672PhosphorylationVKTARELTPQVISAA
HHHHHHHCHHHHHHH
13.61-
692PhosphorylationNPGNQAAYEHFETMK
CCCCHHHHHHHHHHH
16.98-
699AcetylationYEHFETMKNQWIDNV
HHHHHHHHHHHHHHH
54.1022902405
719PhosphorylationLVDEAIDTKSLLDAS
CCCHHHCHHHHHHHC
19.2022668510
721PhosphorylationDEAIDTKSLLDASEE
CHHHCHHHHHHHCHH
35.9423712012
726PhosphorylationTKSLLDASEEAIKKD
HHHHHHHCHHHHHHH
35.3225575281
732AcetylationASEEAIKKDLDKCKV
HCHHHHHHHHHHHCH
58.3622902405
768AcetylationNRILLVAKREVENSE
HHHEEEEEHHHCCCC
41.4322902405
778AcetylationVENSEDPKFREAVKA
HCCCCCHHHHHHHHH
70.1822902405
784AcetylationPKFREAVKAASDELS
HHHHHHHHHHHHHHH
45.3322902405
787PhosphorylationREAVKAASDELSKTI
HHHHHHHHHHHHHCC
36.1622108457
791PhosphorylationKAASDELSKTISPMV
HHHHHHHHHCCCHHH
26.2125575281
793PhosphorylationASDELSKTISPMVMD
HHHHHHHCCCHHHHC
24.2628432305
795PhosphorylationDELSKTISPMVMDAK
HHHHHCCCHHHHCHH
16.5129779826
802AcetylationSPMVMDAKAVAGNIS
CHHHHCHHHHCCCCC
38.8522902405
809PhosphorylationKAVAGNISDPGLQKS
HHHCCCCCCCHHHHH
41.5821738781
815AcetylationISDPGLQKSFLDSGY
CCCCHHHHHHHHHHH
48.4922902405
816PhosphorylationSDPGLQKSFLDSGYR
CCCHHHHHHHHHHHH
20.3423984901
820PhosphorylationLQKSFLDSGYRILGA
HHHHHHHHHHHHHHH
39.6127097102
822PhosphorylationKSFLDSGYRILGAVA
HHHHHHHHHHHHHHH
9.8327097102
915AcetylationEARKWSSKGNDIIAA
HHHHHHHCCHHHHHH
57.1022902405
924AcetylationNDIIAAAKRMALLMA
HHHHHHHHHHHHHHH
37.6722902405
952AcetylationRALIQCAKDIAKASD
HHHHHHHHHHHHCCH
58.2422902405
956AcetylationQCAKDIAKASDEVTR
HHHHHHHHCCHHHHH
49.0822902405
966AcetylationDEVTRLAKEVAKQCT
HHHHHHHHHHHHHCC
58.2622902405
973PhosphorylationKEVAKQCTDKRIRTN
HHHHHHCCCHHHHHH
41.9022673903
1035AcetylationQNLMQSVKETVREAE
HHHHHHHHHHHHHHH
53.5722902405
1061SuccinylationFTLRWVRKTPWYQ--
CEEEEHHCCCCCC--
49.6926843850
1065PhosphorylationWVRKTPWYQ------
EHHCCCCCC------
12.92-

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_RAT !!

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_RAT !!

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

Oops, there are no PPI records of VINC_RAT !!

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

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Related Literatures of Post-Translational Modification

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