VIGLN_MOUSE - dbPTM
VIGLN_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VIGLN_MOUSE
UniProt AC Q8VDJ3
Protein Name Vigilin
Gene Name Hdlbp
Organism Mus musculus (Mouse).
Sequence Length 1268
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Appears to play a role in cell sterol metabolism. It may function to protect cells from over-accumulation of cholesterol (By similarity)..
Protein Sequence MSSVAVLTQESFAEHRSGLVPQQIKVATLNSEEENDPPTYKDAFPPLPEKAACLESAQEPAGAWSNKIRPIKASVITQVFHVPLEERKYKDMNQFGEGEQAKICLEIMQRTGAHLELSLAKDQGLSIMVSGKLDAVMKARKDIVARLQTQASATVPIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSNQIKITGTKEGIEKARHEVLLISAEQDKRAVERLEVEKAFHPFIAGPYNRLVGEIMQETGTRINIPPPSVNRTEIVFTGEKEQLAQAVARIKKIYEEKKKKTTTIAVEVKKSQHKYVIGPKGNSLQEILERTGVSVEIPPSDSISETVILRGEPEKLGQALTEVYAKANSFTVSSVSAPSWLHRFIIGKKGQNLAKITQQMPKVHIEFTEGEDKITLEGPTEDVNVAQEQIEGMVKDLINRMDYVEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKSNLIRIEGDPQGVQQAKRELLELASRMENERTKDLIIEQRFHRTIIGQKGERIREIRDKFPEVIINFPDPAQKSDIVQLRGPKNEVEKCTKYMQKMVADLVENSYSISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENSNSETIIITGKRANCEAARSRILSIQKDLANIAEVEVSIPAKLHNSLIGTKGRLIRSIMEECGGVHIHFPVEGSGSDTVVIRGPSSDVEKAKKQLLHLAEEKQTKSFTVDIRAKPEYHKFLIGKGGGKIRKVRDSTGARIIFPAAEDKDQDLITIIGKEDAVREAQKELEALIQNLENVVEDYMLVDPKHHRHFVIRRGQVLREIAEEYGGVMVSFPRSGTQSDKVTLKGAKDCVEAAKKRIQEIIEDLEAQVTVECAIPQKFHRSVMGPKGSRIQQITRDYNVQIKFPDREENPVHSVEPSIQENGDEAGEGREAKETDPGSPRRCDIIIISGRKEKCEAAKEALEALVPVTIEVEVPFDLHRYIIGQKGSGIRKMMDEFEVNIHVPAPELQSDTIAITGLAANLDRAKAGLLDRVKELQAEQEDRALRSFKLSVTVDPKYHPKIIGRKGAVITQIRLEHEVNIQFPDKDDGNQPQDQITITGYEKNTEAARDAILKIVGELEQMVSEDVPLDHRVHARIIGARGKAIRKIMDEFKVDIRFPQSGAPDPNCVTVTGLPENVEEAIDHILNLEEEYLADVVDSEALQVYMKPPAHEESRAPSKGFVVRDAPWTSNSSEKAPDMSSSEEFPSFGAQVAPKTLPWGPKR
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
2Acetylation------MSSVAVLTQ
------CCCEEEEEH
44.84-
2Phosphorylation------MSSVAVLTQ
------CCCEEEEEH
44.8430352176
3Phosphorylation-----MSSVAVLTQE
-----CCCEEEEEHH
26.4230352176
8PhosphorylationMSSVAVLTQESFAEH
CCCEEEEEHHHHHHH
24.5623984901
11PhosphorylationVAVLTQESFAEHRSG
EEEEEHHHHHHHCCC
21.6830352176
17PhosphorylationESFAEHRSGLVPQQI
HHHHHHCCCCCCCEE
38.0823984901
28PhosphorylationPQQIKVATLNSEEEN
CCEEEEEECCCCCCC
29.4725521595
31PhosphorylationIKVATLNSEEENDPP
EEEEECCCCCCCCCC
49.8827087446
39PhosphorylationEEENDPPTYKDAFPP
CCCCCCCCHHHCCCC
48.9025619855
40PhosphorylationEENDPPTYKDAFPPL
CCCCCCCHHHCCCCC
16.7925619855
41UbiquitinationENDPPTYKDAFPPLP
CCCCCCHHHCCCCCC
45.09-
53S-palmitoylationPLPEKAACLESAQEP
CCCHHHHHHHHCCCC
5.3128526873
67AcetylationPAGAWSNKIRPIKAS
CCCCCCCCCCCCCCH
34.2822826441
90UbiquitinationPLEERKYKDMNQFGE
CHHHHCCCCHHHCCC
54.24-
104S-palmitoylationEGEQAKICLEIMQRT
CHHHHHHHHHHHHHH
2.4828526873
130PhosphorylationQGLSIMVSGKLDAVM
CCCEEEEECCHHHHH
16.9020531401
132AcetylationLSIMVSGKLDAVMKA
CEEEEECCHHHHHHH
35.377719765
138AcetylationGKLDAVMKARKDIVA
CCHHHHHHHHHHHHH
38.1415612653
138MalonylationGKLDAVMKARKDIVA
CCHHHHHHHHHHHHH
38.1426320211
149PhosphorylationDIVARLQTQASATVP
HHHHHHHHHCCCCCC
30.6029514104
152PhosphorylationARLQTQASATVPIPK
HHHHHHCCCCCCCCH
18.0429514104
154PhosphorylationLQTQASATVPIPKEH
HHHHCCCCCCCCHHH
25.0730352176
168UbiquitinationHHRFVIGKNGEKLQD
HCEEEECCCCCEEEC
51.13-
168MalonylationHHRFVIGKNGEKLQD
HCEEEECCCCCEEEC
51.1326320211
197MalonylationDDPSNQIKITGTKEG
CCCCCCEEEECCHHH
25.1726320211
202MalonylationQIKITGTKEGIEKAR
CEEEECCHHHHHHHH
56.1126320211
221UbiquitinationLISAEQDKRAVERLE
EEEHHHHHHHHHHHH
41.78-
231UbiquitinationVERLEVEKAFHPFIA
HHHHHHHHHHCHHHC
62.62-
241PhosphorylationHPFIAGPYNRLVGEI
CHHHCCHHHHHHHHH
16.4029514104
274UbiquitinationEIVFTGEKEQLAQAV
EEEEECCHHHHHHHH
52.70-
295PhosphorylationYEEKKKKTTTIAVEV
HHHHCCCCCEEEEEE
37.74-
296PhosphorylationEEKKKKTTTIAVEVK
HHHCCCCCEEEEEEE
25.69-
303UbiquitinationTTIAVEVKKSQHKYV
CEEEEEEECCCCCEE
32.95-
314UbiquitinationHKYVIGPKGNSLQEI
CCEEECCCCCCHHHH
66.56-
317PhosphorylationVIGPKGNSLQEILER
EECCCCCCHHHHHHH
39.8525521595
349UbiquitinationILRGEPEKLGQALTE
EECCCHHHHHHHHHH
69.50-
358PhosphorylationGQALTEVYAKANSFT
HHHHHHHHHHHCCCE
8.9929514104
389UbiquitinationKKGQNLAKITQQMPK
CCCCCHHHHHHCCCC
49.83-
435OxidationVKDLINRMDYVEINI
HHHHHHHCCEEEEEC
3.6417242355
437PhosphorylationDLINRMDYVEINIDH
HHHHHCCEEEEECCC
7.2225521595
453AcetylationFHRHLIGKSGANINR
HHHHHCCCCCCCHHH
38.4323806337
453MalonylationFHRHLIGKSGANINR
HHHHHCCCCCCCHHH
38.4326320211
454PhosphorylationHRHLIGKSGANINRI
HHHHCCCCCCCHHHC
37.6129514104
468PhosphorylationIKDQYKVSVRIPPDS
CCCEEEEEEECCCCC
11.0920495213
477MalonylationRIPPDSEKSNLIRIE
ECCCCCCCCCCEEEE
48.9026320211
494AcetylationPQGVQQAKRELLELA
HHHHHHHHHHHHHHH
41.9123864654
494UbiquitinationPQGVQQAKRELLELA
HHHHHHHHHHHHHHH
41.91-
494MalonylationPQGVQQAKRELLELA
HHHHHHHHHHHHHHH
41.9126320211
510MalonylationRMENERTKDLIIEQR
HHCCHHHHHHHHHHH
57.6826320211
526MalonylationHRTIIGQKGERIREI
HHHHCCCCCHHHHHH
58.4926320211
536AcetylationRIREIRDKFPEVIIN
HHHHHHHHCCCEEEC
53.6323201123
568MalonylationNEVEKCTKYMQKMVA
HHHHHHHHHHHHHHH
48.4726320211
569PhosphorylationEVEKCTKYMQKMVAD
HHHHHHHHHHHHHHH
6.1428059163
582PhosphorylationADLVENSYSISVPIF
HHHHHCCCCCCHHHH
22.9329514104
585PhosphorylationVENSYSISVPIFKQF
HHCCCCCCHHHHHHH
18.8528059163
599UbiquitinationFHKNIIGKGGANIKK
HHHHCCCCCCCCHHH
43.70-
599MalonylationFHKNIIGKGGANIKK
HHHHCCCCCCCCHHH
43.7026320211
641PhosphorylationANCEAARSRILSIQK
CCHHHHHHHHHHHHH
20.9529472430
645PhosphorylationAARSRILSIQKDLAN
HHHHHHHHHHHHHHC
22.1728725479
663UbiquitinationVEVSIPAKLHNSLIG
EEEECCHHHHCCCCC
44.95-
667PhosphorylationIPAKLHNSLIGTKGR
CCHHHHCCCCCCHHH
15.6029472430
671PhosphorylationLHNSLIGTKGRLIRS
HHCCCCCCHHHHHHH
24.2729176673
672UbiquitinationHNSLIGTKGRLIRSI
HCCCCCCHHHHHHHH
36.50-
714UbiquitinationSDVEKAKKQLLHLAE
CHHHHHHHHHHHHHH
51.54-
714MalonylationSDVEKAKKQLLHLAE
CHHHHHHHHHHHHHH
51.5426320211
723AcetylationLLHLAEEKQTKSFTV
HHHHHHHHCCCCEEE
55.5623806337
726MalonylationLAEEKQTKSFTVDIR
HHHHHCCCCEEEEEE
40.8726320211
745UbiquitinationYHKFLIGKGGGKIRK
HHCEEECCCCCCEEE
47.60-
756PhosphorylationKIRKVRDSTGARIIF
CEEEEECCCCCEEEE
20.4123140645
757PhosphorylationIRKVRDSTGARIIFP
EEEEECCCCCEEEEE
38.8729550500
769AcetylationIFPAAEDKDQDLITI
EEECCCCCCCCEEEE
49.1223954790
779UbiquitinationDLITIIGKEDAVREA
CEEEEECHHHHHHHH
41.85-
830PhosphorylationLREIAEEYGGVMVSF
HHHHHHHHCCEEEEC
15.64-
840PhosphorylationVMVSFPRSGTQSDKV
EEEECCCCCCCCCCE
46.5625777480
842PhosphorylationVSFPRSGTQSDKVTL
EECCCCCCCCCCEEE
26.5825777480
844PhosphorylationFPRSGTQSDKVTLKG
CCCCCCCCCCEEECC
38.9625777480
848PhosphorylationGTQSDKVTLKGAKDC
CCCCCCEEECCHHHH
28.6125777480
853UbiquitinationKVTLKGAKDCVEAAK
CEEECCHHHHHHHHH
61.40-
894PhosphorylationSVMGPKGSRIQQITR
HHCCCCCCHHHHHCC
32.1329514104
900PhosphorylationGSRIQQITRDYNVQI
CCHHHHHCCCCCCEE
17.1018779572
940PhosphorylationEGREAKETDPGSPRR
CCCCCCCCCCCCCCC
46.9526824392
944PhosphorylationAKETDPGSPRRCDII
CCCCCCCCCCCCEEE
22.1825521595
948S-nitrosylationDPGSPRRCDIIIISG
CCCCCCCCEEEEEEC
4.6822178444
948S-palmitoylationDPGSPRRCDIIIISG
CCCCCCCCEEEEEEC
4.6826165157
991AcetylationHRYIIGQKGSGIRKM
HHHHHCCCCCHHHHH
50.2423806337
991UbiquitinationHRYIIGQKGSGIRKM
HHHHHCCCCCHHHHH
50.24-
1039UbiquitinationAGLLDRVKELQAEQE
HHHHHHHHHHHHHHH
54.31-
1062UbiquitinationLSVTVDPKYHPKIIG
EEEEECCCCCCCCCC
52.29-
1066UbiquitinationVDPKYHPKIIGRKGA
ECCCCCCCCCCCCCE
33.37-
1071MalonylationHPKIIGRKGAVITQI
CCCCCCCCCEEEEEE
46.1126320211
1108UbiquitinationITITGYEKNTEAARD
EEEEHHHCCHHHHHH
61.76-
1166PhosphorylationVDIRFPQSGAPDPNC
CEEECCCCCCCCCCE
36.8425367039
1175PhosphorylationAPDPNCVTVTGLPEN
CCCCCEEEECCCCCC
17.9825367039
1177PhosphorylationDPNCVTVTGLPENVE
CCCEEEECCCCCCHH
24.5225367039
1197PhosphorylationILNLEEEYLADVVDS
HHCCCHHHHHHHCCH
15.5225367039
1204PhosphorylationYLADVVDSEALQVYM
HHHHHCCHHHHHHHC
17.1025367039
1210PhosphorylationDSEALQVYMKPPAHE
CHHHHHHHCCCCCCC
6.1025367039
1219PhosphorylationKPPAHEESRAPSKGF
CCCCCCCCCCCCCCE
30.6625367039
1223PhosphorylationHEESRAPSKGFVVRD
CCCCCCCCCCEEEEE
44.4125367039
1224UbiquitinationEESRAPSKGFVVRDA
CCCCCCCCCEEEEEC
56.14-
1224MalonylationEESRAPSKGFVVRDA
CCCCCCCCCEEEEEC
56.1426320211
1234PhosphorylationVVRDAPWTSNSSEKA
EEEECCCCCCCCCCC
19.5723984901
1235PhosphorylationVRDAPWTSNSSEKAP
EEECCCCCCCCCCCC
30.7425521595
1237PhosphorylationDAPWTSNSSEKAPDM
ECCCCCCCCCCCCCC
39.3725521595
1238PhosphorylationAPWTSNSSEKAPDMS
CCCCCCCCCCCCCCC
47.5726643407
1245PhosphorylationSEKAPDMSSSEEFPS
CCCCCCCCCCCCCCC
37.7826525534
1246PhosphorylationEKAPDMSSSEEFPSF
CCCCCCCCCCCCCCC
34.8225521595
1247PhosphorylationKAPDMSSSEEFPSFG
CCCCCCCCCCCCCCC
33.5626525534
1252PhosphorylationSSSEEFPSFGAQVAP
CCCCCCCCCCCCCCC
41.4525521595

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 VIGLN_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VIGLN_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 VIGLN_MOUSE !!

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

Oops, there are no PPI records of VIGLN_MOUSE !!

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-31, AND MASSSPECTROMETRY.
"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 SER-31, AND MASSSPECTROMETRY.

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