MUG1_MOUSE - dbPTM
MUG1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MUG1_MOUSE
UniProt AC P28665
Protein Name Murinoglobulin-1
Gene Name Mug1
Organism Mus musculus (Mouse).
Sequence Length 1476
Subcellular Localization Secreted.
Protein Description A proteinase activates the inhibitor by specific proteolysis in the bait region, which, by an unknown mechanism leads to reaction at the cysteinyl-glutamyl internal thiol ester site and to a conformational change, whereby the proteinase is trapped and/or covalently bound to the inhibitor. While in the tetrameric proteinase inhibitors steric inhibition is sufficiently strong, monomeric forms need a covalent linkage between the activated glutamyl residue of the original thiol ester and a terminal amino group of a lysine or another nucleophilic group on the proteinase, for inhibition to be effective..
Protein Sequence MWKSRRAQLCLFSVLLAFLHSASLLNGDSKYMVLVPSQLYTETPEKICLHLYQLNETVTVTASLVSQSGRKNLFDELVLDKDLFQCVSFIIPRLSSSDEEDFLYVDIKGPTHEFSKRKAVLVKNKESVVFVQTDKPVYKPGQSVKFRVVSMDKMLRPLNELLPLAYIEDPKKNRIMQWRDIKTENGLKQMSFSLAAEPIQGPYKIVVHKESGEKEEHSFTVMEFVLPRFNVDLKVPNAMSVNDEVLSVTACGKYTYGKPVPGHVKINVCRETETGCREVNSQLDNNGCSTQEVNITELQSKKRNYEVQLFHVNATVTEEGTGLEFSRSGTTKIERITNKLIFLKADSHFRHGIPFFVKVRLVDIKGDPIPNEKVFIKAQELSYTSATTTDQHGLAEFSIDTTCISGSSLHIKVNHKEEDSCSYFYCMEERHASAKHVAYAVYSLSKSYIYLDTETSSILPCNQIHTVQAHFILKGDLGVLKELIFYYLVMAQGSIIQTGNHTHQVEPGEAPVKGKFALEIPVEFSMVPMAKMLIYTILPDGEVIADSVNFEIEKCLRNKVDLRFSTSQSLPASQTRLQVTASPQSLCGLRAVDQSVLLLKPESELSPSWIYNLPGMQQNKFVPSSRLSEDQEDCILYSSWLAEKHTNLVPHGTEKDVYRYVEDMGLTAFTNLMIKLPIICFDYGMVPISAPRVEFDLAFTPEISWSLRTTLSKRPEEPPRKDPSSNDPLTETIRKYFPETWVWDIVTVNSTGLAEVEMTVPDTITEWKAGALCLSNDTGLGLSSVVPLQAFKPFFVEVSLPYSVVRGEAFMLKATVMNYLPTSMQMSVQLEASPDFTAVPVGDDQDSYCLSANGRHTSSWLVTPKSLGNVNFSVSAEAQQSSEPCGSEVATVPETGRKDTVVKVLIVEPEGIKQEHTFSSLFCASDAEISEKMSLVLPPTVVKDSARAHFSVMGDILSSAIRNTQNLLHMPYGCGEQNMVLFAPNIYVLKYLNETQQLTQKIKTKALGFLRAGYQRELNYKHKDGSYSAFGDQNGEREGNTWLTAFVLKSFAQARAFIFIDESHITHAFTWLSQKQKDNGCFRSSGSLFNNAMKGGVDDEMTLSAYITMALLESSLPATHPVVSKALSCLESSWKTIEQERNASFVYTKALMAYAFALAGNQNKRDEILKSLDEEAIKENNSIHWKRPQKSRKSEHHLYKPQASSAEVEMNAYVVLARLTAQPAPSPEDLTLSMSTIMWLTKQQNSNGGFSSTQDTVVALDALSKYGAVTFSRSQKTTLVTIQSTGSFSQKFQVENSNRLLLQQVALPDIPGDYTISVSGEGCVYAQTMLRYNMHLEKQLSAFAIWVQTVPLTCNNPKGHNSFQISLEISYTGSRPASNMVIADVKMLSGFIPLKPTVKKLERLEHVSRTEVSNNNVLIYLDQVTNQTLAFSFIIQQDIPVRNLQPAIVKVYDYYETDEMAFAEYSSPCSTDKQNV
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
23PhosphorylationLAFLHSASLLNGDSK
HHHHHHHHHCCCCCC		36.08-
29PhosphorylationASLLNGDSKYMVLVP
HHHCCCCCCEEEEEE		27.38-
55N-linked_GlycosylationCLHLYQLNETVTVTA
EEEEEECCCEEEEEH		27.63-
68PhosphorylationTASLVSQSGRKNLFD
EHHHHCCCCCCCCHH		32.81-
71UbiquitinationLVSQSGRKNLFDELV
HHCCCCCCCCHHHHH		62.6222790023
86S-palmitoylationLDKDLFQCVSFIIPR
CCHHHHHHHHHHHHC		1.8528526873
171UbiquitinationLAYIEDPKKNRIMQW
HHEECCCCCCCEEEE		75.0122790023
172AcetylationAYIEDPKKNRIMQWR
HEECCCCCCCEEEEC		57.772388129
182UbiquitinationIMQWRDIKTENGLKQ
EEEECCCCCCCCCEE		54.8227667366
182SuccinylationIMQWRDIKTENGLKQ
EEEECCCCCCCCCEE		54.8223954790
188UbiquitinationIKTENGLKQMSFSLA
CCCCCCCEEEEEEEE		45.4022790023
204UbiquitinationEPIQGPYKIVVHKES
CCCCCCEEEEEECCC		31.9622790023
251S-palmitoylationEVLSVTACGKYTYGK
EEEEEEECEECCCCC		3.3628526873
294N-linked_GlycosylationGCSTQEVNITELQSK
CCCCCEEEHHHHHHC		34.41-
313N-linked_GlycosylationEVQLFHVNATVTEEG
EEEEEEEEEEECCCC		22.7117330941
339UbiquitinationKIERITNKLIFLKAD
CEEEECCCEEEEECC		34.0222790023
344UbiquitinationTNKLIFLKADSHFRH
CCCEEEEECCCCCCC		39.1222790023
365UbiquitinationKVRLVDIKGDPIPNE
EEEEEECCCCCCCCC		53.4422790023
373UbiquitinationGDPIPNEKVFIKAQE
CCCCCCCCEEEEEEE		49.4322790023
500N-linked_GlycosylationGSIIQTGNHTHQVEP
CCEEECCCCCCCCCC		40.03-
587S-palmitoylationTASPQSLCGLRAVDQ
EECHHHHCCCEEECC		6.1328526873
644UbiquitinationYSSWLAEKHTNLVPH
HHHHHHHHCCCCCCC		50.5522790023
655UbiquitinationLVPHGTEKDVYRYVE
CCCCCCHHHHHHHHH		52.9422790023
655AcetylationLVPHGTEKDVYRYVE
CCCCCCHHHHHHHHH		52.9423954790
680S-palmitoylationMIKLPIICFDYGMVP
CCCCCEEEEECCCEE		1.8928526873
713UbiquitinationSLRTTLSKRPEEPPR
HHEECCCCCCCCCCC		75.0827667366
721UbiquitinationRPEEPPRKDPSSNDP
CCCCCCCCCCCCCCC		78.6827667366
749N-linked_GlycosylationVWDIVTVNSTGLAEV
EEEEEEECCCCCEEE		25.21-
775PhosphorylationKAGALCLSNDTGLGL
CCCEEEECCCCCCCC		31.5028609623
776N-linked_GlycosylationAGALCLSNDTGLGLS
CCEEEECCCCCCCCC		37.6016944957
778PhosphorylationALCLSNDTGLGLSSV
EEEECCCCCCCCCCE		38.2628609623
783PhosphorylationNDTGLGLSSVVPLQA
CCCCCCCCCEEECCC		21.2028609623
784PhosphorylationDTGLGLSSVVPLQAF
CCCCCCCCEEECCCC		31.9828609623
799PhosphorylationKPFFVEVSLPYSVVR
CCEEEEEECCCCCCC		15.3228609623
802PhosphorylationFVEVSLPYSVVRGEA
EEEEECCCCCCCCCC		21.2828609623
803PhosphorylationVEVSLPYSVVRGEAF
EEEECCCCCCCCCCE		16.5228609623
871N-linked_GlycosylationPKSLGNVNFSVSAEA
CHHHCCCEEEEEHHH		27.7217330941
923S-palmitoylationHTFSSLFCASDAEIS
EEECCEEECCCHHHH		4.2626165157
943UbiquitinationVLPPTVVKDSARAHF
ECCCEECCCHHHHHH		41.4522790023
958PhosphorylationSVMGDILSSAIRNTQ
HHHHHHHHHHHHCCC		20.3225195567
959PhosphorylationVMGDILSSAIRNTQN
HHHHHHHHHHHCCCC		25.0325195567
993N-linked_GlycosylationIYVLKYLNETQQLTQ
EEEHHHHHHHHHHHH		47.3716944957
1001UbiquitinationETQQLTQKIKTKALG
HHHHHHHHHHHHHHH		40.7222790023
1005UbiquitinationLTQKIKTKALGFLRA
HHHHHHHHHHHHHHH		36.2922790023
1023UbiquitinationRELNYKHKDGSYSAF
CCCCCCCCCCCCCCC		60.6822790023
1026PhosphorylationNYKHKDGSYSAFGDQ
CCCCCCCCCCCCCCC		26.50-
1027PhosphorylationYKHKDGSYSAFGDQN
CCCCCCCCCCCCCCC		15.00-
1028PhosphorylationKHKDGSYSAFGDQNG
CCCCCCCCCCCCCCC		20.86-
1077UbiquitinationTWLSQKQKDNGCFRS
HHHHHHCCCCCCCCC		61.2622790023
1129S-palmitoylationVVSKALSCLESSWKT
HHHHHHHHHHHHHHH		5.2028526873
1135UbiquitinationSCLESSWKTIEQERN
HHHHHHHHHHHHHHH		41.3922790023
1142N-linked_GlycosylationKTIEQERNASFVYTK
HHHHHHHHCCHHHHH		38.9016944957
1170UbiquitinationNKRDEILKSLDEEAI
CHHHHHHHHCCHHHH		55.4222790023
1178UbiquitinationSLDEEAIKENNSIHW
HCCHHHHHHCCCCCC		62.5322790023
1180N-linked_GlycosylationDEEAIKENNSIHWKR
CHHHHHHCCCCCCCC		42.41-
1246PhosphorylationWLTKQQNSNGGFSST
HHHCCCCCCCCCCCC		32.30-
1265UbiquitinationVALDALSKYGAVTFS
HHHHHHHHHCCEEEE		48.8622790023
1274PhosphorylationGAVTFSRSQKTTLVT
CCEEEECCCCEEEEE		34.53-
1395UbiquitinationLSGFIPLKPTVKKLE
HHCCCCCCCHHHHHH		33.0322790023
1426N-linked_GlycosylationIYLDQVTNQTLAFSF
EEEEECCCCEEEEEE		33.70-
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 MUG1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MUG1_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 MUG1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MUG1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MUG1_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides.";
Bernhard O.K., Kapp E.A., Simpson R.J.;
J. Proteome Res. 6:987-995(2007).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-313; ASN-871; ASN-993 ANDASN-1142, AND MASS SPECTROMETRY.
"Proteome-wide characterization of N-glycosylation events by diagonalchromatography.";
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,Gevaert K.;
J. Proteome Res. 5:2438-2447(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-776; ASN-993 AND ASN-1142,AND MASS SPECTROMETRY.

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