SH319_MOUSE - dbPTM
SH319_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SH319_MOUSE
UniProt AC Q91X43
Protein Name SH3 domain-containing protein 19
Gene Name Sh3d19
Organism Mus musculus (Mouse).
Sequence Length 789
Subcellular Localization Cytoplasm.
Protein Description May play a role in regulating A disintegrin and metalloproteases (ADAMs) in the signaling of EGFR-ligand shedding. May be involved in suppression of Ras-induced cellular transformation and Ras-mediated activation of ELK1. Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity)..
Protein Sequence MNIMNTEQSQNTIVSRIKAFEGQTNTEIPGLPKKPEIIPRTIPPKPAVSSGKPLVAPKPAANRASGEWDTWAENRLKVTSREGLTPYSSPQEAGITPVTKPELPKKPTPGLTRSVNHETSGGRPMAESPDTGKKIPTPAPRPLLPKKSASTDAPPYPSIPPKLVSAPPRLSVASQAKAFRSLGEGLPSNPPVPAPQSKALGDIDLISFDDDVLPTSGSPAEEPTGSETVLDPFQLPTKTEATKERAVQPAPTRKPTVIRIPAKPGKCLHEEPQSPPPLPAEKPVGNTHSAVSGRPSHSDRTRNPELEQASESGGLVQGPPRLPPRPVHGKVIPVWRPPPKGAPERPPPPKLPASKSSNKNLPFNRSSSDMDLQKKQSHFVSGLSKAKSQIFKNQDPVLPPRPKPGHPLYRKYMLSVPHGIANEDIVSRNPTELSCKRGDVLVILKQAENNYLECQRGEGTGRVHPSQMKIVTPLDERPRGRPNDSGHSQKPVDSGAPHAVALHDFPAEQADDLSLTSGEIVYLLEKIDAEWYRGKCRNQTGVFPANYVKVIVDIPEGRSGKRESFSSHCAKGPRCVARFEYIGDQKDELSFSEGEVIILTEYVNEEWGRGEIRDRSGIFPLNFVELVGDHPTSGANILSTKVPPKTKNEDPGSNSQDSSPPGEWCKALHSFTAETSEDLPFKRGDRILILERLDSDWYRGRLHDREGIFPAVFVQPCPAEAKGVASAIPKGRKVKALYDFLGENEDELSFKAGDVITELEPIDDAWMRGELMGRAGMFPKNYVQFLQVS
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
18UbiquitinationNTIVSRIKAFEGQTN
HHHHHHHHHHCCCCC		46.01-
34UbiquitinationEIPGLPKKPEIIPRT
CCCCCCCCCCCCCCC		46.04-
45UbiquitinationIPRTIPPKPAVSSGK
CCCCCCCCCCCCCCC		40.01-
52UbiquitinationKPAVSSGKPLVAPKP
CCCCCCCCCCCCCCC		36.81-
65PhosphorylationKPAANRASGEWDTWA
CCCCCCCCCCCCHHH		33.7326824392
70PhosphorylationRASGEWDTWAENRLK
CCCCCCCHHHHHCEE		27.8723984901
85PhosphorylationVTSREGLTPYSSPQE
EEECCCCCCCCCCHH		30.9122499769
87PhosphorylationSREGLTPYSSPQEAG
ECCCCCCCCCCHHCC		19.2822499769
88PhosphorylationREGLTPYSSPQEAGI
CCCCCCCCCCHHCCC		36.4222499769
89PhosphorylationEGLTPYSSPQEAGIT
CCCCCCCCCHHCCCC		25.4322499769
96PhosphorylationSPQEAGITPVTKPEL
CCHHCCCCCCCCCCC		15.7022499769
100UbiquitinationAGITPVTKPELPKKP
CCCCCCCCCCCCCCC		36.41-
106UbiquitinationTKPELPKKPTPGLTR
CCCCCCCCCCCCCCC		52.78-
114PhosphorylationPTPGLTRSVNHETSG
CCCCCCCCCCCCCCC		23.2627087446
119PhosphorylationTRSVNHETSGGRPMA
CCCCCCCCCCCCCCC		25.7223684622
120PhosphorylationRSVNHETSGGRPMAE
CCCCCCCCCCCCCCC		35.9427087446
128PhosphorylationGGRPMAESPDTGKKI
CCCCCCCCCCCCCCC		20.6627087446
131PhosphorylationPMAESPDTGKKIPTP
CCCCCCCCCCCCCCC		55.0429472430
148PhosphorylationRPLLPKKSASTDAPP
CCCCCCCCCCCCCCC		33.3126643407
150PhosphorylationLLPKKSASTDAPPYP
CCCCCCCCCCCCCCC		33.6326643407
151PhosphorylationLPKKSASTDAPPYPS
CCCCCCCCCCCCCCC		35.5826643407
165PhosphorylationSIPPKLVSAPPRLSV
CCCHHHCCCCCCCCH		45.5625338131
171PhosphorylationVSAPPRLSVASQAKA
CCCCCCCCHHHHHHH		19.5428285833
174PhosphorylationPPRLSVASQAKAFRS
CCCCCHHHHHHHHHH		28.6328285833
177UbiquitinationLSVASQAKAFRSLGE
CCHHHHHHHHHHHCC		40.18-
181PhosphorylationSQAKAFRSLGEGLPS
HHHHHHHHHCCCCCC		33.9828973931
188PhosphorylationSLGEGLPSNPPVPAP
HHCCCCCCCCCCCCC		67.9929550500
197PhosphorylationPPVPAPQSKALGDID
CCCCCCCCCCCCCCC		20.8825338131
207PhosphorylationLGDIDLISFDDDVLP
CCCCCEEECCCCCCC		29.8921743459
215PhosphorylationFDDDVLPTSGSPAEE
CCCCCCCCCCCCCCC		41.3725338131
218PhosphorylationDVLPTSGSPAEEPTG
CCCCCCCCCCCCCCC		22.2423649490
226PhosphorylationPAEEPTGSETVLDPF
CCCCCCCCCCCCCCC		32.3523649490
274PhosphorylationCLHEEPQSPPPLPAE
CCCCCCCCCCCCCCC		50.5226745281
287PhosphorylationAEKPVGNTHSAVSGR
CCCCCCCCCCCCCCC		15.9829472430
289PhosphorylationKPVGNTHSAVSGRPS
CCCCCCCCCCCCCCC		28.4729472430
292PhosphorylationGNTHSAVSGRPSHSD
CCCCCCCCCCCCCCC		28.8929472430
296PhosphorylationSAVSGRPSHSDRTRN
CCCCCCCCCCCCCCC		33.9724719451
298PhosphorylationVSGRPSHSDRTRNPE
CCCCCCCCCCCCCHH		32.8824719451
359UbiquitinationPASKSSNKNLPFNRS
CCCCCCCCCCCCCCC		62.91-
366PhosphorylationKNLPFNRSSSDMDLQ
CCCCCCCCCCCHHHH		34.9925521595
367PhosphorylationNLPFNRSSSDMDLQK
CCCCCCCCCCHHHHH		27.4125521595
368PhosphorylationLPFNRSSSDMDLQKK
CCCCCCCCCHHHHHH		37.9025521595
375UbiquitinationSDMDLQKKQSHFVSG
CCHHHHHHHHHHHHH		44.03-
377PhosphorylationMDLQKKQSHFVSGLS
HHHHHHHHHHHHHHH		27.9829514104
384PhosphorylationSHFVSGLSKAKSQIF
HHHHHHHHHHHHHHH		33.8129514104
388PhosphorylationSGLSKAKSQIFKNQD
HHHHHHHHHHHHCCC		33.1121743459
411UbiquitinationPGHPLYRKYMLSVPH
CCCCHHHHHHHCCCC		22.81-
412PhosphorylationGHPLYRKYMLSVPHG
CCCHHHHHHHCCCCC		8.3525293948
415PhosphorylationLYRKYMLSVPHGIAN
HHHHHHHCCCCCCCC		19.6425293948
434PhosphorylationSRNPTELSCKRGDVL
HCCCCCCCCCCCCEE		16.0327149854
436UbiquitinationNPTELSCKRGDVLVI
CCCCCCCCCCCEEEE		56.91-
451PhosphorylationLKQAENNYLECQRGE
EEECCCCEEEEECCC		18.5629514104
469UbiquitinationRVHPSQMKIVTPLDE
CCCHHHCEEEECCCC		26.79-
547PhosphorylationTGVFPANYVKVIVDI
CCCCCCCEEEEEEEC		12.0729514104
558MethylationIVDIPEGRSGKRESF
EEECCCCCCCCCCCC		40.3458856415
558DimethylationIVDIPEGRSGKRESF
EEECCCCCCCCCCCC		40.34-
564PhosphorylationGRSGKRESFSSHCAK
CCCCCCCCCHHHHCC		34.1726824392
566PhosphorylationSGKRESFSSHCAKGP
CCCCCCCHHHHCCCC		28.5829550500
567PhosphorylationGKRESFSSHCAKGPR
CCCCCCHHHHCCCCE		22.1529550500
571UbiquitinationSFSSHCAKGPRCVAR
CCHHHHCCCCEEEEE		74.88-
641UbiquitinationGANILSTKVPPKTKN
CCCCCCCCCCCCCCC		49.74-
670PhosphorylationEWCKALHSFTAETSE
HHHHHHHHEEECCCC		25.7423984901
672PhosphorylationCKALHSFTAETSEDL
HHHHHHEEECCCCCC		26.9723984901
675PhosphorylationLHSFTAETSEDLPFK
HHHEEECCCCCCCCC		34.6517203969
676PhosphorylationHSFTAETSEDLPFKR
HHEEECCCCCCCCCC		22.1817203969
695PhosphorylationLILERLDSDWYRGRL
EEEEECCCCCCCCCC		34.3429514104
722UbiquitinationQPCPAEAKGVASAIP
EECCHHHCCHHHHCC		45.48-
730UbiquitinationGVASAIPKGRKVKAL
CHHHHCCCCCCEEHH		66.30-
738PhosphorylationGRKVKALYDFLGENE
CCCEEHHHHHHCCCC		14.98-
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 SH319_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SH319_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 SH319_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SH319_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SH319_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-676, AND MASSSPECTROMETRY.

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