SH3K1_MOUSE - dbPTM
SH3K1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SH3K1_MOUSE
UniProt AC Q8R550
Protein Name SH3 domain-containing kinase-binding protein 1
Gene Name Sh3kbp1
Organism Mus musculus (Mouse).
Sequence Length 709
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton. Cytoplasmic vesicle membrane
Peripheral membrane protein. Cell junction, synapse, synaptosome. Cell junction, focal adhesion. Localized in endocytic vesicles containing clustered receptors. Colocalizes with ASAP1
Protein Description Adapter protein involved in regulating diverse signal transduction pathways. Involved in the regulation of endocytosis and lysosomal degradation of ligand-induced receptor tyrosine kinases, including EGFR and MET/hepatocyte growth factor receptor, through an association with CBL and endophilins. The association with CBL, and thus the receptor internalization, may inhibited by an interaction with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3-kinase activity by interaction with its regulatory subunit. May be involved in regulation of cell adhesion; promotes the interaction between TTK2B and PDCD6IP. May be involved in the regulation of cellular stress response via the MAPK pathways through its interaction with MAP3K4. Is involved in modulation of tumor necrosis factor mediated apoptosis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration (By similarity)..
Protein Sequence MVEAIVEFDYQAQHDDELTISVGEVITNIRKEDGGWWEGQINGRRGLFPDNFVREIKKDMKKDLLSNKAPEKPMHDVSSGNALLSSETILRTNKRGERRRRRCQVAFSYLPQNDDELELKVGDIIEVVGEVEEGWWEGVLNGKTGMFPSNFIKELSGESDELGISQDEQLSKSRPEGFLPASLLPFPAHGAKGKTTFEGTILYRAAPGKTEGHRRYYSLRETTGSESDGGDSSSTKSEGANGTMATAAIQPKKVKGVGFGDIFKDKPIKLRPRSIEVENDFLPVEKTIGKKLPPATSTPDPSKTEMDSRTKTKDYCKVIFPYEAQNDDELTIKEGDIVTLINKDCIDVGWWEGELNGRRGVFPDNFVKLLPSDFDKEGNRPKKPPPPSAPVVKQGAGTTERKHEIKKIPPERPETLPNRTEEKERPEREPKLDLQKPSVPAIPPKKPRPPKTNSLNRPGALPPRRPERPVGPLTHTRGDSPKIDLAGSALSGILDKDLSDRSNDIDLEGFDSVISSTEKLSHPTTSRPKATGRRPPSQSLTSSSLSSPDIFDSPSPEEDKEEHISLAHRGIDVSKKTSKTVTISQVSDNKTSLPPKPGTMAAASSGPASLSSVASSPMSSSLGTAGQRASSPSLFSTEGKPKMEPAVSSQAAIEELKMQVRELRTIIETMKDQQKREIKQLLSELDEEKKIRLRLQMEVNDIKKALQSK
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
4 (in isoform 3)Phosphorylation-10.3424759943
10PhosphorylationEAIVEFDYQAQHDDE
EEEEEECEECCCCCE		15.8624704852
10 (in isoform 3)Phosphorylation-15.8626824392
12 (in isoform 3)Phosphorylation-11.4924704852
17 (in isoform 3)Phosphorylation-54.6024759943
108PhosphorylationRRCQVAFSYLPQNDD
HHHEEEEEECCCCCC		18.9327087446
109PhosphorylationRCQVAFSYLPQNDDE
HHEEEEEECCCCCCC		18.8928833060
122 (in isoform 3)Phosphorylation-20.8627566939
128 (in isoform 3)Phosphorylation-3.3427566939
136 (in isoform 3)Phosphorylation-11.8830635358
137 (in isoform 3)Phosphorylation-32.6830635358
141 (in isoform 3)Phosphorylation-47.7330635358
142 (in isoform 3)Phosphorylation-25.4128285833
144 (in isoform 3)Phosphorylation-34.9624453211
146 (in isoform 3)Phosphorylation-5.5926824392
151 (in isoform 3)Phosphorylation-11.2229550500
152 (in isoform 3)Phosphorylation-3.8629550500
153 (in isoform 3)Phosphorylation-48.7629472430
154 (in isoform 3)Phosphorylation-43.2725168779
156PhosphorylationSNFIKELSGESDELG
HHHHHHHCCCCCCCC		41.4225521595
159PhosphorylationIKELSGESDELGISQ
HHHHCCCCCCCCCCH		39.6525521595
159 (in isoform 2)Phosphorylation-39.6527566939
159 (in isoform 8)Phosphorylation-39.6527566939
165PhosphorylationESDELGISQDEQLSK
CCCCCCCCHHHHHHH		29.7628833060
165 (in isoform 2)Phosphorylation-29.7627566939
165 (in isoform 8)Phosphorylation-29.7627566939
173 (in isoform 2)Phosphorylation-50.0930635358
173 (in isoform 8)Phosphorylation-50.0930635358
174 (in isoform 2)Phosphorylation-36.7130635358
174 (in isoform 8)Phosphorylation-36.7130635358
178 (in isoform 2)Phosphorylation-7.6230635358
178 (in isoform 8)Phosphorylation-7.6230635358
179 (in isoform 2)Phosphorylation-5.2128285833
179 (in isoform 8)Phosphorylation-5.2128285833
181 (in isoform 2)Phosphorylation-18.2424453211
181 (in isoform 8)Phosphorylation-18.2424453211
183 (in isoform 2)Phosphorylation-8.3826824392
183 (in isoform 8)Phosphorylation-8.3826824392
188 (in isoform 2)Phosphorylation-17.7129550500
188 (in isoform 8)Phosphorylation-17.7129550500
189 (in isoform 2)Phosphorylation-36.6629550500
189 (in isoform 8)Phosphorylation-36.6629550500
190 (in isoform 2)Phosphorylation-30.9629472430
190 (in isoform 8)Phosphorylation-30.9629472430
191 (in isoform 2)Phosphorylation-13.9425168779
191 (in isoform 8)Phosphorylation-13.9425168779
222PhosphorylationRYYSLRETTGSESDG
EEEEEEECCCCCCCC		29.9826160508
223PhosphorylationYYSLRETTGSESDGG
EEEEEECCCCCCCCC		33.6818779572
225PhosphorylationSLRETTGSESDGGDS
EEEECCCCCCCCCCC		31.6618779572
227PhosphorylationRETTGSESDGGDSSS
EECCCCCCCCCCCCC		43.1627087446
232PhosphorylationSESDGGDSSSTKSEG
CCCCCCCCCCCCCCC		29.4826160508
233PhosphorylationESDGGDSSSTKSEGA
CCCCCCCCCCCCCCC		46.9326160508
234PhosphorylationSDGGDSSSTKSEGAN
CCCCCCCCCCCCCCC		43.7529899451
235PhosphorylationDGGDSSSTKSEGANG
CCCCCCCCCCCCCCC		40.3026160508
237PhosphorylationGDSSSTKSEGANGTM
CCCCCCCCCCCCCCC		41.1527180971
243PhosphorylationKSEGANGTMATAAIQ
CCCCCCCCCCEEEEC		11.9330635358
246PhosphorylationGANGTMATAAIQPKK
CCCCCCCEEEECCCC		13.0530635358
274PhosphorylationPIKLRPRSIEVENDF
CCEECCCEEEEECCC		26.2827087446
296PhosphorylationGKKLPPATSTPDPSK
CCCCCCCCCCCCCCC		38.6225338131
298PhosphorylationKLPPATSTPDPSKTE
CCCCCCCCCCCCCCC		27.6225338131
382AcetylationDKEGNRPKKPPPPSA
CCCCCCCCCCCCCCC		74.756567321
452PhosphorylationKKPRPPKTNSLNRPG
CCCCCCCCCCCCCCC		35.4928833060
454PhosphorylationPRPPKTNSLNRPGAL
CCCCCCCCCCCCCCC		32.0527149854
474PhosphorylationERPVGPLTHTRGDSP
CCCCCCCCCCCCCCC		25.0826060331
476PhosphorylationPVGPLTHTRGDSPKI
CCCCCCCCCCCCCCC		30.9826060331
480PhosphorylationLTHTRGDSPKIDLAG
CCCCCCCCCCCCCCH		30.8026824392
488PhosphorylationPKIDLAGSALSGILD
CCCCCCHHHHHHHHC		22.0428285833
491PhosphorylationDLAGSALSGILDKDL
CCCHHHHHHHHCCCC		24.4129514104
499PhosphorylationGILDKDLSDRSNDID
HHHCCCCCCCCCCCC		40.9029899451
502PhosphorylationDKDLSDRSNDIDLEG
CCCCCCCCCCCCCCC		43.7929899451
512PhosphorylationIDLEGFDSVISSTEK
CCCCCHHHHHHCCCC		21.0625619855
515PhosphorylationEGFDSVISSTEKLSH
CCHHHHHHCCCCCCC		29.1125619855
516PhosphorylationGFDSVISSTEKLSHP
CHHHHHHCCCCCCCC		29.4825619855
517PhosphorylationFDSVISSTEKLSHPT
HHHHHHCCCCCCCCC		30.2825619855
537PhosphorylationATGRRPPSQSLTSSS
CCCCCCCCCCCCCCC		34.7728507225
539PhosphorylationGRRPPSQSLTSSSLS
CCCCCCCCCCCCCCC		37.6426060331
541PhosphorylationRPPSQSLTSSSLSSP
CCCCCCCCCCCCCCC		31.6326060331
542PhosphorylationPPSQSLTSSSLSSPD
CCCCCCCCCCCCCCC		24.1926060331
543PhosphorylationPSQSLTSSSLSSPDI
CCCCCCCCCCCCCCC		30.0220531401
544PhosphorylationSQSLTSSSLSSPDIF
CCCCCCCCCCCCCCC		31.8526060331
546PhosphorylationSLTSSSLSSPDIFDS
CCCCCCCCCCCCCCC		41.6026060331
547PhosphorylationLTSSSLSSPDIFDSP
CCCCCCCCCCCCCCC		31.7026824392
553PhosphorylationSSPDIFDSPSPEEDK
CCCCCCCCCCCHHHH		19.2726824392
555PhosphorylationPDIFDSPSPEEDKEE
CCCCCCCCCHHHHHH		49.2325521595
565PhosphorylationEDKEEHISLAHRGID
HHHHHHHHHHHCCCC		22.7821659605
579AcetylationDVSKKTSKTVTISQV
CCCCCCCCEEEEEEE		52.8515609847
582PhosphorylationKKTSKTVTISQVSDN
CCCCCEEEEEEECCC		21.8329514104
584PhosphorylationTSKTVTISQVSDNKT
CCCEEEEEEECCCCC		18.3729514104
587PhosphorylationTVTISQVSDNKTSLP
EEEEEEECCCCCCCC		28.0327841257
615PhosphorylationASLSSVASSPMSSSL
CCHHHHHCCCCCCCC		32.5826643407
616PhosphorylationSLSSVASSPMSSSLG
CHHHHHCCCCCCCCC		18.1926643407
619PhosphorylationSVASSPMSSSLGTAG
HHHCCCCCCCCCCCC		21.8426643407
620PhosphorylationVASSPMSSSLGTAGQ
HHCCCCCCCCCCCCC		24.2726643407
621PhosphorylationASSPMSSSLGTAGQR
HCCCCCCCCCCCCCC		24.4226643407
624PhosphorylationPMSSSLGTAGQRASS
CCCCCCCCCCCCCCC		32.6726643407
630PhosphorylationGTAGQRASSPSLFST
CCCCCCCCCCCCCCC		44.9927742792
631PhosphorylationTAGQRASSPSLFSTE
CCCCCCCCCCCCCCC		19.9526824392
633PhosphorylationGQRASSPSLFSTEGK
CCCCCCCCCCCCCCC		43.9527742792
636PhosphorylationASSPSLFSTEGKPKM
CCCCCCCCCCCCCCC		30.7325619855
637PhosphorylationSSPSLFSTEGKPKME
CCCCCCCCCCCCCCC		41.2325619855
648PhosphorylationPKMEPAVSSQAAIEE
CCCCCCCCCHHHHHH		20.8828464351
703AcetylationQMEVNDIKKALQSK-
HHHHHHHHHHHHCC-		34.5523864654
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
-KUbiquitinationE3 ubiquitin ligaseCblP22682
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseCblbQ3TTA7
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SH3K1_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 SH3K1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SHIP1_MOUSEInpp5dphysical
21725061
DLG4_MOUSEDlg4physical
20551902
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SH3K1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, AND MASSSPECTROMETRY.
"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-274, AND MASSSPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND MASSSPECTROMETRY.
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND MASSSPECTROMETRY.

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