SHPS1_MOUSE - dbPTM
SHPS1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SHPS1_MOUSE
UniProt AC P97797
Protein Name Tyrosine-protein phosphatase non-receptor type substrate 1
Gene Name Sirpa
Organism Mus musculus (Mouse).
Sequence Length 513
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Immunoglobulin-like cell surface receptor for CD47. Acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. Supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. May play a key role in intracellular signaling during synaptogenesis and in synaptic function. Involved in the negative regulation of receptor tyrosine kinase-coupled cellular responses induced by cell adhesion, growth factors or insulin. Mediates negative regulation of phagocytosis, mast cell activation and dendritic cell activation. CD47 binding prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells (By similarity)..
Protein Sequence MEPAGPAPGRLGPLLLCLLLSASCFCTGVTGKELKVTQPEKSVSVAAGDSTVLNCTLTSLLPVGPIKWYRGVGQSRLLIYSFTGEHFPRVTNVSDATKRNNMDFSIRISNVTPEDAGTYYCVKFQKGPSEPDTEIQSGGGTEVYVLAKPSPPEVSGPADRGIPDQKVNFTCKSHGFSPRNITLKWFKDGQELHHLETTVNPSGKNVSYNISSTVRVVLNSMDVHSKVICEVAHITLDRSPLRGIANLSNFIRVSPTVKVTQQSPTSMNQVNLTCRAERFYPEDLQLIWLENGNVSRNDTPKNLTKNTDGTYNYTSLFLVNSSAHREDVVFTCQVKHDQQPAITRNHTVLGLAHSSDQGSMQTFPGNNATHNWNVFIGVGVACALLVVLLMAALYLLRIKQKKAKGSTSSTRLHEPEKNAREITQVQSLIQDTNDINDITYADLNLPKEKKPAPRAPEPNNHTEYASIETGKVPRPEDTLTYADLDMVHLSRAQPAPKPEPSFSEYASVQVQRK
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
54N-linked_GlycosylationAGDSTVLNCTLTSLL
ECCCEEEEEEEECCC		16.64-
86PhosphorylationIYSFTGEHFPRVTNV
EEEECCCCCCCEECC		39.0829899451
86PhosphorylationIYSFTGEHFPRVTNV
EEEECCCCCCCEECC		39.0829899451
86PhosphorylationIYSFTGEHFPRVTNV
EEEECCCCCCCEECC		39.0829899451
92N-linked_GlycosylationEHFPRVTNVSDATKR
CCCCCEECCCHHHHH		28.56-
105PhosphorylationKRNNMDFSIRISNVT
HHCCCEEEEEECCCC		13.4920047950
105PhosphorylationKRNNMDFSIRISNVT
HHCCCEEEEEECCCC		13.4920047950
105PhosphorylationKRNNMDFSIRISNVT
HHCCCEEEEEECCCC		13.4920047950
144PhosphorylationSGGGTEVYVLAKPSP
CCCCEEEEEEECCCC		5.419712903
168N-linked_GlycosylationGIPDQKVNFTCKSHG
CCCCCCEEEEEECCC		33.28-
173PhosphorylationKVNFTCKSHGFSPRN
CEEEEEECCCCCCCC		30.8728059163
180N-linked_GlycosylationSHGFSPRNITLKWFK
CCCCCCCCEEEEEEC		34.67-
202PhosphorylationLETTVNPSGKNVSYN
EEEEECCCCCCEEEE		58.1425521595
205N-linked_GlycosylationTVNPSGKNVSYNISS
EECCCCCCEEEEECC		31.34-
205PhosphorylationTVNPSGKNVSYNISS
EECCCCCCEEEEECC		31.3425159016
209N-linked_GlycosylationSGKNVSYNISSTVRV
CCCCEEEEECCEEEE		21.84-
210PhosphorylationGKNVSYNISSTVRVV
CCCEEEEECCEEEEE		2.3330635358
217PhosphorylationISSTVRVVLNSMDVH
ECCEEEEEHHCCCCC		2.6830635358
218PhosphorylationSSTVRVVLNSMDVHS
CCEEEEEHHCCCCCC		3.4325159016
239PhosphorylationAHITLDRSPLRGIAN
CCEECCCCCCCCCCH		28.1427149854
246N-linked_GlycosylationSPLRGIANLSNFIRV
CCCCCCCHHHHCEEE		41.9216944957
271N-linked_GlycosylationPTSMNQVNLTCRAER
CCCHHCEEEEEECEE		21.62-
293N-linked_GlycosylationLIWLENGNVSRNDTP
EEEEECCCCCCCCCC		39.92-
299PhosphorylationGNVSRNDTPKNLTKN
CCCCCCCCCCCCCCC		39.4521454597
302N-linked_GlycosylationSRNDTPKNLTKNTDG
CCCCCCCCCCCCCCC		54.89-
304PhosphorylationNDTPKNLTKNTDGTY
CCCCCCCCCCCCCCE		31.4821454597
312N-linked_GlycosylationKNTDGTYNYTSLFLV
CCCCCCEEEEEEEEE		33.18-
320N-linked_GlycosylationYTSLFLVNSSAHRED
EEEEEEECCCCCCCC		32.18-
345N-linked_GlycosylationQQPAITRNHTVLGLA
CCCCCCCCCEEEEEE		26.91-
367N-linked_GlycosylationMQTFPGNNATHNWNV
CEECCCCCCCCCCCC		52.73-
406PhosphorylationKQKKAKGSTSSTRLH
HHHHCCCCCCCCCCC		25.1424925903
407PhosphorylationQKKAKGSTSSTRLHE
HHHCCCCCCCCCCCC		35.0530635358
408PhosphorylationKKAKGSTSSTRLHEP
HHCCCCCCCCCCCCH		31.2630635358
409PhosphorylationKAKGSTSSTRLHEPE
HCCCCCCCCCCCCHH		20.0330635358
410PhosphorylationAKGSTSSTRLHEPEK
CCCCCCCCCCCCHHH		36.7030635358
417UbiquitinationTRLHEPEKNAREITQ
CCCCCHHHCHHHHHH		67.62-
417UbiquitinationTRLHEPEKNAREITQ
CCCCCHHHCHHHHHH		67.6222790023
423PhosphorylationEKNAREITQVQSLIQ
HHCHHHHHHHHHHHH		20.2429899451
423 (in isoform 2)Phosphorylation-20.2425159016
427PhosphorylationREITQVQSLIQDTND
HHHHHHHHHHHCCCC		28.6929899451
428 (in isoform 2)Phosphorylation-1.9730635358
435 (in isoform 2)Phosphorylation-5.6030635358
436 (in isoform 2)Phosphorylation-37.1825159016
440PhosphorylationNDINDITYADLNLPK
CCCCCCCHHCCCCCC		9.84-
460 (in isoform 2)Phosphorylation-54.9219144319
462PhosphorylationAPEPNNHTEYASIET
CCCCCCCCCEEEEEC		32.5830635358
464PhosphorylationEPNNHTEYASIETGK
CCCCCCCEEEEECCC		13.5525159016
466PhosphorylationNNHTEYASIETGKVP
CCCCCEEEEECCCCC		21.7625159016
469PhosphorylationTEYASIETGKVPRPE
CCEEEEECCCCCCCC		40.4030635358
478PhosphorylationKVPRPEDTLTYADLD
CCCCCCCCCCEECEE		21.2425159016
480PhosphorylationPRPEDTLTYADLDMV
CCCCCCCCEECEEEE		20.8225159016
481PhosphorylationRPEDTLTYADLDMVH
CCCCCCCEECEEEEE		10.9620116462
501PhosphorylationPAPKPEPSFSEYASV
CCCCCCCCHHHCEEE		39.4822817900
503PhosphorylationPKPEPSFSEYASVQV
CCCCCCHHHCEEEEE		33.7525619855
505PhosphorylationPEPSFSEYASVQVQR
CCCCHHHCEEEEEEC		11.7225619855
507PhosphorylationPSFSEYASVQVQRK-
CCHHHCEEEEEECC-		16.5125619855
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
440YPhosphorylationKinaseTYR-KINASES-Uniprot
464YPhosphorylationKinaseTYR-KINASES-Uniprot
481YPhosphorylationKinaseTYR-KINASES-Uniprot
505YPhosphorylationKinaseTYR-KINASES-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SHPS1_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 SHPS1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PTN11_MOUSEPtpn11physical
15699129
NR0B2_MOUSENr0b2physical
15699129
FBX2_MOUSEFbxo2physical
14701835
SKP1_MOUSESkp1aphysical
14701835
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SHPS1_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-246, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-144; TYR-481 ANDTYR-505, AND MASS SPECTROMETRY.
"High expression of inhibitory receptor SHPS-1 and its associationwith protein tyrosine phosphatase SHP-1 in macrophages.";
Veillette A., Thibaudeau E., Latour S.;
J. Biol. Chem. 273:22719-22728(1998).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), VARIANTS ALA-29;ARG-67; PRO-74; ALA-83; 86-TYR-VAL-87; ILE-90; ARG-91; THR-96;ALA-114; ILE-118; SER-128; PRO-194; ASN-224; PHE-351 AND ASP-365,GLYCOSYLATION, PHOSPHORYLATION AT TYROSINE RESIDUES, INTERACTION WITHPTPN6, AND TISSUE SPECIFICITY.

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