dbPTM

SHPS1_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SHPS1_RAT
UniProt AC	P97710
Protein Name	Tyrosine-protein phosphatase non-receptor type substrate 1
Gene Name	Sirpa
Organism	Rattus norvegicus (Rat).
Sequence Length	509
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. May play a role in the release of nitric oxide by macrophages (By similarity)..
Protein Sequence	MEPAGPAPGRLGPLLFCLLLSASCFCAGASGKELKVTQADKSVSVAAGDSATLNCTVSSLTPVGPIKWFKGEGQNRSPIYSFIGGEHFPRITNVSDATKRNNMDFSICISNVTPEDAGTYYCVKFQKGIVEPDTEIKSGGGTTLYVLAKPSSPEVSGPDSRGSPGQTVNFTCKSYGFSPRNITLKWLKDGKELSHLETTISSKSNVSYNISSTVSVKLSPEDIHSRVICEVAHVTLEGRPLNGTANFSNIIRVSPTLKITQQPLTPASQVNLTCQVQKFYPKALQLNWLENGNLSRTDKPEHFTDNRDGTYNYTSLFLVNSSAHREDVVFTCQVEHDSQPAITENHTVRAFAHSSSGGSMETIPDNNAYYNWNVFIGVGVACALLVVLLMAALYLLRIKQKKAKGSTSSTRLHEPEKNAREITQIQDTNDINDITYADLNLPKEKKPAPRVPEPNNHTEYASIETGKLPRPEDTLTYADLDMVHLNRAQPTPKPEPSFSEYASVQVQRK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
37	Phosphorylation	SGKELKVTQADKSVS CCCEEEEEECCCEEE	19.22	28551015
42	Phosphorylation	KVTQADKSVSVAAGD EEEECCCEEEEECCC	21.85	28551015
44	Phosphorylation	TQADKSVSVAAGDSA EECCCEEEEECCCCE	17.09	28551015
50	Phosphorylation	VSVAAGDSATLNCTV EEEECCCCEEEEEEE	23.41	28551015
52	Phosphorylation	VAAGDSATLNCTVSS EECCCCEEEEEEECC	23.58	28551015
54	N-linked_Glycosylation	AGDSATLNCTVSSLT CCCCEEEEEEECCCC	18.30	-
56	Phosphorylation	DSATLNCTVSSLTPV CCEEEEEEECCCCCC	23.50	28551015
58	Phosphorylation	ATLNCTVSSLTPVGP EEEEEEECCCCCCCC	11.07	28551015
59	Phosphorylation	TLNCTVSSLTPVGPI EEEEEECCCCCCCCE	31.74	28551015
61	Phosphorylation	NCTVSSLTPVGPIKW EEEECCCCCCCCEEE	20.20	28551015
93	N-linked_Glycosylation	EHFPRITNVSDATKR CCCCCEECCCHHHHH	28.99	24090084
98	Phosphorylation	ITNVSDATKRNNMDF EECCCHHHHHHCCCE	35.21	22108457
145	Phosphorylation	SGGGTTLYVLAKPSS CCCCEEEEEEECCCC	7.42	-
169	N-linked_Glycosylation	GSPGQTVNFTCKSYG CCCCCEEEEEEECCC	29.87	24090084
181	N-linked_Glycosylation	SYGFSPRNITLKWLK CCCCCCCEEEEEEEC	34.67	-
191	Acetylation	LKWLKDGKELSHLET EEEECCCCEEEEEEE	66.66	22902405
205	N-linked_Glycosylation	TTISSKSNVSYNISS EEEECCCCCEEEEEC	30.41	-
209	N-linked_Glycosylation	SKSNVSYNISSTVSV CCCCCEEEEECEEEE	21.84	-
242	N-linked_Glycosylation	TLEGRPLNGTANFSN EEECEECCCCCCCCC	48.75	-
246	N-linked_Glycosylation	RPLNGTANFSNIIRV EECCCCCCCCCEEEE	40.49	-
271	N-linked_Glycosylation	LTPASQVNLTCQVQK CCCHHHCCEEEEEEE	23.23	-
293	N-linked_Glycosylation	LNWLENGNLSRTDKP CEEHHCCCCCCCCCC	46.56	-
312	N-linked_Glycosylation	DNRDGTYNYTSLFLV CCCCCCEEEEEEEEE	33.18	24090084
320	N-linked_Glycosylation	YTSLFLVNSSAHRED EEEEEEECCCCCCCC	32.18	-
345	N-linked_Glycosylation	SQPAITENHTVRAFA CCCCCCCCCEEEEEE	27.72	-
406	Phosphorylation	KQKKAKGSTSSTRLH HHHHCCCCCCCCCCC	25.14	25403869
407	Phosphorylation	QKKAKGSTSSTRLHE HHHCCCCCCCCCCCC	35.05	25403869
408	Phosphorylation	KKAKGSTSSTRLHEP HHCCCCCCCCCCCCC	31.26	25403869
409	Phosphorylation	KAKGSTSSTRLHEPE HCCCCCCCCCCCCCH	20.03	25403869
410	Phosphorylation	AKGSTSSTRLHEPEK CCCCCCCCCCCCCHH	36.70	25403869
417	Ubiquitination	TRLHEPEKNAREITQ CCCCCCHHCHHHCEE	67.62	-
435	Phosphorylation	TNDINDITYADLNLP CCCCCCCCHHHCCCC	18.60	27097102
436	Phosphorylation	NDINDITYADLNLPK CCCCCCCHHHCCCCC	9.84	27097102
458	Phosphorylation	VPEPNNHTEYASIET CCCCCCCCCEEEEEC	32.58	27097102
460	Phosphorylation	EPNNHTEYASIETGK CCCCCCCEEEEECCC	13.55	27097102
462	Phosphorylation	NNHTEYASIETGKLP CCCCCEEEEECCCCC	21.76	27097102
465	Phosphorylation	TEYASIETGKLPRPE CCEEEEECCCCCCCC	37.64	27097102
474	Phosphorylation	KLPRPEDTLTYADLD CCCCCCCCCCEEEEE	21.24	27097102
476	Phosphorylation	PRPEDTLTYADLDMV CCCCCCCCEEEEEEE	20.82	27097102
477	Phosphorylation	RPEDTLTYADLDMVH CCCCCCCEEEEEEEE	10.96	23712012
499	Phosphorylation	PKPEPSFSEYASVQV CCCCCCHHHCEEEEE	33.75	27097102
501	Phosphorylation	PEPSFSEYASVQVQR CCCCHHHCEEEEEEC	11.72	27097102
503	Phosphorylation	PSFSEYASVQVQRK- CCHHHCEEEEEECC-	16.51	27097102

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
436	Y	Phosphorylation	Kinase	TYR-KINASES	-	Uniprot
460	Y	Phosphorylation	Kinase	TYR-KINASES	-	Uniprot
477	Y	Phosphorylation	Kinase	TYR-KINASES	-	Uniprot
501	Y	Phosphorylation	Kinase	TYR-KINASES	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SHPS1_RAT !!

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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SHPS1_RAT !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SHPS1_RAT

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Roles of the complex formation of SHPS-1 with SHP-2 in insulin-stimulated mitogen-activated protein kinase activation."; Takada T., Matozaki T., Takeda H., Fukunaga K., Noguchi T.,Fujioka Y., Okazaki I., Tsuda M., Yamao T., Ochi F., Kasuga M.; J. Biol. Chem. 273:9234-9242(1998). Cited for: PHOSPHORYLATION AT TYR-477 AND TYR-501, AND MUTAGENESIS OF TYR-436;TYR-460; TYR-477 AND TYR-501.	9535915 [Abstract]
"BIT, an immune antigen receptor-like molecule in the brain."; Sano S., Ohnishi H., Omori A., Hasegawa J., Kubota M.; FEBS Lett. 411:327-334(1997). Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-48 AND 446-453,FUNCTION, AND PHOSPHORYLATION AT TYROSINE RESIDUES.	9271230 [Abstract]
"A novel membrane glycoprotein, SHPS-1, that binds the SH2-domain-containing protein tyrosine phosphatase SHP-2 in response to mitogensand cell adhesion."; Fujioka Y., Matozaki T., Noguchi T., Iwamatsu A., Yamao T.,Takahashi N., Tsuda M., Takada T., Kasuga M.; Mol. Cell. Biol. 16:6887-6899(1996). Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 42-60; 68-91; 128-137;150-158; 174-189; 192-202; 204-212; 218-237; 259-270; 279-282; 405-415AND 446-453, GLYCOSYLATION, PHOSPHORYLATION AT TYROSINE RESIDUES, ANDINTERACTION WITH PTPN6 AND PTPN11.	8943344 [Abstract]