dbPTM

SHPS1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SHPS1_HUMAN
UniProt AC	P78324
Protein Name	Tyrosine-protein phosphatase non-receptor type substrate 1
Gene Name	SIRPA
Organism	Homo sapiens (Human).
Sequence Length	504
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 (By similarity). 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..
Protein Sequence	MEPAGPAPGRLGPLLCLLLAASCAWSGVAGEEELQVIQPDKSVLVAAGETATLRCTATSLIPVGPIQWFRGAGPGRELIYNQKEGHFPRVTTVSDLTKRNNMDFSIRIGNITPADAGTYYCVKFRKGSPDDVEFKSGAGTELSVRAKPSAPVVSGPAARATPQHTVSFTCESHGFSPRDITLKWFKNGNELSDFQTNVDPVGESVSYSIHSTAKVVLTREDVHSQVICEVAHVTLQGDPLRGTANLSETIRVPPTLEVTQQPVRAENQVNVTCQVRKFYPQRLQLTWLENGNVSRTETASTVTENKDGTYNWMSWLLVNVSAHRDDVKLTCQVEHDGQPAVSKSHDLKVSAHPKEQGSNTAAENTGSNERNIYIVVGVVCTLLVALLMAALYLVRIRQKKAQGSTSSTRLHEPEKNAREITQDTNDITYADLNLPKGKKPAPQAAEPNNHTEYASIQTSPQPASEDTLTYADLDMVHLNRTPKQPAPKPEPSFSEYASVQVPRK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
83	Ubiquitination	RELIYNQKEGHFPRV CEEEEECCCCCCCCE	63.12	-
98	Ubiquitination	TTVSDLTKRNNMDFS EEHHHHHHHCCCEEE	61.50	-
120	Phosphorylation	PADAGTYYCVKFRKG CCCCCEEEEEEECCC	7.21	-
136	Phosphorylation	PDDVEFKSGAGTELS CCCCEEECCCCCEEE	38.91	29978859
140	Phosphorylation	EFKSGAGTELSVRAK EEECCCCCEEEEEEC	32.97	29978859
143	Phosphorylation	SGAGTELSVRAKPSA CCCCCEEEEEECCCC	11.88	29978859
182 (in isoform 2)	Ubiquitination	-	4.76	21890473
182 (in isoform 1)	Ubiquitination	-	4.76	21890473
183	Ubiquitination	SPRDITLKWFKNGNE CCCCEEEEEEECCCC	41.77	21890473
183	Ubiquitination	SPRDITLKWFKNGNE CCCCEEEEEEECCCC	41.77	21890473
183	Ubiquitination	SPRDITLKWFKNGNE CCCCEEEEEEECCCC	41.77	21890473
183 (in isoform 2)	Ubiquitination	-	41.77	-
186	Ubiquitination	DITLKWFKNGNELSD CEEEEEEECCCCCCC	63.93	22817900
192	Phosphorylation	FKNGNELSDFQTNVD EECCCCCCCCCCCCC	30.15	-
198	Ubiquitination	LSDFQTNVDPVGESV CCCCCCCCCCCCCCC	11.33	23000965
204	Phosphorylation	NVDPVGESVSYSIHS CCCCCCCCCEEEEEE	15.50	-
245	N-linked_Glycosylation	DPLRGTANLSETIRV CCCCCCCCHHCCEEC	43.89	16335952
247	O-linked_Glycosylation	LRGTANLSETIRVPP CCCCCCHHCCEECCC	32.28	28657654
259	Phosphorylation	VPPTLEVTQQPVRAE CCCCEEEECCCCCCC	16.47	30257219
270	N-linked_Glycosylation	VRAENQVNVTCQVRK CCCCCEEEEEEEEEE	17.39	19159218
272	O-linked_Glycosylation	AENQVNVTCQVRKFY CCCEEEEEEEEEECC	7.63	28657654
272	Phosphorylation	AENQVNVTCQVRKFY CCCEEEEEEEEEECC	7.63	30257219
292	N-linked_Glycosylation	LTWLENGNVSRTETA EEEEECCCCCEEEEE	39.92	19159218
301	Phosphorylation	SRTETASTVTENKDG CEEEEECEEEECCCC	29.05	25307156
319	N-linked_Glycosylation	WMSWLLVNVSAHRDD EEEEEEEEEECCCCC	23.23	UniProtKB CARBOHYD
404	Phosphorylation	RQKKAQGSTSSTRLH HHHHCCCCCCCCCCC	17.03	26699800
405	Phosphorylation	QKKAQGSTSSTRLHE HHHCCCCCCCCCCCC	33.26	29514088
406	Phosphorylation	KKAQGSTSSTRLHEP HHCCCCCCCCCCCCC	31.26	25056879
407	Phosphorylation	KAQGSTSSTRLHEPE HCCCCCCCCCCCCCC	20.03	25849741
408	Phosphorylation	AQGSTSSTRLHEPEK CCCCCCCCCCCCCCC	36.70	26699800
415	Ubiquitination	TRLHEPEKNAREITQ CCCCCCCCCHHHHCC	67.62	23000965
424	Phosphorylation	AREITQDTNDITYAD HHHHCCCCCCCCCEE	25.60	28152594
428	Phosphorylation	TQDTNDITYADLNLP CCCCCCCCCEECCCC	18.60	28152594
429	Phosphorylation	QDTNDITYADLNLPK CCCCCCCCEECCCCC	9.84	20007894
435 (in isoform 1)	Ubiquitination	-	42.13	21890473
436	Ubiquitination	YADLNLPKGKKPAPQ CEECCCCCCCCCCCC	83.18	2190698
453	Phosphorylation	EPNNHTEYASIQTSP CCCCCCCEEECCCCC	13.55	10842184
464	Phosphorylation	QTSPQPASEDTLTYA CCCCCCCCCCCCCEE	42.56	26356563
467	Phosphorylation	PQPASEDTLTYADLD CCCCCCCCCCEEEEC	19.56	26356563
469	Phosphorylation	PASEDTLTYADLDMV CCCCCCCCEEEECEE	20.82	26356563
470	Phosphorylation	ASEDTLTYADLDMVH CCCCCCCEEEECEEE	10.96	25884760
483	Acetylation	VHLNRTPKQPAPKPE EECCCCCCCCCCCCC	69.19	23749302
492	Phosphorylation	PAPKPEPSFSEYASV CCCCCCCCCHHCEEE	39.48	28152594
494	Phosphorylation	PKPEPSFSEYASVQV CCCCCCCHHCEEEEC	33.75	28152594
494	O-linked_Glycosylation	PKPEPSFSEYASVQV CCCCCCCHHCEEEEC	33.75	28657654
496	Phosphorylation	PEPSFSEYASVQVPR CCCCCHHCEEEECCC	11.72	27273156
498	Phosphorylation	PSFSEYASVQVPRK- CCCHHCEEEECCCC-	16.51	27273156

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
429	Y	Phosphorylation	Kinase	MATK	P42679	GPS
429	Y	Phosphorylation	Kinase	TYR-KINASES	-	Uniprot
453	Y	Phosphorylation	Kinase	MATK	P42679	GPS
453	Y	Phosphorylation	Kinase	TYR-KINASES	-	Uniprot
470	Y	Phosphorylation	Kinase	IGF1R	P08069	PSP
470	Y	Phosphorylation	Kinase	TYR-KINASES	-	Uniprot
496	Y	Phosphorylation	Kinase	IGF1R	P08069	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO2	Q9UK22	PMID:24658274

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SHPS1_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CCD57_HUMAN	CCDC57	physical	25416956

Drug and Disease Associations

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

Regulatory Network of SHPS1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-270 AND ASN-292, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-245, AND MASSSPECTROMETRY.	16335952 [Abstract]