P97710 · SHPS1_RAT
- ProteinTyrosine-protein phosphatase non-receptor type substrate 1
- GeneSirpa
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids509 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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. Plays a role in antiviral immunity and limits new world arenavirus infection by decreasing virus internalization (By similarity).
Receptor for THBS1 (PubMed:24511121).
Interaction with THBS1 stimulates phosphorylation of SIRPA (PubMed:24511121).
In response to THBS1, involved in ROS signaling in non-phagocytic cells, stimulating NADPH oxidase-derived ROS production (PubMed:24511121).
Receptor for THBS1 (PubMed:24511121).
Interaction with THBS1 stimulates phosphorylation of SIRPA (PubMed:24511121).
In response to THBS1, involved in ROS signaling in non-phagocytic cells, stimulating NADPH oxidase-derived ROS production (PubMed:24511121).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTyrosine-protein phosphatase non-receptor type substrate 1
- Short namesSHP substrate 1; SHPS-1
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP97710
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 32-373 | Extracellular | ||||
Sequence: KELKVTQADKSVSVAAGDSATLNCTVSSLTPVGPIKWFKGEGQNRSPIYSFIGGEHFPRITNVSDATKRNNMDFSICISNVTPEDAGTYYCVKFQKGIVEPDTEIKSGGGTTLYVLAKPSSPEVSGPDSRGSPGQTVNFTCKSYGFSPRNITLKWLKDGKELSHLETTISSKSNVSYNISSTVSVKLSPEDIHSRVICEVAHVTLEGRPLNGTANFSNIIRVSPTLKITQQPLTPASQVNLTCQVQKFYPKALQLNWLENGNLSRTDKPEHFTDNRDGTYNYTSLFLVNSSAHREDVVFTCQVEHDSQPAITENHTVRAFAHSSSGGSMETIPDNNAYYNWN | ||||||
Transmembrane | 374-394 | Helical | ||||
Sequence: VFIGVGVACALLVVLLMAALY | ||||||
Topological domain | 395-509 | Cytoplasmic | ||||
Sequence: LLRIKQKKAKGSTSSTRLHEPEKNAREITQIQDTNDINDITYADLNLPKEKKPAPRVPEPNNHTEYASIETGKLPRPEDTLTYADLDMVHLNRAQPTPKPEPSFSEYASVQVQRK |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 436 | Abolishes tyrosine phosphorylation and PTPN11 binding; when associated with F-460; F-477 and F-501. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 460 | Abolishes tyrosine phosphorylation and PTPN11 binding; when associated with F-436; F-477 and F-501. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 477 | Strongly reduces insulin-induced tyrosine phosphorylation and PTPN11 binding. Abolishes tyrosine phosphorylation and PTPN11 binding; when associated with F-436; F-460 and F-501. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 501 | Strongly reduces insulin-induced tyrosine phosphorylation and PTPN11 binding. Abolishes tyrosine phosphorylation and PTPN11 binding; when associated with F-436; F-460 and F-477. | ||||
Sequence: Y → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 19 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-31 | |||||
Sequence: MEPAGPAPGRLGPLLFCLLLSASCFCAGASG | ||||||
Chain | PRO_0000014943 | 32-509 | Tyrosine-protein phosphatase non-receptor type substrate 1 | |||
Sequence: KELKVTQADKSVSVAAGDSATLNCTVSSLTPVGPIKWFKGEGQNRSPIYSFIGGEHFPRITNVSDATKRNNMDFSICISNVTPEDAGTYYCVKFQKGIVEPDTEIKSGGGTTLYVLAKPSSPEVSGPDSRGSPGQTVNFTCKSYGFSPRNITLKWLKDGKELSHLETTISSKSNVSYNISSTVSVKLSPEDIHSRVICEVAHVTLEGRPLNGTANFSNIIRVSPTLKITQQPLTPASQVNLTCQVQKFYPKALQLNWLENGNLSRTDKPEHFTDNRDGTYNYTSLFLVNSSAHREDVVFTCQVEHDSQPAITENHTVRAFAHSSSGGSMETIPDNNAYYNWNVFIGVGVACALLVVLLMAALYLLRIKQKKAKGSTSSTRLHEPEKNAREITQIQDTNDINDITYADLNLPKEKKPAPRVPEPNNHTEYASIETGKLPRPEDTLTYADLDMVHLNRAQPTPKPEPSFSEYASVQVQRK | ||||||
Glycosylation | 54 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 55↔122 | |||||
Sequence: CTVSSLTPVGPIKWFKGEGQNRSPIYSFIGGEHFPRITNVSDATKRNNMDFSICISNVTPEDAGTYYC | ||||||
Glycosylation | 93 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 169 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 172↔229 | |||||
Sequence: CKSYGFSPRNITLKWLKDGKELSHLETTISSKSNVSYNISSTVSVKLSPEDIHSRVIC | ||||||
Glycosylation | 181 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 205 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 209 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 242 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 246 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 271 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 274↔332 | |||||
Sequence: CQVQKFYPKALQLNWLENGNLSRTDKPEHFTDNRDGTYNYTSLFLVNSSAHREDVVFTC | ||||||
Glycosylation | 293 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 312 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 320 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 345 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 436 | Phosphotyrosine; by Tyr-kinases | ||||
Sequence: Y | ||||||
Modified residue | 460 | Phosphotyrosine; by Tyr-kinases | ||||
Sequence: Y | ||||||
Modified residue | 477 | Phosphotyrosine; by Tyr-kinases | ||||
Sequence: Y | ||||||
Modified residue | 501 | Phosphotyrosine; by Tyr-kinases | ||||
Sequence: Y |
Post-translational modification
N-glycosylated.
Phosphorylated on tyrosine residues in response to insulin, cell adhesion or epidermal growth factors. Dephosphorylated by PTPN11.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in brain, spleen, lung, liver and kidney. Detected at lower levels in heart. Highly expressed in alveolar and peritoneal macrophages, and at lower levels in dendritic cells.
Gene expression databases
Interaction
Subunit
Binds PTPN11 when tyrosine-phosphorylated, except in macrophages, where it primarily binds PTPN6. Binds GRB2 in vitro. Binds FGR. Binds JAK2 irrespective of its phosphorylation status and forms a stable complex. Binds SCAP1 and/or SCAP2. The resulting complex recruits FYB1. Binds PTK2B (By similarity).
Interacts with TRIM2 (By similarity).
Interacts with TRIM2 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P97710 | Nphs1 Q9R044 | 2 | EBI-7945080, EBI-7945021 | |
BINARY | P97710 | Ptpn11 P41499 | 3 | EBI-7945080, EBI-7180604 | |
XENO | P97710 | PTPN11 Q06124 | 3 | EBI-7945080, EBI-297779 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, motif, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 32-138 | Ig-like V-type | ||||
Sequence: KELKVTQADKSVSVAAGDSATLNCTVSSLTPVGPIKWFKGEGQNRSPIYSFIGGEHFPRITNVSDATKRNNMDFSICISNVTPEDAGTYYCVKFQKGIVEPDTEIKS | ||||||
Domain | 150-248 | Ig-like C1-type 1 | ||||
Sequence: PSSPEVSGPDSRGSPGQTVNFTCKSYGFSPRNITLKWLKDGKELSHLETTISSKSNVSYNISSTVSVKLSPEDIHSRVICEVAHVTLEGRPLNGTANFS | ||||||
Domain | 255-349 | Ig-like C1-type 2 | ||||
Sequence: PTLKITQQPLTPASQVNLTCQVQKFYPKALQLNWLENGNLSRTDKPEHFTDNRDGTYNYTSLFLVNSSAHREDVVFTCQVEHDSQPAITENHTVR | ||||||
Motif | 436-439 | SH2-binding | ||||
Sequence: YADL | ||||||
Region | 441-472 | Disordered | ||||
Sequence: LPKEKKPAPRVPEPNNHTEYASIETGKLPRPE | ||||||
Motif | 446-451 | SH3-binding | ||||
Sequence: KPAPRV | ||||||
Motif | 460-463 | SH2-binding | ||||
Sequence: YASI | ||||||
Motif | 477-480 | SH2-binding | ||||
Sequence: YADL | ||||||
Region | 485-509 | Disordered | ||||
Sequence: LNRAQPTPKPEPSFSEYASVQVQRK | ||||||
Compositional bias | 492-509 | Polar residues | ||||
Sequence: PKPEPSFSEYASVQVQRK | ||||||
Motif | 501-504 | SH2-binding | ||||
Sequence: YASV |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length509
- Mass (Da)55,691
- Last updated1997-05-01 v1
- Checksum5BE1FE0A4DD429F4
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6A7V6 | A0A8I6A7V6_RAT | Sirpa | 517 | ||
A0A8I6ADR4 | A0A8I6ADR4_RAT | Sirpa | 495 | ||
Q499T3 | Q499T3_RAT | Sirpa | 513 | ||
A0A8I6A0T2 | A0A8I6A0T2_RAT | Sirpa | 292 | ||
A0A8I5ZU69 | A0A8I5ZU69_RAT | Sirpa | 172 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 8 | in Ref. 4 | ||||
Sequence: P → L | ||||||
Sequence conflict | 10 | in Ref. 4 | ||||
Sequence: Missing | ||||||
Sequence conflict | 25 | in Ref. 3; AAC68478 | ||||
Sequence: F → I | ||||||
Sequence conflict | 58 | in Ref. 4; AAC18089 | ||||
Sequence: S → C | ||||||
Sequence conflict | 99-100 | in Ref. 3; AA sequence | ||||
Sequence: KR → MP | ||||||
Sequence conflict | 162 | in Ref. 2; BAA20368 | ||||
Sequence: G → A | ||||||
Sequence conflict | 189 | in Ref. 3; AAC68478 | ||||
Sequence: D → N | ||||||
Sequence conflict | 205 | in Ref. 3; AA sequence | ||||
Sequence: N → L | ||||||
Sequence conflict | 209 | in Ref. 3; AA sequence | ||||
Sequence: N → G | ||||||
Sequence conflict | 405 | in Ref. 3; AA sequence | ||||
Sequence: G → F | ||||||
Sequence conflict | 416 | in Ref. 3; AA sequence | ||||
Sequence: E → P | ||||||
Sequence conflict | 418-421 | in Ref. 3; AA sequence | ||||
Sequence: NARE → EGQN | ||||||
Sequence conflict | 450 | in Ref. 3; AA sequence | ||||
Sequence: R → E | ||||||
Compositional bias | 492-509 | Polar residues | ||||
Sequence: PKPEPSFSEYASVQVQRK | ||||||
Sequence conflict | 499 | in Ref. 3; AA sequence | ||||
Sequence: Missing |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D85183 EMBL· GenBank· DDBJ | BAA12734.1 EMBL· GenBank· DDBJ | mRNA | ||
D38468 EMBL· GenBank· DDBJ | BAA20368.1 EMBL· GenBank· DDBJ | mRNA | ||
U62328 EMBL· GenBank· DDBJ | AAC68478.1 EMBL· GenBank· DDBJ | mRNA | ||
AF055065 EMBL· GenBank· DDBJ | AAC18089.1 EMBL· GenBank· DDBJ | mRNA |