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0SHPS1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePTPNS1
DescriptionTyrosine-protein phosphatase non-receptor type substrate 1 precursor (shp substrate 1) (shps-1) (inhibitory receptor shps-1) (signal- regulatory protein alpha-1) (sirp-alpha-1) (sirp-alpha-2) (sirp-alpha- 3) (myd-1 antigen) (brain ig-like molecule with tyrosine-based activation motifs) (bit) (macrophage fusion receptor) (p84).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005886 plasma membrane (TAS)
0007155 cell adhesion (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This entry represents the V-set domains.hich are Ig-like domains resembling the antibody variable domain. V-set domains are found in diverse protein families.ncluding immunoglobulin light and heavy chains; in several T-cell receptors such as CD2 (Cluster of Differentiation 2).D4.D80.nd CD86; in myelin membrane adhesion molecules; in junction adhesion molecules (JAM); in tyrosine-protein kinase receptors; and in the programmed cell death protein 1 (PD1).
  IPR013106:Immunoglobulin V-set
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This entry represents C1-set domains.hich are classical Ig-like domains resembling the antibody constant domain. C1-set domains are found almost exclusively in molecules involved in the immune system.uch as in immunoglobulin light and heavy chains.n the major histocompatibility complex (MHC) class I and II complex molecules and in various T-cell receptors.
  IPR003597:Immunoglobulin C1-set
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This subfamily includes:Cell surface receptors containing an immunoglobin domain.Killer cell inhibitory receptors.Oprin a snake venom metalloproteinase inhibitor from Didelphis marsupialis (Southern opossum) .hich belongs to MEROPS inhibitor family I43.lan I- .Oprin homologues.
  IPR003599:Immunoglobulin subtype
This entry represents domains with an immunoglobulin-like (Ig-like) fold.hich consists of a beta-sandwich of seven or more strands in two sheets with a Greek-key topology. Ig-like domains are one of the most common protein modules found in animals.ccurring in a variety of different proteins. These domains are often involved in interactions.ommonly with other Ig-like domains via their beta-sheets . Domains within this fold-family share the same structure.ut can diverge with respect to their sequence. Based on sequence.g-like domains can be classified as V-set domains (antibody variable domain-like).1-set domains (antibody constant domain-like).2-set domains.nd I-set domains (antibody intermediate domain-like). Proteins can contain more than one of these types of Ig-like domains. For example.n the human T-cell receptor antigen CD2.omain 1 (D1) is a V-set domain.hile domain 2 (D2) is a C2-set domain.oth domains having the same Ig-like fold .Domains with an Ig-like fold can be found in many.iverse proteins in addition to immunoglobulin molecules. For example.g-like domains occur in several different types of receptors (such as various T-cell antigen receptors).everal cell adhesion molecules.HC class I and II antigens.s well as the hemolymph protein hemolin.nd the muscle proteins titin.elokin and twitchin.
  IPR013783:Immunoglobulin-like fold
IPR013106:V-set 
Evalue:-23.6382713317871 
Location:33-144IPR003597:C1-set 
Evalue:-10.795880317688 
Location:155-240IPR003597:C1-set 
Evalue:-9.19381999969482 
Location:261-340
SequencesProtein: SHPS1_HUMAN (503 aa)
mRNA: BC026692 BC038510 NM_080792
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
The formation of a synapse.
sdb:0034 synaptogenesis  (Evidence:keywords)
KO assignmentK06551
  Level 3 annotation:
    protein tyrosine phosphatase, non-receptor type substrate 1
  Level 2 annotation:
    CD molecules
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 7 residues, 1823424-1823442Exon2: 31 residues, 1824084-1824172Exon3: 121 residues, 1843744-1844101Exon4: 108 residues, 1850040-1850358Exon5: 113 residues, 1850958-1851291Exon6: 40 residues, 1853409-1853523Exon7: 10 residues, 1856520-1856545Exon8: 15 residues, 1863360-1863400Exon9: 858 residues, 1865965-1868535Exon10: 2 residues, -Jump to SHPS1_HUMANExon1: 9 residues, 1823586-1823612Exon2: 31 residues, 1824084-1824172Exon3: 104 residues, 1843744-1844051Exon4: 15 residues, 1844060-1844101Exon5: 108 residues, 1850040-1850358Exon6: 113 residues, 1850958-1851291Exon7: 40 residues, 1853409-1853523Exon8: 10 residues, 1856520-1856545Exon9: 19 residues, 1863360-1863412Exon10: 860 residues, 1865965-1868539Exon11: 2 residues, -Jump to SHPS1_HUMANExon1: 116 residues, 1823825-1824172Exon2: 104 residues, 1843744-1844051Exon3: 15 residues, 1844060-1844101Exon4: 108 residues, 1850040-1850358Exon5: 113 residues, 1850958-1851291Exon6: 40 residues, 1853409-1853523Exon7: 10 residues, 1856520-1856545Exon8: 15 residues, 1863360-1863400Exon9: 860 residues, 1865965-1868539Exon10: 2 residues, -Jump to SHPS1_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4506 1907402-1922702 ~-15K 22547(PDYN)(-)Loci: 3228 1823424-1868539 ~-45K 22542(PTPNS1)(+)Link out to UCSC