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Reviewed, UniProtKB/Swiss-Prot Q13332 (PTPRS_HUMAN)

Last modified November 25, 2008. Version 85. Feed History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Receptor-type tyrosine-protein phosphatase S
      Short name=R-PTP-S
    EC=3.1.3.48
Alternative name(s):
    Receptor-type tyrosine-protein phosphatase sigma
      Short name=R-PTP-sigma
Gene names
Name: PTPRS
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1948 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Interacts with LAR-interacting protein LIP.1.

Catalytic activity

Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.

Subunit structure

Interacts with PPFIA1, PPFIA2 and PPFIA3.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Detected in all tissues tested except for placenta and liver.

Post-translational modification

A cleavage occurs, separating the extracellular domain from the transmembrane segment. This process called 'ectodomain shedding' is thought to be involved in receptor desensitization, signal transduction and/or membrane localization By similarity.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class 2A subfamily.

Contains 8 fibronectin type-III domains.

Contains 3 Ig-like C2-type (immunoglobulin-like) domains.

Contains 2 tyrosine-protein phosphatase domains.

Ontologies

Keywords

   Biological processCell adhesion
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
   Molecular functionHydrolase
Protein phosphatase
Receptor
   PTMGlycoprotein
   Technical term3D-structure

Gene Ontology (GO)

   Biological processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

protein amino acid dephosphorylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to plasma membrane Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

transmembrane receptor protein tyrosine phosphatase activity Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PTPRNQ168493EBI-711536,EBI-728153

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Notes: Additional isoforms seem to exist.
Isoform PTPS (identifier: Q13332-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform PTPS-MEA (identifier: Q13332-2)

The sequence of this isoform differs from the canonical sequence as follows:
     190-198: Missing.
Isoform PTPS-MEB (identifier: Q13332-3)

The sequence of this isoform differs from the canonical sequence as follows:
     236-239: Missing.
     1350-1365: Missing.
     1366-1366: S → G
Isoform PTPS-MEC (identifier: Q13332-4)

The sequence of this isoform differs from the canonical sequence as follows:
     784-792: Missing.
Isoform PTPS-F4-7 (identifier: Q13332-5)

The sequence of this isoform differs from the canonical sequence as follows:
     617-1034: Missing.
     1035-1035: V → I

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 19481919Receptor-type tyrosine-protein phosphatase S
PRO_0000025462

Regions

Topological domain30 – 12821253Extracellular Potential
Transmembrane1283 – 130321 Potential
Topological domain1304 – 1948645Cytoplasmic Potential
Domain33 – 12391Ig-like C2-type 1
Domain135 – 23399Ig-like C2-type 2
Domain245 – 32783Ig-like C2-type 3
Domain332 – 42089Fibronectin type-III 1
Domain426 – 52095Fibronectin type-III 2
Domain525 – 61490Fibronectin type-III 3
Domain618 – 71598Fibronectin type-III 4
Domain720 – 828109Fibronectin type-III 5
Domain836 – 92388Fibronectin type-III 6
Domain928 – 1031104Fibronectin type-III 7
Domain1033 – 111785Fibronectin type-III 8
Domain1393 – 1648256Tyrosine-protein phosphatase 1
Domain1680 – 1939260Tyrosine-protein phosphatase 2
Compositional bias641 – 6444Poly-Pro

Sites

Active site15891Phosphocysteine intermediate By similarity
Active site18801Phosphocysteine intermediate By similarity
Site1197 – 11982Cleavage By similarity

Amino acid modifications

Glycosylation2631N-linked (GlcNAc...) Potential
Glycosylation3081N-linked (GlcNAc...) Potential
Glycosylation7331N-linked (GlcNAc...)
Glycosylation9401N-linked (GlcNAc...) Potential
Disulfide bond54 ↔ 107 Potential
Disulfide bond156 ↔ 216 Potential
Disulfide bond266 ↔ 311 Potential

Natural variations

Alternative sequence190 – 1989Missing in isoform PTPS-MEA.
VSP_050021
Alternative sequence236 – 2394Missing in isoform PTPS-MEB.
VSP_050022
Alternative sequence617 – 1034418Missing in isoform PTPS-F4-7.
VSP_050023
Alternative sequence784 – 7929Missing in isoform PTPS-MEC.
VSP_050024
Alternative sequence10351V → I in isoform PTPS-F4-7.
VSP_050025
Alternative sequence1350 – 136516Missing in isoform PTPS-MEB.
VSP_050026
Alternative sequence13661S → G in isoform PTPS-MEB.
VSP_050027
Natural variant9961T → M in a colorectal cancer sample; somatic mutation.
VAR_035649
Natural variant14571R → C: dbSNP rs4807697.
VAR_047277

Experimental info

Sequence conflict481G → R in AAC50567. Ref.2
Sequence conflict3101T → HP in AAC50567. Ref.2
Sequence conflict428 – 4292SA → RP in AAC50567. Ref.2
Sequence conflict742 – 7454RSPA → LGPV in AAC50299. Ref.1
Sequence conflict765 – 7662GA → RR in AAC50567. Ref.2
Sequence conflict7681A → G in AAC50299. Ref.1
Sequence conflict771 – 7733PPR → RRS in AAC50567. Ref.2
Sequence conflict9101R → P in AAC50567. Ref.2
Sequence conflict986 – 9949AAEPGAENA → GRLSRARRT in AAC50567. Ref.2
Sequence conflict9951L → V in AAC50299. Ref.1
Sequence conflict1195 – 11962SL → TV in AAC50299. Ref.1
Sequence conflict1310 – 13134Missing in AAC62834. Ref.3
Sequence conflict14311S → F in AAC50299. Ref.1
Sequence conflict15461E → D in AAB21146. Ref.4
Sequence conflict15871V → A in AAB21146. Ref.4
Sequence conflict17051N → K in AAC50567. Ref.2

Secondary structure

............................................................................................... 1948
Helix Strand Turn

Details...