PTPN13

Protein tyrosine phosphatase, non-receptor type 13 (APO-1/CD95 (Fas)-associated phosphatase)
File:PBB Protein PTPN13 image.jpg PDB rendering based on 1d5g.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1d5g​, 1gm1​, 1ozi​, 1q7x​, 1vj6​, 1wch​, 3pdz​
Identifiers
Symbols	PTPN13 ; DKFZp686J1497; FAP-1; PNP1; PTP-BAS; PTP-BL; PTP1E; PTPL1; PTPLE
External IDs	Template:OMIM5 Template:MGI HomoloGene: 7909
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Biological process Template:GNF GO
RNA expression pattern
File:PBB GE PTPN13 204201 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Protein tyrosine phosphatase, non-receptor type 13 (APO-1/CD95 (Fas)-associated phosphatase), also known as PTPN13, is a human gene.

The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP is a large protein that possesses a PTP domain at C-terminus, and multiple noncatalytic domains, which include a domain with similarity to band 4.1 superfamily of cytoskeletal-associated proteins, a region consisting of five PDZ domains, and a leucine zipper motif. This PTP was found to interact with, and dephosphorylate Fas receptor, as well as IkappaBalpha through the PDZ domains, which suggested its role in Fas mediated programmed cell death. This PTP was also shown to interact with GTPase-activating protein, and thus may function as a regulator of Rho signaling pathway. Four alternatively spliced transcript variants, which encode distinct proteins, have been reported.

Further reading

• Sato T, Irie S, Kitada S, Reed JC (1995). "FAP-1: a protein tyrosine phosphatase that associates with Fas". Science. 268 (5209): 411–5. PMID 7536343.CS1 maint: Multiple names: authors list (link)
• Saras J, Claesson-Welsh L, Heldin CH, Gonez LJ (1994). "Cloning and characterization of PTPL1, a protein tyrosine phosphatase with similarities to cytoskeletal-associated proteins". J. Biol. Chem. 269 (39): 24082–9. PMID 7929060.CS1 maint: Multiple names: authors list (link)
• Banville D, Ahmad S, Stocco R, Shen SH (1994). "A novel protein-tyrosine phosphatase with homology to both the cytoskeletal proteins of the band 4.1 family and junction-associated guanylate kinases". J. Biol. Chem. 269 (35): 22320–7. PMID 8071359.CS1 maint: Multiple names: authors list (link)
• Maekawa K, Imagawa N, Nagamatsu M, Harada S (1994). "Molecular cloning of a novel protein-tyrosine phosphatase containing a membrane-binding domain and GLGF repeats". FEBS Lett. 337 (2): 200–6. PMID 8287977.CS1 maint: Multiple names: authors list (link)
• Inazawa J, Ariyama T, Abe T; et al. (1997). "PTPN13, a fas-associated protein tyrosine phosphatase, is located on the long arm of chromosome 4 at band q21.3". Genomics. 31 (2): 240–2. doi:10.1006/geno.1996.0039. PMID 8824809.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Yanagisawa J, Takahashi M, Kanki H; et al. (1997). "The molecular interaction of Fas and FAP-1. A tripeptide blocker of human Fas interaction with FAP-1 promotes Fas-induced apoptosis". J. Biol. Chem. 272 (13): 8539–45. PMID 9079683.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Saras J, Engström U, Góñez LJ, Heldin CH (1997). "Characterization of the interactions between PDZ domains of the protein-tyrosine phosphatase PTPL1 and the carboxyl-terminal tail of Fas". J. Biol. Chem. 272 (34): 20979–81. PMID 9261095.CS1 maint: Multiple names: authors list (link)
• Saras J, Franzén P, Aspenström P; et al. (1997). "A novel GTPase-activating protein for Rho interacts with a PDZ domain of the protein-tyrosine phosphatase PTPL1". J. Biol. Chem. 272 (39): 24333–8. PMID 9305890.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ekiel I, Banville D, Shen SH; et al. (1999). "Main-chain signal assignment for the PDZ2 domain from human protein tyrosine phosphatase hPTP1E and its complex with a C-terminal peptide from the Fas receptor". J. Biomol. NMR. 12 (3): 455–6. PMID 9835052.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Maekawa K, Imagawa N, Naito A; et al. (1999). "Association of protein-tyrosine phosphatase PTP-BAS with the transcription-factor-inhibitory protein IkappaBalpha through interaction between the PDZ1 domain and ankyrin repeats". Biochem. J. 337 ( Pt 2): 179–84. PMID 9882613.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lin D, Gish GD, Songyang Z, Pawson T (1999). "The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif". J. Biol. Chem. 274 (6): 3726–33. PMID 9920925.CS1 maint: Multiple names: authors list (link)
• Murthy KK, Clark K, Fortin Y; et al. (1999). "ZRP-1, a zyxin-related protein, interacts with the second PDZ domain of the cytosolic protein tyrosine phosphatase hPTP1E". J. Biol. Chem. 274 (29): 20679–87. PMID 10400701.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Cuppen E, van Ham M, Pepers B; et al. (1999). "Identification and molecular characterization of BP75, a novel bromodomain-containing protein". FEBS Lett. 459 (3): 291–8. PMID 10526152.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Irie S, Hachiya T, Rabizadeh S; et al. (1999). "Functional interaction of Fas-associated phosphatase-1 (FAP-1) with p75(NTR) and their effect on NF-kappaB activation". FEBS Lett. 460 (2): 191–8. PMID 10544233.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lee SH, Shin MS, Park WS; et al. (2000). "Immunohistochemical localization of FAP-1, an inhibitor of Fas-mediated apoptosis, in normal and neoplastic human tissues". APMIS. 107 (12): 1101–8. PMID 10660140.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kozlov G, Gehring K, Ekiel I (2000). "Solution structure of the PDZ2 domain from human phosphatase hPTP1E and its interactions with C-terminal peptides from the Fas receptor". Biochemistry. 39 (10): 2572–80. PMID 10704206.CS1 maint: Multiple names: authors list (link)
• Cuppen E, van Ham M, Wansink DG; et al. (2000). "The zyxin-related protein TRIP6 interacts with PDZ motifs in the adaptor protein RIL and the protein tyrosine phosphatase PTP-BL". Eur. J. Cell Biol. 79 (4): 283–93. PMID 10826496.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Erdmann KS, Kuhlmann J, Lessmann V; et al. (2000). "The Adenomatous Polyposis Coli-protein (APC) interacts with the protein tyrosine phosphatase PTP-BL via an alternatively spliced PDZ domain". Oncogene. 19 (34): 3894–901. doi:10.1038/sj.onc.1203725. PMID 10951583.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Nakai Y, Irie S, Sato TA (2001). "Identification of IkappaBalpha as a substrate of Fas-associated phosphatase-1". Eur. J. Biochem. 267 (24): 7170–5. PMID 11106428.CS1 maint: Multiple names: authors list (link)
• Gross C, Heumann R, Erdmann KS (2001). "The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif". FEBS Lett. 496 (2–3): 101–4. PMID 11356191.CS1 maint: Multiple names: authors list (link)