PTPN13

Protein-coding gene in the species Homo sapiens
PTPN13
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1D5G, 1Q7X, 1WCH, 2M0Z, 2M10, 3LNX, 3LNY, 3PDZ

Identifiers
AliasesPTPN13, FAP-1, PNP1, PTP-BAS, PTP-BL, PTP1E, PTPL1, PTPLE, hPTP1E, protein tyrosine phosphatase, non-receptor type 13, protein tyrosine phosphatase non-receptor type 13
External IDsOMIM: 600267 MGI: 103293 HomoloGene: 7909 GeneCards: PTPN13
Gene location (Human)
Chromosome 4 (human)
Chr.Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for PTPN13
Genomic location for PTPN13
Band4q21.3Start86,594,315 bp[1]
End86,815,171 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for PTPN13
Genomic location for PTPN13
Band5 E5|5 50.43 cMStart103,573,058 bp[2]
End103,746,169 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • urethra

  • human penis

  • palpebral conjunctiva

  • retinal pigment epithelium

  • renal medulla

  • trigeminal ganglion

  • Achilles tendon

  • spinal ganglia

  • corpus callosum

  • skin of abdomen
Top expressed in
  • corneal stroma

  • hair follicle

  • mucosa of urinary bladder

  • retinal pigment epithelium

  • medullary collecting duct

  • conjunctival fornix

  • skin of back

  • sciatic nerve

  • skin of abdomen

  • seminal vesicula
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • protein tyrosine phosphatase activity
  • phosphatase activity
  • phosphatidylinositol 3-kinase regulatory subunit binding
  • protein binding
  • phosphoprotein phosphatase activity
  • hydrolase activity
Cellular component
  • cytoplasm
  • cell body
  • neuron projection
  • cell projection
  • extracellular exosome
  • cytoskeleton
  • nucleus
  • lamellipodium
  • plasma membrane
  • nucleoplasm
Biological process
  • protein dephosphorylation
  • peptidyl-tyrosine dephosphorylation
  • regulation of phosphatidylinositol 3-kinase signaling
  • dephosphorylation
  • phosphatidylinositol biosynthetic process
  • negative regulation of protein phosphorylation
  • cellular response to cytokine stimulus
  • bicellular tight junction assembly
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5783

19249

Ensembl

ENSG00000163629

ENSMUSG00000034573

UniProt

Q12923

Q64512

RefSeq (mRNA)

NM_006264
NM_080683
NM_080684
NM_080685

NM_011204

RefSeq (protein)

NP_006255
NP_542414
NP_542415
NP_542416

NP_035334

Location (UCSC)Chr 4: 86.59 – 86.82 MbChr 5: 103.57 – 103.75 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Tyrosine-protein phosphatase non-receptor type 13 is an enzyme that in humans is encoded by the PTPN13 gene.[5][6]

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.[6]

Interactions

PTPN13 has been shown to interact with PKN2.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000163629 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000034573 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Maekawa K, Imagawa N, Nagamatsu M, Harada S (Feb 1994). "Molecular cloning of a novel protein-tyrosine phosphatase containing a membrane-binding domain and GLGF repeats". FEBS Lett. 337 (2): 200–206. doi:10.1016/0014-5793(94)80273-4. PMID 8287977. S2CID 46269697.
  6. ^ a b "Entrez Gene: PTPN13 protein tyrosine phosphatase, non-receptor type 13 (APO-1/CD95 (Fas)-associated phosphatase)".
  7. ^ Gross C, Heumann R, Erdmann K S (May 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): 101–104. doi:10.1016/S0014-5793(01)02401-2. ISSN 0014-5793. PMID 11356191. S2CID 205880882.

Further reading

  • Sato T, Irie S, Kitada S, Reed JC (1995). "FAP-1: a protein tyrosine phosphatase that associates with Fas". Science. 268 (5209): 411–415. Bibcode:1995Sci...268..411S. doi:10.1126/science.7536343. PMID 7536343.
  • 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. doi:10.1016/S0021-9258(19)51050-X. PMID 7929060.
  • 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. doi:10.1016/S0021-9258(17)31792-1. PMID 8071359.
  • Inazawa J, Ariyama T, Abe T, Druck T, Ohta M, Huebner K, Yanagisawa J, Reed JC, Sato T (1997). "PTPN13, a fas-associated protein tyrosine phosphatase, is located on the long arm of chromosome 4 at band q21.3". Genomics. 31 (2): 240–242. doi:10.1006/geno.1996.0039. PMID 8824809.
  • Yanagisawa J, Takahashi M, Kanki H, Yano-Yanagisawa H, Tazunoki T, Sawa E, Nishitoba T, Kamishohara M, Kobayashi E (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): 8539–8545. doi:10.1074/jbc.272.13.8539. PMID 9079683.
  • 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): 20979–20981. doi:10.1074/jbc.272.34.20979. PMID 9261095.
  • Saras J, Franzén P, Aspenström P, Hellman U, Gonez LJ, Heldin CH (1997). "A novel GTPase-activating protein for Rho interacts with a PDZ domain of the protein-tyrosine phosphatase PTPL1". J. Biol. Chem. 272 (39): 24333–24338. doi:10.1074/jbc.272.39.24333. PMID 9305890.
  • Ekiel I, Banville D, Shen SH, Slon-Usakiewicz JJ, Koshy A, Gehring K (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): 455–456. doi:10.1023/A:1008267807859. PMID 9835052. S2CID 19976473.
  • Maekawa K, Imagawa N, Naito A, Harada S, Yoshie O, Takagi S (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 (2): 179–84. doi:10.1042/0264-6021:3370179. PMC 1219950. PMID 9882613.
  • 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): 3726–3733. doi:10.1074/jbc.274.6.3726. PMID 9920925.
  • Murthy KK, Clark K, Fortin Y, Shen SH, Banville D (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): 20679–20687. doi:10.1074/jbc.274.29.20679. PMID 10400701.
  • Cuppen E, van Ham M, Pepers B, Wieringa B, Hendriks W (1999). "Identification and molecular characterization of BP75, a novel bromodomain-containing protein". FEBS Lett. 459 (3): 291–298. doi:10.1016/S0014-5793(99)01191-6. PMID 10526152. S2CID 41216030.
  • Irie S, Hachiya T, Rabizadeh S, Maruyama W, Mukai J, Li Y, Reed JC, Bredesen DE, Sato TA (1999). "Functional interaction of Fas-associated phosphatase-1 (FAP-1) with p75(NTR) and their effect on NF-kappaB activation". FEBS Lett. 460 (2): 191–198. doi:10.1016/S0014-5793(99)01324-1. PMID 10544233. S2CID 25143664.
  • Lee SH, Shin MS, Park WS, Kim SY, Kim HS, Lee JH, Han SY, Lee HK, Park JY (2000). "Immunohistochemical localization of FAP-1, an inhibitor of Fas-mediated apoptosis, in normal and neoplastic human tissues". APMIS. 107 (12): 1101–1108. doi:10.1111/j.1699-0463.1999.tb01515.x. PMID 10660140. S2CID 24672576.
  • 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): 2572–2580. doi:10.1021/bi991913c. PMID 10704206.
  • Cuppen E, van Ham M, Wansink DG, De Leeuw A, Wieringa B, Hendriks W (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): 283–293. doi:10.1078/S0171-9335(04)70031-X. PMID 10826496.
  • Erdmann KS, Kuhlmann J, Lessmann V, Herrmann L, Eulenburg V, Müller O, Heumann R (2000). "The Adenomatous Polyposis Coli-protein (APC) interacts with the protein tyrosine phosphatase PTP-BL via an alternatively spliced PDZ domain". Oncogene. 19 (34): 3894–3901. doi:10.1038/sj.onc.1203725. PMID 10951583.
  • Nakai Y, Irie S, Sato TA (2001). "Identification of IkappaBalpha as a substrate of Fas-associated phosphatase-1". Eur. J. Biochem. 267 (24): 7170–7175. doi:10.1046/j.1432-1327.2000.01818.x. PMID 11106428.
  • 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): 101–104. doi:10.1016/S0014-5793(01)02401-2. PMID 11356191. S2CID 205880882.
  • v
  • t
  • e
  • 1d5g: SOLUTION STRUCTURE OF THE PDZ2 DOMAIN FROM HUMAN PHOSPHATASE HPTP1E COMPLEXED WITH A PEPTIDE
    1d5g: SOLUTION STRUCTURE OF THE PDZ2 DOMAIN FROM HUMAN PHOSPHATASE HPTP1E COMPLEXED WITH A PEPTIDE
  • 1gm1: SECOND PDZ DOMAIN (PDZ2) OF PTP-BL
    1gm1: SECOND PDZ DOMAIN (PDZ2) OF PTP-BL
  • 1ozi: The alternatively spliced PDZ2 domain of PTP-BL
    1ozi: The alternatively spliced PDZ2 domain of PTP-BL
  • 1q7x: Solution structure of the alternatively spliced PDZ2 domain (PDZ2b) of PTP-Bas (hPTP1E)
    1q7x: Solution structure of the alternatively spliced PDZ2 domain (PDZ2b) of PTP-Bas (hPTP1E)
  • 1vj6: PDZ2 from PTP-BL in complex with the C-terminal ligand from the APC protein
    1vj6: PDZ2 from PTP-BL in complex with the C-terminal ligand from the APC protein
  • 1wch: CRYSTAL STRUCTURE OF PTPL1 HUMAN TYROSINE PHOSPHATASE MUTATED IN COLORECTAL CANCER - EVIDENCE FOR A SECOND PHOSPHOTYROSINE SUBSTRATE RECOGNITION POCKET
    1wch: CRYSTAL STRUCTURE OF PTPL1 HUMAN TYROSINE PHOSPHATASE MUTATED IN COLORECTAL CANCER - EVIDENCE FOR A SECOND PHOSPHOTYROSINE SUBSTRATE RECOGNITION POCKET
  • 3pdz: SOLUTION STRUCTURE OF THE PDZ2 DOMAIN FROM HUMAN PHOSPHATASE HPTP1E
    3pdz: SOLUTION STRUCTURE OF THE PDZ2 DOMAIN FROM HUMAN PHOSPHATASE HPTP1E
  • v
  • t
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Class I
Classical PTPs
Receptor type PTPs
Non receptor type PTPs
VH1-like or
dual specific
phosphatases
(DSPs)
MAPK phosphatases (MKPs)
Slingshots
PRLs
CDC14s
Atypical DSPs
Phosphatase and tensin
homologs (PTENs)
Myotubularins
Class II
Class III
Class IV