PTPRS

Protein tyrosine phosphatase, receptor type, S

PDB rendering based on 2fh7.

Available structures
PDB	2fh7

Identifiers

Symbols

PTPRS; PTPSIGMA

External IDs

OMIM: 601576 MGI: 97815 HomoloGene: 20626 GeneCards: PTPRS Gene

EC number

3.1.3.48

Gene Ontology
Molecular function	• receptor activity • transmembrane receptor protein tyrosine phosphatase activity • protein binding • hydrolase activity
Cellular component	• integral to plasma membrane • membrane
Biological process	• cell adhesion • spinal cord development • cerebellum development • hippocampus development • cerebral cortex development • corpus callosum development
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

n/a

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 19:
5.17 – 5.34 Mb

Chr 17:
56.55 – 56.62 Mb

PubMed search

[1]

[2]

Receptor-type tyrosine-protein phosphatase S is an enzyme that in humans is encoded by the PTPRS gene.^[1]^[2]^[3]

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 contains an extracellular region, a single transmembrane segment and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. The extracellular region of this protein is composed of multiple Ig-like and fibronectin type III-like domains. Studies of the similar gene in mice suggested that this PTP may be involved in cell-cell interaction, primary axonogenesis, and axon guidance during embryogenesis. This PTP has been also implicated in the molecular control of adult nerve repair. Four alternatively spliced transcript variants, which encode distinct proteins, have been reported.^[3]

Interactions

PTPRS has been shown to interact with PTPRD^[4] and liprin-alpha-1.^[2]^[5]

References

^ Wagner J, Gordon LA, Heng HH, Tremblay ML, Olsen AS (Mar 1997). "Physical mapping of receptor type protein tyrosine phosphatase sigma (PTPRS) to human chromosome 19p13.3". Genomics 38 (1): 76–8. doi:10.1006/geno.1996.0594. PMID 8954782.
^ ^a ^b Pulido R, Serra-Pages C, Tang M, Streuli M (Jan 1996). "The LAR/PTP delta/PTP sigma subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1". Proc Natl Acad Sci U S A 92 (25): 11686–90. doi:10.1073/pnas.92.25.11686. PMC 40467. PMID 8524829. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=40467.
^ ^a ^b "Entrez Gene: PTPRS protein tyrosine phosphatase, receptor type, S". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5802.
^ Wallace, M J; Fladd C, Batt J, Rotin D (May. 1998). "The second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigma". Mol. Cell. Biol. (UNITED STATES) 18 (5): 2608–16. ISSN 0270-7306. PMC 110640. PMID 9566880. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=110640.
^ Serra-Pagès, C; Medley Q G, Tang M, Hart A, Streuli M (Jun. 1998). "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins". J. Biol. Chem. (UNITED STATES) 273 (25): 15611–20. doi:10.1074/jbc.273.25.15611. ISSN 0021-9258. PMID 9624153.

Adachi M, Sekiya M, Arimura Y, et al. (1992). "Protein-tyrosine phosphatase expression in pre-B cell NALM-6.". Cancer Res. 52 (3): 737–40. PMID 1370651.
Endo N, Rutledge SJ, Opas EE, et al. (1997). "Human protein tyrosine phosphatase-sigma: alternative splicing and inhibition by bisphosphonates.". J. Bone Miner. Res. 11 (4): 535–43. doi:10.1002/jbmr.5650110415. PMID 8992885.
Norris K, Norris F, Kono DH, et al. (1997). "Expression of protein-tyrosine phosphatases in the major insulin target tissues.". FEBS Lett. 415 (3): 243–8. doi:10.1016/S0014-5793(97)01133-2. PMID 9357975.
Wallace MJ, Fladd C, Batt J, Rotin D (1998). "The second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigma.". Mol. Cell. Biol. 18 (5): 2608–16. PMC 110640. PMID 9566880. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=110640.
Serra-Pagès C, Medley QG, Tang M, et al. (1998). "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins.". J. Biol. Chem. 273 (25): 15611–20. doi:10.1074/jbc.273.25.15611. PMID 9624153.
Haworth K, Shu KK, Stokes A, et al. (1998). "The expression of receptor tyrosine phosphatases is responsive to sciatic nerve crush.". Mol. Cell. Neurosci. 12 (3): 93–104. doi:10.1006/mcne.1998.0707. PMID 9790732.
Elchebly M, Wagner J, Kennedy TE, et al. (1999). "Neuroendocrine dysplasia in mice lacking protein tyrosine phosphatase sigma.". Nat. Genet. 21 (3): 330–3. doi:10.1038/6859. PMID 10080191.
Wallace MJ, Batt J, Fladd CA, et al. (1999). "Neuronal defects and posterior pituitary hypoplasia in mice lacking the receptor tyrosine phosphatase PTPsigma.". Nat. Genet. 21 (3): 334–8. doi:10.1038/6866. PMID 10080192.
Suárez Pestana E, Tenev T, Gross S, et al. (1999). "The transmembrane protein tyrosine phosphatase RPTPsigma modulates signaling of the epidermal growth factor receptor in A431 cells.". Oncogene 18 (28): 4069–79. doi:10.1038/sj.onc.1202794. PMID 10435588.
Blanchetot C, Tertoolen LG, Overvoorde J, den Hertog J (2003). "Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases.". J. Biol. Chem. 277 (49): 47263–9. doi:10.1074/jbc.M205810200. PMID 12376545.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Grimwood J, Gordon LA, Olsen A, et al. (2004). "The DNA sequence and biology of human chromosome 19.". Nature 428 (6982): 529–35. doi:10.1038/nature02399. PMID 15057824.
Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation.". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Hu YF, Zhang HL, Cai T, et al. (2006). "The IA-2 interactome.". Diabetologia 48 (12): 2576–81. doi:10.1007/s00125-005-0037-y. PMID 16273344.
Liu T, Qian WJ, Gritsenko MA, et al. (2006). "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.". J. Proteome Res. 4 (6): 2070–80. doi:10.1021/pr0502065. PMC 1850943. PMID 16335952. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1850943.
Lajus S, Lang J (2006). "Splice variant 3, but not 2 of receptor protein-tyrosine phosphatase sigma can mediate stimulation of insulin-secretion by alpha-latrotoxin.". J. Cell. Biochem. 98 (6): 1552–9. doi:10.1002/jcb.20871. PMID 16552719.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948.

PDB gallery

2fh7: Crystal structure of the phosphatase domains of human PTP SIGMA

Esterase: protein tyrosine phosphatases (EC 3.1.3.48)

Class I

Classical PTPs	Receptor type PTPs (PTPRA, PTPRB, PTPRC, PTPRD, PTPRE, PTPRF, PTPRG, PTPRH, PTPRJ, PTPRK, PTPRM, PTPRN, PTPRN2, PTPRO, PTPRQ, PTPRR, PTPRS, PTPRT, PTPRU, PTPRZ1, PTPRZ2) Non receptor type PTPs (PTPN1, PTPN2, PTPN3, PTPN4, PTPN5, PTPN6, PTPN7, PTPN9, PTPN11, PTPN12, PTPN13, PTPN14, PTPN18, PTPN20, PTPN21, PTPN22, PTPN23

VH1-like or dual specific phosphatases (DSPs)	MAPK phosphatases (MKPs) (DUSP1, DUSP2, DUSP4, DUSP5, DUSP6, DUSP7, DUSP8, DUSP9, DUSP10, DUSP16, MK-STYX) Slingshots (SSH1, SSH2, SSH3) PRLs (PTP4A1, PTP4A2, PTP4A3) CDC14s (CDC14A, CDC14B, CDKN3, PTP9Q22) Atypical DSPs (DUSP3, DUSP11, DUSP12, DUSP13A, DUSP13B, DUSP14, DUSP15, DUSP18, DUSP19, DUSP21, DUSP22, DUSP23, DUSP24, DUSP25, DUSP26, DUSP27, EMP2A, RNGTT, STYX) Phosphatase and tensin homologs (PTENs) (PTEN, TPIP, TPTE, TNS, TENC1) Myotubularins (MTM1, MTMR2, MTMR3, MTMR4, MTMR5, MTMR6, MTMR7, MTMR8, MTMR9, MTMR10, MTMR11, MTMR12, MTMR13, MTMR14, MTMR15)

Class II

ACP1

Class III

Cdc25: CDC25A, CDC25B, CDC25C

Class IV

Eyes absent homolog (EYA1, EYA2, EYA3, EYA4)

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

PTPRS

Interactions

References

Further reading