PTPRT

Protein tyrosine phosphatase, receptor type, T

PDB rendering based on 2ooq.

Available structures
PDB	2ooq

Identifiers

Symbols

PTPRT; KIAA0283; RPTPrho

External IDs

OMIM: 608712 MGI: 1321152 HomoloGene: 56924 GeneCards: PTPRT Gene

EC number

3.1.3.48

Gene Ontology
Molecular function	• protein tyrosine phosphatase activity • receptor activity • protein binding • beta-catenin binding • hydrolase activity • thiolester hydrolase activity • alpha-catenin binding • gamma-catenin binding • cadherin binding • alpha-actinin binding • delta-catenin binding
Cellular component	• plasma membrane • cell surface • integral to membrane
Biological process	• protein dephosphorylation • cell adhesion • homophilic cell adhesion • signal transduction • transmembrane receptor protein tyrosine kinase signaling pathway • peptidyl-tyrosine dephosphorylation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 20:
40.7 – 41.82 Mb

Chr 2:
161.35 – 162.49 Mb

PubMed search

[1]

[2]

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

PTPRT is also known as human accelerated region 9. It may, therefore, have played a key role in differentiating humans from apes.^[4]

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 possesses an extracellular region, a single transmembrane region, and two tandem intracellular catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains a meprin-A5 antigen-PTP (MAM) domain, Ig-like and fibronectin type III-like repeats. The protein domain structure and the expression pattern of the mouse counterpart of this PTP suggest its roles in both signal transduction and cellular adhesion in the central nervous system. Two alternatively spliced transcript variants of this gene, which encode distinct proteins, have been reported.^[3]

References

^ McAndrew PE, Frostholm A, Evans JE, Zdilar D, Goldowitz D, Chiu IM, Burghes AH, Rotter A (Mar 1998). "Novel receptor protein tyrosine phosphatase (RPTPrho) and acidic fibroblast growth factor (FGF-1) transcripts delineate a rostrocaudal boundary in the granule cell layer of the murine cerebellar cortex". J Comp Neurol 391 (4): 444–55. doi:10.1002/(SICI)1096-9861(19980222)391:4<444::AID-CNE3>3.0.CO;2-0. PMID 9486824.
^ McAndrew PE, Frostholm A, White RA, Rotter A, Burghes AH (Jan 1999). "Identification and characterization of RPTP rho, a novel RPTP mu/kappa-like receptor protein tyrosine phosphatase whose expression is restricted to the central nervous system". Brain Res Mol Brain Res 56 (1–2): 9–21. doi:10.1016/S0169-328X(98)00014-X. PMID 9602027.
^ ^a ^b "Entrez Gene: PTPRT protein tyrosine phosphatase, receptor type, T". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11122.
^ Pollard KS, Salama SR, Lambert N, Lambot MA, Coppens S, Pedersen JS, Katzman S, King B, Onodera C, Siepel A, Kern AD, Dehay C, Igel H, Ares M Jr, Vanderhaeghen P, Haussler D (2006-08-16). "An RNA gene expressed during cortical development evolved rapidly in humans". Nature 443 (7108): 167–172. doi:10.1038/nature05113. PMID 16915236. supplement

Zhang X, Guo A, Yu J, et al. (2007). "Identification of STAT3 as a substrate of receptor protein tyrosine phosphatase T". Proc. Natl. Acad. Sci. U.S.A. 104 (10): 4060–4. doi:10.1073/pnas.0611665104. PMC 1802729. PMID 17360477. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1802729.
Lee JW, Jeong EG, Lee SH, et al. (2007). "Mutational analysis of PTPRT phosphatase domains in common human cancers". APMIS 115 (1): 47–51. doi:10.1111/j.1600-0463.2007.apm_554.x. PMID 17223850.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129.
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.
Wang Z, Shen D, Parsons DW, et al. (2004). "Mutational analysis of the tyrosine phosphatome in colorectal cancers". Science 304 (5674): 1164–6. doi:10.1126/science.1096096. PMID 15155950.
Besco JA, Frostholm A, Popesco MC, et al. (2003). "Genomic organization and alternative splicing of the human and mouse RPTPrho genes: Correction". BMC Genomics 2: 5. doi:10.1186/1471-2164-2-5. PMC 48155. PMID 11814386. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=48155.
Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
Besco JA, Frostholm A, Popesco MC, et al. (2003). "Genomic organization and alternative splicing of the human and mouse RPTPrho genes". BMC Genomics 2: 1. doi:10.1186/1471-2164-2-1. PMC 33392. PMID 11423001. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=33392.
Ohara O, Nagase T, Ishikawa K, et al. (1997). "Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins". DNA Res. 4 (1): 53–9. doi:10.1093/dnares/4.1.53. PMID 9179496.
Hillier LD, Lennon G, Becker M, et al. (1997). "Generation and analysis of 280,000 human expressed sequence tags". Genome Res. 6 (9): 807–28. doi:10.1101/gr.6.9.807. PMID 8889549.

PDB gallery

2ooq: Crystal Structure of the Human Receptor Phosphatase PTPRT

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

PTPRT

References

Further reading