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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Protein tyrosine phosphatase receptor-type R''' is an [[enzyme]] that in humans is encoded by the ''PTPRR'' [[gene]].<ref name="pmid7557444">{{cite journal | vauthors = Shiozuka K, Watanabe Y, Ikeda T, Hashimoto S, Kawashima H | title = Cloning and expression of PCPTP1 encoding protein tyrosine phosphatase | journal = Gene | volume = 162 | issue = 2 | pages = 279–84 | date = Nov 1995 | pmid = 7557444 | pmc =  | doi = 10.1016/0378-1119(95)00306-Q }}</ref><ref name="pmid10393441">{{cite journal | vauthors = van den Maagdenberg AM, Schepens JT, Schepens MT, Merkx GF, Darroudi F, Wieringa B, Geurts van Kessel A, Hendriks WJ | title = Assignment1 of the PTP-SL/PTPBR7 gene (Ptprr/PTPRR) to mouse chromosome region 8A2 by in situ hybridization | journal = Cytogenet Cell Genet | volume = 84 | issue = 3-4 | pages = 243–4 | date = Jul 1999 | pmid = 10393441 | pmc = | doi = 10.1159/000015268 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PTPRR protein tyrosine phosphatase, receptor type, R| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5801| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_PTPRR_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1jln.
| PDB = {{PDB2|1jln}}, {{PDB2|2a8b}}
| Name = Protein tyrosine phosphatase, receptor type, R
| HGNCid = 9680
| Symbol = PTPRR
| AltSymbols =; DKFZp781C1038; EC-PTP; FLJ34328; MGC131968; MGC148170; PCPTP1; PTP-SL; PTPBR7; PTPRQ
| OMIM = 602853
| ECnumber = 
| Homologene = 2135
| MGIid = 109559
| GeneAtlas_image1 = PBB_GE_PTPRR_210675_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PTPRR_206084_at_tn.png
| Function = {{GNF_GO|id=GO:0004725 |text = protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005001 |text = transmembrane receptor protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0019901 |text = protein kinase binding}}
| Component = {{GNF_GO|id=GO:0009986 |text = cell surface}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0001701 |text = in utero embryonic development}} {{GNF_GO|id=GO:0006470 |text = protein amino acid dephosphorylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5801
    | Hs_Ensembl = ENSG00000153233
    | Hs_RefseqProtein = NP_002840
    | Hs_RefseqmRNA = NM_002849
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 69318129
    | Hs_GenLoc_end = 69600853
    | Hs_Uniprot = Q15256
    | Mm_EntrezGene = 19279
    | Mm_Ensembl = ENSMUSG00000020151
    | Mm_RefseqmRNA = NM_011217
    | Mm_RefseqProtein = NP_035347
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 115422509
    | Mm_GenLoc_end = 115679039
    | Mm_Uniprot = Q5U1U5
  }}
}}
'''Protein tyrosine phosphatase, receptor type, R''', also known as '''PTPRR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTPRR protein tyrosine phosphatase, receptor type, R| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5801| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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 a single intracellular catalytic domains, and thus represents a receptor-type PTP. The similar gene predominately expressed in mouse brain was found to associate with, and thus regulate the activity and cellular localization of MAP kinases. The rat counterpart of this gene was reported to be regulated by the nerve growth factor, which suggested the function of this gene in neuronal growth and differentiation.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = 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 a single intracellular catalytic domains, and thus represents a receptor-type PTP. The similar gene predominately expressed in mouse brain was found to associate with, and thus regulate the activity and cellular localization of MAP kinases. The rat counterpart of this gene was reported to be regulated by the nerve growth factor, which suggested the function of this gene in neuronal growth and differentiation.<ref name="entrez">{{cite web | title = Entrez Gene: PTPRR protein tyrosine phosphatase, receptor type, R| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5801| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
PTPRR has been shown to [[Protein-protein interaction|interact]] with [[MAPK7]].<ref name=pmid12042304>{{cite journal | vauthors = Buschbeck M, Eickhoff J, Sommer MN, Ullrich A | title = Phosphotyrosine-specific phosphatase PTP-SL regulates the ERK5 signaling pathway | journal = J. Biol. Chem. | volume = 277 | issue = 33 | pages = 29503–9 | date = Aug 2002 | pmid = 12042304 | doi = 10.1074/jbc.M202149200 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Sharma E, Lombroso PJ | title = A neuronal protein tyrosine phosphatase induced by nerve growth factor. | journal = J. Biol. Chem. | volume = 270 | issue = 1 | pages = 49–53 | year = 1995 | pmid = 7814416 | doi = 10.1074/jbc.270.1.49 }}
| citations =
* {{cite journal | vauthors = Ogata M, Sawada M, Fujino Y, Hamaoka T | title = cDNA cloning and characterization of a novel receptor-type protein tyrosine phosphatase expressed predominantly in the brain. | journal = J. Biol. Chem. | volume = 270 | issue = 5 | pages = 2337–43 | year = 1995 | pmid = 7836467 | doi = 10.1074/jbc.270.5.2337 }}
*{{cite journal  | author=Shiozuka K, Watanabe Y, Ikeda T, ''et al.'' |title=Cloning and expression of PCPTP1 encoding protein tyrosine phosphatase. |journal=Gene |volume=162 |issue= 2 |pages= 279-84 |year= 1995 |pmid= 7557444 |doi=  }}
* {{cite journal | vauthors = Pulido R, Zúñiga A, Ullrich A | title = PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif. | journal = EMBO J. | volume = 17 | issue = 24 | pages = 7337–50 | year = 1999 | pmid = 9857190 | pmc = 1171079 | doi = 10.1093/emboj/17.24.7337 }}
*{{cite journal | author=Sharma E, Lombroso PJ |title=A neuronal protein tyrosine phosphatase induced by nerve growth factor. |journal=J. Biol. Chem. |volume=270 |issue= 1 |pages= 49-53 |year= 1995 |pmid= 7814416 |doi= }}
* {{cite journal | vauthors = Ogata M, Oh-hora M, Kosugi A, Hamaoka T | title = Inactivation of mitogen-activated protein kinases by a mammalian tyrosine-specific phosphatase, PTPBR7. | journal = Biochem. Biophys. Res. Commun. | volume = 256 | issue = 1 | pages = 52–6 | year = 1999 | pmid = 10066421 | doi = 10.1006/bbrc.1999.0278 }}
*{{cite journal | author=Ogata M, Sawada M, Fujino Y, Hamaoka T |title=cDNA cloning and characterization of a novel receptor-type protein tyrosine phosphatase expressed predominantly in the brain. |journal=J. Biol. Chem. |volume=270 |issue= 5 |pages= 2337-43 |year= 1995 |pmid= 7836467 |doi= }}
* {{cite journal | vauthors = Zúñiga A, Torres J, Ubeda J, Pulido R | title = Interaction of mitogen-activated protein kinases with the kinase interaction motif of the tyrosine phosphatase PTP-SL provides substrate specificity and retains ERK2 in the cytoplasm. | journal = J. Biol. Chem. | volume = 274 | issue = 31 | pages = 21900–7 | year = 1999 | pmid = 10419510 | doi = 10.1074/jbc.274.31.21900 }}
*{{cite journal | author=Pulido R, Zúñiga A, Ullrich A |title=PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif. |journal=EMBO J. |volume=17 |issue= 24 |pages= 7337-50 |year= 1999 |pmid= 9857190 |doi= 10.1093/emboj/17.24.7337 }}
* {{cite journal | vauthors = Blanco-Aparicio C, Torres J, Pulido R | title = A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase. | journal = J. Cell Biol. | volume = 147 | issue = 6 | pages = 1129–36 | year = 2000 | pmid = 10601328 | pmc = 2168101 | doi = 10.1083/jcb.147.6.1129 }}
*{{cite journal | author=Ogata M, Oh-hora M, Kosugi A, Hamaoka T |title=Inactivation of mitogen-activated protein kinases by a mammalian tyrosine-specific phosphatase, PTPBR7. |journal=Biochem. Biophys. Res. Commun. |volume=256 |issue= 1 |pages= 52-6 |year= 1999 |pmid= 10066421 |doi= 10.1006/bbrc.1999.0278 }}
* {{cite journal | vauthors = Augustine KA, Silbiger SM, Bucay N, Ulias L, Boynton A, Trebasky LD, Medlock ES | title = Protein tyrosine phosphatase (PC12, Br7,S1) family: expression characterization in the adult human and mouse. | journal = Anat. Rec. | volume = 258 | issue = 3 | pages = 221–34 | year = 2000 | pmid = 10705342 | doi = 10.1002/(SICI)1097-0185(20000301)258:3<221::AID-AR1>3.0.CO;2-W }}
*{{cite journal | author=van den Maagdenberg AM, Schepens JT, Schepens MT, ''et al.'' |title=Assignment1 of the PTP-SL/PTPBR7 gene (Ptprr/PTPRR) to mouse chromosome region 8A2 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=84 |issue= 3-4 |pages= 243-4 |year= 1999 |pmid= 10393441 |doi=  }}
* {{cite journal | vauthors = Bektas A, Hughes JN, Warram JH, Krolewski AS, Doria A | title = Type 2 diabetes locus on 12q15. Further mapping and mutation screening of two candidate genes. | journal = Diabetes | volume = 50 | issue = 1 | pages = 204–8 | year = 2001 | pmid = 11147789 | doi = 10.2337/diabetes.50.1.204 }}
*{{cite journal  | author=Zúñiga A, Torres J, Ubeda J, Pulido R |title=Interaction of mitogen-activated protein kinases with the kinase interaction motif of the tyrosine phosphatase PTP-SL provides substrate specificity and retains ERK2 in the cytoplasm. |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21900-7 |year= 1999 |pmid= 10419510 |doi= }}
* {{cite journal | vauthors = Szedlacsek SE, Aricescu AR, Fulga TA, Renault L, Scheidig AJ | title = Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for MAP kinase regulation. | journal = J. Mol. Biol. | volume = 311 | issue = 3 | pages = 557–68 | year = 2001 | pmid = 11493009 | doi = 10.1006/jmbi.2001.4890 }}
*{{cite journal | author=Blanco-Aparicio C, Torres J, Pulido R |title=A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase. |journal=J. Cell Biol. |volume=147 |issue= 6 |pages= 1129-36 |year= 2000 |pmid= 10601328 |doi= }}
* {{cite journal | vauthors = Buschbeck M, Eickhoff J, Sommer MN, Ullrich A | title = Phosphotyrosine-specific phosphatase PTP-SL regulates the ERK5 signaling pathway. | journal = J. Biol. Chem. | volume = 277 | issue = 33 | pages = 29503–9 | year = 2002 | pmid = 12042304 | doi = 10.1074/jbc.M202149200 }}
*{{cite journal | author=Augustine KA, Silbiger SM, Bucay N, ''et al.'' |title=Protein tyrosine phosphatase (PC12, Br7,S1) family: expression characterization in the adult human and mouse. |journal=Anat. Rec. |volume=258 |issue= 3 |pages= 221-34 |year= 2000 |pmid= 10705342 |doi= }}
* {{cite journal | vauthors = Shin BK, Wang H, Yim AM, Le Naour F, Brichory F, Jang JH, Zhao R, Puravs E, Tra J, Michael CW, Misek DE, Hanash SM | title = Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function. | journal = J. Biol. Chem. | volume = 278 | issue = 9 | pages = 7607–16 | year = 2003 | pmid = 12493773 | doi = 10.1074/jbc.M210455200 }}
*{{cite journal | author=Bektas A, Hughes JN, Warram JH, ''et al.'' |title=Type 2 diabetes locus on 12q15. Further mapping and mutation screening of two candidate genes. |journal=Diabetes |volume=50 |issue= 1 |pages= 204-8 |year= 2001 |pmid= 11147789 |doi= }}
* {{cite journal | vauthors = Tárrega C, Ríos P, Cejudo-Marín R, Blanco-Aparicio C, van den Berk L, Schepens J, Hendriks W, Tabernero L, Pulido R | title = ERK2 shows a restrictive and locally selective mechanism of recognition by its tyrosine phosphatase inactivators not shared by its activator MEK1. | journal = J. Biol. Chem. | volume = 280 | issue = 45 | pages = 37885–94 | year = 2006 | pmid = 16148006 | doi = 10.1074/jbc.M504366200 }}
*{{cite journal | author=Szedlacsek SE, Aricescu AR, Fulga TA, ''et al.'' |title=Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for MAP kinase regulation. |journal=J. Mol. Biol. |volume=311 |issue= 3 |pages= 557-68 |year= 2001 |pmid= 11493009 |doi= 10.1006/jmbi.2001.4890 }}
* {{cite journal | vauthors = Eswaran J, von Kries JP, Marsden B, Longman E, Debreczeni JE, Ugochukwu E, Turnbull A, Lee WH, Knapp S, Barr AJ | title = Crystal structures and inhibitor identification for PTPN5, PTPRR and PTPN7: a family of human MAPK-specific protein tyrosine phosphatases. | journal = Biochem. J. | volume = 395 | issue = 3 | pages = 483–91 | year = 2006 | pmid = 16441242 | pmc = 1462698 | doi = 10.1042/BJ20051931 }}
*{{cite journal | author=Buschbeck M, Eickhoff J, Sommer MN, Ullrich A |title=Phosphotyrosine-specific phosphatase PTP-SL regulates the ERK5 signaling pathway. |journal=J. Biol. Chem. |volume=277 |issue= 33 |pages= 29503-9 |year= 2002 |pmid= 12042304 |doi= 10.1074/jbc.M202149200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Shin BK, Wang H, Yim AM, ''et al.'' |title=Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function. |journal=J. Biol. Chem. |volume=278 |issue= 9 |pages= 7607-16 |year= 2003 |pmid= 12493773 |doi= 10.1074/jbc.M210455200 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Tárrega C, Ríos P, Cejudo-Marín R, ''et al.'' |title=ERK2 shows a restrictive and locally selective mechanism of recognition by its tyrosine phosphatase inactivators not shared by its activator MEK1. |journal=J. Biol. Chem. |volume=280 |issue= 45 |pages= 37885-94 |year= 2006 |pmid= 16148006 |doi= 10.1074/jbc.M504366200 }}
*{{cite journal | author=Eswaran J, von Kries JP, Marsden B, ''et al.'' |title=Crystal structures and inhibitor identification for PTPN5, PTPRR and PTPN7: a family of human MAPK-specific protein tyrosine phosphatases. |journal=Biochem. J. |volume=395 |issue= 3 |pages= 483-91 |year= 2006 |pmid= 16441242 |doi= 10.1042/BJ20051931 }}
*{{cite journal  | author=Scherer SE, Muzny DM, Buhay CJ, ''et al.'' |title=The finished DNA sequence of human chromosome 12. |journal=Nature |volume=440 |issue= 7082 |pages= 346-51 |year= 2006 |pmid= 16541075 |doi= 10.1038/nature04569 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=5801}}
{{WikiDoc Sources}}
 
{{Protein tyrosine phosphatases}}
 
 
{{gene-12-stub}}

Latest revision as of 18:59, 7 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

n/a

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RefSeq (mRNA)

n/a

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RefSeq (protein)

n/a

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Protein tyrosine phosphatase receptor-type R is an enzyme that in humans is encoded by the PTPRR gene.[1][2][3]

Function

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 a single intracellular catalytic domains, and thus represents a receptor-type PTP. The similar gene predominately expressed in mouse brain was found to associate with, and thus regulate the activity and cellular localization of MAP kinases. The rat counterpart of this gene was reported to be regulated by the nerve growth factor, which suggested the function of this gene in neuronal growth and differentiation.[3]

Interactions

PTPRR has been shown to interact with MAPK7.[4]

References

  1. ↑ Shiozuka K, Watanabe Y, Ikeda T, Hashimoto S, Kawashima H (Nov 1995). "Cloning and expression of PCPTP1 encoding protein tyrosine phosphatase". Gene. 162 (2): 279–84. doi:10.1016/0378-1119(95)00306-Q. PMID 7557444.
  2. ↑ van den Maagdenberg AM, Schepens JT, Schepens MT, Merkx GF, Darroudi F, Wieringa B, Geurts van Kessel A, Hendriks WJ (Jul 1999). "Assignment1 of the PTP-SL/PTPBR7 gene (Ptprr/PTPRR) to mouse chromosome region 8A2 by in situ hybridization". Cytogenet Cell Genet. 84 (3–4): 243–4. doi:10.1159/000015268. PMID 10393441.
  3. ↑ 3.0 3.1 "Entrez Gene: PTPRR protein tyrosine phosphatase, receptor type, R".
  4. ↑ Buschbeck M, Eickhoff J, Sommer MN, Ullrich A (Aug 2002). "Phosphotyrosine-specific phosphatase PTP-SL regulates the ERK5 signaling pathway". J. Biol. Chem. 277 (33): 29503–9. doi:10.1074/jbc.M202149200. PMID 12042304.

Further reading


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