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PTPRR protein, human

Known as: Protein Tyrosine Phosphatase Cr1PTPase, NC-PTPCOM1, Protein Tyrosine Phosphatase Receptor Type R 
Receptor-type tyrosine-protein phosphatase R (657 aa, ~74 kDa) is encoded by the human PTPRR gene. This protein is involved in both protein… Expand
National Institutes of Health

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14 relations
DephosphorylationEnzyme GeneEsterase GeneHydrolase
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Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2006
2006
Altered MAP kinase phosphorylation and impaired motor coordination in PTPRR deficient mice.
The neuronal protein tyrosine phosphatases encoded by mouse gene Ptprr (PTPBR7, PTP-SL, PTPPBSgamma-42 and PTPPBSgamma-37) have… Expand
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2006
2006
Crystal structures and inhibitor identification for PTPN5, PTPRR and PTPN7: a family of human MAPK-specific protein tyrosine phosphatases.
Protein tyrosine phosphatases PTPN5, PTPRR and PTPN7 comprise a family of phosphatases that specifically inactivate MAPKs… Expand
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2005
2005
ERK2 Shows a Restrictive and Locally Selective Mechanism of Recognition by Its Tyrosine Phosphatase Inactivators Not Shared by Its Activator MEK1*
The two regulatory residues that control the enzymatic activity of the mitogen-activated protein (MAP) kinase ERK2 are… Expand
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2002
2002
Phosphotyrosine-specific Phosphatase PTP-SL Regulates the ERK5 Signaling Pathway*
The duration and the magnitude of mitogen-activated protein kinase (MAPK) activation specifies signal identity and thus allows… Expand
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2002
2002
Two Clusters of Residues at the Docking Groove of Mitogen-activated Protein Kinases Differentially Mediate Their Functional Interaction with the Tyrosine Phosphatases PTP-SL and STEP*
Regulated function of mitogen-activated protein (MAP) kinases involves their selective association through docking sites with… Expand
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2001
2001
Altered Regulation of ERK1b by MEK1 and PTP-SL and Modified Elk1 Phosphorylation by ERK1b Are Caused by Abrogation of the Regulatory C-terminal Sequence of ERKs*
ERK1b is an alternatively spliced form of ERK1, containing a 26-amino acid insertion between residues 340 and 341 of ERK1… Expand
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2001
2001
Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for MAP kinase regulation.
Protein tyrosine phosphatases PTP-SL and PTPBR7 are isoforms belonging to cytosolic membrane-associated and to receptor-like PTPs… Expand
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1999
1999
The mouse Ptprr gene encodes two protein tyrosine phosphatases, PTP-SL and PTPBR7, that display distinct patterns of expression during neural development.
The protein tyrosine phosphatases PTP-SL and PTPBR7 differ only in the length of their N-terminal domain. We show here that PTP… Expand
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Highly Cited
1999
Highly Cited
1999
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*
ERK1 and ERK2 associate with the tyrosine phosphatase PTP-SL through a kinase interaction motif (KIM) located in the… Expand
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Highly Cited
1998
Highly Cited
1998
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.
Protein kinases and phosphatases regulate the activity of extracellular signal-regulated kinases 1 and 2 (ERK1/2) by controlling… Expand
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