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Human Phosphatases
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Statistics

241 human active and 13 inactive phosphatases in total;
194 phosphatases have substrate data;
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336 protein substrates;
83 non-protein substrates;
1215 dephosphorylation interactions;
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299 KEGG pathways;
876 Reactome pathways;
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last scientific update:
11 Mar, 2019

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INPP5B

Basic Information
Substrates
Pathway
Interacting Proteins
Phosphorylating Kinases

Gene Name	INPP5B (QuickGO)	Interactive visualization of INPP5B structures (A quick tutorial to explore the interactive visualization)
Synonyms	INPP5B, OCRL2
Protein Name	INPP5B
Alternative Name(s)	Type II inositol 1,4,5-trisphosphate 5-phosphatase;3.1.3.36;75 kDa inositol polyphosphate-5-phosphatase;Phosphoinositide 5-phosphatase;5PTase;
EntrezGene ID	3633 (Comparative Toxicogenomics)
UniProt AC (Human)	P32019 (protein sequence)
Enzyme Class	EC 3.1.3.36 (BRENDA )
Molecular Weight	112852 Dalton
Protein Length	993 amino acids (AA)
Genome Browsers	NCBI \| ENSG00000204084 (Ensembl) \| UCSC
Crosslinking annotations	Query our ID-mapping table
Orthologues	Quest For Orthologues (QFO) \| GeneTree
Classification	Superfamily: inositol-5-phosphatases (IP) \| Historic class: Inositol-1,4,5-trisphosphate 5-phosphatase \| CATH ID: 3.60.10.10 \| SCOP Fold: DNase I
Phosphatase activity	active \| Catalytic signature motif: unknown
Phosphorylation Network	Visualize

Domain organization, Expression, Diseases

Localization, Function, Catalytic activity and Sequence

Motif information from Eukaryotic Linear Motif atlas (ELM)

Gene Ontology (P: Process; F: Function and C: Component terms)

KEGG Pathway
Reactome Pathway

Pathway ID	Pathway Name	Pathway Description (Reactome)
R-HSA-1855183	Synthesis of IP2, IP, and Ins in the cytosol.	Inositol phosphates IP2, IP and the six-carbon cyclic alcohol inositol (Ins) are produced by various phosphatases and the inositol-3-phosphate synthase 1 (ISYNA1) (Ju et al. 2004, Ohnishi et al. 2007, Irvine & Schell 2001, Bunney & Katan 2010)
R-HSA-1855204	Synthesis of IP3 and IP4 in the cytosol.	An array of inositol trisphosphate (IP3) and tetrakisphosphate (IP4) molecules are synthesised by the action of various kinases and phosphatases in the cytosol (Irvine & Schell 2001, Bunney & Katan 2010)
R-HSA-194840	Rho GTPase cycle.	The cycling of Rho GTPases is tightly controlled by three classes of protein. These are (1) guanine nucleotide dissociation inhibitors or GDIs, which maintain Rho proteins in an inactive state in the cytoplasm, (2) guanine nucleotide exchange factors or GEFs, which destabilize the interaction between Rho proteins and their bound nucleotide, the net result of which is the exchange of bound GDP for the more abundant GTP, and (3) GTPase Activating Proteins or GAPs, which stimulate the low intrinsic GTP hydrolysis activity of Rho family members, thus promoting their inactivation. GDIs, GEFs, and GAPs are themselves subject to tight regulation, and the overall level of Rho activity reflects the balance of their activities.<p>In their active GTP-bound state, Rho family members have the ability to interact with a large variety of so-called effector proteins. By changing the subcellular localization of effectors, by altering their enzymatic properties, or by directing the formation of specific effector complexes, members of the Rho family mediate their various effects.<p>This Rho GTPase cycle is diagrammed in the figure below. External or internal cues promote the release of Rho GTPases from the inhibitory complex (1) which allows them to associate with the plasma membrane (2) where they are activated by GEFs (3) and can signal to effector proteins. Then, GAPs inactivate the GTPases by accelerating the intrinsic GTPase activity, leading to the GDP bound form (4). Once again, the GDI molecules stabilize the inactive GDP bound form in the cytoplasm, waiting for further instructions (5). (Figure and text from Tcherkezian and Lamarche Vane, 2007)