Q60676

SS
Gene name
Ppp5c
Protein name
Serine/threonine-protein phosphatase 5
Names
PP5, Protein phosphatase T, PPT
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:19060
EC number
3.1.3.16: Phosphoric monoester hydrolases
Protein Class

Descriptions

Protein phosphatase 5 (Ppp5) is a serine/threonine protein phosphatase comprising a regulatory tetratricopeptide repeat (TPR) domain N-terminal to its phosphatase domain. Ppp5 functions in signaling pathways that control cellular responses to stress, glucocorticoids and DNA damage. Its phosphatase activity is suppressed by an autoinhibited conformation maintained by the TPR domain and a C-terminal subdomain. The TPR domain engages with the catalytic channel of the phosphate domain, restricting access to the catalytic site. This autoinhibited conformation of Ppp5 is stabilized by the C-terminal αJ helix. In a study with rat PPP5C (P53042), the protein also contains a C-terminal regulatory region that may interact with the TPR domain. The autoinhibitory regions were inferred by sequence similarity with the human PPP5C (P53041) and rat PPP5C (P53042).

Autoinhibitory domains (AIDs)

28-129 (N-terminal tetratricopeptide repeat) SS

Target domain

204-480 (Phosphatase domain)

Relief mechanism

Cleavage, Ligand binding

Assay

495-499 (C-terminal autoinhibitory region) SS

Target domain

204-480 (Phosphatase domain)

Relief mechanism

Ligand binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q60676

Entry ID Method Resolution Chain Position Source
AF-Q60676-F1 Predicted AlphaFoldDB

2 variants for Q60676

Variant ID(s) Position Change Description Diseaes Association Provenance
rs262156459 14 T>P No Ensembl
rs13469893 24 T>A No Ensembl

No associated diseases with Q60676

2 regional properties for Q60676

Type Name Position InterPro Accession
domain MerR-type HTH domain 1 - 70 IPR000551
domain TipAS antibiotic-recognition domain 128 - 242 IPR012925

Functions

Description
EC Number 3.1.3.16 Phosphoric monoester hydrolases
Subcellular Localization
  • Nucleus
  • Cytoplasm
  • Cell membrane
  • Predominantly nuclear
  • But also present in the cytoplasm
  • Translocates from the cytoplasm to the plasma membrane in a RAC1-dependent manner
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

12 GO annotations of cellular component

Name Definition
cell periphery The part of a cell encompassing the cell cortex, the plasma membrane, and any external encapsulating structures.
chaperone complex A protein complex required for the non-covalent folding or unfolding, maturation, stabilization or assembly or disassembly of macromolecular structures. Usually active during or immediately after completion of translation. Many chaperone complexes contain heat shock proteins.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
intracellular membrane-bounded organelle Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
neuron projection A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
neuronal cell body The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
perikaryon The portion of the cell soma (neuronal cell body) that excludes the nucleus.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
protein-containing complex A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
proximal dendrite The dendrite of the dendritic tree that is closest to the neuronal cell body (the soma).

13 GO annotations of molecular function

Name Definition
ADP binding Binding to ADP, adenosine 5'-diphosphate.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
G-protein alpha-subunit binding Binding to a G-protein alpha subunit. The alpha subunit binds a guanine nucleotide.
heat shock protein binding Binding to a heat shock protein, a protein synthesized or activated in response to heat shock.
Hsp90 protein binding Binding to Hsp90 proteins, any of a group of heat shock proteins around 90kDa in size.
identical protein binding Binding to an identical protein or proteins.
metal ion binding Binding to a metal ion.
microtubule binding Binding to a microtubule, a filament composed of tubulin monomers.
phosphatase activity Catalysis of the hydrolysis of phosphoric monoesters, releasing inorganic phosphate.
phosphoprotein phosphatase activity Catalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cellular proteins and thereby provide an important mechanism for regulating cellular activity.
protein serine/threonine phosphatase activity Catalysis of the reaction: protein serine phosphate + H2O = protein serine + phosphate, and protein threonine phosphate + H2O = protein threonine + phosphate.
protein-containing complex binding Binding to a macromolecular complex.
RNA binding Binding to an RNA molecule or a portion thereof.

10 GO annotations of biological process

Name Definition
histone dephosphorylation OBSOLETE. The modification of histones by removal of phosphate groups.
negative regulation of cell death Any process that decreases the rate or frequency of cell death. Cell death is the specific activation or halting of processes within a cell so that its vital functions markedly cease, rather than simply deteriorating gradually over time, which culminates in cell death.
negative regulation of neuron death Any process that stops, prevents or reduces the frequency, rate or extent of neuron death.
negative regulation of protein phosphorylation Any process that stops, prevents or reduces the rate of addition of phosphate groups to amino acids within a protein.
peptidyl-serine dephosphorylation The removal of phosphoric residues from peptidyl-O-phospho-L-serine to form peptidyl-serine.
positive regulation of glucocorticoid receptor signaling pathway Any process that activates or increases the frequency, rate or extent of glucocorticoid receptor signaling pathway.
protein dephosphorylation The process of removing one or more phosphoric residues from a protein.
response to arachidonic acid Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an arachidonic acid stimulus.
response to lead ion Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lead ion stimulus.
response to morphine Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a morphine stimulus. Morphine is an opioid alkaloid, isolated from opium, with a complex ring structure.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P53043 PPT1 Serine/threonine-protein phosphatase T Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SS
P53041 PPP5C Serine/threonine-protein phosphatase 5 Homo sapiens (Human) EV
P53042 Ppp5c Serine/threonine-protein phosphatase 5 Rattus norvegicus (Rat) EV
Q9NES8 pph-5 Serine/threonine-protein phosphatase 5 Caenorhabditis elegans EV
Q84XU2 PAPP5 Serine/threonine-protein phosphatase 5 Arabidopsis thaliana (Mouse-ear cress) SS
Q84K11 PP5 Serine/threonine-protein phosphatase 5 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) PR
10 20 30 40 50 60
MAMAEGERTE CAETPRDEPP ADGTLKRAEE LKTQANDYFK AKDYENAIKF YSQAIELNPG
70 80 90 100 110 120
NAIYYGNRSL AYLRTECYGY ALGDATRAIE LDKKYIKGYY RRAASNMALG KFRAALRDYE
130 140 150 160 170 180
TVVKVKPNDK DAKMKYQECS KIVKQKAFER AIAGDEHRRS VVDSLDIESM TIEDEYSGPK
190 200 210 220 230 240
LEDGKVTITF MKDLMQWYKD QKKLHRKCAY QILVQVKEVL CKLSTLVETT LKETEKITVC
250 260 270 280 290 300
GDTHGQFYDL LNIFELNGLP SETNPYIFNG DFVDRGSFSV EVILTLFGFK LLYPDHFHLL
310 320 330 340 350 360
RGNHETDNMN QIYGFEGEVK AKYTAQMYEL FSEVFEWLPL AQCINGKVLI MHGGLFSEDG
370 380 390 400 410 420
VTLDDIRKIE RNRQPPDSGP MCDLLWSDPQ PQNGRSVSKR GVSCQFGPDV TKAFLEENQL
430 440 450 460 470 480
DYIIRSHEVK AEGYEVAHGG RCVTVFSAPN YCDQMGNKAS YIHLQGSDLR PQFHQFTAVP
490
HPNVKPMAYA NTLLQLGMM