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0PPP5_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePPP5C
DescriptionSerine/threonine protein phosphatase 5 (ec 3.1.3.16) (pp5) (protein phosphatase t) (pp-t) (ppt).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005634 nucleus (TAS)
0004722 protein serine/threonine phosphatase activity (TAS)
0004871 signal transducer activity (IMP)
0007067 mitosis (TAS)
0043123 positive regulation of I-kappaB kinase/NF-k... (IMP)
0006470 protein amino acid dephosphorylation (TAS)
0006350 transcription (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This domain is specific to the PPP5 subfamily of serine/threonine phosphatases.
  IPR013235:Serine/threonine phosphatase, PPP5
Protein phosphorylation plays a central role in the regulation of cell functions .ausing the activation or inhibition of many enzymes involved in various biochemical pathways . Kinases and phosphatases are the enzymes responsible for this.nd may themselves be subject to control through the action of hormones and growth factors . Serine/threonine (S/T) phosphatases catalyse the dephosphorylation of phosphoserine and phosphothreonine residues. In mammalian tissues four different types of PP have been identified and are known as PP1.P2A.P2B and PP2C. Except for PP2C.hese enzymes are evolutionary related. The catalytic regions of the proteins are well conserved and have a slow mutation rate.uggesting that major changes in these regions are highly detrimental . The metallo-phosphoesterase motif is found in a large number of proteins invoved in phosphoryation. These include serine/threonine phosphatases.NA polymerase.xonucleases.nd other phosphatases.
  IPR004843:Metallophosphoesterase
The tetratrico peptide repeat (TPR) is a structural motif present in a wide range of proteins . It mediates proteinprotein interactions and the assembly of multiprotein complexes . The TPR motif consists of 316 tandem-repeats of 34 amino acids residues.lthough individual TPR motifs can be dispersed in the protein sequence. Sequence alignment of the TPR domains reveals a consensus sequence defined by a pattern of small and large amino acids. TPR motifs have been identified in various different organisms.anging from bacteria to humans. Proteins containing TPRs are involved in a variety of biological processes.uch as cell cycle regulation.ranscriptional control.itochondrial and peroxisomal protein transport.eurogenesis and protein folding. The X-ray structure of a domain containing three TPRs from protein phosphatase 5 revealed that TPR adopts a helixturnhelix arrangement.ith adjacent TPR motifs packing in a parallel fashion.esulting in a spiral of repeating anti-parallel alpha-helices . The two helices are denoted helix A and helix B. The packing angle between helix A and helix B is ~24° within a single TPR and generates a right-handed superhelical shape. Helix A interacts with helix B and with helix A of the next TPR. Two protein surfaces are generated: the inner concave surface is contributed to mainly by residue on helices A.nd the other surface presents residues from both helices A and B.
  IPR001440:Tetratricopeptide TPR_1
The tetratrico peptide repeat region (TPR) is a structural motif present in a wide range of proteins . It mediates proteinprotein interactions and the assembly of multiprotein complexes . The TPR motif consists of 316 tandem-repeats of 34 amino acids residues.lthough individual TPR motifs can be dispersed in the protein sequence. Sequence alignment of the TPR domains reveals a consensus sequence defined by a pattern of small and large amino acids. TPR motifs have been identified in various different organisms.anging from bacteria to humans. Proteins containing TPRs are involved in a variety of biological processes.uch as cell cycle regulation.ranscriptional control.itochondrial and peroxisomal protein transport.eurogenesis and protein folding. The X-ray structure of a domain containing three TPRs from protein phosphatase 5 revealed that TPR adopts a helixturnhelix arrangement.ith adjacent TPR motifs packing in a parallel fashion.esulting in a spiral of repeating anti-parallel alpha-helices . The two helices are denoted helix A and helix B. The packing angle between helix A and helix B is ~24° within a single TPR and generates a right-handed superhelical shape. Helix A interacts with helix B and with helix A of the next TPR. Two protein surfaces are generated: the inner concave surface is contributed to mainly by residue on helices A.nd the other surface presents residues from both helices A and B.
  IPR013026:Tetratricopeptide region
Protein phosphorylation plays a central role in the regulation of cell functions .ausing the activation or inhibition of many enzymes involved in various biochemical pathways . Kinases and phosphatases are the enzymes responsible for this.nd may themselves be subject to control through the action of hormones and growth factors . Serine/threonine(S/T) phosphatases () catalyse the dephosphorylation of phosphoserine and phosphothreonine residues. In mammalian tissues four different types of PP have been identified and are known as PP1.P2A.P2B and PP2C. Except for PP2C.hese enzymes are evolutionary related. The catalytic regions of the proteins arewell conserved and have a slow mutation rate.uggesting that major changes in these regions are highly detrimental . Protein phosphatase-1 (PP1) and protein phosphatase-2A (PP2A) have a broad specificity and there are two closely related isoforms of each.lpha and beta. PP2A is a trimeric enzyme that consists of a core composed of a catalytic subunit associated with a 65 kDa regulatory subunit and a third variable subunit. Protein phosphatase-2B (PP2B or calcineurin). calcium-dependent enzyme whose activity is stimulated by calmodulin.s composed of two subunits the catalytic A-subunit and the calcium-binding B-subunit. The specificity of PP2B is restricted. Other serine/threonine specific protein phosphatases that have been characterized include mammalian phosphatase-X (PP-X).nd Drosophila phosphatase-V (PP-V).hich are closely related but yet distinct from PP2A; yeast phosphatase PPH3.hich is similar to PP2A.ut with different enzymatic properties; and Drosophila phosphatase-Y (PP-Y).nd yeastphosphatases Z1 and Z2 which are closely related but yet distinct from PP1.
  IPR006186:Serine/threonine-specific protein phosphatase and bis(5-nucleosyl)-tetraphosphatase
These eukaryotic serine/threonine phosphoprotein phosphatases.irst described from human (PP5) and Saccharomyces cerevisiae (PPT1).re distinguished from related protein phosphatases by anN-terminal region of about 200 residues that contains three tandem tetratricopeptide repeats (TPR) . Structurally.PR repeats form a helical scaffold of antiparallel alpha-helices with anamphipathic groove that mediates protein-protein interactions . The TPR domainscontribute to regulation of PP5 activity.hich is normally low but stimulated by interaction with lipid .nd to interaction with other proteins .
  IPR011236:Protein phosphatase 5
This domain consists of a multi-helical fold comprised of two curved layers of alpha helices arranged in a regular right-handed superhelix.here the repeats that make up this structure are arranged about a common axis . These superhelical structures present an extensive solvent-accessible surface that is well suited to binding large substrates such as proteins and nucleic acids. This topology has been found with a number of repeats and domains.ncluding the tetratricopeptide repeat (TPR) (found in kinesin light chains.NAP regulatory proteins.lathrin heavy chains and bacterial aspartyl-phosphate phosphatases).nd the pentatricopeptide repeat (PPR) (RNA-processing proteins). The TRP is likely to be an ancient repeat.ince it is found in eukaryotes.acteria and archaea.hereas the PPR repeat is found predominantly in higher plants. The superhelix formed from these repeats can bind ligands at a number of different regions.nd has the ability to acquire multiple functional roles .
  IPR011990:Tetratricopeptide-like helical
IPR006186:PP2Ac 
Evalue:-164.721246399047 
Location:204-480IPR001440:TPR_1 
Evalue:-7.63827228546143 
Location:28-61IPR001440:TPR_1 
Evalue:-4.88605642318726 
Location:96-129IPR001440:TPR_1 
Evalue:-0.958607316017151 
Location:62-95
SequencesProtein: PPP5_HUMAN (499 aa)
mRNA: NM_006247
Local Annotation
Synapse Ontology
A process that increases short-term neuronal synaptic plasticity, the ability of neuronal synapses to change in the short-term as circumstances require. Short-term neuronal synaptic plasticity generally involves increasing or decreasing synaptic sensitivity.
sdb:0043 positive regulation of short-term neuronal synaptic plasticity  (Evidence:keywords)
KO assignmentK04460
  Level 3 annotation:
    protein phosphatase 5
  Level 2 annotation:
    MAPK signaling pathway
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 61 residues, 51542133-51542314Exon2: 82 residues, 51548844-51549086Exon3: 51 residues, 51570700-51570848Exon4: 42 residues, 51571549-51571671Exon5: 24 residues, 51578507-51578573Exon6: 35 residues, 51578876-51578975Exon7: 37 residues, 51579900-51580006Exon8: 49 residues, 51582189-51582332Exon9: 31 residues, 51582462-51582550Exon10: 15 residues, 51583504-51583545Exon11: 61 residues, 51583649-51583828Exon12: 29 residues, 51585147-51585229Exon13: 189 residues, 51585380-51585943Exon14: 2 residues, -Jump to PPP5_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3116 50100878-50104489 ~-4K 19057(APOE)(+)Loci: 3117 50234137-50266053 ~-32K 19065(SFRS16)(+)Loci: 4398 50407718-50429309 ~-22K 19076(-)Loci: 3118 50446389-50500381 ~-54K 19078(MARK4)(+)Loci: 4399 50546685-50565669 ~-19K 19089(ERCC2)(-)Loci: 4400 50747641-50779917 ~-32K 19109(OPA3)(-)Loci: 4401 50804499-50834509 ~-30K 19111(EML2)(-)Loci: 3119 50863341-50877557 ~-14K 19113(GIPR)(+)Loci: 4402 51134630-51168497 ~-34K 19134(NOVA2)(-)Loci: 3120 51542133-51585943 ~-44K 19149(PPP5C)(+)Loci: 3121 51796351-51805878 ~-10K 19157(CALM1)(+)Loci: 4403 51869413-51911506 ~-42K 19161(PRKD2)(-)Loci: 4404 52033262-52046043 ~-13K 19167(AP2S1)(-)Loci: 3115 50004177-50016517 ~-12K 19053(LU)(+)Link out to UCSC