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1Q96AU5_HUMAN*   Trembl (?) | Description Local Annotation Link Reference
General Information
NameN/A
DescriptionProtein tyrosine phosphatase, non-receptor type 2.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0016787 hydrolase activity (IEA)
0004725 protein tyrosine phosphatase activity (IEA)
0004872 receptor activity (IEA)
0006470 protein amino acid dephosphorylation (IEA)

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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:
Tyrosine specific protein phosphatases () (PTPase) areenzymes that catalyse the removal of a phosphate group attached to a tyrosineresidue.Protein tyrosine phosphate + H2O = protein tyrosine + PiThese enzymes are very important in the control of cell growth.roliferation.ifferentiation and transformation. Multiple forms of PTPasehave been characterised and can be classified into two categories: solublePTPases and transmembrane receptor proteins that contain PTPase domain(s).Structurally.ll known receptor PTPases.re made up of a variable lengthextracellular domain.ollowed by a transmembrane region and a C-terminalcatalytic cytoplasmic domain. Some of the receptor PTPases contain fibronectintype III (FN-III) repeats.mmunoglobulin-like domains.AM domains orcarbonic anhydrase-like domains in their extracellular region. The cytoplasmicregion generally contains two copies of the PTPase domain. The first seems tohave enzymatic activity.hile the second is inactive. The inactive domains of tandem phosphatases can be divided into two classes. Those which bind phosphorylated tyrosine residues may recruit multi-phosphorylated substrates for the adjacent active domains and are more conserved.hile the other class have accumulated several variable amino acid substitutions and have a complete loss of tyrosine binding capability. The second class shows a release of evolutionary constraint for the sites around the catalytic centre.hich emphasises a difference in function from the first group. There is a region of higher conservation common to both classes.uggesting a new regulatory centre.PTPase domains consist of about 300 amino acids. There are two conservedcysteines.he second one has been shown to be absolutely required foractivity. Furthermore. number of conserved residues in its immediatevicinity have also been shown to be important.
  IPR000242:Tyrosine specific protein phosphatase
Protein tyrosine phosphorylation is a common posttranslational modification which can create novel recognition motifs for protein interactions and cellular localisation.ffect protein stability.nd regulate enzyme activity. Consequently.aintaining an appropriate level of protein tyrosine phosphorylation is essential for many cellular functions. Tyrosine-specific protein phosphatases () (PTPase) catalyse the removal of a phosphate group attached to a tyrosine residue. Protein-tyrosine-phosphate + H2O = protein tyrosine + PiThese enzymes are very important in the control of cell growth.roliferation.ifferentiation and transformation. Multiple forms of PTPase have been characterised and can be classified into two categories: soluble non-receptor PTPases and transmembrane receptor proteins that contain PTPase domain(s).This entry represents non-receptor PTPase types 1 and 2 (also known as T-cell PTPase). These types appear to have different biological functions: in knock-out mice.ype1 knock-outs showed increased insulin sensitivity but a normal lifespan.hile type 2 knock-outs died when only a few weeks old . Substrate-trapping experiments suggest that these types recognise different cellular targets.hough it is not known if this is due to sequence differences or to other regulatory mechanisms. Regulation of function and activity can occur at the transcriptional.lternative splicing.roteolytic processing and covalent modification levels. For example.-cell PTPase has two different isoforms generated by alternative splicing.ne of which recognises nuclear substrates.hile the other recognises cytoplasmic substrates. These proteins adopt an alpha-beta-alpha fold where the active site is located in a deep cleft located on the surface of the protein .
  IPR012265:Protein-tyrosine phosphatase, non-receptor 1/2
IPR000242:Y_phosphatase 
Evalue:-117.69896697998 
Location:42-274
SequencesProtein: Q96AU5_HUMAN (353 aa)
mRNA: NM_080422 NM_080423
Local Annotation
Synapse Ontology
Various stages of the synaptic vesicle cycle, including attachment, prefusion, triggering, recycling and reloading of the vesicles with transmitter.
sdb:0098 synaptic vesicle cycling  (Evidence:keywords)
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
?
sdb:0328 transmitters release and endocytosis  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 122 residues, 12775480-12775843Exon2: 36 residues, 12784382-12784484Exon3: 62 residues, 12791968-12792150Exon4: 53 residues, 12804201-12804354Exon5: 72 residues, 12807154-12807364Exon6: 47 residues, 12815808-12815943Exon7: 35 residues, 12820941-12821040Exon8: 35 residues, 12826789-12826890Exon9: 32 residues, 12849162-12849253Exon10: 89 residues, 12874071-12874334Exon11: 2 residues, -Jump to Q96AU5_HUMANExon1: 120 residues, 12775486-12775843Exon2: 62 residues, 12791968-12792150Exon3: 53 residues, 12804201-12804354Exon4: 72 residues, 12807154-12807364Exon5: 47 residues, 12815808-12815943Exon6: 35 residues, 12820941-12821040Exon7: 35 residues, 12826789-12826890Exon8: 32 residues, 12849162-12849253Exon9: 89 residues, 12874071-12874334Exon10: 2 residues, -Jump to Q96AU5_HUMAN  
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