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0PTN1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePTPN1
DescriptionTyrosine-protein phosphatase, non-receptor type 1 (ec 3.1.3.48) (protein-tyrosine phosphatase 1b) (ptp-1b).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0004725 protein tyrosine phosphatase activity (TAS)
0007165 signal transduction (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:
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
The von Willebrand factor is a large multimeric glycoprotein found in bloodplasma. Mutant forms are involved in the aetiology of bleeding disorders . In von Willebrand factor.he type A domain (vWF) is the prototype fora protein superfamily. The vWF domain is found in various plasma proteins:complement factors B.2.R3 and CR4; the integrins (I-domains); collagen types VI.II.II and XIV; and other extracellular proteins . Although the majority of VWA-containing proteins are extracellular.he most ancient ones present in all eukaryotes are all intracellular proteins involved in functions such as transcription.NA repair.ibosomal and membrane transport and the proteasome. A common feature appears to be involvement in multiprotein complexes. Proteinsthat incorporate vWF domains participate in numerous biological events(e.g. cell adhesion.igration.oming.attern formation.nd signaltransduction).nvolving interaction with a large array of ligands . A number of human diseases arise from mutations in VWA domains. Secondary structure prediction from 75 aligned vWF sequences has revealed a largely alternating sequence of alpha-helices and beta-strands . Foldrecognition algorithms were used to score sequence compatibility with alibrary of known structures: the vWF domain fold was predicted to be adoubly-wound.pen.wisted beta-sheet flanked by alpha-helices . 3D structures have been determined for the I-domains of integrins CD11b(with bound magnesium) and CD11a (with bound manganese) . The domain adopts a classic alpha/beta Rossmann fold and contains an unusual metal ion coordination site at its surface. It has been suggested that this siterepresents a general metal ion-dependent adhesion site (MIDAS) for binding protein ligands . The residues constituting the MIDAS motif in the CD11band CD11a I-domains are completely conserved.ut the manner in which the metal ion is coordinated differs slightly .
  IPR002035:von Willebrand factor, type A
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:PTPc 
Evalue:-124.677780705266 
Location:15-279IPR002035:VWFADOMAIN 
Evalue:0 
Location:415-423
SequencesProtein: PTN1_HUMAN (435 aa)
mRNA: NM_002827
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 assignmentK05696
  Level 3 annotation:
    protein tyrosine phosphatase, non-receptor type 1
  Level 2 annotation:
    Insulin signaling pathway
    Adherens junction
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 80 residues, 48560297-48560534Exon2: 32 residues, 48611306-48611397Exon3: 35 residues, 48614912-48615013Exon4: 35 residues, 48618323-48618422Exon5: 48 residues, 48624460-48624598Exon6: 72 residues, 48628363-48628573Exon7: 56 residues, 48629111-48629273Exon8: 76 residues, 48629646-48629870Exon9: 67 residues, 48631208-48631404Exon10: 620 residues, 48632635-48634491Exon11: 2 residues, -Jump to PTN1_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3266 48781487-48803684 ~-22K 23338(PARD6B)(+)Loci: 4530 48940289-48980934 ~-41K 23342(ADNP)(-)Loci: 4531 49053600-49060282 ~-7K 23345(KCNG1)(-)Loci: 3265 48560297-48634491 ~-74K 23336(PTPN1)(+)Link out to UCSC