SynDB Home Page
SynDB Home Page

blue bulletSynDB protein details  

Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0PTPRB_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionReceptor-type tyrosine-protein phosphatase beta precursor (ec (protein-tyrosine phosphatase beta) (r-ptp-beta).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005887 integral to plasma membrane (TAS)
0005001 transmembrane receptor protein tyrosine pho... (TAS)
0006796 phosphate metabolism (TAS)
0006470 protein amino acid dephosphorylation (TAS)

Warning: fopen(/home/kongl/syndb/www/temp/ [function.fopen]: failed to open stream: Permission denied in /home/kongl/syndb/www/sdb_pro.php on line 269

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 270

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 271

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 272

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 273

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 274

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 299

Warning: fclose(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 300
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 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
Fibronectins are multi-domain glycoproteins found in a soluble form in plasma.nd in an insoluble form in loose connective tissue and basement membranes . They contain multiple copies of 3 repeat regions (types I.I and III).hich bind to a variety of substances including heparin.ollagen.NA.ctin.ibrin and fibronectin receptors on cell surfaces. The wide variety of these substances means that fibronectins are involved in a number of important functions: e.g..ound healing; cell adhesion; blood coagulation; cell differentiation and migration; maintenance of the cellular cytoskeleton; and tumour metastasis . The role of fibronectin in cell differentiation is demonstrated by the marked reduction in the expression of its gene when neoplastic transformation occurs. Cell attachment has been found to be mediated by the binding of the tetrapeptide RGDS to integrins on the cell surface .lthough related sequences can also display cell adhesion activity.Plasma fibronectin occurs as a dimer of 2 different subunits.inked together by 2 disulphide bonds near the C-terminus. The difference in the 2 chains occurs in the type III repeat region and is caused by alternative splicing of the mRNA from one gene . The observation that.n a given protein.n individual repeat of one of the 3 types (e.g..he first FnIII repeat) shows much less similarity to its subsequent tandem repeats within that protein than to its equivalent repeat between fibronectins from other suggested that the repeating structure of fibronectin arose at an early stage of evolution. It also seems to suggest that the structure is subject to high selective pressure .The fibronectin type III repeat region is an approximately 100 amino acid domain.ifferent tandem repeats of which contain binding sites for DNA.eparin and the cell surface . The superfamily of sequences believed to contain FnIII repeats represents 45 different families.he majority of which are involved in cell surface binding in some manner.r are receptor protein tyrosine kinases.r cytokine receptors.
  IPR003961:Fibronectin, type III
Fibronectin is composed of three repeating structural motifs.f which one is the FnIII module. The three modules form a linear sequence of multiple tandem copies connected by short linker peptides. The secondary structure of the FnIII10 module.hich is the only fibronectin module to possess an integrin binding RGD motif.onsists of two beta-sheets containing the antiparallel beta-strands ABE and DCFG.espectively.hich fold up to form a beta-sandwich. The RGD sequence is located in the loop connecting the beta-strands .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008957:Fibronectin, type III-like fold
SequencesProtein: PTPRB_HUMAN (1997 aa)
mRNA: NM_002837
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 assignmentK05694
  Level 3 annotation:
    protein tyrosine phosphatase, receptor type, B
  Level 2 annotation:
    Adherens junction
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 110 residues, 69201231-69201558Exon2: 42 residues, 69204517-69204638Exon3: 47 residues, 69212081-69212217Exon4: 56 residues, 69214534-69214698Exon5: 43 residues, 69214879-69215002Exon6: 47 residues, 69216071-69216206Exon7: 27 residues, 69218201-69218278Exon8: 32 residues, 69218970-69219061Exon9: 29 residues, 69219671-69219753Exon10: 8 residues, 69219873-69219891Exon11: 30 residues, 69219985-69220069Exon12: 35 residues, 69220904-69221004Exon13: 37 residues, 69224603-69224710Exon14: 83 residues, 69232823-69233067Exon15: 52 residues, 69235206-69235356Exon16: 95 residues, 69235916-69236195Exon17: 96 residues, 69239389-69239671Exon18: 90 residues, 69240717-69240981Exon19: 90 residues, 69242890-69243154Exon20: 92 residues, 69246481-69246751Exon21: 90 residues, 69249721-69249985Exon22: 90 residues, 69251072-69251336Exon23: 90 residues, 69251870-69252134Exon24: 90 residues, 69256428-69256692Exon25: 91 residues, 69261082-69261349Exon26: 89 residues, 69267053-69267314Exon27: 92 residues, 69270010-69270280Exon28: 90 residues, 69272328-69272592Exon29: 88 residues, 69274513-69274771Exon30: 95 residues, 69276095-69276374Exon31: 92 residues, 69289115-69289386Exon32: 30 residues, 69289807-69289891Exon33: 2 residues, -Jump to PTPRB_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4061 69201231-69289891 ~-89K 9319(PTPRB)(-)Loci: 2773 69046328-69111244 ~-65K 9318(KCNMB4)(+)Link out to UCSC