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1Q5JPJ6_HUMAN*   Trembl (?) | Description Local Annotation Link Reference
General Information
NameN/A
DescriptionHypothetical protein dkfzp686j072.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005856 cytoskeleton (IEA)
0005515 protein binding (IEA)
0007155 cell adhesion (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:
This domain is found in a number of cytoskeletal-associated proteins that associate with various proteins at the interface between the plasma membrane and the cytoskeleton. It is a conserved N-terminal domain of about 150 residues .nvolved in the linkage of cytoplasmic proteins to the membrane.
  IPR000299:Band 4.1
The microtubule-based kinesin motors and actin-based myosin motors generate movements required for intracellular trafficking.ell division.nd muscle contraction. In general.hese proteins consist of a motor domain that generates movement and a tail region that varies widely from class to class and is thought to mediate many of the regulatory or cargo binding functions specific to each class of motor . The Myosin Tail Homology 4 (MyTH4) domain has been identified as a conserved domain in the tail domains of several different unconventional myosins and a plant kinesin-like protein .ut has more recently been found in several non-motor proteins . Although the function is not yet fully understood.here is an evidence that the MyTH4 domain of Myosin-X (Myo10) binds to microtubules and thus could provide a link between an actin-based motor protein and the microtubule cytoskeleton .The MyTH4 domain is found in one or two copies associatedwith other domains.uch as myosin head.inesin motor.ERM.H.H3 and IQ. The domain is predicted to be largely alpha-helical.nterrupted by three orfour turns. The MyTH4 domain contains four highly conserved regions designatedMGD (consensus sequence L(K/R)(F/Y)MGDhP.RDE (consensus LRDEhYCQhhKQHxxxN).GW (consensus RGWxLh).nd ELEA (RxxPPSxhELEA).here h indicates ahydrophobic residue and x is any residue .
  IPR000857:Unconventional myosin/plant kinesin-like protein/non-motor protein conserved region MyTH4
The pleckstrin homology (PH) domain is a domain of about 100 residues that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton .The function of this domain is not clear.everal putative functions have been suggested:binding to the beta/gamma subunit of heterotrimeric G proteins.inding to lipids..g. phosphatidylinositol-4.-bisphosphate.inding to phosphorylated Ser/Thr residues.ttachment to membranes by an unknown mechanism.It is possible that different PH domains have totally different ligand requirements.The 3D structure of several PH domains has been determined . All known cases have a common structure consisting of two perpendicular anti-parallel beta sheets.ollowed by a C-terminal amphipathic helix. The loops connecting the beta-strands differ greatly in length.aking the PH domain relatively difficult to detect. There are no totally invariant residues within the PH domain.Proteins reported to contain one more PH domains belong to the following families:Pleckstrin.he protein where this domain was first detected.s the major substrate of protein kinase C in platelets. Pleckstrin is one of the rare proteins to contains two PH domains.Ser/Thr protein kinases such as the Akt/Rac family.he beta-adrenergic receptor kinases.he mu isoform of PKC and the trypanosomal NrkA family.Tyrosine protein kinases belonging to the Btk/Itk/Tec subfamily.Insulin Receptor Substrate 1 (IRS-1).Regulators of small G-proteins like guanine nucleotide releasing factor GNRP (Ras-GRF) (which contains 2 PH domains).uanine nucleotide exchange proteins like vav.bl.oS and Saccharomyces cerevisiae CDC24.TPase activating proteins like rasGAP and BEM2/IPL2.nd the human break point cluster protein bcr.Cytoskeletal proteins such as dynamin (see ).aenorhabditis elegans kinesin-like protein unc-104 (see ).pectrin beta-chain.yntrophin (2 PH domains) and S. cerevisiae nuclear migration protein NUM1.Mammalian phosphatidylinositol-specific phospholipase C (PI-PLC) (see ) isoforms gamma and delta. Isoform gamma contains two PH domains.he second one is split into two parts separated by about 400 residues.Oxysterol binding proteins OSBP.. cerevisiae OSH1 and YHR073w.Mouse protein citron. putative rho/rac effector that binds to the GTP-bound forms of rho and rac.Several S. cerevisiae proteins involved in cell cycle regulation and bud formation like BEM2.EM3.UD4 and the BEM1-binding proteins BOI2 (BEB1) and BOI1 (BOB1).C. elegans protein MIG-10.C. elegans hypothetical proteins C04D8.1.06H7.4 and ZK632.12.S. cerevisiae hypothetical proteins YBR129c and YHR155w.
  IPR001849:Pleckstrin-like
FERM domains (band F ezrin-radixin-moesin homology domains) are a common membrane-binding module involved in localising proteins to the plasma membrane . Proteins containing a FERM domain include cytoskeletal proteins such as erythrocyte membrane protein 4.1R.alin.nd the ezrin-radixin-moesin protein family.s well as several protein tyrosine kinases and phosphatases.nd the neurofibromatosis 2 tumour suppressor protein merlin. The ezrin-radixin-moesin protein family function to crosslink the actin filaments of cytoskeletal structures to the plasma membrane.
  IPR009065:FERM
Pleckstrin homology (PH) domains are small modular domains that occur once.r occasionally several times.n a large variety of signalling proteins.here they serve as simple targeting domains that recognize only phosphoinositide headgroups . PH domains can target their host protein to the plasma and internal membranes through its association with phosphoinositides. PH domains have a partly opened beta-barrel topology that is capped by an alpha helix. Proteins containing PH domains include pleckstrin (N-terminal).hospholipase C delta-1.eta-spectrin.ynamin.on-of-sevenless.rp1.nc-89.app1 and Rac-alpha kinase.The structure of PH domains is similar to the phosphotyrosine-binding domain (PTB) found in IRS-1 (insulin receptor substrate 1).hc adaptor and Numb; to the Ran-binding domain.ound in Nup nuclear pore complex and Ranbp1; to the Enabled/VASP homology domain 1 (EVH1 domain).ound in Enabled.ASP (vasodilator-stimulated phosphoprotein).omer and WASP actin regulatory protein; to the third domain of FERM.ound in moesin.adixin.zrin.erlin and talin; and to the PH-like domain of neurobeachin.
  IPR011993:Pleckstrin homology-type
IPR000857:MyTH4 
Evalue:-37.7212463990472 
Location:955-1110IPR000299:B41 
Evalue:-24.8239087409443 
Location:1117-1354IPR001849:PH 
Evalue:-23.6020603179932 
Location:704-797IPR001849:PH 
Evalue:-6.72124639904717 
Location:812-921
SequencesProtein: Q5JPJ6_HUMAN (1493 aa)
mRNA: NM_172069
Local Annotation
Synapse Ontology
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)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 24 residues, 43717950-43718019Exon2: 45 residues, 43725310-43725439Exon3: 23 residues, 43759505-43759568Exon4: 52 residues, 43773156-43773306Exon5: 30 residues, 43775073-43775157Exon6: 29 residues, 43775785-43775867Exon7: 64 residues, 43777813-43777999Exon8: 322 residues, 43780289-43781251Exon9: 27 residues, 43784623-43784699Exon10: 33 residues, 43786964-43787059Exon11: 50 residues, 43788043-43788188Exon12: 47 residues, 43790632-43790769Exon13: 39 residues, 43790862-43790973Exon14: 31 residues, 43791131-43791218Exon15: 55 residues, 43792867-43793026Exon16: 29 residues, 43801311-43801392Exon17: 62 residues, 43806914-43807094Exon18: 38 residues, 43810279-43810388Exon19: 39 residues, 43812132-43812245Exon20: 62 residues, 43818983-43819163Exon21: 34 residues, 43821588-43821686Exon22: 61 residues, 43823383-43823561Exon23: 54 residues, 43824476-43824632Exon24: 34 residues, 43826508-43826606Exon25: 49 residues, 43834261-43834403Exon26: 50 residues, 43837761-43837907Exon27: 45 residues, 43839542-43839672Exon28: 31 residues, 43842946-43843033Exon29: 48 residues, 43844870-43845008Exon30: 860 residues, 43846055-43848629Exon31: 2 residues, -Jump to Q5JPJ6_HUMAN  
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