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0HAPIP_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameHAPIP
DescriptionHuntingtin-associated protein-interacting protein (duo protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005085 guanyl-nucleotide exchange factor activity (TAS)
0007165 signal transduction (TAS)
0016192 vesicle-mediated transport (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 entry defines the C-terminal of various retinaldehyde/retinal-binding proteins that may befunctional components of the visual cycle. Cellular retinaldehyde-binding protein (CRALBP) carries 11-cis-retinol or 11-cis-retinaldehyde as endogenous ligands and may function as a substrate carrier protein that modulates interaction of these retinoids with visual cycle enzymes . The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase.ontains a protein kinase domain.nd has separate rac-specific and rho-specific guanine nucleotide exchange factor domains . Trio is a multifunctional protein that integrates and amplifies signals involved in coordinating actin remodeling.hich is necessary for cell migration and growth.Other members of the family are transfer proteins that include.uanine nucleotide exchange factor that may function as an effector of RAC1.hosphatidylinositol/phosphatidylcholine transfer protein that is required for the transport of secretory proteins from the golgicomplex and alpha-tocopherol transfer protein that enhances the transfer of the ligand between separate membranes.
  IPR001251:Cellular retinaldehyde-binding/triple function, C-terminal
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
Spectrin repeats are found in several proteins involved incytoskeletal structure. These include spectrin.lpha-actininand dystrophin. The spectrin repeat forms athree helix bundle. The second helix is interrupted by prolinein some sequences. The repeats are defined by a characteristictryptophan (W) residue at position 17 in helix A and a leucine(L) at 2 residues from the carboxyl end of helix C.
  IPR002017:Spectrin repeat
The Rho family GTPases Rho.ac and CDC42 regulate a diverse array of cellularprocesses. Like all members of the Ras superfamily.he Rho proteins cycle between active GTP-bound and inactive GDP-bound conformational states.Activation of Rho proteins through release of bound GDP and subsequentbinding of GTP.s catalyzed by guanine nucleotide exchange factors (GEFs) inthe Dbl family. The proteins encoded by members of the Dbl family share acommon domain.resented in this entry.f about 200 residues (designated the Dbl homology or DH domain)that has been shown to encode a GEF activity specific for a number of Rhofamily members. In addition.ll family members possess a second.hareddomain designated the pleckstrin homology (PH) domain (). Trioand its homolog UNC-73 are unique within the Dbl family insomuch as theyencode two distinct DH/PH domain modules. The PH domain is invariably locatedimmediately C-terminal to the DH domain and this invariant topography suggestsa functional interdependence between these two structural modules. Biochemicaldata have established the role of the conserved DH domain in Rho GTPaseinteraction and activation.nd the role of the tandem PH domain inintracellular targeting and/or regulation of DH domain function. The DH domainof Dbl has been shown to mediate oligomerization that is mostly homophilic innature. In addition to the tandem DH/PH domains Dbl family GEFs containdiverse structural motifs like serine/threonine kinase.BD.DZ.GS.Q.EM.dc25RasGEF.H.H2.H3.F.pectrin or Ig.The DH domain is composed of three structurally conserved regions separated bymore variable regions. It does not share significant sequence homology withother subtypes of small G-protein GEF motifs such as the Cdc25 domain and theSec7 domain.hich specifically interact with Ras and ARFfamily small GTPases.espectively.or with other Rho protein interactivemotifs.ndicating that the Dbl family proteins are evolutionarily unique. TheDH domain is composed of 11 alpha helices that are folded into a flattened.longated alpha-helix bundle in which two of the three conserved regions.onserved region 1 (CR1) and conserved region 3 (CR3).re exposed near thecenter of one surface. CR1 and CR3.ogether with a part of alpha-6 and theDH/PH junction site.onstitute the Rho GTPase interacting pocket.
  IPR000219:DH
IPR000219:RhoGEF 
Evalue:-55.6575773191778 
Location:1285-1455IPR001251:SEC14 
Evalue:-29.6575773191778 
Location:38-177IPR001849:PH 
Evalue:-13 
Location:1475-1580IPR002017:SPEC 
Evalue:-12.0222763947112 
Location:539-641IPR002017:SPEC 
Evalue:-9.30102999566398 
Location:1133-1235IPR002017:SPEC 
Evalue:-8.72124639904717 
Location:313-415IPR002017:SPEC 
Evalue:-8.25963731050576 
Location:191-307IPR002017:SPEC 
Evalue:-7.82390874094432 
Location:893-1003IPR002017:SPEC 
Evalue:-1.82390874094432 
Location:644-766IPR001331:DH_1 
Evalue:0 
Location:0-0IPR002017:SPEC 
Evalue:0.176091259055681 
Location:418-533
SequencesProtein: HAPIP_HUMAN (1663 aa)
mRNA: NM_003947
Local Annotation
Synapse Ontology
?
sdb:0329 actin in synaptic vesicle cycling  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 56 residues, 125296274-125296441Exon2: 27 residues, 125429526-125429601Exon3: 40 residues, 125436365-125436480Exon4: 66 residues, 125466034-125466227Exon5: 173 residues, 125470279-125470792Exon6: 43 residues, 125500327-125500450Exon7: 66 residues, 125527516-125527708Exon8: 46 residues, 125531397-125531529Exon9: 79 residues, 125535801-125536032Exon10: 43 residues, 125548679-125548802Exon11: 66 residues, 125586381-125586573Exon12: 71 residues, 125596671-125596880Exon13: 60 residues, 125600233-125600408Exon14: 67 residues, 125615006-125615202Exon15: 57 residues, 125624348-125624515Exon16: 42 residues, 125632192-125632312Exon17: 75 residues, 125635843-125636062Exon18: 52 residues, 125640424-125640574Exon19: 40 residues, 125643481-125643596Exon20: 40 residues, 125647697-125647813Exon21: 43 residues, 125648299-125648422Exon22: 63 residues, 125656713-125656896Exon23: 41 residues, 125658146-125658265Exon24: 24 residues, 125663426-125663493Exon25: 38 residues, 125664060-125664170Exon26: 25 residues, 125676199-125676269Exon27: 32 residues, 125678781-125678871Exon28: 33 residues, 125684344-125684437Exon29: 39 residues, 125689740-125689852Exon30: 65 residues, 125692230-125692421Exon31: 36 residues, 125692859-125692961Exon32: 49 residues, 125694276-125694419Exon33: 36 residues, 125697847-125697950Exon34: 486 residues, 125719936-125721388Exon35: 2 residues, -Jump to HAPIP_HUMAN  
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