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0GIT1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameGIT1
DescriptionArf gtpase-activating protein git1 (g protein-coupled receptor kinase- interactor 1) (grk-interacting protein 1) (cool-associated and tyrosine-phosphorylated protein 1) (cat-1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005515 protein binding (IPI)
0008277 regulation of G-protein coupled receptor pr... (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 describes a family of small GTPase activating proteins.or example ARF1-directed GTPase-activating protein.he cycle control GTPaseactivating protein (GAP) GCS1 which is important for the regulation ofthe ADP ribosylation factor ARF. member of the Ras superfamily of GTP-bindingproteins . The GTP-bound form of ARF is essential for the maintenance of normalGolgi morphology.t participates in recruitment of coat proteins which arerequired for budding and fission of membranes. Before the fusion with anacceptor compartment the membrane must be uncoated. This step required thehydrolysis of GTP associated to ARF. These proteins contain a characteristic zinc finger motif(Cys-x2-Cys-x(16.7)-x2-Cys) which displays some similarity to the C4-typeGATA zinc finger. The ARFGAP domain display no obvious similarity to other GAPproteins. The 3D structure of the ARFGAP domain of the PYK2-associated protein beta hasbeen solved . It consists of a three-stranded beta-sheet surrounded by 5alpha helices. The domain is organized around a central zinc atom which iscoordinated by 4 cysteines. The ARFGAP domain is clearlyunrelated to the other GAP proteins structures which are exclusively helical.Classical GAP proteins accelerate GTPase activity by supplying an argininefinger to the active site. The crystal structure of ARFGAP bound to ARFrevealed that the ARFGAP domain does not supply an arginine to the active sitewhich suggests a more indirect role of the ARFGAP domain in the GTPasehydrolysis . The Rev protein of human immunodeficiency virus type 1 (HIV-1) facilitates nuclear export of unspliced and partly-spliced viral RNAs . Rev contains an RNA-binding domain and an effector domain; the latter is believed to interact with a cellular cofactor required for the Rev response and hence HIV-1 replication. Human Rev interacting protein (hRIP) specifically interacts with the Rev effector. The amino acid sequence of hRIP is characterised by an N-terminal.-4 class zinc finger motif.
  IPR001164:Arf GTPase activating protein
GIT proteins are signalling integrators with GTPase-activating function which may be involved in the organisation of the cytoskeletal matrix assembled at active zones (CAZ). The function of the CAZ might be to define sites of neurotransmitter release. Mutations in the Spa2 homology domain (SHD) domain of GIT1 described here interfere with the association of GIT1 with Piccolo.eta-PIX.nd focal adhesion kinase .
  IPR013724:Spa2 homology (SHD) of GIT
The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes. The few known examples from prokaryotes and viruses may be the result of horizontal gene transfers . The repeat has been found in proteins of diverse function such as transcriptional initiators.ell-cycle regulators.ytoskeletal.on transporters and signal transducers. The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures . Each repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90o angle. The repeats stack together to form an L-shaped structure .
  IPR002110:Ankyrin
IPR001164:ArfGap 
Evalue:-44.7447274948967 
Location:1-124IPR013724:GIT_SHD 
Evalue:-16.8860569000244 
Location:328-358IPR013724:GIT_SHD 
Evalue:-16.7212467193604 
Location:264-294IPR002110:Ank 
Evalue:-5.55284214019775 
Location:166-198IPR002110:Ank 
Evalue:-1.30980396270752 
Location:199-231IPR002110:Ank 
Evalue:0.875061273574829 
Location:137-160
SequencesProtein: GIT1_HUMAN (761 aa)
mRNA: AB209537 BC067358 NM_014030
Local Annotation
Synapse Ontology
?
sdb:0329 actin in synaptic vesicle cycling  (Evidence:keywords)
KO assignmentK05737
  Level 3 annotation:
    G protein-coupled receptor kinase interactor 1
  Level 2 annotation:
    Regulation of actin cytoskeleton
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 480 residues, 24924619-24926058Exon2: 23 residues, 24926222-24926286Exon3: 63 residues, 24926431-24926614Exon4: 26 residues, 24926773-24926847Exon5: 31 residues, 24926955-24927042Exon6: 20 residues, 24927221-24927275Exon7: 79 residues, 24927363-24927594Exon8: 53 residues, 24927665-24927818Exon9: 46 residues, 24928006-24928140Exon10: 39 residues, 24928279-24928391Exon11: 34 residues, 24928788-24928886Exon12: 26 residues, 24929442-24929515Exon13: 18 residues, 24929874-24929923Exon14: 16 residues, 24932481-24932524Exon15: 33 residues, 24932885-24932980Exon16: 74 residues, 24933070-24933288Exon17: 37 residues, 24933841-24933947Exon18: 39 residues, 24934068-24934181Exon19: 46 residues, 24934626-24934760Exon20: 90 residues, 24940470-24940735Exon21: 2 residues, -Jump to GIT1_HUMANExon1: 170 residues, 24925598-24926105Exon2: 23 residues, 24926222-24926286Exon3: 63 residues, 24926431-24926614Exon4: 26 residues, 24926773-24926847Exon5: 31 residues, 24926955-24927042Exon6: 20 residues, 24927221-24927275Exon7: 79 residues, 24927363-24927594Exon8: 53 residues, 24927665-24927818Exon9: 46 residues, 24928006-24928140Exon10: 39 residues, 24928279-24928391Exon11: 34 residues, 24928788-24928886Exon12: 26 residues, 24929442-24929515Exon13: 18 residues, 24929874-24929923Exon14: 16 residues, 24932481-24932524Exon15: 33 residues, 24932885-24932980Exon16: 74 residues, 24933070-24933288Exon17: 37 residues, 24933841-24933947Exon18: 39 residues, 24934068-24934181Exon19: 46 residues, 24934626-24934760Exon20: 90 residues, 24940470-24940736Exon21: 2 residues, -Jump to GIT1_HUMANExon1: 113 residues, 24925721-24926058Exon2: 23 residues, 24926222-24926286Exon3: 63 residues, 24926431-24926614Exon4: 26 residues, 24926773-24926847Exon5: 31 residues, 24926955-24927042Exon6: 20 residues, 24927221-24927275Exon7: 79 residues, 24927363-24927594Exon8: 53 residues, 24927665-24927818Exon9: 46 residues, 24928006-24928140Exon10: 39 residues, 24928279-24928391Exon11: 34 residues, 24928788-24928886Exon12: 26 residues, 24929442-24929515Exon13: 18 residues, 24929874-24929923Exon14: 11 residues, 24930105-24930132Exon15: 16 residues, 24932481-24932524Exon16: 33 residues, 24932885-24932980Exon17: 74 residues, 24933070-24933288Exon18: 37 residues, 24933841-24933947Exon19: 39 residues, 24934068-24934181Exon20: 46 residues, 24934626-24934760Exon21: 23 residues, 24940470-24940535Exon22: 2 residues, -Jump to GIT1_HUMAN  
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