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1Q9VHK3_DROME*   Trembl (?) | Description Local Annotation Link Reference
General Information
DescriptionCg31349-pa, isoform a.
SpeciesDrosophila melanogaster (NCBI taxonomy ID: 7227)
GO0005912 adherens junction (TAS)
0007391 dorsal closure (TAS)
0007163 establishment and/or maintenance of cell po... (NAS)
0046328 regulation of JNK cascade (NAS)

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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 represents a domain found in guanylate kinase () and in L-type calcium channel.Guanylate kinase () (GK) catalyzes the ATP-dependent phosphorylation of GMP into GDP.It is essential for recycling GMP and indirectly.GMP. In prokaryotes (such as Escherichia coli).ower eukaryotes(such as yeast) and in vertebrates.K is a highly conserved monomeric protein of about 200 amino acids. GKhas been shown to be structurally similar to protein A57R (or SalG2R)from various strains of Vaccinia virus. L-type calcium channnels are formed from different alpha-1 subunit isoforms that determine the pharmacological properties of the channel.ince they form the drug binding domain. Other properties.uch as gating voltage-dependence. protein modulation and kinase influenced by alpha-2.elta and beta subunits.
  IPR008145:Guanylate kinase/L-type calcium channel region
PDZ domains are found in diverse signaling proteins in bacteria.easts.lants.nsects and vertebrates . PDZ domains can occur in one or multiple copies and are nearly always found in cytoplasmic proteins. They bind either the carboxyl-terminal sequences of proteins or internal peptide sequences . In most cases.nteraction between a PDZ domain and its target is constitutive.ith a binding affinity of 1 to 10 ┬ÁM. However.gonist-dependent activation of cell surface receptors is sometimes required to promote interaction with a PDZ protein. PDZ domain proteins are frequently associated with the plasma membrane. compartment where high concentrations of phosphatidylinositol 4.-bisphosphate (PIP2) are found. Direct interaction between PIP2 and a subset of class II PDZ domains (syntenin.ASK.iam-1) has been demonstrated. PDZ domains consist of 80 to 90 amino acids comprising six beta-strands (betaA to betaF) and two alpha-helices. and B.ompactly arranged in a globular structure. Peptide binding of the ligand takes place in an elongated surface groove as an antiparallel beta-strand interacts with the betaB strand and the B helix. The structure of PDZ domains allows binding to a free carboxylate group at the end of a peptide through a carboxylate-binding loop between the betaA and betaB strands.
This is a domain of unknown function.resent in ZO-1 and Unc5-like netrin receptors. It is also found in different variants of ankyrin.hich are responsible for attaching integral membrane proteins to cytoskeletal elements.
SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organisation. These were first described in the Src cytoplasmic tyrosine kinase . The structure is a partly opened beta barrel.
  IPR011511:Variant SH3
SH3 (src Homology-3) domains are small protein modules containing approximately 50 amino acid residues . They are found in a great variety of intracellular or membrane-associated proteins for example.n a variety of proteins with enzymatic activity.n adaptor proteins that lack catalytic sequences and in cytoskeletal proteins.uch as fodrin and yeast actin binding protein ABP-1. The SH3 domain has a characteristic fold which consists of five or six beta-strands arranged as two tightly packed anti-parallel beta sheets. The linker regions may contain short helices . The surface of the SH2-domain bears a flat.ydrophobic ligand-binding pocket which consists of three shallow grooves defined by conservative aromatic residues in which the ligand adopts an extended left-handed helical arrangement. The ligand binds with low affinity but this may be enhanced by multiple interactions.The region bound by the SH3 domain is in all cases proline-rich and contains PXXP as a core-conserved binding motif. The function of the SH3 domain is not well understood but they may mediate many diverse processes such as increasing local concentration of proteins.ltering their subcellular location and mediating the assembly of large multiprotein complexes .
  IPR001452:Src homology-3
SequencesProtein: Q9VHK3_DROME (2090 aa)
mRNA: No corresponding mRNA found
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
sdb:0265 cAMP mediated STP  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Family_id: 599 Tight junction protein ZO-2 (Zonula occludens 2 protein) (Zona occludens 2 protein) (Tight junction protein 2). 
Cross Links
Ensembl familyNot mapped to Ensembl families
Protein InteractionNot mapped to Bind and PPID
PDB2FE5A: Chain A, The Crystal Structure Of The Second Pdz Domain Of Human Dlg3
1KGDA: Chain A, Crystal Structure Of The Guanylate Kinase-Like Domain Of Human Cask
1V5LA: Chain A, Solution Structure Of Pdz Domain Of Mouse Alpha-Actinin-2 Associated Lim Protein
1UJDA: Chain A, Solution Structure Of Rsgi Ruh-003, A Pdz Domain Of Hypothetical Kiaa0559 Protein From Human Cdna
ModBaseLink out to the theoretical structure model
OMIMNot mapped to OMIM
PTMLink out to dbPTM
Gene-centric linksGEO: Expression
dbSNP: Signle Nucleotide Polymorphism
1Science 287:2185-2195(2000) The genome sequence of Drosophila melanogaster.
2Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002) Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster euchromatic genome sequence.
3Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002) The transposable elements of the Drosophila melanogaster euchromatin: a genomics perspective.
4Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.
5Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Drosophila melanogaster release 4 sequence.
6Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases

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