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0CHIN_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionN-chimaerin (nc) (n-chimerin) (alpha chimerin) (a-chimaerin) (rho- gtpase-activating protein 2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005070 SH3/SH2 adaptor activity (TAS)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Diacylglycerol (DAG) is an important second messenger. Phorbol esters (PE) are analogues of DAG and potent tumor promoters that cause a variety of physiological changes when administered to both cells and tissues. DAG activates a family of serine/threonine protein kinases.ollectively known as protein kinase C (PKC) . Phorbol esters can directly stimulate PKC. The N-terminal region of PKC.nown as been shown to bind PE and DAG in a phospholipid and zinc-dependent fashion. The C1 region contains one or two copies (depending on the isozyme of PKC) of a cysteine-rich domain.hich is about 50 amino-acid residues long.nd which is essential for DAG/PE-binding. The DAG/PE-binding domain binds two zinc ions; the ligands of these metal ions are probably the six cysteines and two histidines that are conserved in this domain.
  IPR002219:Protein kinase C, phorbol ester/diacylglycerol binding
Members of the Rho family of small G proteins transduce signals from plasma-membranereceptors and control cell adhesion.otility and shape by actin cytoskeleton formation.Like all other GTPases.ho proteins act as molecular switches.ith an activeGTP-bound form and an inactive GDP-bound form. The active conformation is promoted byguanine-nucleotide exchange factors.nd the inactive state by GTPase-activating proteins(GAPs) which stimulate the intrinsic GTPase activity of small G proteins.This entry is a Rho/Rac/Cdc42-like GAP domain.hat is found in a wide variety of large.ulti-functional proteins .A number of structure are known for this family .The domain is composed of seven alpha helices.This domain is also known as the breakpoint cluster region-homology (BH) domain.
The Src homology 2 (SH2) domain is a protein domain of about 100 amino-acid residues first identified as a conserved sequence region between the oncoproteins Src and Fps . Similar sequences were later found in many other intracellular signal-transducing proteins . SH2 domains function as regulatory modules of intracellular signalling cascades by interacting with high affinity to phosphotyrosine-containing target peptides in a sequence-specific.H2 domains recognize between 3-6 residues C-terminal to the phosphorylated tyrosine in a fashion that differs fromone SH2 domain to another.nd strictly phosphorylation-dependent manner . They are found in a wide variety of protein contexts e.g..n association with catalytic domains of phospholipase Cy (PLCy) and the non-receptor protein tyrosine kinases; within structural proteins such as fodrin and tensin; and in a group of small adaptor molecules..e Crk and Nck. The domains are frequently found as repeats in a single protein sequence and will then often bind both mono- and di-phosphorylated substrates. The structure of the SH2 domain belongs to the alpha+beta class.ts overall shape forming a compact flattened hemisphere. The core structural elements comprise a central hydrophobic anti-parallel beta-sheet.lanked by 2 short alpha-helices. The loop between strands 2 and 3 provides many of the binding interactions with the phosphate group of its phosphopeptide ligand.nd is hence designated the phosphate binding loop.he phosphorylated ligand binds perpendicular to the beta-sheet and typically interacts with the phosphate binding loop and a hydrophobic binding pocket that interacts with a pY+3 side chain. The N- and C-termini of the domain are close together in space and on the opposite face from the phosphopeptide binding surface and it has been speculated that this has facilitated their integration into surface-exposed regions of host proteins .
  IPR000980:SH2 motif
Proteins containing a RhoGAP (Rho GTPase Activating Protein) domain usually function to catalyze the hydrolysis of GTP that is bound to and/or Cdc42.nactivating these regulators of the actin cytoskeleton. The 53 known human RhoGAP domain-containing proteins are the largest known group of Rho GTPase regulators and significantly outnumber the 21 Rho GTPases they presumably regulate. This excess of GAP proteins probably indicates complex regulation of the Rho GTPases and is consistent with the existence of almost as many (48) human Dbl domain-containing Rho GEFs that act antagonistically to the RhoGAP proteins by activating the Rho GTPases. Phylogenetic analysis offers evidence for frequent domain duplication and for duplication of the entire genes containing these GAP domains .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008936:Rho GTPase activation protein
SequencesProtein: CHIN_HUMAN (459 aa)
mRNA: NM_001822
Local Annotation
Synapse Ontology
The formation of a synapse.
sdb:0034 synaptogenesis  (Evidence:keywords)
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 309 residues, 175372337-175373261Exon2: 37 residues, 175374680-175374786Exon3: 48 residues, 175381878-175382016Exon4: 28 residues, 175384484-175384562Exon5: 60 residues, 175385282-175385456Exon6: 30 residues, 175397407-175397492Exon7: 28 residues, 175419853-175419931Exon8: 98 residues, 175450813-175451102Exon9: 40 residues, 175488031-175488145Exon10: 12 residues, 175491507-175491539Exon11: 20 residues, 175517861-175517917Exon12: 15 residues, 175525137-175525176Exon13: 166 residues, 175577867-175578361Exon14: 2 residues, -Jump to CHIN_HUMAN  
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Loci Cluster (Details)Loci: 4480 175320852-175337416 ~-17K 21613(CHRNA1)(-)Loci: 4481 175372337-175578361 ~-206K 21615(CHN1)(-)Loci: 4482 175647253-175741143 ~-94K 21619(ATF2)(-)Loci: 4479 175132548-175255873 ~-123K 21610(WASPIP)(-)Link out to UCSC