SynDB Home Page
SynDB Home Page
Browse
Search
Download
Help
People
links

blue bulletSynDB protein details  


Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0RAPSN_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameRAPSN
Description43 kda receptor-associated protein of the synapse (rapsyn) (acetylcholine receptor-associated 43 kda protein) (43 kda postsynaptic protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0007268 synaptic transmission (TAS)
Domain Architecture (Details)
InterPro domains assigned to SynO:
The 43kDa postsynaptic protein is a peripheral membrane protein thought to be involved in the anchoring or stabilisation of the nicotinic acetylcholine receptor at synaptic sites . It may link the receptor to the postsynaptic cytoskeleton through direct association with actin or spectrin. The 43 kDa protein is highly conserved across species. Two highly conserved regions.ne encompassing the N-terminus and the other near the C-terminus.ay be important for interaction of the protein with other components of the postsynaptic membrane.
  IPR001237:43 kDa postsynaptic protein
InterPro domains unassigned to SynO:
Quality control of intracellular proteins is essential for cellular homeostasis. Molecular chaperones recognise and contribute to the refolding of misfolded or unfolded proteins.hereas the ubiquitin-proteasome system mediates the degradation of such abnormal proteins. Ubiquitin-protein ligases (E3s) determine the substrate specificity for ubiquitylation and have been classified into HECT and RING-finger families. More recently.owever.-box proteins.hich contain a domain (the U box) of about 70 amino acids that is conserved from yeast to humans.ave been identified as a new type of E3 .The RING-finger is a specialised type of Zn-finger of 40 to 60 residues that binds two atoms of zinc.nd is probably involved in mediating protein-protein interactions. . There are two different variants.he C3HC4-type and a C3H2C3-type.hich is clearly related despite the different cysteine/histidine pattern. The latter type is sometimes referred to as RING-H2 finger. The RING domain is a protein interaction domain which has been implicated in a range of diverse biological processes.E3 ubiquitin-protein ligase activity is intrinsic to the RING domain ofc-Cbl and is likely to be a general function of this domain; Various RINGfingers exhibit binding to E2 ubiquitin-conjugating enzymes (Ubcs) .Several 3D-structures for RING-fingers are known . The 3D structure of the zinc ligation system is unique to the RING domain and is referred to as the cross-brace motif. The spacing of the cysteines in such a domain is C-x(2)-C-x(9 to 39)-C-x(1 to 3)-H-x(2 to 3)-C-x(2)-C-x(4 to 48)-C-x(2)-C. Metal ligand pairs one and three co-ordinate to bind one zinc ion.hilst pairs two and four bind the second.s illustrated in the following schematic representation:Note that in the older literature.ome RING-fingers are denoted as LIM-domains. The LIM-domain Zn-finger is a fundamentally different family.lbeit with similar Cys-spacing (see ).
  IPR001841:Zinc finger, RING-type
The tetratrico peptide repeat (TPR) is a structural motif present in a wide range of proteins . It mediates proteinprotein interactions and the assembly of multiprotein complexes . The TPR motif consists of 316 tandem-repeats of 34 amino acids residues.lthough individual TPR motifs can be dispersed in the protein sequence. Sequence alignment of the TPR domains reveals a consensus sequence defined by a pattern of small and large amino acids. TPR motifs have been identified in various different organisms.anging from bacteria to humans. Proteins containing TPRs are involved in a variety of biological processes.uch as cell cycle regulation.ranscriptional control.itochondrial and peroxisomal protein transport.eurogenesis and protein folding. The X-ray structure of a domain containing three TPRs from protein phosphatase 5 revealed that TPR adopts a helixturnhelix arrangement.ith adjacent TPR motifs packing in a parallel fashion.esulting in a spiral of repeating anti-parallel alpha-helices . The two helices are denoted helix A and helix B. The packing angle between helix A and helix B is ~24° within a single TPR and generates a right-handed superhelical shape. Helix A interacts with helix B and with helix A of the next TPR. Two protein surfaces are generated: the inner concave surface is contributed to mainly by residue on helices A.nd the other surface presents residues from both helices A and B.
  IPR001440:Tetratricopeptide TPR_1
Protein prenyltransferases catalyze the transfer of the carbon moiety of C15 farnesyl pyrophosphate or geranylgeranyl pyrophosphate synthase to a conserved cysteine residue in a CaaX motif of protein and peptide substrates. The addition of a farnesyl group is required to anchor proteins to the cell membrane. In the 3D structure of a mammalian Ras farnesyltransferases (Ftase).oth subunits are largely composed of alpha-helices. The alpha-2 to alpha-15 helices in the alpha subunit fold into a novel helical hairpin structure.esulting in a crescent-shape domain that envelopes part of the subunit. The 12 helices of the beta-subunit form an alpha-alpha barrel. Six additional helices connect the inner core of helices and form the outside of the helical barrel. A deep cleft surrounded by hydrophobic amino acids in the centre of the barrel is proposed as the FPP-binding pocket. A single Zn2+ ion is located at the junction between the hydrophilic surface groove near the subunit interface. The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008940:Protein prenyltransferase
This entry represents a region of TPR-repeats.hich are believed to function in protein-protein interactions.
  IPR011595:Tetratricopeptide-related region
This domain consists of a multi-helical fold comprised of two curved layers of alpha helices arranged in a regular right-handed superhelix.here the repeats that make up this structure are arranged about a common axis . These superhelical structures present an extensive solvent-accessible surface that is well suited to binding large substrates such as proteins and nucleic acids. This topology has been found with a number of repeats and domains.ncluding the tetratricopeptide repeat (TPR) (found in kinesin light chains.NAP regulatory proteins.lathrin heavy chains and bacterial aspartyl-phosphate phosphatases).nd the pentatricopeptide repeat (PPR) (RNA-processing proteins). The TRP is likely to be an ancient repeat.ince it is found in eukaryotes.acteria and archaea.hereas the PPR repeat is found predominantly in higher plants. The superhelix formed from these repeats can bind ligands at a number of different regions.nd has the ability to acquire multiple functional roles .
  IPR011990:Tetratricopeptide-like helical
The tetratrico peptide repeat region (TPR) is a structural motif present in a wide range of proteins . It mediates proteinprotein interactions and the assembly of multiprotein complexes . The TPR motif consists of 316 tandem-repeats of 34 amino acids residues.lthough individual TPR motifs can be dispersed in the protein sequence. Sequence alignment of the TPR domains reveals a consensus sequence defined by a pattern of small and large amino acids. TPR motifs have been identified in various different organisms.anging from bacteria to humans. Proteins containing TPRs are involved in a variety of biological processes.uch as cell cycle regulation.ranscriptional control.itochondrial and peroxisomal protein transport.eurogenesis and protein folding. The X-ray structure of a domain containing three TPRs from protein phosphatase 5 revealed that TPR adopts a helixturnhelix arrangement.ith adjacent TPR motifs packing in a parallel fashion.esulting in a spiral of repeating anti-parallel alpha-helices . The two helices are denoted helix A and helix B. The packing angle between helix A and helix B is ~24° within a single TPR and generates a right-handed superhelical shape. Helix A interacts with helix B and with helix A of the next TPR. Two protein surfaces are generated: the inner concave surface is contributed to mainly by residue on helices A.nd the other surface presents residues from both helices A and B.
  IPR013026:Tetratricopeptide region
IPR001841:RING 
Evalue:-4.56863623584101 
Location:362-401IPR001440:TPR_1 
Evalue:-1.53760194778442 
Location:205-238IPR001440:TPR_1 
Evalue:-1.3665314912796 
Location:122-155IPR001440:TPR_1 
Evalue:-0.744727492332459 
Location:285-318IPR011595:TPR_related 
Evalue:0 
Location:1-74IPR013026:TPR 
Evalue:0 
Location:162-195IPR001841:ZF_RING_1 
Evalue:0 
Location:0-0IPR013026:TPR 
Evalue:1.41497334797082 
Location:82-115
SequencesProtein: RAPSN_HUMAN (411 aa)
mRNA: NM_005055
Local Annotation
Synapse Ontology
all
sdb:0004 Presynaptic compartment  (Evidence:keywords,domains)
Postsynaptic compartment is represented by a patch of plasma membrane containing a packed array of neurotransmitter receptors and by an underlying dense matrix, the postsynaptic density (PSD).
sdb:0005 Postsynaptic compartment  (Evidence:keywords,domains)
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords,domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 95 residues, 47415890-47416174Exon2: 68 residues, 47416858-47417058Exon3: 20 residues, 47419285-47419339Exon4: 43 residues, 47419738-47419861Exon5: 35 residues, 47419950-47420049Exon6: 55 residues, 47420783-47420942Exon7: 115 residues, 47425939-47426278Exon8: 137 residues, 47426900-47427306Exon9: 2 residues, -Jump to RAPSN_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3949 47415890-47427306 ~-11K 6678(RAPSN)(-)Loci: 2664 47557207-47562689 ~-5K 6687(NDUFS3)(+)Loci: 3950 47595443-47620640 ~-25K 6689(MTCH2)(-)Loci: 3948 47155660-47164534 ~-9K 6654(PACSIN3)(-)Link out to UCSC