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0ASPP1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePPP1R13B
DescriptionApoptosis stimulating of p53 protein 1 (protein phosphatase 1 regulatory subunit 13b).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
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
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
IPR001452:SH3 
Evalue:-17.0043648054025 
Location:1022-1080IPR002110:Ank 
Evalue:-9.82390880584717 
Location:920-952IPR002110:Ank 
Evalue:-7.45593214035034 
Location:953-985IPR002110:ANK 
Evalue:0 
Location:65-90
SequencesProtein: ASPP1_HUMAN (1090 aa)
mRNA: NM_015316
Local Annotation
Synapse Ontology
?
sdb:0265 cAMP mediated STP  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 482 residues, 103269841-103271285Exon2: 68 residues, 103272092-103272292Exon3: 57 residues, 103273783-103273950Exon4: 46 residues, 103274768-103274902Exon5: 48 residues, 103274975-103275113Exon6: 258 residues, 103275913-103276683Exon7: 169 residues, 103277879-103278381Exon8: 58 residues, 103278743-103278913Exon9: 62 residues, 103282462-103282643Exon10: 49 residues, 103285883-103286024Exon11: 67 residues, 103289089-103289286Exon12: 60 residues, 103290159-103290334Exon13: 36 residues, 103293739-103293841Exon14: 27 residues, 103314834-103314911Exon15: 42 residues, 103320884-103321004Exon16: 51 residues, 103333460-103333608Exon17: 57 residues, 103383388-103383555Exon18: 2 residues, -Jump to ASPP1_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2865 103165326-103247461 ~-82K 11833(KNS2)(+)Loci: 4154 103269841-103383555 ~-114K 11841(PPP1R13B)(-)Loci: 2864 102921523-103039917 ~-118K 11819(MARK3)(+)Link out to UCSC