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0LIPA3_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePPFIA3
DescriptionLiprin-alpha 3 (protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha 3) (ptprf-interacting protein alpha 3).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This entry represents a second domain related to the SAM domain. Sterile alpha motif (SAM) domains are known to be involved in diverse protein-protein interactions.ssociating with both SAM-containing and non-SAM-containing protein pathways.
  IPR011510:Sterile alpha motif homology 2
The sterile alpha motif (SAM) domain is a putative protein interaction module present in a wide variety of proteins involved in many biological processes. The SAM domain that spreads over around 70 residues is found in diverse eukaryotic organisms . SAM domains have been shown to homo- and hetero-oligomerise.orming multiple self-association architectures and also binding to various non-SAM domain-containing proteins .evertheless with a low affinity constant . SAM domains also appear to possess the ability to bind RNA . Smaug a protein that helps to establish a morphogen gradient in Drosophila embryos by repressing the translation of nanos (nos) mRNA binds to the 3 untranslated region (UTR) of nos mRNA via two similar hairpin structures. The 3D crystal structure of the Smaug RNA-binding region shows a cluster of positively charged residues on the Smaug-SAM domain.hich could be the RNA-binding surface. This electropositive potential is unique among all previously determined SAM-domain structures and is conserved among Smaug-SAM homologs. These results suggest that the SAM domain might have a primary role in RNA binding. Structural analyses show that the SAM domain is arranged in a small five-helix bundle with two large interfaces . In the case of the SAM domain of EphB2.ach of these interfaces is able to form dimers. The presence of these two distinct intermonomers binding surface suggest that SAM could form extended polymeric structures .
  IPR001660:Sterile alpha motif SAM
The Prefoldin/GimC family of proteins are found in eukaryotes and archaea . Prefoldin is part of a molecular chaperone system that promotes the correct folding of nascent polypeptide chains. Prefoldin/GimC interacts with the nascent chain to stabilise it prior to its folding within the central cavity of a chaperonin. Prefoldin/GimC is a hexamer consisting of two types of subunits.lpha and beta. Archaeal prefoldin contains one type of alpha and one type of beta subunit .hile eukaryotic prefoldin/GimC contains two different but related alpha subunits and four related beta subunits .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR009053:Prefoldin
The tRNA-binding arm domain is conserved between class I and class II enzymes.onsisting of two alpha helices in an antiparallel hairpin with a left-handed twist. The appended tRNA-binding domains recognize a small number of nucleotides that are conserved specifically in each cognate tRNA species for the discrimination between the cognate and noncognate tRNAs . These nucleotides are called identity elements.nd constitute the identity set. The tRNA-binding arm occurs as the C-terminal domain in some class I enzymes.uch as valyl-tRNA synthetase.nd as the N-terminal domain in some class II enzymes.uch as phenylalanyl-tRNA synthetase.The methicillin resistance protein.emA (factors essential for methicillin resistance).ontains a probable tRNA-binding arm that is similar in structure to those found in tRNA synthetases. In FemA.he tRNA-binding arm is inserted into the C-terminal NAT-like domain.nd is thought to bind tRNA-glycine. FemA.long with FemB and FemX.lays a vital role in peptidoglycan biosynthesis specific to Staphylococci .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR010978:tRNA-binding arm
Sterile alpha motif (SAM) domains are known to be involved in diverse protein-protein interactions.ssociating with both SAM-containing and non-SAM-containing proteins pathway . SAM domains exhibit a conserved structure.onsisting of a 4-5-helical bundle of two orthogonally packed alpha-hairpins. However SAM domains display a diversity of function.eing involved in interactions with proteins.NA and RNA . The name sterile alpha motif arose from its presence in proteins that are essential for yeast sexual differentiation. The SAM domain has had various names.ncluding SPM.TN (pointed).EP (yeast sterility.ts-related.cG proteins).CR (N-terminal conserved region) and HLH (helix-loop-helix) domain.ll of which are related and can be classified as SAM domains. SAM domains occur in eukaryotic and in some bacterial proteins. Structures have been determined for several proteins that contain SAM domains.ncluding Ets-1 transcription factor.hich plays a role in the development and invasion of tumour cells by regulating the expression of matrix-degrading proteases ; Etv6 transcription factor.ene rearrangements of which have been demonstrated in several malignancies ; EphA4 receptor tyrosine kinase.hich is believed to be important for the correct localization of a motoneuron pool to a specific position in the spinal cord ; EphB2 receptor.hich is involved in spine morphogenesis via intersectin.dc42 and N-Wasp ; p73. p53 homologue involved in neuronal development ; and polyhomeotic.hich is a member of the Polycomb group of genes (Pc-G) required for the maintenance of the spatial expression pattern of homeotic genes .
  IPR013761:Sterile alpha motif-type
IPR001660:SAM_1 
Evalue:-11.9208183288574 
Location:951-1015IPR001660:SAM 
Evalue:-9.82390874094432 
Location:835-904IPR011510:SAM_2 
Evalue:-8.95860767364502 
Location:1038-1110IPR010978:tRNA_binding_arm 
Evalue:0 
Location:42-120IPR009053:Prefoldin 
Evalue:0 
Location:597-642
SequencesProtein: LIPA3_HUMAN (1194 aa)
mRNA: NM_003660
Local Annotation
Synapse Ontology
Various stages of the synaptic vesicle cycle, including attachment, prefusion, triggering, recycling and reloading of the vesicles with transmitter.
sdb:0098 synaptic vesicle cycling  (Evidence:keywords)
attachment of the vesicle filled with transmitters involves a specific interaction between the vesicle membrane and the presynaptic active zone.
sdb:0148 docking  (Evidence:keywords)
the plasma membrane is thicked into an active zone to which several synaptic vesicles are attached.
sdb:0151 active zone  (Evidence:keywords)
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 106 residues, 54314474-54314791Exon2: 87 residues, 54322927-54323182Exon3: 36 residues, 54323435-54323537Exon4: 57 residues, 54323916-54324081Exon5: 27 residues, 54324448-54324523Exon6: 27 residues, 54325061-54325136Exon7: 76 residues, 54325446-54325668Exon8: 51 residues, 54328069-54328216Exon9: 47 residues, 54328305-54328440Exon10: 30 residues, 54328864-54328948Exon11: 46 residues, 54329102-54329234Exon12: 23 residues, 54329707-54329770Exon13: 28 residues, 54329904-54329984Exon14: 50 residues, 54330847-54330992Exon15: 64 residues, 54331792-54331980Exon16: 76 residues, 54333273-54333496Exon17: 56 residues, 54334736-54334900Exon18: 44 residues, 54335029-54335157Exon19: 33 residues, 54336488-54336582Exon20: 29 residues, 54337102-54337184Exon21: 69 residues, 54337872-54338073Exon22: 23 residues, 54341011-54341074Exon23: 11 residues, 54341234-54341261Exon24: 60 residues, 54343151-54343327Exon25: 34 residues, 54343734-54343832Exon26: 60 residues, 54344061-54344237Exon27: 25 residues, 54344325-54344394Exon28: 59 residues, 54344615-54344787Exon29: 26 residues, 54345148-54345220Exon30: 264 residues, 54345304-54346090Exon31: 2 residues, -Jump to LIPA3_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3124 53589943-53639205 ~-49K 19224(GRIN2D)(+)Loci: 3125 53656317-53661179 ~-5K 19226(KCNJ14)(+)Loci: 3126 53747240-53794495 ~-47K 19229(SULT2B1)(+)Loci: 4406 53833083-53841263 ~-8K 19240(CA11)(-)Loci: 4407 53990131-54006113 ~-16K 19255(BCAT2)(-)Loci: 4408 54262487-54268010 ~-6K 19284(-)Loci: 3127 54309429-54313528 ~-4K 19290(LIN7B)(+)Loci: 3128 54314474-54346090 ~-32K 19292(PPFIA3)(+)Loci: 4409 54484705-54520286 ~-36K 19297(SLC6A16)(-)Loci: 3129 54669297-54681299 ~-12K 19311(FLT3LG)(+)Loci: 4410 54854641-54860926 ~-6K 19323(IRF3)(-)Loci: 3130 54886218-54908800 ~-23K 19334(CPT1C)(+)Loci: 3131 54961991-55002179 ~-40K 19337(AP2A1)(+)Loci: 3132 55124271-55129003 ~-5K 19355(ATF5)(+)Loci: 4411 55510576-55524446 ~-14K 19365(KCNC3)(-)Loci: 4412 55817047-55833114 ~-16K 19382(SYT3)(-)Loci: 4413 55856895-55912007 ~-55K 19383(SHANK1)(-)Loci: 3123 53559468-53571439 ~-12K 19220(SYNGR4)(+)Link out to UCSC