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0SHAN1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSHANK1
DescriptionSh3 and multiple ankyrin repeat domains protein 1 (shank1) (somatostatin receptor interacting protein) (sstr interacting protein) (sstrip).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0030425 dendrite (NAS)
0005622 intracellular (NAS)
0005624 membrane fraction (IEP)
0005515 protein binding (IPI)
0007016 cytoskeletal anchoring (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:
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
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
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.
  IPR001478:PDZ/DHR/GLGF
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
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:-23.3665313720703 
Location:2096-2159IPR001452:SH3 
Evalue:-15.2006594505464 
Location:557-612IPR001478:PDZ 
Evalue:-12.6777807052661 
Location:672-761IPR002110:Ank 
Evalue:-7.45593214035034 
Location:346-378IPR002110:Ank 
Evalue:-5.53760194778442 
Location:246-278IPR002110:Ank 
Evalue:-3.23657202720642 
Location:313-345IPR002110:Ank 
Evalue:-2.79588007926941 
Location:212-245IPR002110:Ank 
Evalue:-1.55284202098846 
Location:279-312IPR002110:Ank 
Evalue:0.672097861766815 
Location:379-395IPR002110:Ank 
Evalue:1.17609131336212 
Location:195-210
SequencesProtein: SHAN1_HUMAN (2161 aa)
mRNA: NM_016148
Local Annotation
Synapse Ontology
introduce the substructure of the synapse and the location where the molecule can be seen. It will contain all the constructive special organelle and molecule we known.
sdb:0001 Structure/Biochemistry of synapse  (Evidence:keywords)
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)
the plasma membrane of the postsynaptic neuron. It apposes with presynaptic actiove zone.
sdb:0108 postsynaptic plasma membrane  (Evidence:keywords)
?
sdb:0265 cAMP mediated STP  (Evidence:keywords)
?
sdb:0297 NMDA receptor  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 286 residues, 55856895-55857751Exon2: 1033 residues, 55861260-55864354Exon3: 34 residues, 55867086-55867183Exon4: 41 residues, 55881305-55881424Exon5: 25 residues, 55881812-55881881Exon6: 29 residues, 55882650-55882731Exon7: 47 residues, 55882991-55883127Exon8: 43 residues, 55883912-55884037Exon9: 29 residues, 55884265-55884348Exon10: 11 residues, 55892164-55892191Exon11: 27 residues, 55892657-55892733Exon12: 40 residues, 55892911-55893025Exon13: 66 residues, 55897535-55897729Exon14: 112 residues, 55898568-55898899Exon15: 24 residues, 55899188-55899255Exon16: 28 residues, 55899505-55899583Exon17: 41 residues, 55906439-55906556Exon18: 58 residues, 55907015-55907183Exon19: 52 residues, 55908866-55909018Exon20: 38 residues, 55909250-55909359Exon21: 26 residues, 55910727-55910799Exon22: 70 residues, 55911343-55911547Exon23: 93 residues, 55911733-55912007Exon24: 2 residues, -Jump to SHAN1_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