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0SHC1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSHC1
DescriptionShc transforming protein 1 (sh2 domain protein c1) (src homology 2 domain containing transforming protein c1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005886 plasma membrane (IDA)
0005543 phospholipid binding (TAS)
0005515 protein binding (IPI)
0005068 transmembrane receptor protein tyrosine kin... (TAS)
0000187 activation of MAPK activity (IDA)
0008284 positive regulation of cell proliferation (NAS)
0045840 positive regulation of mitosis (NAS)
0007176 regulation of epidermal growth factor recep... (TAS)

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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 PI domain has a similar structure to the insulin receptor substrate-1 PTB domain. 7-stranded beta-sandwich.apped by a C-terminal helix.However.he PI domain contains an additional short N-terminal helix and alarge insertion between strands 1 and 2.hich forms a helix and 2 longconnecting loops. The substrate peptide fits into a surface cleft formedfrom the C-terminal helix and strand 5 .
  IPR006020:Phosphotyrosine interaction region
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
Shc proteins contain an SH2 domain and a phosphotyrosine interaction (PI) domain. These domains facilitate interaction with various activated tyrosine-phosphorylated receptors.ncluding those of growth factors.nsulin.ytokines and lymphocytes. The PI domain comprises 165 residues. of which (Arg67.rg175.er151 and Lys169 ) are responsible for binding phosphotyrosine on a IIENPQYFSDA(NPxPY) peptide . The PI domain has a similar structure to the insulin receptor substrate-1 PTB domain. 7-stranded beta-sandwich.apped by a C-terminal helix.However.he PI domain contains an additional short N-terminal helix and alarge insertion between strands 1 and 2.hich forms a helix and 2 longconnecting loops. The substrate peptide fits into a surface cleft formedfrom the C-terminal helix and strand 5 .
  IPR006019:Phosphotyrosine interaction (PID or PI)
Pleckstrin homology (PH) domains are small modular domains that occur once.r occasionally several times.n a large variety of signalling proteins.here they serve as simple targeting domains that recognize only phosphoinositide headgroups . PH domains can target their host protein to the plasma and internal membranes through its association with phosphoinositides. PH domains have a partly opened beta-barrel topology that is capped by an alpha helix. Proteins containing PH domains include pleckstrin (N-terminal).hospholipase C delta-1.eta-spectrin.ynamin.on-of-sevenless.rp1.nc-89.app1 and Rac-alpha kinase.The structure of PH domains is similar to the phosphotyrosine-binding domain (PTB) found in IRS-1 (insulin receptor substrate 1).hc adaptor and Numb; to the Ran-binding domain.ound in Nup nuclear pore complex and Ranbp1; to the Enabled/VASP homology domain 1 (EVH1 domain).ound in Enabled.ASP (vasodilator-stimulated phosphoprotein).omer and WASP actin regulatory protein; to the third domain of FERM.ound in moesin.adixin.zrin.erlin and talin; and to the PH-like domain of neurobeachin.
  IPR011993:Pleckstrin homology-type
IPR006020:PID 
Evalue:-67.1611480712891 
Location:162-318IPR000980:SH2 
Evalue:-26.5528411865234 
Location:488-559IPR000980:SH2 
Evalue:0 
Location:378-455
SequencesProtein: SHC1_HUMAN (583 aa)
mRNA: BX647149 NM_183001
Local Annotation
Synapse Ontology
A process that increases short-term neuronal synaptic plasticity, the ability of neuronal synapses to change in the short-term as circumstances require. Short-term neuronal synaptic plasticity generally involves increasing or decreasing synaptic sensitivity.
sdb:0043 positive regulation of short-term neuronal synaptic plasticity  (Evidence:keywords)
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
The Myelin Sheath of a neuron consists of fat-containing cells that insulate the axon from electrical activity. This insulation acts to increase the rate of transmission of signals. A gap exists between each myelin sheath cell along the axon. Since fat inhibits the propagation of electricity, the signals jump from one gap to the next.
sdb:0224 AP propagation through axon process  (Evidence:keywords)
KO assignmentK06279
  Level 3 annotation:
    src homology 2 domain-containing transforming protein C
  Level 2 annotation:
    Insulin signaling pathway
    Focal adhesion
    Natural killer cell mediated cytotoxicity
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 545 residues, 153201398-153203031Exon2: 81 residues, 153204642-153204881Exon3: 47 residues, 153205045-153205180Exon4: 25 residues, 153205261-153205331Exon5: 68 residues, 153205418-153205617Exon6: 44 residues, 153206770-153206897Exon7: 19 residues, 153207079-153207131Exon8: 20 residues, 153207303-153207357Exon9: 42 residues, 153207594-153207714Exon10: 23 residues, 153207870-153207934Exon11: 25 residues, 153208477-153208548Exon12: 240 residues, 153209131-153209847Exon13: 2 residues, -Jump to SHC1_HUMANExon1: 44 residues, 153202902-153203031Exon2: 81 residues, 153204642-153204881Exon3: 46 residues, 153205045-153205177Exon4: 25 residues, 153205261-153205331Exon5: 68 residues, 153205418-153205617Exon6: 44 residues, 153206770-153206897Exon7: 19 residues, 153207079-153207131Exon8: 20 residues, 153207303-153207357Exon9: 42 residues, 153207594-153207714Exon10: 23 residues, 153207870-153207934Exon11: 25 residues, 153208477-153208548Exon12: 167 residues, 153209131-153209626Exon13: 2 residues, -Jump to SHC1_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3833 152220753-152225430 ~-5K 2681(RAB13)(-)Loci: 2551 152511662-152514973 ~-3K 2706(HAX1)(+)Loci: 2552 152806880-152815707 ~-9K 2720(CHRNB2)(+)Loci: 3834 152821158-152847306 ~-26K 2722(ADAR)(-)Loci: 3835 153201398-153209847 ~-8K 2739(SHC1)(-)Loci: 2553 153412983-153424069 ~-11K 2783(TRIM46)(+)Loci: 2554 153513997-153526262 ~-12K 2831(HCN3)(+)Loci: 3836 153526253-153537835 ~-12K 2833(PKLR)(-)Loci: 2555 153669594-153670676 ~-1K 2846(POU5FLC1)(+)Loci: 2556 154095923-154121459 ~-26K 2875(SYT11)(+)Loci: 3837 154183269-154214942 ~-32K 2882(ARHGEF2)(-)Loci: 2557 154297589-154306917 ~-9K 2890(RAB25)(+)Loci: 2558 154362603-154374280 ~-12K 2897(+)Loci: 2559 154855709-154862142 ~-6K 2944(HAPLN2)(+)Loci: 2560 154878363-154895942 ~-18K 2945(BCAN)(+)Loci: 3838 154905181-154913813 ~-9K 2947(NES)(-)Loci: 2561 155097294-155118266 ~-21K 2961(NTRK1)(+)Loci: 3839 155171256-155281786 ~-111K 2965(ARHGEF11)(-)Loci: 2550 151897823-151900928 ~-3K 2658(SNAPAP)(+)Link out to UCSC