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0PSN1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePSEN1
DescriptionPresenilin-1 (ps-1) (s182 protein) .
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005783 endoplasmic reticulum (IDA)
0005794 Golgi apparatus (IDA)
0005639 integral to nuclear inner membrane (TAS)
0005887 integral to plasma membrane (IDA)
0000776 kinetochore (TAS)
0005624 membrane fraction (TAS)
0005739 mitochondrion (IDA)
0005515 protein binding (IPI)
0042987 amyloid precursor protein catabolism (TAS)
0006916 anti-apoptosis (TAS)
0007001 chromosome organization and biogenesis (sen... (TAS)
0007059 chromosome segregation (TAS)
0006509 membrane protein ectodomain proteolysis (IDA)
0007220 Notch receptor processing (TAS)
0043085 positive regulation of enzyme activity (IDA)
0016485 protein processing (IDA)

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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:
Peptidases are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry. Families are grouped by their catalytic type.he first character representing the catalytic type: A.spartic; C.ysteine; G.lutamic acid; M.etallo; S.erine; T.hreonine; and U.nknown. A clan that contains families of more than one type is described as being of type P. The serine.hreonine and cysteine peptidases utilise the catalytic part of an amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic.lutamic and metallopeptidases.he nucleophile is an activated water molecule. Aspartic endopeptidases () of vertebrate.ungal and retroviral origin have been characterised .Aspartate peptidases are so named because Asp residues are the ligands of the activated water molecule in all examples where the catalytic residues have been identified.lthough at least one viral enzyme is believed to have an Asp and an Asn as its catalytic dyad. All or most aspartate peptidases are endopeptidases. These enzymes have been assigned into clans (proteins which are evolutionary related).nd further sub-divided into families.argely on the basis of their tertiary structure.This group of aspartic peptidases belong to MEROPS peptidase family A22 (presenilin family.lan AD): subfamily A22A.he type example being presenilin 1 from Homo sapiens.Presenilins are polytopic transmembrane (TM) proteins.utations in whichare associated with the occurrence of early-onset familial Alzheimersdisease. rare form of the disease that results from a single-genemutation . The physiological functions of presenilins are unknown.ut they may be related to developmental signalling.poptotic signal transduction.r processing of selected proteins.uch as the beta-amyloid precursor protein(beta-APP). There are a number of subtypes which belong to this presenilin family. That presenilin homologues have been identified in species that do not have an Alzhemiers disease correlate suggests that they may have functions unrelated to the disease.omologues having been identified in mouse.rosophila melanogaster.aenorhabditis elegans and other members of the eukarya including plants.
  IPR001108:Peptidase A22A, presenilin
Peptidases are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry. Families are grouped by their catalytic type.he first character representing the catalytic type: A.spartic; C.ysteine; G.lutamic acid; M.etallo; S.erine; T.hreonine; and U.nknown. A clan that contains families of more than one type is described as being of type P. The serine.hreonine and cysteine peptidases utilise the catalytic part of an amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic.lutamic and metallopeptidases.he nucleophile is an activated water molecule. Aspartic endopeptidases () of vertebrate.ungal and retroviral origin have been characterised .Aspartate peptidases are so named because Asp residues are the ligands of the activated water molecule in all examples where the catalytic residues have been identified.lthough at least one viral enzyme is believed to have an Asp and an Asn as its catalytic dyad. All or most aspartate peptidases are endopeptidases. These enzymes have been assigned into clans (proteins which are evolutionary related).nd further sub-divided into families.argely on the basis of their tertiary structure.This group of aspartic peptidases belong to MEROPS peptidase family A22 (presenilin family.lan AD).SPP and potential eukaryotic homologs represent a family of aspartic proteases that promote intramembrane proteolysis to release biologically important peptides. Signal peptide peptidase (SPP) catalyses intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein. In humans.PP activity is required to generate signal sequence-derived human lymphocyte antigen-E epitopes that are recognised by the immune system.nd are required in the processing of the hepatitis C virus core protein.
  IPR006639:Peptidase A22, presenilin signal peptide
Peptidases are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry. Families are grouped by their catalytic type.he first character representing the catalytic type: A.spartic; C.ysteine; G.lutamic acid; M.etallo; S.erine; T.hreonine; and U.nknown. A clan that contains families of more than one type is described as being of type P. The serine.hreonine and cysteine peptidases utilise the catalytic part of an amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic.lutamic and metallopeptidases.he nucleophile is an activated water molecule. Aspartic endopeptidases () of vertebrate.ungal and retroviral origin have been characterised .Aspartate peptidases are so named because Asp residues are the ligands of the activated water molecule in all examples where the catalytic residues have been identified.lthough at least one viral enzyme is believed to have an Asp and an Asn as its catalytic dyad. All or most aspartate peptidases are endopeptidases. These enzymes have been assigned into clans (proteins which are evolutionary related).nd further sub-divided into families.argely on the basis of their tertiary structure.This group of aspartic peptidases belong to MEROPS peptidase family A22 (presenilin family.lan AD): subfamily A22A.he type example being presenilin 1 from Homo sapiens.Presenilins are polytopic transmembrane (TM) proteins.utations in whichare associated with the occurrence of early-onset familial Alzheimersdisease. rare form of the disease that results from a single-genemutation . The physiological functions of presenilins are unknown.ut they may be related to developmental signalling.poptotic signal transduction.r processing of selected proteins.uch as the beta-amyloid precursor protein(beta-APP). There are a number of subtypes which belong to this presenilin family. That presenilin homologues have been identified in species that do not have an Alzhemiers disease correlate suggests that they may have functions unrelated to the disease.omologues having been identified in mouse.rosophila melanogaster.aenorhabditis elegans and other members of the eukarya including plants. In humans.here are two presenilin genes (PS1 and PS2)that share 67% amino acid identity.he greatest divergence between the two falling in the N-terminus and in the large hydrophilic loop towards the C-terminus of each molecule. Six to nine TM domains are predicted for each.nd biochemical analysis has demonstrated that their C-termini are cytoplasmic; but the orientation of their N-termini and large hydrophilic loops remains to be resolved. They are expressed in almost all tissues.ncluding the brain and.t a cellular level.hey have been localised to the nuclear envelope.ndoplasmicreticulum and Golgi apparatus. This signature defines vertebrate presenilin 1 proteins. Presenilin 1 has been shown to be phosphorylated by protein kinase C.nd isendogenously cleaved into 28 kDa N-terminal and 19 kDa C-terminal fragments.Consequently.ittle of the uncleaved peptide is detectable in vivo. PS1gene mutations are thought to account for the majority of early-onsetfamilial Alzheimers disease cases. To date.5 different mutations havebeen identified in PS1.ll but one of which result in a single amino changein the presenilin 1 molecule. Affected residues always occur in regions ofthe sequence that are conserved between presenilins 1 and 2.nd the C. eleganshomologue.el-12 . The mutations are thought to be responsible for ~50%of cases of early-onset familial Alzheimers disease.n contrast.ess than1% resulting from mutations in PS2. How the mutations trigger disease is unknown.ut one biochemical effect consistently associated with them is analteration in the proteolytic cleavage of beta-APP such that there isoverproduction of long-tailed beta-amyloid peptide derivatives.
  IPR002031:Peptidase A22A, presenilin 1
IPR001108:Presenilin 
Evalue:-268.356536865234 
Location:70-458IPR002031:PRESENILIN1 
Evalue:0 
Location:1-21IPR002031:PRESENILIN1 
Evalue:0 
Location:44-58
SequencesProtein: PSN1_HUMAN (467 aa)
mRNA: NM_000021
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)
Typical ecretory organelles, some 50 nm in diameter, of presynaptic nerve terminals; accumulate high concentrations of nonpeptide neurotransmitters and secrete these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
sdb:0094 typical synaptic vesicle  (Evidence:keywords)
?
sdb:0265 cAMP mediated STP  (Evidence:keywords)
KO assignmentK04505
  Level 3 annotation:
    presenilin 1 (Alzheimer disease 3)
  Level 2 annotation:
    Wnt signaling pathway
    Notch signaling pathway
    Alzheimer's disease
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 38 residues, 72672931-72673044Exon2: 29 residues, 72684255-72684337Exon3: 48 residues, 72684427-72684567Exon4: 85 residues, 72707257-72707508Exon5: 49 residues, 72710026-72710168Exon6: 24 residues, 72723313-72723381Exon7: 75 residues, 72729104-72729325Exon8: 35 residues, 72734491-72734590Exon9: 31 residues, 72742846-72742933Exon10: 60 residues, 72748229-72748403Exon11: 41 residues, 72753586-72753705Exon12: 424 residues, 72755594-72756862Exon13: 2 residues, -Jump to PSN1_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2852 72672931-72756862 ~-84K 11422(PSEN1)(+)Loci: 4139 72811670-72995039 ~-183K 11431(NUMB)(-)Loci: 4138 72505912-72563592 ~-58K 11418(ZFYVE1)(-)Link out to UCSC