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0CLPP_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionPutative atp-dependent clp protease proteolytic subunit, mitochondrial precursor (ec (endopeptidase clp).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0008233 peptidase activity (TAS)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Proteolytic enzymes that exploit serine in their catalytic activity areubiquitous.eing found in viruses.acteria and eukaryotes . Theyinclude a wide range of peptidase activity.ncluding exopeptidase.ndopeptidase.ligopeptidase and omega-peptidase activity. Over 20 families(denoted S1 - S27) of serine protease have been identified.hese beinggrouped into 6 clans (SA.B.C.E.F and SG) on the basis of structuralsimilarity and other functional evidence . Structures are known for fourof the clans (SA.B.C and SE): these appear to be totally unrelated.uggesting at least four evolutionary origins of serine peptidases andpossibly many more .Notwithstanding their different evolutionary are similaritiesin the reaction mechanisms of several peptidases. Chymotrypsin.ubtilisinand carboxypeptidase C clans have a catalytic triad of serine.spartate andhistidine in common: serine acts as a nucleophile.spartate as anelectrophile.nd histidine as a base . The geometric orientations ofthe catalytic residues are similar between families.espite differentprotein folds . The linear arrangements of the catalytic residuescommonly reflect clan relationships. For example the catalytic triad inthe chymotrypsin clan (SA) is ordered HDS.ut is ordered DHS in thesubtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) .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. This group of serine peptidases belong to the MEROPS peptidase family S14 (ClpP endopeptidase family.lan SK). ClpP is an ATP-dependent protease that cleaves a number of proteins.uch as casein and albumin . It exists as a heterodimer of ATP-binding regulatory A and catalytic P subunits.oth of which are required for effective levels of protease activity in the presence ofATP .lthough the P subunit alone does possess some catalytic activity. This family of sequences represent the P subunit.Proteases highly similar to ClpP have been found to be encoded in the genomeof bacteria.etazoa.ome viruses and in the chloroplast of plants. A number of the proteins in this family are classified as non-peptidase homologues as they have been found experimentally to be without peptidase activity.r lack amino acid residues that are believed to be essential for catalytic activity.
  IPR001907:Peptidase S14, ClpP
SequencesProtein: CLPP_HUMAN (277 aa)
mRNA: NM_006012
Local Annotation
Synapse Ontology
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)
KO assignmentK01358
  Level 3 annotation:
    ATP-dependent Clp protease, protease subunit
  Level 2 annotation:
    Protein folding and associated processing
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 108 residues, 6312462-6312783Exon2: 26 residues, 6312879-6312951Exon3: 34 residues, 6313456-6313553Exon4: 64 residues, 6315462-6315650Exon5: 37 residues, 6317268-6317374Exon6: 124 residues, 6319548-6319915Exon7: 2 residues, -Jump to CLPP_HUMAN  
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Loci Cluster (Details)Loci: 4358 6377049-6384790 ~-8K 17799(-)Loci: 4359 6391074-6410781 ~-20K 17803(-)Loci: 4360 6445329-6453330 ~-8K 17809(TUBB4)(-)Loci: 3083 6312462-6319915 ~-7K 17793(CLPP)(+)Link out to UCSC