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Protein

Tripeptidyl-peptidase 1

Gene

TPP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus (By similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity. EC:3.4.14.9

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+2 PublicationsNote: Binds 1 Ca2+ ion per subunit.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei272Charge relay system2 Publications1
Active sitei276Charge relay system2 Publications1
Active sitei475Charge relay system2 Publications1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi517Calcium2 Publications1
Metal bindingi518Calcium; via carbonyl oxygen2 Publications1
Metal bindingi539Calcium; via carbonyl oxygen2 Publications1
Metal bindingi541Calcium; via carbonyl oxygen2 Publications1
Metal bindingi543Calcium2 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • endopeptidase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • peptidase activity Source: UniProtKB
  • peptide binding Source: UniProtKB
  • serine-type endopeptidase activity Source: InterPro
  • serine-type peptidase activity Source: UniProtKB
  • tripeptidyl-peptidase activity Source: UniProtKB

GO - Biological processi

  • bone resorption Source: UniProtKB
  • central nervous system development Source: GO_Central
  • epithelial cell differentiation Source: UniProtKB
  • IRE1-mediated unfolded protein response Source: Reactome
  • lipid metabolic process Source: ProtInc
  • lysosome organization Source: UniProtKB
  • nervous system development Source: UniProtKB
  • neuromuscular process controlling balance Source: UniProtKB
  • peptide catabolic process Source: UniProtKB
  • protein catabolic process Source: UniProtKB
  • proteolysis Source: UniProtKB

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protease, Serine protease
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.14.9 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-381038 XBP1(S) activates chaperone genes

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
O14773

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
O14773

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S53.003

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Tripeptidyl-peptidase 1 (EC:3.4.14.9)
Short name:
TPP-1
Alternative name(s):
Cell growth-inhibiting gene 1 protein
Lysosomal pepstatin-insensitive protease
Short name:
LPIC
Tripeptidyl aminopeptidase
Tripeptidyl-peptidase I
Short name:
TPP-I
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:TPP1
Synonyms:CLN2
ORF Names:GIG1, UNQ267/PRO304
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000166340.14

Human Gene Nomenclature Database

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HGNCi
HGNC:2073 TPP1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
607998 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O14773

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Lysosome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Ceroid lipofuscinosis, neuronal, 2 (CLN2)14 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of neuronal ceroid lipofuscinosis. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. The lipopigment pattern seen most often in CLN2 consists of curvilinear profiles.
See also OMIM:204500
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_06688362S → T in CLN2. 1 Publication1
Natural variantiVAR_00960377G → R in CLN2; displays very low residual enzyme activity; altered intracellular trafficking. 2 PublicationsCorresponds to variant dbSNP:rs121908195EnsemblClinVar.1
Natural variantiVAR_016790127R → Q in CLN2; displays residual enzyme activity; effectively transported to the lysosome. 3 PublicationsCorresponds to variant dbSNP:rs121908204EnsemblClinVar.1
Natural variantiVAR_016791153S → P in CLN2. 1
Natural variantiVAR_063640202P → L in CLN2; displays no residual enzyme activity; altered intracellular trafficking. 2 PublicationsCorresponds to variant dbSNP:rs121908205EnsemblClinVar.1
Natural variantiVAR_009605206R → C in CLN2; displays no residual enzyme activity; altered intracellular trafficking. 2 PublicationsCorresponds to variant dbSNP:rs28940573EnsemblClinVar.1
Natural variantiVAR_016792206R → H in CLN2. 1 PublicationCorresponds to variant dbSNP:rs121908209EnsemblClinVar.1
Natural variantiVAR_066884209Y → H in CLN2. 1 PublicationCorresponds to variant dbSNP:rs1218678626Ensembl.1
Natural variantiVAR_066885266R → Q in CLN2. 1 PublicationCorresponds to variant dbSNP:rs757953998EnsemblClinVar.1
Natural variantiVAR_016793277V → M in CLN2; displays no residual enzyme activity; altered intracellular trafficking; demonstrates enhanced processing in response to folding improvement treatment. 2 PublicationsCorresponds to variant dbSNP:rs121908207EnsemblClinVar.1
Natural variantiVAR_016794278Q → P in CLN2. 1 PublicationCorresponds to variant dbSNP:rs796053439EnsemblClinVar.1
Natural variantiVAR_072749278Q → R in CLN2. 1 PublicationCorresponds to variant dbSNP:rs796053439EnsemblClinVar.1
Natural variantiVAR_016795284G → V in CLN2; displays no residual enzyme activity; altered intracellular trafficking. 3 PublicationsCorresponds to variant dbSNP:rs119455957EnsemblClinVar.1
Natural variantiVAR_016796286N → S in CLN2; enzymatically inactive; lacks one oligosaccharide chain resulting in enzymatic inactivation and possibly prelysosomal protein degradation; altered intracellular trafficking. 3 PublicationsCorresponds to variant dbSNP:rs119455958EnsemblClinVar.1
Natural variantiVAR_009606287I → N in CLN2; displays no residual enzyme activity; altered intracellular trafficking. 2 PublicationsCorresponds to variant dbSNP:rs121908196EnsemblClinVar.1
Natural variantiVAR_066886339R → Q in CLN2. 1 PublicationCorresponds to variant dbSNP:rs765380155EnsemblClinVar.1
Natural variantiVAR_009607343E → K in CLN2; displays no residual enzyme activity; altered intracellular trafficking. 2 PublicationsCorresponds to variant dbSNP:rs121908197EnsemblClinVar.1
Natural variantiVAR_016797353T → P in CLN2. 1 PublicationCorresponds to variant dbSNP:rs121908206EnsemblClinVar.1
Natural variantiVAR_005643365C → R in CLN2; displays no residual enzyme activity; altered intracellular trafficking. 3 PublicationsCorresponds to variant dbSNP:rs119455953EnsemblClinVar.1
Natural variantiVAR_005644365C → Y in CLN2. 2 PublicationsCorresponds to variant dbSNP:rs119455954EnsemblClinVar.1
Natural variantiVAR_066887382S → R in CLN2. 1 Publication1
Natural variantiVAR_009608385V → D in CLN2. 1 PublicationCorresponds to variant dbSNP:rs121908198EnsemblClinVar.1
Natural variantiVAR_009609389G → E in CLN2. 2 PublicationsCorresponds to variant dbSNP:rs121908199EnsemblClinVar.1
Natural variantiVAR_009610422Q → H in CLN2; displays no residual enzyme activity; altered intracellular trafficking;. 3 PublicationsCorresponds to variant dbSNP:rs121908200EnsemblClinVar.1
Natural variantiVAR_016798428K → N in CLN2. 1 Publication1
Natural variantiVAR_005645447R → H in CLN2; displays very low residual enzyme activity; altered intracellular trafficking; demonstrates enhanced processing in response to folding improvement treatment; shows a five fold increase under permissive temperature conditions. 3 PublicationsCorresponds to variant dbSNP:rs119455956EnsemblClinVar.1
Natural variantiVAR_066888448A → V in CLN2. 1 Publication1
Natural variantiVAR_009611454A → E in CLN2. 1 PublicationCorresponds to variant dbSNP:rs121908201EnsemblClinVar.1
Natural variantiVAR_016799473G → R in CLN2. 2 PublicationsCorresponds to variant dbSNP:rs121908203EnsemblClinVar.1
Natural variantiVAR_009612475S → L in CLN2; displays no residual enzyme activity; effectively transported to the lysosome. 2 PublicationsCorresponds to variant dbSNP:rs121908202EnsemblClinVar.1
Natural variantiVAR_016800481F → C in CLN2. 1 Publication1
Natural variantiVAR_058435482G → R in CLN2. 1 PublicationCorresponds to variant dbSNP:rs121908208EnsemblClinVar.1
Natural variantiVAR_066889501G → C in CLN2. 1 Publication1
Natural variantiVAR_066890504N → Y in CLN2. 1 Publication1
Natural variantiVAR_063641544P → S in CLN2; displays residual enzyme activity; effectively transported to the lysosome. 1 PublicationCorresponds to variant dbSNP:rs121908210EnsemblClinVar.1
Natural variantiVAR_066891548W → R in CLN2. 1 PublicationCorresponds to variant dbSNP:rs1348967263Ensembl.1
Spinocerebellar ataxia, autosomal recessive, 7 (SCAR7)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionSpinocerebellar ataxia defines a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR7 patients show difficulty walking and writing, dysarthria, limb ataxia, and cerebellar atrophy.
See also OMIM:609270
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070917466V → G in SCAR7. 1 PublicationCorresponds to variant dbSNP:rs398122959EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi236H → A: No effect. 1 Publication1
Mutagenesisi360D → A: Inactive. Impaired processing. 1 Publication1
Mutagenesisi475S → A: Inactive. Impaired processing. 1 Publication1
Mutagenesisi517D → A: Inactive. Impaired processing. 1 Publication1

Keywords - Diseasei

Disease mutation, Epilepsy, Neurodegeneration, Neuronal ceroid lipofuscinosis, Spinocerebellar ataxia

Organism-specific databases

DisGeNET

More...
DisGeNETi
1200

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...
GeneReviewsi
TPP1

MalaCards human disease database

More...
MalaCardsi
TPP1
MIMi204500 phenotype
609270 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000166340

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
284324 Childhood-onset autosomal recessive slowly progressive spinocerebellar ataxia
228349 CLN2 disease

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA26600

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
TPP1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 191 PublicationAdd BLAST19
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002737420 – 195Removed in mature formCombined sources1 PublicationAdd BLAST176
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000027375196 – 563Tripeptidyl-peptidase 1Add BLAST368

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi111 ↔ 1222 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi210N-linked (GlcNAc...) asparagine3 Publications1
Glycosylationi222N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi286N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi313N-linked (GlcNAc...) asparagine3 Publications1
Disulfide bondi365 ↔ 5262 Publications
Glycosylationi443N-linked (GlcNAc...) asparagine4 Publications1
Disulfide bondi522 ↔ 5372 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Activated by autocatalytic proteolytical processing upon acidification. N-glycosylation is required for processing and activity.4 Publications

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O14773

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O14773

MaxQB - The MaxQuant DataBase

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MaxQBi
O14773

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
O14773

PeptideAtlas

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PeptideAtlasi
O14773

PRoteomics IDEntifications database

More...
PRIDEi
O14773

ProteomicsDB human proteome resource

More...
ProteomicsDBi
48224
48225 [O14773-2]

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
1858

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O14773

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
O14773

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
O14773

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in all tissues examined with highest levels in heart and placenta and relatively similar levels in other tissues.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000166340 Expressed in 215 organ(s), highest expression level in right adrenal gland cortex

CleanEx database of gene expression profiles

More...
CleanExi
HS_TPP1

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
O14773 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O14773 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA037709
HPA044868

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer (PubMed:19038967). Interacts with CLN5 (PubMed:19941651).2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
107611, 25 interactors

Database of interacting proteins

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DIPi
DIP-47434N

Protein interaction database and analysis system

More...
IntActi
O14773, 33 interactors

Molecular INTeraction database

More...
MINTi
O14773

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000299427

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1563
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R60model-A196-563[»]
3EDYX-ray1.85A20-563[»]
3EE6X-ray2.35A/B1-563[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O14773

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
O14773

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
O14773

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini199 – 563Peptidase S53Add BLAST365

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IICY Eukaryota
COG4934 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000008684

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000171253

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG004449

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O14773

KEGG Orthology (KO)

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KOi
K01279

Identification of Orthologs from Complete Genome Data

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OMAi
PGRHESQ

Database of Orthologous Groups

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OrthoDBi
1294880at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O14773

TreeFam database of animal gene trees

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TreeFami
TF333497

Family and domain databases

Conserved Domains Database

More...
CDDi
cd04056 Peptidases_S53, 1 hit
cd11377 Pro-peptidase_S53, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.200, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036852 Peptidase_S8/S53_dom_sf
IPR015366 S53_propep
IPR030400 Sedolisin_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF09286 Pro-kuma_activ, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00944 Pro-kuma_activ, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52743 SSF52743, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51695 SEDOLISIN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 12 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O14773-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MGLQACLLGL FALILSGKCS YSPEPDQRRT LPPGWVSLGR ADPEEELSLT
60 70 80 90 100
FALRQQNVER LSELVQAVSD PSSPQYGKYL TLENVADLVR PSPLTLHTVQ
110 120 130 140 150
KWLLAAGAQK CHSVITQDFL TCWLSIRQAE LLLPGAEFHH YVGGPTETHV
160 170 180 190 200
VRSPHPYQLP QALAPHVDFV GGLHRFPPTS SLRQRPEPQV TGTVGLHLGV
210 220 230 240 250
TPSVIRKRYN LTSQDVGSGT SNNSQACAQF LEQYFHDSDL AQFMRLFGGN
260 270 280 290 300
FAHQASVARV VGQQGRGRAG IEASLDVQYL MSAGANISTW VYSSPGRHEG
310 320 330 340 350
QEPFLQWLML LSNESALPHV HTVSYGDDED SLSSAYIQRV NTELMKAAAR
360 370 380 390 400
GLTLLFASGD SGAGCWSVSG RHQFRPTFPA SSPYVTTVGG TSFQEPFLIT
410 420 430 440 450
NEIVDYISGG GFSNVFPRPS YQEEAVTKFL SSSPHLPPSS YFNASGRAYP
460 470 480 490 500
DVAALSDGYW VVSNRVPIPW VSGTSASTPV FGGILSLINE HRILSGRPPL
510 520 530 540 550
GFLNPRLYQQ HGAGLFDVTR GCHESCLDEE VEGQGFCSGP GWDPVTGWGT
560
PNFPALLKTL LNP
Length:563
Mass (Da):61,248
Last modified:May 30, 2006 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i7299D902F6AE8555
GO
Isoform 2 (identifier: O14773-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-243: Missing.

Note: No experimental confirmation available.
Show »
Length:320
Mass (Da):34,464
Checksum:i707AE6D4A90B0FBC
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 12 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A2R8YD45A0A2R8YD45_HUMAN
Tripeptidyl-peptidase 1
TPP1
500Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8YGD1A0A2R8YGD1_HUMAN
Tripeptidyl-peptidase 1
TPP1
470Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8Y7U1A0A2R8Y7U1_HUMAN
Tripeptidyl-peptidase 1
TPP1
400Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8YE64A0A2R8YE64_HUMAN
Tripeptidyl-peptidase 1
TPP1
162Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8YCK4A0A2R8YCK4_HUMAN
Tripeptidyl-peptidase 1
TPP1
81Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8Y7I4A0A2R8Y7I4_HUMAN
Tripeptidyl-peptidase 1
TPP1
162Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PPA4E9PPA4_HUMAN
Tripeptidyl-peptidase 1
TPP1
39Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PME9E9PME9_HUMAN
Tripeptidyl-peptidase 1
TPP1
30Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E7EV34E7EV34_HUMAN
Tripeptidyl-peptidase 1
TPP1
170Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8YD72A0A2R8YD72_HUMAN
Tripeptidyl-peptidase 1
TPP1
92Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
There are more potential isoformsShow all

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAM08412 differs from that shown. Incorrectly indicated as originating from bovine.Curated
The sequence AAQ88866 differs from that shown. Reason: Frameshift at position 551.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti115I → N in BAD96219 (Ref. 6) Curated1
Sequence conflicti373Q → E in AAH14863 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03757262S → L. Corresponds to variant dbSNP:rs2734715EnsemblClinVar.1
Natural variantiVAR_06688362S → T in CLN2. 1 Publication1
Natural variantiVAR_00960377G → R in CLN2; displays very low residual enzyme activity; altered intracellular trafficking. 2 PublicationsCorresponds to variant dbSNP:rs121908195EnsemblClinVar.1
Natural variantiVAR_009604100Q → R2 PublicationsCorresponds to variant dbSNP:rs1800746EnsemblClinVar.1
Natural variantiVAR_016790127R → Q in CLN2; displays residual enzyme activity; effectively transported to the lysosome. 3 PublicationsCorresponds to variant dbSNP:rs121908204EnsemblClinVar.1
Natural variantiVAR_016791153S → P in CLN2. 1
Natural variantiVAR_005642175R → H1 PublicationCorresponds to variant dbSNP:rs764922748EnsemblClinVar.1
Natural variantiVAR_037573185R → C. Corresponds to variant dbSNP:rs34758634EnsemblClinVar.1
Natural variantiVAR_063640202P → L in CLN2; displays no residual enzyme activity; altered intracellular trafficking. 2 PublicationsCorresponds to variant dbSNP:rs121908205EnsemblClinVar.1
Natural variantiVAR_009605206R → C in CLN2; displays no residual enzyme activity; altered intracellular trafficking. 2 PublicationsCorresponds to variant dbSNP:rs28940573EnsemblClinVar.1
Natural variantiVAR_016792206R → H in CLN2. 1 PublicationCorresponds to variant dbSNP:rs121908209EnsemblClinVar.1
Natural variantiVAR_066884209Y → H in CLN2. 1 PublicationCorresponds to variant dbSNP:rs1218678626Ensembl.1
Natural variantiVAR_066885266R → Q in CLN2. 1 PublicationCorresponds to variant dbSNP:rs757953998EnsemblClinVar.1
Natural variantiVAR_016793277V → M in CLN2; displays no residual enzyme activity; altered intracellular trafficking; demonstrates enhanced processing in response to folding improvement treatment. 2 PublicationsCorresponds to variant dbSNP:rs121908207EnsemblClinVar.1
Natural variantiVAR_016794278Q → P in CLN2. 1 PublicationCorresponds to variant dbSNP:rs796053439EnsemblClinVar.1
Natural variantiVAR_072749278Q → R in CLN2. 1 PublicationCorresponds to variant dbSNP:rs796053439EnsemblClinVar.1
Natural variantiVAR_016795284G → V in CLN2; displays no residual enzyme activity; altered intracellular trafficking. 3 PublicationsCorresponds to variant dbSNP:rs119455957EnsemblClinVar.1
Natural variantiVAR_016796286N → S in CLN2; enzymatically inactive; lacks one oligosaccharide chain resulting in enzymatic inactivation and possibly prelysosomal protein degradation; altered intracellular trafficking. 3 PublicationsCorresponds to variant dbSNP:rs119455958EnsemblClinVar.1
Natural variantiVAR_009606287I → N in CLN2; displays no residual enzyme activity; altered intracellular trafficking. 2 PublicationsCorresponds to variant dbSNP:rs121908196EnsemblClinVar.1
Natural variantiVAR_066886339R → Q in CLN2. 1 PublicationCorresponds to variant dbSNP:rs765380155EnsemblClinVar.1
Natural variantiVAR_009607343E → K in CLN2; displays no residual enzyme activity; altered intracellular trafficking. 2 PublicationsCorresponds to variant dbSNP:rs121908197EnsemblClinVar.1
Natural variantiVAR_016797353T → P in CLN2. 1 PublicationCorresponds to variant dbSNP:rs121908206EnsemblClinVar.1
Natural variantiVAR_005643365C → R in CLN2; displays no residual enzyme activity; altered intracellular trafficking. 3 PublicationsCorresponds to variant dbSNP:rs119455953EnsemblClinVar.1
Natural variantiVAR_005644365C → Y in CLN2. 2 PublicationsCorresponds to variant dbSNP:rs119455954EnsemblClinVar.1
Natural variantiVAR_066887382S → R in CLN2. 1 Publication1
Natural variantiVAR_009608385V → D in CLN2. 1 PublicationCorresponds to variant dbSNP:rs121908198EnsemblClinVar.1
Natural variantiVAR_009609389G → E in CLN2. 2 PublicationsCorresponds to variant dbSNP:rs121908199EnsemblClinVar.1
Natural variantiVAR_009610422Q → H in CLN2; displays no residual enzyme activity; altered intracellular trafficking;. 3 PublicationsCorresponds to variant dbSNP:rs121908200EnsemblClinVar.1
Natural variantiVAR_016798428K → N in CLN2. 1 Publication1
Natural variantiVAR_005645447R → H in CLN2; displays very low residual enzyme activity; altered intracellular trafficking; demonstrates enhanced processing in response to folding improvement treatment; shows a five fold increase under permissive temperature conditions. 3 PublicationsCorresponds to variant dbSNP:rs119455956EnsemblClinVar.1
Natural variantiVAR_066888448A → V in CLN2. 1 Publication1
Natural variantiVAR_009611454A → E in CLN2. 1 PublicationCorresponds to variant dbSNP:rs121908201EnsemblClinVar.1
Natural variantiVAR_070917466V → G in SCAR7. 1 PublicationCorresponds to variant dbSNP:rs398122959EnsemblClinVar.1
Natural variantiVAR_016799473G → R in CLN2. 2 PublicationsCorresponds to variant dbSNP:rs121908203EnsemblClinVar.1
Natural variantiVAR_009612475S → L in CLN2; displays no residual enzyme activity; effectively transported to the lysosome. 2 PublicationsCorresponds to variant dbSNP:rs121908202EnsemblClinVar.1
Natural variantiVAR_016800481F → C in CLN2. 1 Publication1
Natural variantiVAR_058435482G → R in CLN2. 1 PublicationCorresponds to variant dbSNP:rs121908208EnsemblClinVar.1
Natural variantiVAR_066889501G → C in CLN2. 1 Publication1
Natural variantiVAR_066890504N → Y in CLN2. 1 Publication1
Natural variantiVAR_063641544P → S in CLN2; displays residual enzyme activity; effectively transported to the lysosome. 1 PublicationCorresponds to variant dbSNP:rs121908210EnsemblClinVar.1
Natural variantiVAR_066891548W → R in CLN2. 1 PublicationCorresponds to variant dbSNP:rs1348967263Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0131181 – 243Missing in isoform 2. 1 PublicationAdd BLAST243

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF017456 mRNA Translation: AAB80725.1
AF039704 Genomic DNA Translation: AAC98480.1
AF491290 mRNA Translation: AAM08412.1 Sequence problems.
AY268890 mRNA Translation: AAQ72732.1
AY358502 mRNA Translation: AAQ88866.1 Frameshift.
AK222499 mRNA Translation: BAD96219.1
BC014863 mRNA Translation: AAH14863.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS7770.1 [O14773-1]

NCBI Reference Sequences

More...
RefSeqi
NP_000382.3, NM_000391.3 [O14773-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.523454

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000299427; ENSP00000299427; ENSG00000166340 [O14773-1]
ENST00000533371; ENSP00000437066; ENSG00000166340 [O14773-2]
ENST00000642892; ENSP00000494165; ENSG00000166340 [O14773-2]
ENST00000645620; ENSP00000493657; ENSG00000166340 [O14773-2]
ENST00000647152; ENSP00000495893; ENSG00000166340 [O14773-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1200

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:1200

UCSC genome browser

More...
UCSCi
uc001mek.2 human [O14773-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NCL CLN2

Neural Ceroid Lipofuscinoses mutation db

Mendelian genes trieptidyl peptidase I (TPP1)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017456 mRNA Translation: AAB80725.1
AF039704 Genomic DNA Translation: AAC98480.1
AF491290 mRNA Translation: AAM08412.1 Sequence problems.
AY268890 mRNA Translation: AAQ72732.1
AY358502 mRNA Translation: AAQ88866.1 Frameshift.
AK222499 mRNA Translation: BAD96219.1
BC014863 mRNA Translation: AAH14863.1
CCDSiCCDS7770.1 [O14773-1]
RefSeqiNP_000382.3, NM_000391.3 [O14773-1]
UniGeneiHs.523454

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R60model-A196-563[»]
3EDYX-ray1.85A20-563[»]
3EE6X-ray2.35A/B1-563[»]
ProteinModelPortaliO14773
SMRiO14773
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107611, 25 interactors
DIPiDIP-47434N
IntActiO14773, 33 interactors
MINTiO14773
STRINGi9606.ENSP00000299427

Protein family/group databases

MEROPSiS53.003

PTM databases

GlyConnecti1858
iPTMnetiO14773
PhosphoSitePlusiO14773

Polymorphism and mutation databases

BioMutaiTPP1

Proteomic databases

EPDiO14773
jPOSTiO14773
MaxQBiO14773
PaxDbiO14773
PeptideAtlasiO14773
PRIDEiO14773
ProteomicsDBi48224
48225 [O14773-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
1200
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000299427; ENSP00000299427; ENSG00000166340 [O14773-1]
ENST00000533371; ENSP00000437066; ENSG00000166340 [O14773-2]
ENST00000642892; ENSP00000494165; ENSG00000166340 [O14773-2]
ENST00000645620; ENSP00000493657; ENSG00000166340 [O14773-2]
ENST00000647152; ENSP00000495893; ENSG00000166340 [O14773-2]
GeneIDi1200
KEGGihsa:1200
UCSCiuc001mek.2 human [O14773-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1200
DisGeNETi1200
EuPathDBiHostDB:ENSG00000166340.14

GeneCards: human genes, protein and diseases

More...
GeneCardsi
TPP1
GeneReviewsiTPP1

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0009410
HGNCiHGNC:2073 TPP1
HPAiHPA037709
HPA044868
MalaCardsiTPP1
MIMi204500 phenotype
607998 gene
609270 phenotype
neXtProtiNX_O14773
OpenTargetsiENSG00000166340
Orphaneti284324 Childhood-onset autosomal recessive slowly progressive spinocerebellar ataxia
228349 CLN2 disease
PharmGKBiPA26600

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IICY Eukaryota
COG4934 LUCA
GeneTreeiENSGT00390000008684
HOGENOMiHOG000171253
HOVERGENiHBG004449
InParanoidiO14773
KOiK01279
OMAiPGRHESQ
OrthoDBi1294880at2759
PhylomeDBiO14773
TreeFamiTF333497

Enzyme and pathway databases

BRENDAi3.4.14.9 2681
ReactomeiR-HSA-381038 XBP1(S) activates chaperone genes
SABIO-RKiO14773
SignaLinkiO14773

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
TPP1 human
EvolutionaryTraceiO14773

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Tripeptidyl_peptidase_I

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
1200
PMAP-CutDBiO14773

Protein Ontology

More...
PROi
PR:O14773

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000166340 Expressed in 215 organ(s), highest expression level in right adrenal gland cortex
CleanExiHS_TPP1
ExpressionAtlasiO14773 baseline and differential
GenevisibleiO14773 HS

Family and domain databases

CDDicd04056 Peptidases_S53, 1 hit
cd11377 Pro-peptidase_S53, 1 hit
Gene3Di3.40.50.200, 1 hit
InterProiView protein in InterPro
IPR036852 Peptidase_S8/S53_dom_sf
IPR015366 S53_propep
IPR030400 Sedolisin_dom
PfamiView protein in Pfam
PF09286 Pro-kuma_activ, 1 hit
SMARTiView protein in SMART
SM00944 Pro-kuma_activ, 1 hit
SUPFAMiSSF52743 SSF52743, 1 hit
PROSITEiView protein in PROSITE
PS51695 SEDOLISIN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTPP1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O14773
Secondary accession number(s): Q53HT1
, Q5JAK6, Q6UX56, Q71JP6, Q96C37
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 30, 2006
Last modified: January 16, 2019
This is version 194 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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