TPP1 | ENSG00000166340 | NCBI 1200

Details for: TPP1

Gene ID: 1200

Symbol: TPP1

Ensembl ID: ENSG00000166340

Description: tripeptidyl peptidase 1

Associated with

Cellular responses to stimuli
(R-HSA-8953897)
Cellular responses to stress
(R-HSA-2262752)
Ire1alpha activates chaperones
(R-HSA-381070)
Unfolded protein response (upr)
(R-HSA-381119)
Xbp1(s) activates chaperone genes
(R-HSA-381038)
Bone resorption
(GO:0045453)
Central nervous system development
(GO:0007417)
Endopeptidase activity
(GO:0004175)
Epithelial cell differentiation
(GO:0030855)
Extracellular exosome
(GO:0070062)
Golgi apparatus
(GO:0005794)
Lipid metabolic process
(GO:0006629)
Lysophosphatidic acid binding
(GO:0035727)
Lysosomal lumen
(GO:0043202)
Lysosomal protein catabolic process
(GO:1905146)
Lysosome
(GO:0005764)
Lysosome organization
(GO:0007040)
Melanosome
(GO:0042470)
Membrane raft
(GO:0045121)
Metal ion binding
(GO:0046872)
Nervous system development
(GO:0007399)
Neuromuscular process controlling balance
(GO:0050885)
Peptidase activity
(GO:0008233)
Peptide binding
(GO:0042277)
Peptide catabolic process
(GO:0043171)
Protein binding
(GO:0005515)
Protein catabolic process
(GO:0030163)
Protein localization to chromosome, telomeric region
(GO:0070198)
Proteolysis
(GO:0006508)
Recycling endosome
(GO:0055037)
Serine-type endopeptidase activity
(GO:0004252)
Serine-type peptidase activity
(GO:0008236)
Sulfatide binding
(GO:0120146)
Tripeptidyl-peptidase activity
(GO:0008240)

Other Information

Proteins

Tripeptidyl-peptidase 1

Genular Protein ID: 1332768125

Symbol: TPP1_HUMAN

Name: Tripeptidyl-peptidase 1

UniProtKB Accession Codes:

O14773 Q53HT1 Q5JAK6 Q6UX56 Q71JP6 Q96C37

Database IDs:

Citations:

PubMed ID: 9295267

Title: Association of mutations in a lysosomal protein with classical late-infantile neuronal ceroid lipofuscinosis.

PubMed ID: 9295267

DOI: 10.1126/science.277.5333.1802

PubMed ID: 9653647

Title: Structural organization and sequence of CLN2, the defective gene in classical late infantile neuronal ceroid lipofuscinosis.

PubMed ID: 9653647

DOI: 10.1006/geno.1998.5328

PubMed ID: 12975309

Title: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.

PubMed ID: 12975309

DOI: 10.1101/gr.1293003

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 11054422

Title: The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH.

PubMed ID: 11054422

DOI: 10.1074/jbc.m008562200

PubMed ID: 12643545

Title: Proteomic analysis of early melanosomes: identification of novel melanosomal proteins.

PubMed ID: 12643545

DOI: 10.1021/pr025562r

PubMed ID: 12754519

Title: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.

PubMed ID: 12754519

DOI: 10.1038/nbt827

PubMed ID: 10477428

Title: Molecular basis of the neuronal ceroid lipofuscinoses: mutations in CLN1, CLN2, CLN3, and CLN5.

PubMed ID: 10477428

DOI: 10.1002/(sici)1098-1004(1999)14:3<199::aid-humu3>3.0.co;2-a

PubMed ID: 17081065

Title: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.

PubMed ID: 17081065

DOI: 10.1021/pr060363j

PubMed ID: 17237713

Title: Neuronal ceroid lipofuscinosis: a common pathway?

PubMed ID: 17237713

DOI: 10.1203/pdr.0b013e31802d8a4a

PubMed ID: 19941651

Title: Novel interactions of CLN5 support molecular networking between neuronal ceroid lipofuscinosis proteins.

PubMed ID: 19941651

DOI: 10.1186/1471-2121-10-83

PubMed ID: 19159218

Title: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.

PubMed ID: 19159218

DOI: 10.1021/pr8008012

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 19038966

Title: Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.

PubMed ID: 19038966

DOI: 10.1074/jbc.m806947200

PubMed ID: 19038967

Title: Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.

PubMed ID: 19038967

DOI: 10.1074/jbc.m806943200

PubMed ID: 10330339

Title: Mutational analysis of the defective protease in classic late-infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.

PubMed ID: 10330339

DOI: 10.1086/302427

PubMed ID: 10665500

Title: Prenatal testing for late infantile neuronal ceroid lipofuscinosis.

PubMed ID: 10665500

DOI: 10.1002/1531-8249(200002)47:2<254::aid-ana19>3.3.co;2-z

PubMed ID: 11339651

Title: Heterogeneity of late-infantile neuronal ceroid lipofuscinosis.

PubMed ID: 11339651

DOI: 10.1097/00125817-200011000-00002

PubMed ID: 11241479

Title: Two novel CLN2 gene mutations in a Chinese patient with classical late-infantile neuronal ceroid lipofuscinosis.

PubMed ID: 11241479

DOI: 10.1002/1096-8628(2001)9999:9999<::aid-ajmg1145>3.0.co;2-z

PubMed ID: 11589012

Title: New mutations in the neuronal ceroid lipofuscinosis genes.

PubMed ID: 11589012

DOI: 10.1053/ejpn.2000.0427

PubMed ID: 11462245

Title: Expression and analysis of CLN2 variants in CHO cells: Q100R represents a polymorphism, and G389E and R447H represent loss-of-function mutations.

PubMed ID: 11462245

DOI: 10.1002/humu.1170

PubMed ID: 12376936

Title: Late infantile neuronal ceroid lipofuscinosis: quantitative description of the clinical course in patients with CLN2 mutations.

PubMed ID: 12376936

DOI: 10.1002/ajmg.10660

PubMed ID: 12414822

Title: Identification of novel CLN2 mutations shows Canadian specific NCL2 alleles.

PubMed ID: 12414822

DOI: 10.1136/jmg.39.11.822

PubMed ID: 12698559

Title: Tripeptidyl peptidase 1 deficiency in neuronal ceroid lipofuscinosis. A novel mutation.

PubMed ID: 12698559

PubMed ID: 14736728

Title: Mutation of the glycosylated asparagine residue 286 in human CLN2 protein results in loss of enzymatic activity.

PubMed ID: 14736728

DOI: 10.1093/glycob/cwh054

PubMed ID: 19201763

Title: Mutations in CLN7/MFSD8 are a common cause of variant late-infantile neuronal ceroid lipofuscinosis.

PubMed ID: 19201763

DOI: 10.1093/brain/awn366

PubMed ID: 20340139

Title: Functional consequences and rescue potential of pathogenic missense mutations in tripeptidyl peptidase I.

PubMed ID: 20340139

DOI: 10.1002/humu.21251

PubMed ID: 22612257

Title: Targeted next generation sequencing as a diagnostic tool in epileptic disorders.

PubMed ID: 22612257

DOI: 10.1111/j.1528-1167.2012.03516.x

PubMed ID: 21990111

Title: Update of the mutation spectrum and clinical correlations of over 360 mutations in eight genes that underlie the neuronal ceroid lipofuscinoses.

PubMed ID: 21990111

DOI: 10.1002/humu.21624

PubMed ID: 23418007

Title: Autosomal recessive spinocerebellar ataxia 7 (SCAR7) is caused by variants in TPP1, the gene involved in classic late-infantile neuronal ceroid lipofuscinosis 2 disease (CLN2 disease).

PubMed ID: 23418007

DOI: 10.1002/humu.22292

Sequence Information:

Length: 563
Mass: 61248
Checksum: 7299D902F6AE8555
Sequence:

MGLQACLLGL FALILSGKCS YSPEPDQRRT LPPGWVSLGR ADPEEELSLT FALRQQNVER 
LSELVQAVSD PSSPQYGKYL TLENVADLVR PSPLTLHTVQ KWLLAAGAQK CHSVITQDFL 
TCWLSIRQAE LLLPGAEFHH YVGGPTETHV VRSPHPYQLP QALAPHVDFV GGLHRFPPTS 
SLRQRPEPQV TGTVGLHLGV TPSVIRKRYN LTSQDVGSGT SNNSQACAQF LEQYFHDSDL 
AQFMRLFGGN FAHQASVARV VGQQGRGRAG IEASLDVQYL MSAGANISTW VYSSPGRHEG 
QEPFLQWLML LSNESALPHV HTVSYGDDED SLSSAYIQRV NTELMKAAAR GLTLLFASGD 
SGAGCWSVSG RHQFRPTFPA SSPYVTTVGG TSFQEPFLIT NEIVDYISGG GFSNVFPRPS 
YQEEAVTKFL SSSPHLPPSS YFNASGRAYP DVAALSDGYW VVSNRVPIPW VSGTSASTPV 
FGGILSLINE HRILSGRPPL GFLNPRLYQQ HGAGLFDVTR GCHESCLDEE VEGQGFCSGP 
GWDPVTGWGT PNFPALLKTL LNP

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: TPP1

Associated with

Other Information

Association of mutations in a lysosomal protein with classical late-infantile neuronal ceroid lipofuscinosis. PubMed ID: 9295267

Structural organization and sequence of CLN2, the defective gene in classical late infantile neuronal ceroid lipofuscinosis. PubMed ID: 9653647

The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. PubMed ID: 12975309

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH. PubMed ID: 11054422

Proteomic analysis of early melanosomes: identification of novel melanosomal proteins. PubMed ID: 12643545

Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. PubMed ID: 12754519

Molecular basis of the neuronal ceroid lipofuscinoses: mutations in CLN1, CLN2, CLN3, and CLN5. PubMed ID: 10477428

Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. PubMed ID: 17081065

Neuronal ceroid lipofuscinosis: a common pathway? PubMed ID: 17237713

Novel interactions of CLN5 support molecular networking between neuronal ceroid lipofuscinosis proteins. PubMed ID: 19941651

Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. PubMed ID: 19159218

Initial characterization of the human central proteome. PubMed ID: 21269460

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

N-terminome analysis of the human mitochondrial proteome. PubMed ID: 25944712

Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis. PubMed ID: 19038966

Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis. PubMed ID: 19038967

Mutational analysis of the defective protease in classic late-infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder. PubMed ID: 10330339

Prenatal testing for late infantile neuronal ceroid lipofuscinosis. PubMed ID: 10665500

Heterogeneity of late-infantile neuronal ceroid lipofuscinosis. PubMed ID: 11339651

Two novel CLN2 gene mutations in a Chinese patient with classical late-infantile neuronal ceroid lipofuscinosis. PubMed ID: 11241479

New mutations in the neuronal ceroid lipofuscinosis genes. PubMed ID: 11589012

Expression and analysis of CLN2 variants in CHO cells: Q100R represents a polymorphism, and G389E and R447H represent loss-of-function mutations. PubMed ID: 11462245

Late infantile neuronal ceroid lipofuscinosis: quantitative description of the clinical course in patients with CLN2 mutations. PubMed ID: 12376936

Identification of novel CLN2 mutations shows Canadian specific NCL2 alleles. PubMed ID: 12414822

Tripeptidyl peptidase 1 deficiency in neuronal ceroid lipofuscinosis. A novel mutation. PubMed ID: 12698559

Mutation of the glycosylated asparagine residue 286 in human CLN2 protein results in loss of enzymatic activity. PubMed ID: 14736728

Mutations in CLN7/MFSD8 are a common cause of variant late-infantile neuronal ceroid lipofuscinosis. PubMed ID: 19201763

Functional consequences and rescue potential of pathogenic missense mutations in tripeptidyl peptidase I. PubMed ID: 20340139

Targeted next generation sequencing as a diagnostic tool in epileptic disorders. PubMed ID: 22612257

Update of the mutation spectrum and clinical correlations of over 360 mutations in eight genes that underlie the neuronal ceroid lipofuscinoses. PubMed ID: 21990111

Autosomal recessive spinocerebellar ataxia 7 (SCAR7) is caused by variants in TPP1, the gene involved in classic late-infantile neuronal ceroid lipofuscinosis 2 disease (CLN2 disease). PubMed ID: 23418007