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Showing Protein Tripeptidyl-peptidase 1 (HMDBP14587)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP14587
Secondary Accession Numbers None
Name Tripeptidyl-peptidase 1
Synonyms
  1. TPP-1
  2. Cell growth-inhibiting gene 1 protein
  3. Lysosomal pepstatin-insensitive protease
  4. Tripeptidyl aminopeptidase
  5. Tripeptidyl-peptidase I
  6. LPIC
  7. TPP-I
Gene Name TPP1
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Lysosomal serine protease with tripeptidyl-peptidase I activity (PubMed:11054422, PubMed:19038966, PubMed:19038967). May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases (PubMed:11054422, PubMed:19038966, PubMed:19038967). Requires substrates with an unsubstituted N-terminus (PubMed:19038966).
Pathways
  • Lysosome
Reactions Not Available
GO Classification
Biological Process
neuromuscular process controlling balance
protein localization to chromosome, telomeric region
protein catabolic process
peptide catabolic process
IRE1-mediated unfolded protein response
nervous system development
proteolysis
lysosomal protein catabolic process
lipid metabolic process
bone resorption
epithelial cell differentiation
central nervous system development
lysosome organization
Cellular Component
membrane raft
extracellular vesicular exosome
Golgi apparatus
lysosomal lumen
melanosome
lysosome
recycling endosome
Molecular Function
endopeptidase activity
metal ion binding
peptidase activity
lysophosphatidic acid binding
sulfatide binding
tripeptidyl-peptidase activity
peptide binding
serine-type peptidase activity
serine-type endopeptidase activity
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 563
Molecular Weight 61247.46
Theoretical pI 6.479
Pfam Domain Function
Signals
  • 1-19;
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID O14773
UniProtKB/Swiss-Prot Entry Name TPP1_HUMAN
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
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  5. Basrur V, Yang F, Kushimoto T, Higashimoto Y, Yasumoto K, Valencia J, Muller J, Vieira WD, Watabe H, Shabanowitz J, Hearing VJ, Hunt DF, Appella E: Proteomic analysis of early melanosomes: identification of novel melanosomal proteins. J Proteome Res. 2003 Jan-Feb;2(1):69-79. [PubMed:12643545 ]
  6. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed:12754519 ]
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  9. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [PubMed:24275569 ]
  10. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [PubMed:25944712 ]
  11. Lyly A, von Schantz C, Heine C, Schmiedt ML, Sipila T, Jalanko A, Kyttala A: Novel interactions of CLN5 support molecular networking between Neuronal Ceroid Lipofuscinosis proteins. BMC Cell Biol. 2009 Nov 26;10:83. doi: 10.1186/1471-2121-10-83. [PubMed:19941651 ]
  12. Sleat DE, Donnelly RJ, Lackland H, Liu CG, Sohar I, Pullarkat RK, Lobel P: Association of mutations in a lysosomal protein with classical late-infantile neuronal ceroid lipofuscinosis. Science. 1997 Sep 19;277(5333):1802-5. doi: 10.1126/science.277.5333.1802. [PubMed:9295267 ]
  13. Liu CG, Sleat DE, Donnelly RJ, Lobel P: Structural organization and sequence of CLN2, the defective gene in classical late infantile neuronal ceroid lipofuscinosis. Genomics. 1998 Jun 1;50(2):206-12. doi: 10.1006/geno.1998.5328. [PubMed:9653647 ]
  14. Lin L, Sohar I, Lackland H, Lobel P: The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH. J Biol Chem. 2001 Jan 19;276(3):2249-55. doi: 10.1074/jbc.M008562200. Epub 2000 Oct 27. [PubMed:11054422 ]
  15. Mole SE, Mitchison HM, Munroe PB: Molecular basis of the neuronal ceroid lipofuscinoses: mutations in CLN1, CLN2, CLN3, and CLN5. Hum Mutat. 1999;14(3):199-215. doi: 10.1002/(SICI)1098-1004(1999)14:3<199::AID-HUMU3>3.0.CO;2-A. [PubMed:10477428 ]
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  17. Guhaniyogi J, Sohar I, Das K, Stock AM, Lobel P: Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis. J Biol Chem. 2009 Feb 6;284(6):3985-97. doi: 10.1074/jbc.M806943200. Epub 2008 Nov 26. [PubMed:19038967 ]
  18. Sleat DE, Gin RM, Sohar I, Wisniewski K, Sklower-Brooks S, Pullarkat RK, Palmer DN, Lerner TJ, Boustany RM, Uldall P, Siakotos AN, Donnelly RJ, Lobel P: Mutational analysis of the defective protease in classic late-infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder. Am J Hum Genet. 1999 Jun;64(6):1511-23. doi: 10.1086/302427. [PubMed:10330339 ]
  19. Berry-Kravis E, Sleat DE, Sohar I, Meyer P, Donnelly R, Lobel P: Prenatal testing for late infantile neuronal ceroid lipofuscinosis. Ann Neurol. 2000 Feb;47(2):254-7. [PubMed:10665500 ]
  20. Zhong N, Moroziewicz DN, Ju W, Jurkiewicz A, Johnston L, Wisniewski KE, Brown WT: Heterogeneity of late-infantile neuronal ceroid lipofuscinosis. Genet Med. 2000 Nov-Dec;2(6):312-8. doi: 10.1097/00125817-200011000-00002. [PubMed:11339651 ]
  21. Mole SE, Zhong NA, Sarpong A, Logan WP, Hofmann S, Yi W, Franken PF, van Diggelen OP, Breuning MH, Moroziewicz D, Ju W, Salonen T, Holmberg V, Jarvela I, Taschner PE: New mutations in the neuronal ceroid lipofuscinosis genes. Eur J Paediatr Neurol. 2001;5 Suppl A:7-10. doi: 10.1053/ejpn.2000.0427. [PubMed:11589012 ]
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  23. Steinfeld R, Heim P, von Gregory H, Meyer K, Ullrich K, Goebel HH, Kohlschutter A: Late infantile neuronal ceroid lipofuscinosis: quantitative description of the clinical course in patients with CLN2 mutations. Am J Med Genet. 2002 Nov 1;112(4):347-54. doi: 10.1002/ajmg.10660. [PubMed:12376936 ]
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  25. Tsiakas K, Steinfeld R, Storch S, Ezaki J, Lukacs Z, Kominami E, Kohlschutter A, Ullrich K, Braulke T: Mutation of the glycosylated asparagine residue 286 in human CLN2 protein results in loss of enzymatic activity. Glycobiology. 2004 Apr;14(4):1C-5C. doi: 10.1093/glycob/cwh054. Epub 2004 Jan 21. [PubMed:14736728 ]
  26. Walus M, Kida E, Golabek AA: Functional consequences and rescue potential of pathogenic missense mutations in tripeptidyl peptidase I. Hum Mutat. 2010 Jun;31(6):710-21. doi: 10.1002/humu.21251. [PubMed:20340139 ]
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  28. Sun Y, Almomani R, Breedveld GJ, Santen GW, Aten E, Lefeber DJ, Hoff JI, Brusse E, Verheijen FW, Verdijk RM, Kriek M, Oostra B, Breuning MH, Losekoot M, den Dunnen JT, van de Warrenburg BP, Maat-Kievit AJ: 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). Hum Mutat. 2013 May;34(5):706-13. doi: 10.1002/humu.22292. Epub 2013 Mar 11. [PubMed:23418007 ]