TPP1
entrez
1200
canonical
uniprot
O14773
canonical
ensembl
ENSG00000166340
resolver
ensp
ENSP00000299427
resolver
genesymbol
TPP1
resolver
genesymbol_syn
CLN2
resolver
hgnc
HGNC:2073
resolver
uniprot
Q53HT1
resolver
uniprot
Q5JAK6
resolver
uniprot
Q6UX56
resolver
uniprot
Q71JP6
resolver
uniprot
Q96C37
resolver
uniprot_entry
TPP1_HUMAN
resolver
uniprot_sec
Q53HT1
resolver
uniprot_sec
Q5JAK6
resolver
uniprot_sec
Q6UX56
resolver
uniprot_sec
Q71JP6
resolver
uniprot_sec
Q96C37
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by diisopropyl fluorophosphate (DFP). {ECO:0000269|PubMed:11054422}.
uniprot
proteins
amino_acid_sequence
MGLQACLLGLFALILSGKCSYSPEPDQRRTLPPGWVSLGRADPEEELSLTFALRQQNVERLSELVQAVSDPSSPQYGKYLTLENVADLVRPSPLTLHTVQKWLLAAGAQKCHSVITQDFLTCWLSIRQAELLLPGAEFHHYVGGPTETHVVRSPHPYQLPQALAPHVDFVGGLHRFPPTSSLRQRPEPQVTGTVGLHLGVTPSVIRKRYNLTSQDVGSGTSNNSQACAQFLEQYFHDSDLAQFMRLFGGNFAHQASVARVVGQQGRGRAGIEASLDVQYLMSAGANISTWVYSSPGRHEGQEPFLQWLMLLSNESALPHVHTVSYGDDEDSLSSAYIQRVNTELMKAAARGLTLLFASGDSGAGCWSVSGRHQFRPTFPASSPYVTTVGGTSFQEPFLITNEIVDYISGGGFSNVFPRPSYQEEAVTKFLSSSPHLPPSSYFNASGRAYPDVAALSDGYWVVSNRVPIPWVSGTSASTPVFGGILSLINEHRILSGRPPLGFLNPRLYQQHGAGLFDVTRGCHESCLDEEVEGQGFCSGPGWDPVTGWGTPNFPALLKTLLNP
uniprot
proteins
disease_involvement
DISEASE: Ceroid lipofuscinosis, neuronal, 2 (CLN2) [MIM:204500]: A 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. {ECO:0000269|PubMed:10330339, ECO:0000269|PubMed:10665500, ECO:0000269|PubMed:11241479, ECO:0000269|PubMed:11339651, ECO:0000269|PubMed:11589012, ECO:0000269|PubMed:12376936, ECO:0000269|PubMed:12414822, ECO:0000269|PubMed:12698559, ECO:0000269|PubMed:14736728, ECO:0000269|PubMed:19201763, ECO:0000269|PubMed:20340139, ECO:0000269|PubMed:21990111, ECO:0000269|PubMed:22612257, ECO:0000269|PubMed:9295267}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Spinocerebellar ataxia, autosomal recessive, 7 (SCAR7) [MIM:609270]: A form of spinocerebellar ataxia, 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. {ECO:0000269|PubMed:23418007}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.14.9
uniprot
proteins
function
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). {ECO:0000269|PubMed:11054422, ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967}.
uniprot
proteins
mass_dalton
61248
uniprot
proteins
mutagenesis
MUTAGEN 236; /note="H->A: No effect."; /evidence="ECO:0000269|PubMed:11054422"; MUTAGEN 360; /note="D->A: Inactive. Impaired processing."; /evidence="ECO:0000269|PubMed:11054422"; MUTAGEN 475; /note="S->A: Inactive. Impaired processing."; /evidence="ECO:0000269|PubMed:11054422"; MUTAGEN 517; /note="D->A: Inactive. Impaired processing."; /evidence="ECO:0000269|PubMed:11054422
uniprot
proteins
post_translational_modification
PTM: Activated by autocatalytic proteolytical processing upon acidification (PubMed:11054422, PubMed:19038966, PubMed:19038967). N-glycosylation is required for processing and activity (PubMed:19038966, PubMed:19038967). {ECO:0000269|PubMed:11054422, ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967}.
uniprot
proteins
pubmed
10330339
uniprot
proteins
pubmed
10477428
uniprot
proteins
pubmed
10665500
uniprot
proteins
pubmed
11054422
uniprot
proteins
pubmed
11241479
uniprot
proteins
pubmed
11339651
uniprot
proteins
pubmed
11462245
uniprot
proteins
pubmed
11589012
uniprot
proteins
pubmed
12376936
uniprot
proteins
pubmed
12414822
uniprot
proteins
pubmed
12643545
uniprot
proteins
pubmed
12698559
uniprot
proteins
pubmed
12754519
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
14736728
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17081065
uniprot
proteins
pubmed
17237713
uniprot
proteins
pubmed
19038966
uniprot
proteins
pubmed
19038967
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19201763
uniprot
proteins
pubmed
19941651
uniprot
proteins
pubmed
20340139
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21990111
uniprot
proteins
pubmed
22612257
uniprot
proteins
pubmed
23418007
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
9295267
uniprot
proteins
pubmed
9653647
uniprot
proteins
sequence_length
563
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:19941651}. Melanosome {ECO:0000269|PubMed:12643545}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000269|PubMed:12643545}.
uniprot
proteins