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HUMAN:TPP1

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) TPP1 (synonyms: CLN2)
Protein Name(s) Tripeptidyl-peptidase 1

TPP-1 Cell growth-inhibiting gene 1 protein Lysosomal pepstatin-insensitive protease LPIC Tripeptidyl aminopeptidase Tripeptidyl-peptidase I TPP-I

External Links
UniProt O14773
EMBL AF017456
AF039704
AF491290
AY268890
AY358502
AK222499
BC014863
CCDS CCDS7770.1
RefSeq NP_000382.3
UniGene Hs.523454
PDB 1R60
3EDY
3EE6
PDBsum 1R60
3EDY
3EE6
ProteinModelPortal O14773
SMR O14773
BioGrid 107611
DIP DIP-47434N
IntAct O14773
MINT MINT-5002180
STRING 9606.ENSP00000299427
MEROPS S53.003
iPTMnet O14773
PhosphoSite O14773
BioMuta TPP1
EPD O14773
MaxQB O14773
PaxDb O14773
PRIDE O14773
DNASU 1200
Ensembl ENST00000299427
ENST00000533371
GeneID 1200
KEGG hsa:1200
UCSC uc001mek.2
CTD 1200
GeneCards TPP1
GeneReviews TPP1
H-InvDB HIX0009410
HGNC HGNC:2073
HPA HPA037709
MalaCards TPP1
MIM 204500
607998
609270
neXtProt NX_O14773
Orphanet 284324
228349
PharmGKB PA26600
eggNOG ENOG410IICY
COG4934
GeneTree ENSGT00390000008684
HOGENOM HOG000171253
HOVERGEN HBG004449
InParanoid O14773
KO K01279
OMA GNFAHQA
OrthoDB EOG7RNJZW
PhylomeDB O14773
TreeFam TF333497
BRENDA 3.4.14.9
Reactome [www.reactome.org/content/detail/R-HSA-381038 R-HSA-381038]
SABIO-RK O14773
SignaLink O14773
ChiTaRS TPP1
EvolutionaryTrace O14773
GeneWiki Tripeptidyl_peptidase_I
GenomeRNAi 1200
PMAP-CutDB O14773
PRO PR:O14773
Proteomes UP000005640
Bgee O14773
CleanEx HS_TPP1
ExpressionAtlas O14773
Genevisible O14773
GO GO:0070062
GO:0043202
GO:0005764
GO:0042470
GO:0005739
GO:0004175
GO:0046872
GO:0008233
GO:0042277
GO:0004252
GO:0008236
GO:0008240
GO:0045453
GO:0007417
GO:0030855
GO:0036498
GO:0006629
GO:0007040
GO:0007399
GO:0050885
GO:0043171
GO:0030163
GO:0006508
Gene3D 3.40.50.200
InterPro IPR015366
IPR000209
IPR009020
IPR030400
Pfam PF09286
SMART SM00944
SUPFAM SSF52743
SSF54897
PROSITE PS51695

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0070198

protein localization to chromosome, telomeric region

PMID:20404094[1]

ECO:0000315

P

Figure 1: D and E show hTR associates less with telomeres in HeLa cells when TPP1 is knocked down.

complete
CACAO 12103

part_of

GO:0005764

lysosome

PMID:19941651[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0070062

extracellular exosome

PMID:23533145[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0070062

extracellular exosome

PMID:19056867[4]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(UBERON:0001088)

Seeded From UniProt

complete

involved_in

GO:0030855

epithelial cell differentiation

PMID:21492153[5]

ECO:0000270

expression pattern evidence used in manual assertion

P

results_in_acquisition_of_features_of:(CL:1000334)

Seeded From UniProt

complete

involved_in

GO:0050885

neuromuscular process controlling balance

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:O89023

P

Seeded From UniProt

complete

involved_in

GO:0045453

bone resorption

PMID:8215436[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043171

peptide catabolic process

PMID:15158442[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043171

peptide catabolic process

PMID:9989590[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042277

peptide binding

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q9EQV6

F

Seeded From UniProt

complete

involved_in

GO:0030163

protein catabolic process

PMID:10740217[9]

ECO:0000303

author statement without traceable support used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008240

tripeptidyl-peptidase activity

PMID:10679303[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008240

tripeptidyl-peptidase activity

PMID:10617131[11]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008240

tripeptidyl-peptidase activity

PMID:10965052[12]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008240

tripeptidyl-peptidase activity

PMID:12134079[13]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008240

tripeptidyl-peptidase activity

PMID:11054422[14]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008236

serine-type peptidase activity

PMID:11054422[14]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

PMID:9295267[15]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0007399

nervous system development

PMID:9295267[15]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0007040

lysosome organization

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:O89023

P

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

PMID:9295267[15]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

PMID:10965052[12]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005764

lysosome

PMID:9295267[15]

ECO:0000315

mutant phenotype evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005764

lysosome

PMID:15317752[16]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004175

endopeptidase activity

PMID:10679303[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004175

endopeptidase activity

PMID:10965052[12]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008240

tripeptidyl-peptidase activity

PMID:21873635[17]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000368455
RGD:621296
UniProtKB:O14773
UniProtKB:Q70J59
dictyBase:DDB_G0269914

F

Seeded From UniProt

complete

involved_in

GO:0007417

central nervous system development

PMID:21873635[17]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001022357
ZFIN:ZDB-GENE-030131-6654

P

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

PMID:21873635[17]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000368455
RGD:621296
UniProtKB:O14773
UniProtKB:Q70DX9

P

Seeded From UniProt

complete

enables

GO:0004175

endopeptidase activity

PMID:21873635[17]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000368455
RGD:621296
UniProtKB:O14773

F

Seeded From UniProt

complete

involved_in

GO:0050885

neuromuscular process controlling balance

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O89023
ensembl:ENSMUSP00000033184

P

Seeded From UniProt

complete

involved_in

GO:0007040

lysosome organization

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O89023
ensembl:ENSMUSP00000033184

P

Seeded From UniProt

complete

part_of

GO:0005764

lysosome

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O89023
ensembl:ENSMUSP00000033184

C

Seeded From UniProt

complete

enables

GO:0004252

serine-type endopeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR036852

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR030400
InterPro:IPR036852

P

Seeded From UniProt

complete

enables

GO:0008236

serine-type peptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR015366

F

Seeded From UniProt

complete

involved_in

GO:0006629

lipid metabolic process

PMID:9295267[15]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0043202

lysosomal lumen

Reactome:R-HSA-1791138

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0036498

IRE1-mediated unfolded protein response

Reactome:R-HSA-381070

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005764

lysosome

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0458
UniProtKB-SubCell:SL-0158

C

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0008236

serine-type peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0720

F

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

part_of

GO:0042470

melanosome

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0161

C

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ Abreu, E et al. (2010) TIN2-tethered TPP1 recruits human telomerase to telomeres in vivo. Mol. Cell. Biol. 30 2971-82 PubMed GONUTS page
  2. ↑ Lyly, A et al. (2009) Novel interactions of CLN5 support molecular networking between Neuronal Ceroid Lipofuscinosis proteins. BMC Cell Biol. 10 83 PubMed GONUTS page
  3. ↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
  4. ↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
  5. ↑ Buhrke, T et al. (2011) Analysis of proteomic changes induced upon cellular differentiation of the human intestinal cell line Caco-2. Dev. Growth Differ. 53 411-26 PubMed GONUTS page
  6. ↑ Page, AE et al. (1993) Purification and characterization of a tripeptidyl peptidase I from human osteoclastomas: evidence for its role in bone resorption. Arch. Biochem. Biophys. 306 354-9 PubMed GONUTS page
  7. ↑ Kopan, S et al. (2004) The lysosomal degradation of neuromedin B is dependent on tripeptidyl peptidase-I: evidence for the impairment of neuropeptide degradation in late-infantile neuronal ceroid lipofuscinosis. Biochem. Biophys. Res. Commun. 319 58-65 PubMed GONUTS page
  8. ↑ Vines, DJ & Warburton, MJ (1999) Classical late infantile neuronal ceroid lipofuscinosis fibroblasts are deficient in lysosomal tripeptidyl peptidase I. FEBS Lett. 443 131-5 PubMed GONUTS page
  9. ↑ Dawson, G & Cho, S (2000) Batten's disease: clues to neuronal protein catabolism in lysosomes. J. Neurosci. Res. 60 133-40 PubMed GONUTS page
  10. ↑ 10.0 10.1 Ezaki, J et al. (2000) Characterization of endopeptidase activity of tripeptidyl peptidase-I/CLN2 protein which is deficient in classical late infantile neuronal ceroid lipofuscinosis. Biochem. Biophys. Res. Commun. 268 904-8 PubMed GONUTS page
  11. ↑ Junaid, MA et al. (2000) Purification and characterization of bovine brain lysosomal pepstatin-insensitive proteinase, the gene product deficient in the human late-infantile neuronal ceroid lipofuscinosis. J. Neurochem. 74 287-94 PubMed GONUTS page
  12. ↑ 12.0 12.1 12.2 Ezaki, J et al. (2000) Tripeptidyl peptidase I, the late infantile neuronal ceroid lipofuscinosis gene product, initiates the lysosomal degradation of subunit c of ATP synthase. J. Biochem. 128 509-16 PubMed GONUTS page
  13. ↑ Vesa, J et al. (2002) Neuronal ceroid lipofuscinoses are connected at molecular level: interaction of CLN5 protein with CLN2 and CLN3. Mol. Biol. Cell 13 2410-20 PubMed GONUTS page
  14. ↑ 14.0 14.1 Lin, L et al. (2001) The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH. J. Biol. Chem. 276 2249-55 PubMed GONUTS page
  15. ↑ 15.0 15.1 15.2 15.3 15.4 Sleat, DE et al. (1997) Association of mutations in a lysosomal protein with classical late-infantile neuronal ceroid lipofuscinosis. Science 277 1802-5 PubMed GONUTS page
  16. ↑ Steinfeld, R et al. (2004) Mutations in classical late infantile neuronal ceroid lipofuscinosis disrupt transport of tripeptidyl-peptidase I to lysosomes. Hum. Mol. Genet. 13 2483-91 PubMed GONUTS page
  17. ↑ 17.0 17.1 17.2 17.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
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