dbPTM

TPP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TPP1_HUMAN
UniProt AC	O14773
Protein Name	Tripeptidyl-peptidase 1
Gene Name	TPP1
Organism	Homo sapiens (Human).
Sequence Length	563
Subcellular Localization	Lysosome . Melanosome . Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Protein Description	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)..
Protein Sequence	MGLQACLLGLFALILSGKCSYSPEPDQRRTLPPGWVSLGRADPEEELSLTFALRQQNVERLSELVQAVSDPSSPQYGKYLTLENVADLVRPSPLTLHTVQKWLLAAGAQKCHSVITQDFLTCWLSIRQAELLLPGAEFHHYVGGPTETHVVRSPHPYQLPQALAPHVDFVGGLHRFPPTSSLRQRPEPQVTGTVGLHLGVTPSVIRKRYNLTSQDVGSGTSNNSQACAQFLEQYFHDSDLAQFMRLFGGNFAHQASVARVVGQQGRGRAGIEASLDVQYLMSAGANISTWVYSSPGRHEGQEPFLQWLMLLSNESALPHVHTVSYGDDEDSLSSAYIQRVNTELMKAAARGLTLLFASGDSGAGCWSVSGRHQFRPTFPASSPYVTTVGGTSFQEPFLITNEIVDYISGGGFSNVFPRPSYQEEAVTKFLSSSPHLPPSSYFNASGRAYPDVAALSDGYWVVSNRVPIPWVSGTSASTPVFGGILSLINEHRILSGRPPLGFLNPRLYQQHGAGLFDVTRGCHESCLDEEVEGQGFCSGPGWDPVTGWGTPNFPALLKTLLNP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
193	O-linked_Glycosylation	PEPQVTGTVGLHLGV CCCCCCCEEEEECCC	11.31	OGP
201	Phosphorylation	VGLHLGVTPSVIRKR EEEECCCCHHHHHHH	14.19	22817900
210	N-linked_Glycosylation	SVIRKRYNLTSQDVG HHHHHHCCCCCCCCC	40.66	19038967
222	N-linked_Glycosylation	DVGSGTSNNSQACAQ CCCCCCCCHHHHHHH	52.59	16399764
222	N-linked_Glycosylation	DVGSGTSNNSQACAQ CCCCCCCCHHHHHHH	52.59	16399764
256	Phosphorylation	GNFAHQASVARVVGQ CCHHHHHHHHHHHCC	15.11	23312004
286	N-linked_Glycosylation	YLMSAGANISTWVYS HHHHCCCCEEEEEEC	28.03	19038966
313	N-linked_Glycosylation	QWLMLLSNESALPHV HHHHHHCCCCCCCCE	47.41	19038967
346	Ubiquitination	RVNTELMKAAARGLT HHCHHHHHHHHCCCE	47.72	24816145
428	Sumoylation	YQEEAVTKFLSSSPH CCHHHHHHHHHCCCC	37.40	-
443	N-linked_Glycosylation	LPPSSYFNASGRAYP CCHHHHCCCCCCCCC	25.59	19038967
459	Phosphorylation	VAALSDGYWVVSNRV EEEECCCEEEEECCC	10.46	-
478	Phosphorylation	VSGTSASTPVFGGIL CCCCCCCCCCHHHHH	24.16	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
201	T	Phosphorylation	Kinase	CDK1	P06493	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	RNF8	O76064	PMID:22101936

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TPP1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of TPP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBP7_HUMAN	USP7	physical	25172512
TINF2_HUMAN	TINF2	physical	25172512
TERT_HUMAN	TERT	physical	25172512
POTE1_HUMAN	POT1	physical	25172512
CTC1_HUMAN	CTC1	physical	25172512
STN1_HUMAN	OBFC1	physical	25172512
OMA1_HUMAN	OMA1	physical	28514442
NDKM_HUMAN	NME4	physical	28514442
GDC_HUMAN	SLC25A16	physical	28514442
RPTOR_HUMAN	RPTOR	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
204500	Ceroid lipofuscinosis, neuronal, 2 (CLN2)
609270	Spinocerebellar ataxia, autosomal recessive, 7 (SCAR7)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TPP1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Crystal structure and autoactivation pathway of the precursor form ofhuman tripeptidyl-peptidase 1, the enzyme deficient in late infantileceroid lipofuscinosis."; Guhaniyogi J., Sohar I., Das K., Stock A.M., Lobel P.; J. Biol. Chem. 284:3985-3997(2009). Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 20-563, ACTIVE SITE,DISULFIDE BONDS, CALCIUM-BINDING SITES, SUBUNIT, AUTOPROTEOLYTICCLEAVAGE, AND GLYCOSYLATION AT ASN-210; ASN-286; ASN-313 AND ASN-443.	19038967 [Abstract]
"Structure of tripeptidyl-peptidase I provides insight into themolecular basis of late infantile neuronal ceroid lipofuscinosis."; Pal A., Kraetzner R., Gruene T., Grapp M., Schreiber K., Gronborg M.,Urlaub H., Becker S., Asif A.R., Gartner J., Sheldrick G.M.,Steinfeld R.; J. Biol. Chem. 284:3976-3984(2009). Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS), ACTIVE SITE, CALCIUM-BINDINGSITES, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-210; ASN-286; ASN-313AND ASN-443.	19038966 [Abstract]
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-210; ASN-222; ASN-313 ANDASN-443, AND MASS SPECTROMETRY.	19159218 [Abstract]
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry."; Zhang H., Li X.-J., Martin D.B., Aebersold R.; Nat. Biotechnol. 21:660-666(2003). Cited for: GLYCOSYLATION AT ASN-443.	12754519 [Abstract]