CATC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CATC_HUMAN
• UniProt AC: P53634
• Protein Name: Dipeptidyl peptidase 1
• Gene Name: CTSC
• Organism: Homo sapiens (Human).
• Sequence Length: 463
• Subcellular Localization: Lysosome.
• Protein Description: Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII..
• Protein Sequence: MGAGPSLLLAALLLLLSGDGAVRCDTPANCTYLDLLGTWVFQVGSSGSQRDVNCSVMGPQEKKVVVYLQKLDTAYDDLGNSGHFTIIYNQGFEIVLNDYKWFAFFKYKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKKVGTASENVYVNIAHLKNSQEKYSNRLYKYDHNFVKAINAIQKSWTATTYMEYETLTLGDMIRRSGGHSRKIPRPKPAPLTAEIQQKILHLPTSWDWRNVHGINFVSPVRNQASCGSCYSFASMGMLEARIRILTNNSQTPILSPQEVVSCSQYAQGCEGGFPYLIAGKYAQDFGLVEEACFPYTGTDSPCKMKEDCFRYYSSEYHYVGGFYGGCNEALMKLELVHHGPMAVAFEVYDDFLHYKKGIYHHTGLRDPFNPFELTNHAVLLVGYGTDSASGMDYWIVKNSWGTGWGENGYFRIRRGTDECAIESIAVAATPIPKL

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
29	N-linked_Glycosylation	VRCDTPANCTYLDLL CCCCCCCCCCCHHHC	21.62	19167329
53	N-linked_Glycosylation	SGSQRDVNCSVMGPQ CCCCCEEEEEEECCC	19.35	19167329
53	N-linked_Glycosylation	SGSQRDVNCSVMGPQ CCCCCEEEEEEECCC	19.35	16399764
55	Phosphorylation	SQRDVNCSVMGPQEK CCCEEEEEEECCCCC	15.22	25690035
63	Acetylation	VMGPQEKKVVVYLQK EECCCCCEEEEEEEE	39.24	26051181
67	Phosphorylation	QEKKVVVYLQKLDTA CCCEEEEEEEECCCC	7.57	30108239
119	N-linked_Glycosylation	SKVTTYCNETMTGWV CEEEEEECHHHCHHH	37.04	19167329
133 (in isoform 2)	Ubiquitination	-	28.97	-
140	Acetylation	NWACFTGKKVGTASE CEEEECCCCEECCCC	41.02	26051181
141	Ubiquitination	WACFTGKKVGTASEN EEEECCCCEECCCCC	47.44	-
150	Phosphorylation	GTASENVYVNIAHLK ECCCCCEEEEEEHHH	10.20	-
169	Ubiquitination	KYSNRLYKYDHNFVK HHHHCCEECCHHHHH	49.12	-
188	Phosphorylation	IQKSWTATTYMEYET HHHHCCEEECCEEEE	15.87	30576142
190	Phosphorylation	KSWTATTYMEYETLT HHCCEEECCEEEEEE	5.43	30576142
195	Phosphorylation	TTYMEYETLTLGDMI EECCEEEEEEHHHHH	24.92	30576142
216	Ubiquitination	SRKIPRPKPAPLTAE CCCCCCCCCCCCCHH	55.90	29967540
254	Phosphorylation	SPVRNQASCGSCYSF CCCCCCCCCCCCHHH	14.83	-
257	Phosphorylation	RNQASCGSCYSFASM CCCCCCCCCHHHHHH	17.76	-
276	N-linked_Glycosylation	ARIRILTNNSQTPIL HHEEHHHCCCCCCCC	42.59	16399764
276	N-linked_Glycosylation	ARIRILTNNSQTPIL HHEEHHHCCCCCCCC	42.59	16399764
329	Phosphorylation	FPYTGTDSPCKMKED CCCCCCCCCCCCCHH	31.84	25627689
334	Ubiquitination	TDSPCKMKEDCFRYY CCCCCCCCHHHHHHH	35.58	-
334	Acetylation	TDSPCKMKEDCFRYY CCCCCCCCHHHHHHH	35.58	26822725
345	Phosphorylation	FRYYSSEYHYVGGFY HHHHHCCCEECCEEC	10.61	-
347	Phosphorylation	YYSSEYHYVGGFYGG HHHCCCEECCEECCC	10.41	-
352	Phosphorylation	YHYVGGFYGGCNEAL CEECCEECCCHHHHH	18.84	-
388	Phosphorylation	LHYKKGIYHHTGLRD HHHCCCCCCCCCCCC	9.02	-
452	Phosphorylation	TDECAIESIAVAATP CCCCCEEEEEEECCC	15.10	-

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

Oops, there are no upstream regulatory protein records of CATC_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
29	N	Glycosylation	While glycosylation at Asn-53, Asn-119 and Asn-276 is mediated by STT3A-containing complexes, glycosylation at Asn-29 is mediated STT3B-containing complexes.	19167329
53	N	Glycosylation	While glycosylation at Asn-53, Asn-119 and Asn-276 is mediated by STT3A-containing complexes, glycosylation at Asn-29 is mediated STT3B-containing complexes.	19167329
119	N	Glycosylation	While glycosylation at Asn-53, Asn-119 and Asn-276 is mediated by STT3A-containing complexes, glycosylation at Asn-29 is mediated STT3B-containing complexes.	19167329
276	N	Glycosylation	While glycosylation at Asn-53, Asn-119 and Asn-276 is mediated by STT3A-containing complexes, glycosylation at Asn-29 is mediated STT3B-containing complexes.	19167329

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CATC_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CD81_HUMAN	CD81	physical	22939629
PUR8_HUMAN	ADSL	physical	22863883
ANKY2_HUMAN	ANKMY2	physical	22863883
ARI1_HUMAN	ARIH1	physical	22863883
ARMC9_HUMAN	ARMC9	physical	22863883

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 245000: Papillon-Lefevre syndrome (PLS)
• 245010: Haim-Munk syndrome (HMS)
• 170650: Periodontititis, aggressive, 1 (AP1)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Structure of human dipeptidyl peptidase I (cathepsin C): exclusiondomain added to an endopeptidase framework creates the machine foractivation of granular serine proteases.";
Turk D., Janjic V., Stern I., Podobnik M., Lamba D., Dahl S.W.,Lauritzen C., Pedersen J., Turk V., Turk B.;
EMBO J. 20:6570-6582(2001).
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 25-143 AND 231-463 INCOMPLEX WITH CHLORIDE IONS, SUBUNIT, DISULFIDE BONDS, ANDGLYCOSYLATION AT ASN-29.
PubMed: 11726493

"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-53, AND MASS SPECTROMETRY.
PubMed: 19159218