CATL1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CATL1_HUMAN
• UniProt AC: P07711
• Protein Name: Cathepsin L1
• Gene Name: CTSL
• Organism: Homo sapiens (Human).
• Sequence Length: 333
• Subcellular Localization: Lysosome.
• Protein Description: Important for the overall degradation of proteins in lysosomes..
• Protein Sequence: MNPTLILAAFCLGIASATLTFDHSLEAQWTKWKAMHNRLYGMNEEGWRRAVWEKNMKMIELHNQEYREGKHSFTMAMNAFGDMTSEEFRQVMNGFQNRKPRKGKVFQEPLFYEAPRSVDWREKGYVTPVKNQGQCGSCWAFSATGALEGQMFRKTGRLISLSEQNLVDCSGPQGNEGCNGGLMDYAFQYVQDNGGLDSEESYPYEATEESCKYNPKYSVANDTGFVDIPKQEKALMKAVATVGPISVAIDAGHESFLFYKEGIYFEPDCSSEDMDHGVLVVGYGFESTESDNNKYWLVKNSWGEEWGMGGYVKMAKDRRNHCGIASAASYPTV

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
104	Ubiquitination	NRKPRKGKVFQEPLF CCCCCCCCCCCCCCC	42.80	21906983
104	Sumoylation	NRKPRKGKVFQEPLF CCCCCCCCCCCCCCC	42.80	-
104	Sumoylation	NRKPRKGKVFQEPLF CCCCCCCCCCCCCCC	42.80	-
123	Ubiquitination	RSVDWREKGYVTPVK CCCCHHHHCCEECCC	47.14	-
127	Phosphorylation	WREKGYVTPVKNQGQ HHHHCCEECCCCCCC	17.55	29396449
142	Phosphorylation	CGSCWAFSATGALEG CCCCEEEECCCCCCC	19.71	22210691
216	Ubiquitination	ESCKYNPKYSVANDT HHHCCCCCCCCCCCC	46.66	21906983
218	O-linked_Glycosylation	CKYNPKYSVANDTGF HCCCCCCCCCCCCCC	22.37	30059200
221	N-linked_Glycosylation	NPKYSVANDTGFVDI CCCCCCCCCCCCCCC	45.26	2275556
221	N-linked_Glycosylation	NPKYSVANDTGFVDI CCCCCCCCCCCCCCC	45.26	2275556
223	Phosphorylation	KYSVANDTGFVDIPK CCCCCCCCCCCCCCH	32.12	-
230	Ubiquitination	TGFVDIPKQEKALMK CCCCCCCHHHHHHHH	72.00	-
271	Phosphorylation	YFEPDCSSEDMDHGV EECCCCCCCCCCCCE	43.90	29457462
295	Phosphorylation	TESDNNKYWLVKNSW CCCCCCEEEEEECCC	13.19	-
301	Phosphorylation	KYWLVKNSWGEEWGM EEEEEECCCCCCCCC	30.64	28509920
311	Phosphorylation	EEWGMGGYVKMAKDR CCCCCHHHHHCCCCC	7.38	28509920
322	S-nitrosylation	AKDRRNHCGIASAAS CCCCCCCCCCCCCCC	4.88	2212679

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

Oops, there are no upstream regulatory protein records of CATL1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CATL1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CATL1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RXRA_HUMAN	RXRA	physical	9837884
BAG6_HUMAN	BAG6	physical	21900206
EED_HUMAN	EED	physical	21900206
RELB_HUMAN	RELB	physical	21988832
SGTA_HUMAN	SGTA	physical	25416956
CLH2_HUMAN	CLTCL1	physical	26186194
CATH_HUMAN	CTSH	physical	26186194
GRDN_HUMAN	CCDC88A	physical	26186194
6PGD_HUMAN	PGD	physical	26344197
GRDN_HUMAN	CCDC88A	physical	28514442
CLH2_HUMAN	CLTCL1	physical	28514442
CATH_HUMAN	CTSH	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• 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

"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-221, AND MASSSPECTROMETRY.
PubMed: 19159218

"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221, AND MASSSPECTROMETRY.
PubMed: 16335952

"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-221.
PubMed: 12754519