CATH_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CATH_HUMAN
• UniProt AC: P09668
• Protein Name: Pro-cathepsin H
• Gene Name: CTSH
• Organism: Homo sapiens (Human).
• Sequence Length: 335
• Subcellular Localization: Lysosome.
• Protein Description: Important for the overall degradation of proteins in lysosomes..
• Protein Sequence: MWATLPLLCAGAWLLGVPVCGAAELCVNSLEKFHFKSWMSKHRKTYSTEEYHHRLQTFASNWRKINAHNNGNHTFKMALNQFSDMSFAEIKHKYLWSEPQNCSATKSNYLRGTGPYPPSVDWRKKGNFVSPVKNQGACGSCWTFSTTGALESAIAIATGKMLSLAEQQLVDCAQDFNNHGCQGGLPSQAFEYILYNKGIMGEDTYPYQGKDGYCKFQPGKAIGFVKDVANITIYDEEAMVEAVALYNPVSFAFEVTQDFMMYRTGIYSSTSCHKTPDKVNHAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLIERGKNMCGLAACASYPIPLV

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
68	Ubiquitination	NWRKINAHNNGNHTF CHHHHHCCCCCCCCH	24.65	21890473
83	Phosphorylation	KMALNQFSDMSFAEI HHHHHHCCCCCHHHH	23.73	24732914
86	Phosphorylation	LNQFSDMSFAEIKHK HHHCCCCCHHHHHHH	26.71	24732914
88	Ubiquitination	QFSDMSFAEIKHKYL HCCCCCHHHHHHHHH	15.42	21890473
94	Phosphorylation	FAEIKHKYLWSEPQN HHHHHHHHHHCCCCC	17.08	22115753
97	Phosphorylation	IKHKYLWSEPQNCSA HHHHHHHCCCCCCCC	36.48	22115753
101	N-linked_Glycosylation	YLWSEPQNCSATKSN HHHCCCCCCCCCCCC	32.21	3342889
103	Phosphorylation	WSEPQNCSATKSNYL HCCCCCCCCCCCCCC	46.66	22115753
105	Phosphorylation	EPQNCSATKSNYLRG CCCCCCCCCCCCCCC	20.79	22115753
106	Ubiquitination	PQNCSATKSNYLRGT CCCCCCCCCCCCCCC	36.10	22817900
106	Ubiquitination	PQNCSATKSNYLRGT CCCCCCCCCCCCCCC	36.10	21890473
107	Phosphorylation	QNCSATKSNYLRGTG CCCCCCCCCCCCCCC	26.76	22115753
109	Phosphorylation	CSATKSNYLRGTGPY CCCCCCCCCCCCCCC	12.60	22115753
141	S-nitrosylation	NQGACGSCWTFSTTG CCCCCCCCEEECCCC	2.11	25040305
204	Phosphorylation	KGIMGEDTYPYQGKD CCCCCCCCCCCCCCC	23.30	29083192
205	Phosphorylation	GIMGEDTYPYQGKDG CCCCCCCCCCCCCCC	16.56	29083192
207	Phosphorylation	MGEDTYPYQGKDGYC CCCCCCCCCCCCCCC	21.34	29083192
230	N-linked_Glycosylation	GFVKDVANITIYDEE EEEEECEEEEECCHH	31.61	3342889

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CATH_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 CATH_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of CATH_HUMAN !!

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-230, AND MASSSPECTROMETRY.
PubMed: 19159218

"Amino acid sequences of the human kidney cathepsins H and L.";
Ritonja A., Popovic T., Kotnik M., Machleidt W., Turk V.;
FEBS Lett. 228:341-345(1988).
Cited for: PROTEIN SEQUENCE OF 98-105 AND 114-335, AND GLYCOSYLATION AT ASN-101AND ASN-230.
PubMed: 3342889