CYTS_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CYTS_HUMAN
• UniProt AC: P01036
• Protein Name: Cystatin-S
• Gene Name: CST4
• Organism: Homo sapiens (Human).
• Sequence Length: 141
• Subcellular Localization: Secreted .
• Protein Description: This protein strongly inhibits papain and ficin, partially inhibits stem bromelain and bovine cathepsin C, but does not inhibit porcine cathepsin B or clostripain. Papain is inhibited non-competitively..
• Protein Sequence: MARPLCTLLLLMATLAGALASSSKEENRIIPGGIYDADLNDEWVQRALHFAISEYNKATEDEYYRRPLQVLRAREQTFGGVNYFFDVEVGRTICTKSQPNLDTCAFHEQPELQKKQLCSFEIYEVPWEDRMSLVNSRCQEA

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
7	Phosphorylation	-MARPLCTLLLLMAT -CCHHHHHHHHHHHH	28.29	-
21	Phosphorylation	TLAGALASSSKEENR HHHHHHHCCCCCCCC	35.67	22817900
23	Phosphorylation	AGALASSSKEENRII HHHHHCCCCCCCCCC	41.41	1898055
35	Phosphorylation	RIIPGGIYDADLNDE CCCCCCCCCCCCCHH	14.35	-
63	Phosphorylation	NKATEDEYYRRPLQV HCCCCCHHHHHHHHH	18.00	-
119	Phosphorylation	LQKKQLCSFEIYEVP HHHCCCCEEEEEECC	34.21	1898055
132	Phosphorylation	VPWEDRMSLVNSRCQ CCHHHHHHHHHHHHH	30.02	1898055
136	Phosphorylation	DRMSLVNSRCQEA-- HHHHHHHHHHHCC--	27.27	1898055

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CYTS_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 CYTS_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference

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

Phosphorylation

"Confident assignment of intact mass tags to human salivary cystatinsusing top-down Fourier-transform ion cyclotron resonance massspectrometry.";
Ryan C.M., Souda P., Halgand F., Wong D.T., Loo J.A., Faull K.F.,Whitelegge J.P.;
J. Am. Soc. Mass Spectrom. 21:908-917(2010).
Cited for: PHOSPHORYLATION AT SER-21 AND SER-23, DISULFIDE BONDS, TISSUESPECIFICITY, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
PubMed: 20189825

"The effects of human salivary cystatins and statherin onhydroxyapatite crystallization.";
Johnsson M., Richardson C.F., Bergey E.J., Levine M.J.,Nancollas G.H.;
Arch. Oral Biol. 36:631-636(1991).
Cited for: PROTEIN SEQUENCE OF 21-36, AND PHOSPHORYLATION AT SER-23.
PubMed: 1741693

"Identification of full-sized forms of salivary (S-type) cystatins(cystatin SN, cystatin SA, cystatin S, and two phosphorylated forms ofcystatin S) in human whole saliva and determination of phosphorylationsites of cystatin S.";
Isemura S., Saitoh E., Sanada K., Minakata K.;
J. Biochem. 110:648-654(1991).
Cited for: PROTEIN SEQUENCE OF 21-36, AND PHOSPHORYLATION AT SER-21 AND SER-23.
PubMed: 1778989

"Large-scale purification and characterization of the majorphosphoproteins and mucins of human submandibular-sublingual saliva.";
Ramasubbu N., Reddy M.S., Bergey E.J., Haraszthy G.G., Soni S.-D.,Levine M.J.;
Biochem. J. 280:341-352(1991).
Cited for: PROTEIN SEQUENCE OF 21-55, AND PHOSPHORYLATION AT SER-23.
PubMed: 1747107