STC2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: STC2_HUMAN
• UniProt AC: O76061
• Protein Name: Stanniocalcin-2
• Gene Name: STC2
• Organism: Homo sapiens (Human).
• Sequence Length: 302
• Subcellular Localization: Secreted .
• Protein Description: Has an anti-hypocalcemic action on calcium and phosphate homeostasis..
• Protein Sequence: MCAERLGQFMTLALVLATFDPARGTDATNPPEGPQDRSSQQKGRLSLQNTAEIQHCLVNAGDVGCGVFECFENNSCEIRGLHGICMTFLHNAGKFDAQGKSFIKDALKCKAHALRHRFGCISRKCPAIREMVSQLQRECYLKHDLCAAAQENTRVIVEMIHFKDLLLHEPYVDLVNLLLTCGEEVKEAITHSVQVQCEQNWGSLCSILSFCTSAIQKPPTAPPERQPQVDRTKLSRAHHGEAGHHLPEPSSRETGRGAKGERGSKSHPNAHARGRVGGLGAQGPSGSSEWEDEQSEYSDIRR

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
28	O-linked_Glycosylation	PARGTDATNPPEGPQ CCCCCCCCCCCCCCC	51.58	OGP
28	Phosphorylation	PARGTDATNPPEGPQ CCCCCCCCCCCCCCC	51.58	22817900
73	N-linked_Glycosylation	GVFECFENNSCEIRG CCHHHHCCCCCEEEC	26.01	UniProtKB CARBOHYD
100	Ubiquitination	GKFDAQGKSFIKDAL CCCCCCCCHHHHHHH	30.07	2190698
101	Phosphorylation	KFDAQGKSFIKDALK CCCCCCCHHHHHHHH	38.74	24719451
104	Ubiquitination	AQGKSFIKDALKCKA CCCCHHHHHHHHHHH	34.63	-
142	Ubiquitination	LQRECYLKHDLCAAA HHHHHHHHCHHHHHH	14.48	-
212	O-linked_Glycosylation	CSILSFCTSAIQKPP HHHHHHHHHHHCCCC	21.12	OGP
232	O-linked_Glycosylation	RQPQVDRTKLSRAHH CCCCCCCHHHHHHCC	31.69	55835643
250	O-linked_Glycosylation	GHHLPEPSSRETGRG CCCCCCCCCCCCCCC	40.12	OGP
250	Phosphorylation	GHHLPEPSSRETGRG CCCCCCCCCCCCCCC	40.12	29116813
251	Phosphorylation	HHLPEPSSRETGRGA CCCCCCCCCCCCCCC	44.87	29116813
251	O-linked_Glycosylation	HHLPEPSSRETGRGA CCCCCCCCCCCCCCC	44.87	OGP
254	Phosphorylation	PEPSSRETGRGAKGE CCCCCCCCCCCCCCC	30.94	26330541
285	Phosphorylation	GLGAQGPSGSSEWED CCCCCCCCCCCCCCC	59.12	22199227
287	Phosphorylation	GAQGPSGSSEWEDEQ CCCCCCCCCCCCCHH	29.44	22199227
288	Phosphorylation	AQGPSGSSEWEDEQS CCCCCCCCCCCCHHH	50.70	23927012
295	Phosphorylation	SEWEDEQSEYSDIRR CCCCCHHHHCCCCCC	36.13	23927012
297	Phosphorylation	WEDEQSEYSDIRR-- CCCHHHHCCCCCC--	19.52	28102081
298	Phosphorylation	EDEQSEYSDIRR--- CCHHHHCCCCCC---	23.62	28102081

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
250	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
251	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
254	T	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
288	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
288	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of STC2_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 STC2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PTN_HUMAN	PTN	physical	16169070

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

"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-28, AND MASSSPECTROMETRY.
PubMed: 15302935