SPRC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SPRC_HUMAN
• UniProt AC: P09486
• Protein Name: SPARC
• Gene Name: SPARC
• Organism: Homo sapiens (Human).
• Sequence Length: 303
• Subcellular Localization: Secreted, extracellular space, extracellular matrix, basement membrane . In or around the basement membrane.
• Protein Description: Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity..
• Protein Sequence: MRAWIFFLLCLAGRALAAPQQEALPDETEVVEETVAEVTEVSVGANPVQVEVGEFDDGAEETEEEVVAENPCQNHHCKHGKVCELDENNTPMCVCQDPTSCPAPIGEFEKVCSNDNKTFDSSCHFFATKCTLEGTKKGHKLHLDYIGPCKYIPPCLDSELTEFPLRMRDWLKNVLVTLYERDEDNNLLTEKQKLRVKKIHENEKRLEAGDHPVELLARDFEKNYNMYIFPVHWQFGQLDQHPIDGYLSHTELAPLRAPLIPMEHCTTRFFETCDLDNDKYIALDEWAGCFGIKQKDIDKDLVI

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
39	O-linked_Glycosylation	EETVAEVTEVSVGAN EEHEEEEEEEECCCC	23.36	OGP
88	N-linked_Glycosylation	KVCELDENNTPMCVC CEEEECCCCCEEEEE	58.29	-
88	N-linked_Glycosylation	KVCELDENNTPMCVC CEEEECCCCCEEEEE	58.29	7559469
116	N-linked_Glycosylation	EKVCSNDNKTFDSSC EEHHCCCCCEECCCC	49.90	7559469
116	N-linked_Glycosylation	EKVCSNDNKTFDSSC EEHHCCCCCEECCCC	49.90	7559469
140	Malonylation	EGTKKGHKLHLDYIG CCCCCCCEEECEEEC	46.39	26320211
145	Phosphorylation	GHKLHLDYIGPCKYI CCEEECEEECCCCCC	17.71	-
198	Ubiquitination	KQKLRVKKIHENEKR HHHHHHHHHHHCHHH	46.57	29967540
262	Sulfoxidation	LRAPLIPMEHCTTRF CCCCEECHHHHCCCE	4.33	30846556

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SPRC_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 SPRC_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VEGFA_HUMAN	VEGFA	physical	9792673
PDGFB_HUMAN	PDGFB	physical	1311092
ZN579_HUMAN	ZNF579	physical	21900206
XRCC6_HUMAN	XRCC6	physical	21900206

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

"Crystal structure and mapping by site-directed mutagenesis of thecollagen-binding epitope of an activated form of BM-40/SPARC/osteonectin.";
Sasaki T., Hohenester E., Gohring W., Timpl R.;
EMBO J. 17:1625-1634(1998).
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 71-303 IN COMPLEX WITHCALCIUM IONS, GLYCOSYLATION AT ASN-116, INTERACTION WITH COLLAGEN, ANDMUTAGENESIS OF ARG-166; ASN-173; LEU-259; MET-262 AND GLU-263.
PubMed: 9501084

"Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40.";
Hohenester E., Maurer P., Timpl R.;
EMBO J. 16:3778-3786(1997).
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 71-303 IN COMPLEX WITHCALCIUM IONS, GLYCOSYLATION AT ASN-116, AND DISULFIDE BONDS.
PubMed: 9233787