SAMP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SAMP_HUMAN
• UniProt AC: P02743
• Protein Name: Serum amyloid P-component
• Gene Name: APCS
• Organism: Homo sapiens (Human).
• Sequence Length: 223
• Subcellular Localization: Secreted.
• Protein Description: Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. May also function as a calcium-dependent lectin..
• Protein Sequence: MNKPLLWISVLTSLLEAFAHTDLSGKVFVFPRESVTDHVNLITPLEKPLQNFTLCFRAYSDLSRAYSLFSYNTQGRDNELLVYKERVGEYSLYIGRHKVTSKVIEKFPAPVHICVSWESSSGIAEFWINGTPLVKKGLRQGYFVEAQPKIVLGQEQDSYGGKFDRSQSFVGEIGDLYMWDSVLPPENILSAYQGTPLPANILDWQALNYEIRGYVIIKPLVWV

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
1	Acetylation	-------MNKPLLWI -------CCCCHHHH	15.24	-
12	Phosphorylation	LLWISVLTSLLEAFA HHHHHHHHHHHHHHH	18.38	29759185
13	Phosphorylation	LWISVLTSLLEAFAH HHHHHHHHHHHHHHC	27.13	19413330
21	Phosphorylation	LLEAFAHTDLSGKVF HHHHHHCCCCCCCEE	34.89	19413330
51	N-linked_Glycosylation	PLEKPLQNFTLCFRA CCCCCCCCCEEEEEH	39.28	4055725
51	N-linked_Glycosylation	PLEKPLQNFTLCFRA CCCCCCCCCEEEEEH	39.28	4055725
59	Phosphorylation	FTLCFRAYSDLSRAY CEEEEEHHHHHHHHH	9.84	-
63	Phosphorylation	FRAYSDLSRAYSLFS EEHHHHHHHHHHHHC	21.61	30622161
84	Acetylation	DNELLVYKERVGEYS CCEEEEEEEEEEEEE	31.40	27178108
142	Phosphorylation	KKGLRQGYFVEAQPK CCCCCCCCEEEECCE	8.98	-
195	O-linked_Glycosylation	ILSAYQGTPLPANIL HHHHHCCCCCCCCCC	13.21	OGP
218	Acetylation	IRGYVIIKPLVWV-- EEEEEEEEEEECC--	22.60	27178108

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SAMP_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 SAMP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SAMP_HUMAN	APCS	physical	8114934
FCG3A_HUMAN	FCGR3A	physical	11359830
FCGR1_HUMAN	FCGR1A	physical	11359830
FCG3B_HUMAN	FCGR3B	physical	11359830
HES1_HUMAN	HES1	physical	21900206
AATM_HUMAN	GOT2	physical	21900206
GLPK_HUMAN	GK	physical	21988832
CSN5_HUMAN	COPS5	physical	21988832

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

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-12; SER-13 AND THR-21, AND MASS SPECTROMETRY.
PubMed: 19413330

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-51, AND MASS SPECTROMETRY.
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-51, AND MASS SPECTROMETRY.
PubMed: 16335952

Phosphorylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-12; SER-13 AND THR-21, AND MASS SPECTROMETRY.
PubMed: 19413330