Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Serum amyloid P-component  

UniProtKB / Swiss-Prot ID :  SAMP_HUMAN

Gene Name (Synonyms) : 
APCS, PTX2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Secreted. 

Protein Function :  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 MNKPLLWISVLTSLLEAFAHTDLSGKVFVFPRESVTDHVNLITPLEKPLQNFTLCFRAYSDLSRAYSLFS...
Predicted Secondary Structure CHHHHHHHHHHHHHHHHHHCCCCCCCEEEEECCCCCCEEEEEECCCHHHHHHHHHHHHHHHCCCCCCEEE...
Protein Variant
LocationDescription
141G -> S (in a breast cancer sample;somatic mutation).
155E -> G. VAR_006054
158S -> G. VAR_006055
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
1N-acetylmethionine.----MNKPL
----CHHHH
15.24UniProtKB
Link-
12PhosphothreonineISVLTSLLE
HHHHHHHHH
18.38HPRD
Link-
12Phosphothreonine.ISVLTSLLE
HHHHHHHHH
18.38UniProtKB
Link-
13PhosphoserineSVLTSLLEA
HHHHHHHHH
27.13HPRD
Link-
13Phosphoserine.SVLTSLLEA
HHHHHHHHH
27.13UniProtKB
Link-
21PhosphothreonineAFAHTDLSG
HHHCCCCCC
34.89HPRD
Link
21Phosphothreonine.AFAHTDLSG
HHHCCCCCC
34.89UniProtKB
Link
51N-linked (Glc...)KPLQNFTLC
HHHHHHHHH
39.28HPRD
Link
51N-linked (GlcNAc...)./FTId=CAR_000169.KPLQNFTLC
HHHHHHHHH
39.28UniProtKB
Link
55S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)NFTLCFRAY
HHHHHHHHH
1.65HPRD
Link
114S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)PVHICVSWE
CEEEEEEEE
0.89HPRD
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SAMP_HUMANin vitroHPRD:00101HPRD12126626
3029048
3172210
8114934
9217261
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.
N-linked Glycosylation
ReferencePubMed
"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.
"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.
Phosphorylation
ReferencePubMed
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures