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P02743 (SAMP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 168. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serum amyloid P-component

Short name=SAP
Alternative name(s):
9.5S alpha-1-glycoprotein

Cleaved into the following chain:

  1. Serum amyloid P-component(1-203)
Gene names
Name:APCS
Synonyms:PTX2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length223 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Cofactor

Binds 2 calcium ions per subunit.

Subunit structure

Homopentamer. Pentaxin (or pentraxin) have a discoid arrangement of 5 non-covalently bound subunits.

Subcellular location

Secreted.

Tissue specificity

Found in serum and urine. Ref.10

Post-translational modification

N-glycosylated with a complex biantennary oligosaccharide chain with a sialic acid at the end (disialo-SAP). Monosialo-SAP as well as asioalo-SAP are also detected (Ref.10). Ref.9

Involvement in disease

SAP is a precursor of amyloid component P which is found in basement membrane and associated with amyloid deposits.

Sequence similarities

Belongs to the pentaxin family.

Contains 1 pentaxin domain.

Mass spectrometry

Molecular mass is 25462.5±1.1 Da from positions 20 - 223. Determined by ESI. Ref.9

Molecular mass is 25463±3 Da from positions 20 - 223. Determined by MALDI. Ref.10

Molecular mass is 1285.78 Da from positions 213 - 223. Determined by MALDI. Ref.10

Molecular mass is 1186.71 Da from positions 213 - 222. Determined by MALDI. Ref.10

Ontologies

Keywords
   Cellular componentAmyloid
Secreted
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandCalcium
Lectin
Metal-binding
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Traceable author statement Ref.1. Source: ProtInc

chaperone-mediated protein complex assembly

Traceable author statement PubMed 10972085. Source: ProtInc

innate immune response

Inferred from direct assay PubMed 23544079. Source: BHF-UCL

negative regulation of acute inflammatory response

Inferred by curator PubMed 14607961. Source: BHF-UCL

negative regulation of exo-alpha-sialidase activity

Inferred from direct assay PubMed 23544079. Source: BHF-UCL

negative regulation of glycoprotein metabolic process

Inferred from direct assay PubMed 23544079. Source: BHF-UCL

negative regulation of monocyte differentiation

Inferred from direct assay PubMed 14607961. Source: BHF-UCL

negative regulation of viral entry into host cell

Inferred from direct assay PubMed 23544079. Source: BHF-UCL

negative regulation of viral process

Inferred from direct assay PubMed 23544079. Source: BHF-UCL

negative regulation of wound healing

Inferred by curator PubMed 14607961. Source: BHF-UCL

protein folding

Traceable author statement PubMed 10812074. Source: ProtInc

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 14607961PubMed 20551380PubMed 23544079. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium ion binding

Inferred from direct assay PubMed 23544079. Source: BHF-UCL

complement component C1q binding

Inferred from direct assay PubMed 23544079. Source: BHF-UCL

unfolded protein binding

Traceable author statement PubMed 10812074. Source: ProtInc

virion binding

Inferred from direct assay PubMed 23544079. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.7 Ref.8
Chain20 – 223204Serum amyloid P-component
PRO_0000023540
Chain20 – 222203Serum amyloid P-component(1-203)
PRO_0000023541

Regions

Domain20 – 223204Pentaxin

Sites

Metal binding771Calcium 1
Metal binding781Calcium 1
Metal binding1551Calcium 1
Metal binding1551Calcium 2
Metal binding1561Calcium 1; via carbonyl oxygen
Metal binding1571Calcium 1
Metal binding1571Calcium 2
Metal binding1671Calcium 2

Amino acid modifications

Glycosylation511N-linked (GlcNAc...) Ref.11 Ref.12
CAR_000169
Disulfide bond55 ↔ 114 Ref.7

Natural variations

Natural variant1411G → S in a breast cancer sample; somatic mutation. Ref.16
VAR_035814
Natural variant1551E → G.
VAR_006054
Natural variant1581S → G.
VAR_006055

Experimental info

Sequence conflict1011S → P in AAA60302. Ref.1

Secondary structure

..................................... 223
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02743 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: 6C88A515FE88B393

FASTA22325,387
        10         20         30         40         50         60 
MNKPLLWISV LTSLLEAFAH TDLSGKVFVF PRESVTDHVN LITPLEKPLQ NFTLCFRAYS 

        70         80         90        100        110        120 
DLSRAYSLFS YNTQGRDNEL LVYKERVGEY SLYIGRHKVT SKVIEKFPAP VHICVSWESS 

       130        140        150        160        170        180 
SGIAEFWING TPLVKKGLRQ GYFVEAQPKI VLGQEQDSYG GKFDRSQSFV GEIGDLYMWD 

       190        200        210        220 
SVLPPENILS AYQGTPLPAN ILDWQALNYE IRGYVIIKPL VWV 

« Hide

References

« Hide 'large scale' references
[1]"Human serum amyloid P component. cDNA isolation, complete sequence of pre-serum amyloid P component, and localization of the gene to chromosome 1."
Mantzouranis E.C., Dowton S.B., Whitehead A.S., Edge M.D., Bruns G.A.P., Colten H.R.
J. Biol. Chem. 260:7752-7756(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation and characterization of the complete complementary and genomic DNA sequences of human serum amyloid P component."
Ohnishi S., Maeda S., Shimada K., Arao T.
J. Biochem. 100:849-858(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skeletal muscle.
[7]"The primary structure of human tissue amyloid P component from a patient with primary idiopathic amyloidosis."
Prelli F., Pras M., Frangione B.
J. Biol. Chem. 260:12895-12898(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-223.
[8]"Human plasma P component: isolation and characterization."
Thompson A.R., Enfield D.L.
Biochemistry 17:4304-4311(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-49.
[9]"Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure."
Pepys M.B., Rademacher T.W., Amatayakul-Chantler S., Williams P., Noble G.E., Hutchinson W.L., Hawkins P.N., Nelson S.R., Gallimore J.R., Herbert J., Hutton T., Dwek R.A.
Proc. Natl. Acad. Sci. U.S.A. 91:5602-5606(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATE, MASS SPECTROMETRY.
[10]"Proteomic characterization of novel serum amyloid P component variants from human plasma and urine."
Kiernan U.A., Nedelkov D., Tubbs K.A., Niederkofler E.E., Nelson R.W.
Proteomics 4:1825-1829(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, MASS SPECTROMETRY.
[11]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-51.
Tissue: Plasma.
[12]"Glycoproteomics analysis of human liver tissue by combination of multiple 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) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-51.
Tissue: Liver.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Structure of pentameric human serum amyloid P component."
Emsley J., White H.E., O'Hara B., Oliva G., Srinivasan N., Tickle I.J., Blundell T.L., Pepys M.B., Wood S.P.
Nature 367:338-345(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[15]"Crystal structure of a decameric complex of human serum amyloid P component with bound dAMP."
Hohenester E., Hutchinson W.L., Pepys M.B., Wood S.P.
J. Mol. Biol. 269:570-578(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[16]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-141.
+Additional computationally mapped references.

Web resources

Wikipedia

Serum amyloid P component entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00097 Genomic DNA. Translation: BAA00060.1.
M10944 mRNA. Translation: AAA60302.1.
X04608 mRNA. Translation: CAA28275.1.
CR450313 mRNA. Translation: CAG29309.1.
AL445528 Genomic DNA. Translation: CAH73651.1.
BT006750 mRNA. Translation: AAP35396.1.
BC007039 mRNA. Translation: AAH07039.1.
BC007058 mRNA. Translation: AAH07058.1.
CCDSCCDS1186.1.
PIRYLHUP. A25503.
RefSeqNP_001630.1. NM_001639.3.
UniGeneHs.507080.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GYKX-ray2.20A/B/C/D/E20-223[»]
1LGNX-ray2.80A/B/C/D/E20-223[»]
1SACX-ray2.00A/B/C/D/E20-223[»]
2A3WX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T20-223[»]
2A3XX-ray3.00A/B/C/D/E/F/G/H/I/J20-223[»]
2A3YX-ray2.00A/B/C/D/E20-223[»]
2W08X-ray1.70A/B/C/D/E20-223[»]
3D5OX-ray2.80A/B/C/D/E20-223[»]
3KQRX-ray1.50A/B/C/D/E20-223[»]
4AVSX-ray1.40A/B/C/D/E20-223[»]
4AVTX-ray3.20A/B/C/D/E/F/G/H/I/J20-223[»]
4AVVX-ray1.60A/B/C/D/E20-223[»]
4AYUX-ray1.50A/B/C/D/E20-223[»]
ProteinModelPortalP02743.
SMRP02743. Positions 20-223.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106822. 13 interactions.
DIPDIP-46911N.
IntActP02743. 5 interactions.
MINTMINT-4723480.
STRING9606.ENSP00000255040.

Chemistry

ChEMBLCHEMBL4929.

Protein family/group databases

TCDB1.C.92.1.2. the pentraxin (pentraxin) family.

PTM databases

PhosphoSiteP02743.
UniCarbKBP02743.

Polymorphism databases

DMDM730704.

2D gel databases

DOSAC-COBS-2DPAGEP02743.
OGPP02743.
REPRODUCTION-2DPAGEIPI00022391.
P02743.
SWISS-2DPAGEP02743.

Proteomic databases

PaxDbP02743.
PeptideAtlasP02743.
PRIDEP02743.

Protocols and materials databases

DNASU325.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000255040; ENSP00000255040; ENSG00000132703.
GeneID325.
KEGGhsa:325.
UCSCuc001ftv.3. human.

Organism-specific databases

CTD325.
GeneCardsGC01P159557.
HGNCHGNC:584. APCS.
HPACAB007817.
HPA053294.
MIM104770. gene.
neXtProtNX_P02743.
PharmGKBPA24877.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44770.
HOGENOMHOG000247043.
HOVERGENHBG005405.
InParanoidP02743.
OMAAEFWING.
OrthoDBEOG71RXMB.
PhylomeDBP02743.
TreeFamTF330208.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.

Gene expression databases

BgeeP02743.
CleanExHS_APCS.
GenevestigatorP02743.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR001759. Pentaxin.
[Graphical view]
PfamPF00354. Pentaxin. 1 hit.
[Graphical view]
PRINTSPR00895. PENTAXIN.
SMARTSM00159. PTX. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS00289. PENTAXIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02743.
GeneWikiSerum_amyloid_P_component.
GenomeRNAi325.
NextBio1333.
PROP02743.
SOURCESearch...

Entry information

Entry nameSAMP_HUMAN
AccessionPrimary (citable) accession number: P02743
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 168 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM