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Protein

Serum amyloid P-component

Gene

APCS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. May also function as a calcium-dependent lectin.

Cofactori

Ca2+Note: Binds 2 calcium ions per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi77Calcium 1PROSITE-ProRule annotation1
Metal bindingi78Calcium 1PROSITE-ProRule annotation1
Metal bindingi155Calcium 1PROSITE-ProRule annotation1
Metal bindingi155Calcium 2PROSITE-ProRule annotation1
Metal bindingi156Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi157Calcium 1PROSITE-ProRule annotation1
Metal bindingi157Calcium 2PROSITE-ProRule annotation1
Metal bindingi167Calcium 2PROSITE-ProRule annotation1

GO - Molecular functioni

  • calcium ion binding Source: BHF-UCL
  • carbohydrate binding Source: UniProtKB-KW
  • complement component C1q binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • unfolded protein binding Source: ProtInc
  • virion binding Source: BHF-UCL

GO - Biological processi

  • acute-phase response Source: ProtInc
  • cellular protein metabolic process Source: Reactome
  • chaperone-mediated protein complex assembly Source: ProtInc
  • innate immune response Source: BHF-UCL
  • negative regulation by host of viral exo-alpha-sialidase activity Source: BHF-UCL
  • negative regulation by host of viral glycoprotein metabolic process Source: BHF-UCL
  • negative regulation of acute inflammatory response Source: BHF-UCL
  • negative regulation of exo-alpha-sialidase activity Source: BHF-UCL
  • negative regulation of glycoprotein metabolic process Source: BHF-UCL
  • negative regulation of monocyte differentiation Source: BHF-UCL
  • negative regulation of viral entry into host cell Source: BHF-UCL
  • negative regulation of viral process Source: BHF-UCL
  • negative regulation of wound healing Source: BHF-UCL
  • protein folding Source: ProtInc

Keywordsi

LigandCalcium, Lectin, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-977225 Amyloid fiber formation

Protein family/group databases

TCDBi1.C.92.1.2 the pentraxin (pentraxin) family
UniLectiniP02743

Names & Taxonomyi

Protein namesi
Recommended name:
Serum amyloid P-component
Short name:
SAP
Alternative name(s):
9.5S alpha-1-glycoprotein
Cleaved into the following chain:
Gene namesi
Name:APCS
Synonyms:PTX2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000132703.3
HGNCiHGNC:584 APCS
MIMi104770 gene
neXtProtiNX_P02743

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Amyloid, Secreted

Pathology & Biotechi

Involvement in diseasei

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

Organism-specific databases

DisGeNETi325
OpenTargetsiENSG00000132703
PharmGKBiPA24877

Chemistry databases

ChEMBLiCHEMBL4929
GuidetoPHARMACOLOGYi2839

Polymorphism and mutation databases

BioMutaiAPCS
DMDMi730704

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 192 PublicationsAdd BLAST19
ChainiPRO_000002354020 – 223Serum amyloid P-componentAdd BLAST204
ChainiPRO_000002354120 – 222Serum amyloid P-component(1-203)Add BLAST203

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
GlycosylationiCAR_00016951N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi55 ↔ 114PROSITE-ProRule annotation1 Publication

Post-translational modificationi

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 (PubMed:15174148).3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP02743
PeptideAtlasiP02743
PRIDEiP02743
ProteomicsDBi51560

2D gel databases

DOSAC-COBS-2DPAGEiP02743
OGPiP02743
REPRODUCTION-2DPAGEiIPI00022391
P02743
SWISS-2DPAGEiP02743

PTM databases

CarbonylDBiP02743
GlyConnecti560
iPTMnetiP02743
PhosphoSitePlusiP02743
UniCarbKBiP02743

Expressioni

Tissue specificityi

Found in serum and urine.1 Publication

Gene expression databases

BgeeiENSG00000132703
CleanExiHS_APCS
ExpressionAtlasiP02743 baseline and differential
GenevisibleiP02743 HS

Organism-specific databases

HPAiCAB007817
HPA053294

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-2115799,EBI-2115799

GO - Molecular functioni

  • complement component C1q binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • unfolded protein binding Source: ProtInc

Protein-protein interaction databases

BioGridi106822, 13 interactors
DIPiDIP-46911N
IntActiP02743, 6 interactors
MINTiP02743
STRINGi9606.ENSP00000255040

Structurei

Secondary structure

1223
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi26 – 30Combined sources5
Beta strandi38 – 41Combined sources4
Beta strandi49 – 59Combined sources11
Beta strandi66 – 73Combined sources8
Beta strandi76 – 86Combined sources11
Beta strandi89 – 94Combined sources6
Beta strandi97 – 102Combined sources6
Beta strandi111 – 118Combined sources8
Turni119 – 121Combined sources3
Beta strandi123 – 128Combined sources6
Beta strandi149 – 154Combined sources6
Beta strandi157 – 160Combined sources4
Helixi165 – 167Combined sources3
Beta strandi171 – 181Combined sources11
Helixi185 – 193Combined sources9
Beta strandi200 – 203Combined sources4
Helixi204 – 206Combined sources3
Beta strandi209 – 214Combined sources6
Beta strandi216 – 219Combined sources4

3D structure databases

ProteinModelPortaliP02743
SMRiP02743
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02743

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 223Pentraxin (PTX)PROSITE-ProRule annotationAdd BLAST200

Sequence similaritiesi

Belongs to the pentraxin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J1FD Eukaryota
ENOG410YN8S LUCA
GeneTreeiENSGT00760000119128
HOGENOMiHOG000247043
HOVERGENiHBG005405
InParanoidiP02743
OMAiFTLCFRA
OrthoDBiEOG091G0H6X
PhylomeDBiP02743
TreeFamiTF330208

Family and domain databases

CDDicd00152 PTX, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR030476 Pentaxin_CS
IPR001759 Pentraxin-related
PfamiView protein in Pfam
PF00354 Pentaxin, 1 hit
PRINTSiPR00895 PENTAXIN
SMARTiView protein in SMART
SM00159 PTX, 1 hit
SUPFAMiSSF49899 SSF49899, 1 hit
PROSITEiView protein in PROSITE
PS00289 PTX_1, 1 hit
PS51828 PTX_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02743-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKPLLWISV LTSLLEAFAH TDLSGKVFVF PRESVTDHVN LITPLEKPLQ
60 70 80 90 100
NFTLCFRAYS DLSRAYSLFS YNTQGRDNEL LVYKERVGEY SLYIGRHKVT
110 120 130 140 150
SKVIEKFPAP VHICVSWESS SGIAEFWING TPLVKKGLRQ GYFVEAQPKI
160 170 180 190 200
VLGQEQDSYG GKFDRSQSFV GEIGDLYMWD SVLPPENILS AYQGTPLPAN
210 220
ILDWQALNYE IRGYVIIKPL VWV
Length:223
Mass (Da):25,387
Last modified:February 1, 1995 - v2
Checksum:i6C88A515FE88B393
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti101S → P in AAA60302 (PubMed:2987268).Curated1

Mass spectrometryi

Molecular mass is 25462.5±1.1 Da from positions 20 - 223. Determined by ESI. 2 Publications
Molecular mass is 25463±3 Da from positions 20 - 223. Determined by MALDI. 2 Publications
Molecular mass is 1285.78 Da from positions 213 - 223. Determined by MALDI. 1 Publication
Molecular mass is 1186.71 Da from positions 213 - 222. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035814141G → S in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_006054155E → G. 1
Natural variantiVAR_006055158S → G. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00097 Genomic DNA Translation: BAA00060.1
M10944 mRNA Translation: AAA60302.1
X04608 mRNA Translation: CAA28275.1
CR450313 mRNA Translation: CAG29309.1
AL445528 Genomic DNA No translation available.
BT006750 mRNA Translation: AAP35396.1
BC007039 mRNA Translation: AAH07039.1
BC007058 mRNA Translation: AAH07058.1
CCDSiCCDS1186.1
PIRiA25503 YLHUP
RefSeqiNP_001630.1, NM_001639.3
UniGeneiHs.507080

Genome annotation databases

EnsembliENST00000255040; ENSP00000255040; ENSG00000132703
GeneIDi325
KEGGihsa:325

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiSAMP_HUMAN
AccessioniPrimary (citable) accession number: P02743
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1995
Last modified: July 18, 2018
This is version 203 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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