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P02743

- SAMP_HUMAN

UniProt

P02743 - SAMP_HUMAN

Protein

Serum amyloid P-component

Gene

APCS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      Previous versions | rss
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    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

    Binds 2 calcium ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi77 – 771Calcium 1
    Metal bindingi78 – 781Calcium 1
    Metal bindingi155 – 1551Calcium 1
    Metal bindingi155 – 1551Calcium 2
    Metal bindingi156 – 1561Calcium 1; via carbonyl oxygen
    Metal bindingi157 – 1571Calcium 1
    Metal bindingi157 – 1571Calcium 2
    Metal bindingi167 – 1671Calcium 2

    GO - Molecular functioni

    1. calcium ion binding Source: BHF-UCL
    2. complement component C1q binding Source: BHF-UCL
    3. unfolded protein binding Source: ProtInc
    4. virion binding Source: BHF-UCL

    GO - Biological processi

    1. acute-phase response Source: ProtInc
    2. chaperone-mediated protein complex assembly Source: ProtInc
    3. innate immune response Source: BHF-UCL
    4. negative regulation of acute inflammatory response Source: BHF-UCL
    5. negative regulation of exo-alpha-sialidase activity Source: BHF-UCL
    6. negative regulation of glycoprotein metabolic process Source: BHF-UCL
    7. negative regulation of monocyte differentiation Source: BHF-UCL
    8. negative regulation of viral entry into host cell Source: BHF-UCL
    9. negative regulation of viral process Source: BHF-UCL
    10. negative regulation of wound healing Source: BHF-UCL
    11. protein folding Source: ProtInc

    Keywords - Ligandi

    Calcium, Lectin, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_75925. Amyloids.

    Protein family/group databases

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

    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
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:584. APCS.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. extracellular region Source: UniProtKB
    3. extracellular space Source: BHF-UCL
    4. extracellular vesicular exosome Source: UniProt
    5. nucleus Source: UniProt
    6. protein complex Source: Ensembl

    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

    PharmGKBiPA24877.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19192 PublicationsAdd
    BLAST
    Chaini20 – 223204Serum amyloid P-componentPRO_0000023540Add
    BLAST
    Chaini20 – 222203Serum amyloid P-component(1-203)PRO_0000023541Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi51 – 511N-linked (GlcNAc...)2 PublicationsCAR_000169
    Disulfide bondi55 ↔ 1141 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.

    2D gel databases

    DOSAC-COBS-2DPAGEP02743.
    OGPiP02743.
    REPRODUCTION-2DPAGEIPI00022391.
    P02743.
    SWISS-2DPAGEP02743.

    PTM databases

    PhosphoSiteiP02743.
    UniCarbKBiP02743.

    Expressioni

    Tissue specificityi

    Found in serum and urine.1 Publication

    Gene expression databases

    BgeeiP02743.
    CleanExiHS_APCS.
    GenevestigatoriP02743.

    Organism-specific databases

    HPAiCAB007817.
    HPA053294.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi106822. 13 interactions.
    DIPiDIP-46911N.
    IntActiP02743. 5 interactions.
    MINTiMINT-4723480.
    STRINGi9606.ENSP00000255040.

    Structurei

    Secondary structure

    1
    223
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 305
    Beta strandi38 – 414
    Beta strandi49 – 5911
    Beta strandi66 – 738
    Beta strandi76 – 8611
    Beta strandi89 – 946
    Beta strandi97 – 1026
    Beta strandi111 – 1188
    Turni119 – 1213
    Beta strandi123 – 1286
    Beta strandi149 – 1546
    Beta strandi157 – 1604
    Helixi165 – 1673
    Beta strandi171 – 18111
    Helixi185 – 1939
    Beta strandi200 – 2034
    Helixi204 – 2063
    Beta strandi209 – 2146
    Beta strandi216 – 2194

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP02743.
    SMRiP02743. Positions 20-223.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02743.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 223204PentaxinAdd
    BLAST

    Sequence similaritiesi

    Belongs to the pentaxin family.Curated
    Contains 1 pentaxin domain.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG44770.
    HOGENOMiHOG000247043.
    HOVERGENiHBG005405.
    InParanoidiP02743.
    OMAiAEFWING.
    OrthoDBiEOG71RXMB.
    PhylomeDBiP02743.
    TreeFamiTF330208.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR001759. Pentaxin.
    [Graphical view]
    PfamiPF00354. Pentaxin. 1 hit.
    [Graphical view]
    PRINTSiPR00895. PENTAXIN.
    SMARTiSM00159. PTX. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS00289. PENTAXIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P02743-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKPLLWISV LTSLLEAFAH TDLSGKVFVF PRESVTDHVN LITPLEKPLQ    50
    NFTLCFRAYS DLSRAYSLFS YNTQGRDNEL LVYKERVGEY SLYIGRHKVT 100
    SKVIEKFPAP VHICVSWESS SGIAEFWING TPLVKKGLRQ GYFVEAQPKI 150
    VLGQEQDSYG GKFDRSQSFV GEIGDLYMWD SVLPPENILS AYQGTPLPAN 200
    ILDWQALNYE IRGYVIIKPL VWV 223
    Length:223
    Mass (Da):25,387
    Last modified:February 1, 1995 - v2
    Checksum:i6C88A515FE88B393
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti101 – 1011S → P in AAA60302. (PubMed:2987268)Curated

    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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti141 – 1411G → S in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035814
    Natural varianti155 – 1551E → G.
    VAR_006054
    Natural varianti158 – 1581S → G.
    VAR_006055

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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. Translation: CAH73651.1.
    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.
    UCSCiuc001ftv.3. human.

    Polymorphism databases

    DMDMi730704.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Serum amyloid P component entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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. Translation: CAH73651.1 .
    BT006750 mRNA. Translation: AAP35396.1 .
    BC007039 mRNA. Translation: AAH07039.1 .
    BC007058 mRNA. Translation: AAH07058.1 .
    CCDSi CCDS1186.1.
    PIRi A25503. YLHUP.
    RefSeqi NP_001630.1. NM_001639.3.
    UniGenei Hs.507080.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GYK X-ray 2.20 A/B/C/D/E 20-223 [» ]
    1LGN X-ray 2.80 A/B/C/D/E 20-223 [» ]
    1SAC X-ray 2.00 A/B/C/D/E 20-223 [» ]
    2A3W X-ray 2.20 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T 20-223 [» ]
    2A3X X-ray 3.00 A/B/C/D/E/F/G/H/I/J 20-223 [» ]
    2A3Y X-ray 2.00 A/B/C/D/E 20-223 [» ]
    2W08 X-ray 1.70 A/B/C/D/E 20-223 [» ]
    3D5O X-ray 2.80 A/B/C/D/E 20-223 [» ]
    3KQR X-ray 1.50 A/B/C/D/E 20-223 [» ]
    4AVS X-ray 1.40 A/B/C/D/E 20-223 [» ]
    4AVT X-ray 3.20 A/B/C/D/E/F/G/H/I/J 20-223 [» ]
    4AVV X-ray 1.60 A/B/C/D/E 20-223 [» ]
    4AYU X-ray 1.50 A/B/C/D/E 20-223 [» ]
    ProteinModelPortali P02743.
    SMRi P02743. Positions 20-223.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106822. 13 interactions.
    DIPi DIP-46911N.
    IntActi P02743. 5 interactions.
    MINTi MINT-4723480.
    STRINGi 9606.ENSP00000255040.

    Chemistry

    ChEMBLi CHEMBL4929.

    Protein family/group databases

    TCDBi 1.C.92.1.2. the pentraxin (pentraxin) family.

    PTM databases

    PhosphoSitei P02743.
    UniCarbKBi P02743.

    Polymorphism databases

    DMDMi 730704.

    2D gel databases

    DOSAC-COBS-2DPAGE P02743.
    OGPi P02743.
    REPRODUCTION-2DPAGE IPI00022391.
    P02743.
    SWISS-2DPAGE P02743.

    Proteomic databases

    PaxDbi P02743.
    PeptideAtlasi P02743.
    PRIDEi P02743.

    Protocols and materials databases

    DNASUi 325.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000255040 ; ENSP00000255040 ; ENSG00000132703 .
    GeneIDi 325.
    KEGGi hsa:325.
    UCSCi uc001ftv.3. human.

    Organism-specific databases

    CTDi 325.
    GeneCardsi GC01P159557.
    HGNCi HGNC:584. APCS.
    HPAi CAB007817.
    HPA053294.
    MIMi 104770. gene.
    neXtProti NX_P02743.
    PharmGKBi PA24877.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG44770.
    HOGENOMi HOG000247043.
    HOVERGENi HBG005405.
    InParanoidi P02743.
    OMAi AEFWING.
    OrthoDBi EOG71RXMB.
    PhylomeDBi P02743.
    TreeFami TF330208.

    Enzyme and pathway databases

    Reactomei REACT_75925. Amyloids.

    Miscellaneous databases

    EvolutionaryTracei P02743.
    GeneWikii Serum_amyloid_P_component.
    GenomeRNAii 325.
    NextBioi 1333.
    PROi P02743.
    SOURCEi Search...

    Gene expression databases

    Bgeei P02743.
    CleanExi HS_APCS.
    Genevestigatori P02743.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR001759. Pentaxin.
    [Graphical view ]
    Pfami PF00354. Pentaxin. 1 hit.
    [Graphical view ]
    PRINTSi PR00895. PENTAXIN.
    SMARTi SM00159. PTX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS00289. PENTAXIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-141.

    Entry informationi

    Entry nameiSAMP_HUMAN
    AccessioniPrimary (citable) accession number: P02743
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 170 of the entry and version 2 of the sequence. [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

    External Data

    Dasty 3