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P0DJI8

- SAA1_HUMAN

UniProt

P0DJI8 - SAA1_HUMAN

Protein

Serum amyloid A-1 protein

Gene

SAA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Major acute phase protein.

    GO - Molecular functioni

    1. G-protein coupled receptor binding Source: UniProtKB
    2. heparin binding Source: UniProtKB-KW

    GO - Biological processi

    1. acute-phase response Source: UniProtKB
    2. innate immune response Source: Reactome
    3. lymphocyte chemotaxis Source: UniProtKB
    4. macrophage chemotaxis Source: UniProtKB
    5. negative regulation of inflammatory response Source: UniProtKB
    6. neutrophil chemotaxis Source: UniProtKB
    7. platelet activation Source: UniProtKB
    8. positive regulation of cell adhesion Source: UniProtKB
    9. positive regulation of cytokine secretion Source: UniProtKB
    10. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
    11. positive regulation of interleukin-1 secretion Source: UniProtKB
    12. regulation of protein secretion Source: UniProtKB

    Keywords - Biological processi

    Acute phase

    Keywords - Ligandi

    Heparin-binding

    Enzyme and pathway databases

    ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
    REACT_163679. Scavenging by Class B Receptors.
    REACT_18283. G alpha (q) signalling events.
    REACT_19231. G alpha (i) signalling events.
    REACT_21264. Formyl peptide receptors bind formyl peptides and many other ligands.
    REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_24969. TRAF6 mediated NF-kB activation.
    REACT_25195. Advanced glycosylation endproduct receptor signaling.
    REACT_75925. Amyloids.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serum amyloid A-1 protein
    Short name:
    SAA
    Cleaved into the following 6 chains:
    Gene namesi
    Name:SAA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:10513. SAA1.

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. endocytic vesicle lumen Source: Reactome
    2. extracellular region Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. high-density lipoprotein particle Source: UniProtKB-KW

    Keywords - Cellular componenti

    Amyloid, HDL, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Reactive, secondary amyloidosis is characterized by the extracellular accumulation in various tissues of the SAA1 protein. These deposits are highly insoluble and resistant to proteolysis; they disrupt tissue structure and compromise function.1 Publication
    Elevated serum SAA1 protein levels may be associated with lung cancer.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi19 – 191R → A: Reduces affinity for heparin and nearly abolishes association with HDL; when associated with A-80 and A-89. 1 Publication
    Mutagenesisi33 – 331R → A: Reduces affinity for heparin; when associated with A-37 and A-65. 1 Publication
    Mutagenesisi37 – 371R → A: Reduces affinity for heparin; when associated with A-33 and A-65. 1 Publication
    Mutagenesisi65 – 651R → A: Reduces affinity for heparin; when associated with A-33 and A-37. 1 Publication
    Mutagenesisi80 – 801R → A: Reduces affinity for heparin and nearly abolishes association with HDL; when associated with A-18 and A-89. 1 Publication
    Mutagenesisi89 – 891H → A: Reduces affinity for heparin and nearly abolishes association with HDL; when associated with A-18 and A-80. 1 Publication

    Keywords - Diseasei

    Amyloidosis

    Organism-specific databases

    Orphaneti85445. Secondary amyloidosis.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18189 PublicationsAdd
    BLAST
    Chaini19 – 122104Serum amyloid A-1 proteinPRO_0000031575Add
    BLAST
    Chaini19 – 9476Amyloid protein APRO_0000031576Add
    BLAST
    Chaini20 – 122103Serum amyloid protein A(2-104)PRO_0000031577Add
    BLAST
    Chaini20 – 121102Serum amyloid protein A(2-103)PRO_0000031578Add
    BLAST
    Chaini20 – 120101Serum amyloid protein A(2-102)PRO_0000031579Add
    BLAST
    Chaini21 – 122102Serum amyloid protein A(3-104)PRO_0000031580Add
    BLAST
    Chaini22 – 11998Serum amyloid protein A(4-101)PRO_0000031581Add
    BLAST
    Propeptidei95 – 12228Often cleaved during amyloidogenesisPRO_0000031582Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei101 – 1011N4,N4-dimethylasparagine1 Publication

    Post-translational modificationi

    This protein is the precursor of amyloid protein A, which is formed by the removal of approximately 24 residues from the C-terminal end.

    Keywords - PTMi

    Methylation

    Proteomic databases

    PeptideAtlasiP02735.
    PRIDEiP0DJI8.

    2D gel databases

    UCD-2DPAGEP02735.

    Miscellaneous databases

    PMAP-CutDBQ6FG67.

    Expressioni

    Tissue specificityi

    Expressed by the liver; secreted in plasma (at protein level).3 Publications

    Inductioni

    Upon cytokine stimulation.

    Gene expression databases

    BgeeiP0DJI8.
    CleanExiHS_SAA1.
    GenevestigatoriP02735.

    Interactioni

    Subunit structurei

    Homohexamer; dimer of trimers. Can form amyloid fibrils after partial proteolysis; the native, undenatured protein does not form amyloid fibrils (in vitro). Apolipoprotein of the HDL complex. Binds to heparin.2 Publications

    Structurei

    Secondary structure

    1
    122
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi19 – 4527
    Helixi51 – 6515
    Helixi67 – 8620
    Helixi91 – 10515
    Helixi110 – 1134

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4IP8X-ray2.19A/B/C/D19-122[»]
    4IP9X-ray2.50A/B19-122[»]
    ProteinModelPortaliP0DJI8.
    SMRiP0DJI8. Positions 19-122.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni19 – 4527Important for amyloid formation; forms amyloid fibrils in vitroAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SAA family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG26520.
    HOVERGENiHBG016327.
    InParanoidiP02735.
    KOiK17310.
    OrthoDBiEOG7QVM4V.
    PhylomeDBiP0DJI8.
    TreeFamiTF332544.

    Family and domain databases

    InterProiIPR000096. Serum_amyloid_A.
    [Graphical view]
    PfamiPF00277. SAA. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002472. Serum_amyloid_A. 1 hit.
    PRINTSiPR00306. SERUMAMYLOID.
    SMARTiSM00197. SAA. 1 hit.
    [Graphical view]
    PROSITEiPS00992. SAA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0DJI8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLLTGLVFC SLVLGVSSRS FFSFLGEAFD GARDMWRAYS DMREANYIGS    50
    DKYFHARGNY DAAKRGPGGV WAAEAISDAR ENIQRFFGHG AEDSLADQAA 100
    NEWGRSGKDP NHFRPAGLPE KY 122
    Length:122
    Mass (Da):13,532
    Last modified:July 11, 2012 - v1
    Checksum:i43A57D56B37CB173
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti71 – 711W → R AA sequence (PubMed:6155694)Curated
    Sequence conflicti71 – 711W → R AA sequence (PubMed:5055786)Curated
    Sequence conflicti77 – 771S → T in AC107948. (PubMed:16554811)Curated
    Sequence conflicti96 – 1016ADQAAN → SEATVK AA sequence (PubMed:1546977)Curated
    Sequence conflicti101 – 1011N → D in AAH07022. (PubMed:15489334)Curated
    Sequence conflicti119 – 1191P → S in AAA60297. (PubMed:3839415)Curated

    Mass spectrometryi

    Molecular mass is 11702±14 Da from positions 19 - 122. Determined by MALDI. 1 Publication
    Molecular mass is 11682.7 Da from positions 19 - 122. Determined by MALDI. 1 Publication
    Molecular mass is 11526.5 Da from positions 20 - 122. Determined by MALDI. 1 Publication
    Molecular mass is 11439.6 Da from positions 21 - 122. Determined by MALDI. 1 Publication
    Molecular mass is 11363.6 Da from positions 20 - 121. Determined by MALDI. 1 Publication
    Molecular mass is 11235.6 Da from positions 20 - 120. Determined by MALDI. 1 Publication
    Molecular mass is 10872.6 Da from positions 22 - 119. Determined by MALDI. 1 Publication
    Molecular mass is 8337.5±0.8 Da from positions 19 - 94. Determined by ESI. With variants Ala-70, Val-75, Asn-78 and 86-Leu-Thr-87.1 Publication
    Molecular mass is 8390.9±0.2 Da from positions 19 - 94. Determined by ESI. With variant Ala-70.1 Publication

    Polymorphismi

    At least 5 different SAA1 alleles have been described: SAA1.1 (SAA1alpha), SAA1.2 (SAA1beta), SAA1.3 (SAA1gamma), SAA1.4 (SAA1delta), SAA1.5 (also named SAA1beta but which differs from SAA1.2). We use here the revised nomenclature described in PubMed:10211414. The sequence shown is that of SAA1.1.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151G → S.
    Corresponds to variant rs712021 [ dbSNP | Ensembl ].
    VAR_006925
    Natural varianti70 – 701V → A in allele SAA1.2, SAA1.3, SAA1.4 and SAA1.5. 1 Publication
    VAR_006926
    Natural varianti75 – 751A → V in allele SAA1.2, SAA1.4 and SAA1.5. 2 Publications
    VAR_006927
    Natural varianti78 – 781D → N in allele SAA1.4. 2 Publications
    VAR_006928
    Natural varianti86 – 861F → L.
    Corresponds to variant rs1059559 [ dbSNP | Ensembl ].
    VAR_057167
    Natural varianti90 – 901G → D in allele SAA1.2.
    VAR_006931

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10906 mRNA. Translation: AAA60297.1.
    M23698 mRNA. Translation: AAA64799.1.
    X56652 Genomic DNA. Translation: CAA39974.1.
    CR542241 mRNA. Translation: CAG47037.1.
    AC107948 Genomic DNA. No translation available.
    BC007022 mRNA. Translation: AAH07022.1.
    BC105796 mRNA. Translation: AAI05797.1.
    X51439 mRNA. Translation: CAA35804.1.
    X51441 mRNA. Translation: CAA35806.1.
    X51442 mRNA. Translation: CAA35807.1.
    CCDSiCCDS7835.1.
    PIRiA22342. YLHUS.
    I39456.
    RefSeqiNP_000322.2. NM_000331.4.
    NP_001171477.1. NM_001178006.1.
    NP_954630.1. NM_199161.3.
    UniGeneiHs.632144.
    Hs.731376.
    Hs.734161.

    Genome annotation databases

    EnsembliENST00000356524; ENSP00000348918; ENSG00000173432.
    ENST00000405158; ENSP00000384906; ENSG00000173432.
    GeneIDi6288.
    KEGGihsa:6288.

    Polymorphism databases

    DMDMi395406826.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10906 mRNA. Translation: AAA60297.1 .
    M23698 mRNA. Translation: AAA64799.1 .
    X56652 Genomic DNA. Translation: CAA39974.1 .
    CR542241 mRNA. Translation: CAG47037.1 .
    AC107948 Genomic DNA. No translation available.
    BC007022 mRNA. Translation: AAH07022.1 .
    BC105796 mRNA. Translation: AAI05797.1 .
    X51439 mRNA. Translation: CAA35804.1 .
    X51441 mRNA. Translation: CAA35806.1 .
    X51442 mRNA. Translation: CAA35807.1 .
    CCDSi CCDS7835.1.
    PIRi A22342. YLHUS.
    I39456.
    RefSeqi NP_000322.2. NM_000331.4.
    NP_001171477.1. NM_001178006.1.
    NP_954630.1. NM_199161.3.
    UniGenei Hs.632144.
    Hs.731376.
    Hs.734161.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4IP8 X-ray 2.19 A/B/C/D 19-122 [» ]
    4IP9 X-ray 2.50 A/B 19-122 [» ]
    ProteinModelPortali P0DJI8.
    SMRi P0DJI8. Positions 19-122.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    DrugBanki DB00062. Human Serum Albumin.
    DB00064. Serum albumin iodonated.

    Polymorphism databases

    DMDMi 395406826.

    2D gel databases

    UCD-2DPAGE P02735.

    Proteomic databases

    PeptideAtlasi P02735.
    PRIDEi P0DJI8.

    Protocols and materials databases

    DNASUi 6288.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356524 ; ENSP00000348918 ; ENSG00000173432 .
    ENST00000405158 ; ENSP00000384906 ; ENSG00000173432 .
    GeneIDi 6288.
    KEGGi hsa:6288.

    Organism-specific databases

    CTDi 6288.
    GeneCardsi GC11P018287.
    H-InvDB HIX0009484.
    HGNCi HGNC:10513. SAA1.
    MIMi 104750. gene.
    neXtProti NX_P0DJI8.
    Orphaneti 85445. Secondary amyloidosis.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG26520.
    HOVERGENi HBG016327.
    InParanoidi P02735.
    KOi K17310.
    OrthoDBi EOG7QVM4V.
    PhylomeDBi P0DJI8.
    TreeFami TF332544.

    Enzyme and pathway databases

    Reactomei REACT_118563. RIP-mediated NFkB activation via ZBP1.
    REACT_163679. Scavenging by Class B Receptors.
    REACT_18283. G alpha (q) signalling events.
    REACT_19231. G alpha (i) signalling events.
    REACT_21264. Formyl peptide receptors bind formyl peptides and many other ligands.
    REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_24969. TRAF6 mediated NF-kB activation.
    REACT_25195. Advanced glycosylation endproduct receptor signaling.
    REACT_75925. Amyloids.

    Miscellaneous databases

    ChiTaRSi SAA1. human.
    GeneWikii Serum_amyloid_A1.
    GenomeRNAii 6288.
    NextBioi 24415.
    PMAP-CutDB Q6FG67.
    PROi P0DJI8.
    SOURCEi Search...

    Gene expression databases

    Bgeei P0DJI8.
    CleanExi HS_SAA1.
    Genevestigatori P02735.

    Family and domain databases

    InterProi IPR000096. Serum_amyloid_A.
    [Graphical view ]
    Pfami PF00277. SAA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002472. Serum_amyloid_A. 1 hit.
    PRINTSi PR00306. SERUMAMYLOID.
    SMARTi SM00197. SAA. 1 hit.
    [Graphical view ]
    PROSITEi PS00992. SAA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human serum amyloid A (SAA): biosynthesis and postsynthetic processing of preSAA and structural variants defined by complementary DNA."
      Sipe J.D., Colten H.R., Goldberger G., Edge M.D., Tack B.F., Cohen A.S., Whitehead A.S.
      Biochemistry 24:2931-2936(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE SAA1.1).
    2. "Human serum amyloid A. Three hepatic mRNAs and the corresponding proteins in one person."
      Kluve-Beckerman B., Dwulet F.E., Benson M.D.
      J. Clin. Invest. 82:1670-1675(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE SAA1.1).
      Tissue: Liver.
    3. "The human acute-phase serum amyloid A gene family: structure, evolution and expression in hepatoma cells."
      Betts J., Edbrooke M., Thakker R., Woo P.
      Scand. J. Immunol. 34:471-482(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE SAA1.5).
      Tissue: Liver.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE SAA1.5).
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE SAA1.5).
    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] (ALLELE SAA1.1).
      Tissue: Liver.
    7. "Heterogeneity of human serum amyloid A protein. Five different variants from one individual demonstrated by cDNA sequence analysis."
      Steinkasserer A., Weiss E.H., Schwaeble W., Linke R.P.
      Biochem. J. 268:187-193(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 73-122, VARIANTS VAL-75 AND ASN-78.
      Tissue: Liver.
    8. "Amino acid sequence of amyloid-related apoprotein (apoSAA1) from human high-density lipoprotein."
      Parmelee D.C., Titani K., Ericsson L.H., Eriksen N., Benditt E.P., Walsh K.A.
      Biochemistry 21:3298-3303(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-122, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY.
    9. "Human serum amyloid A protein. Complete amino acid sequence of a new variant."
      Beach C.M., de Beer M.C., Sipe J.D., Loose L.D., de Beer F.C.
      Biochem. J. 282:615-620(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-122 (ALLELE SAA1.2).
    10. "An unusually large (83 amino acid residues) amyloid fibril protein AA from a patient with Waldenstrom's macroglobulinaemia and amyloidosis."
      Moyner K., Sletten K., Husby G., Natvig J.B.
      Scand. J. Immunol. 11:549-554(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-101.
    11. "Amino acid sequence of an amyloid fibril protein of unknown origin."
      Ein D., Kimura S., Terry W.D., Magnotta J., Glenner G.G.
      J. Biol. Chem. 247:5653-5655(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-94.
    12. "The amino acid sequence of a major nonimmunoglobulin component of some amyloid fibrils."
      Levin M., Franklin E.C., Frangione B., Pras M.
      J. Clin. Invest. 51:2773-2776(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-94 (FAMILIAL MEDITERRANEAN FEVER PATIENT).
    13. "The complete amino-acid sequence of non-immunoglobulin amyloid fibril protein AS in rheumatoid arthritis."
      Sletten K., Husby G.
      Eur. J. Biochem. 41:117-125(1974) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-94, TISSUE SPECIFICITY.
    14. "Identification of two novel amyloid A protein subsets coexisting in an individual patient of AA-amyloidosis."
      Baba S., Takahashi T., Kasama T., Shirasawa H.
      Biochim. Biophys. Acta 1180:195-200(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-94, MASS SPECTROMETRY, DISEASE, VARIANTS ALA-70; VAL-75 AND ASN-78, ALLELE SAA1.3.
      Tissue: Thyroid.
    15. "The complete amino acid sequence of an amyloid fibril protein AA1 of unusual size (64 residues)."
      Sletten K., Husby G., Natvig J.B.
      Biochem. Biophys. Res. Commun. 69:19-25(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-82.
    16. "The major proteins of human and monkey amyloid substance: common properties including unusual N-terminal amino acid sequences."
      Benditt E.P., Eriksen N., Hermodson M.A., Ericsson L.H.
      FEBS Lett. 19:169-173(1971) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-42.
    17. "Degradation and deposition of amyloid AA fibrils are tissue specific."
      Prelli F., Pras M., Frangione B.
      Biochemistry 26:8251-8256(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-100.
    18. "Identification and validation of a potential lung cancer serum biomarker detected by matrix-assisted laser desorption/ionization-time of flight spectra analysis."
      Howard B.A., Wang M.Z., Campa M.J., Corro C., Fitzgerald M.C., Patz E.F. Jr.
      Proteomics 3:1720-1724(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-33; 44-57; 64-80 AND 86-122, TISSUE SPECIFICITY, MASS SPECTROMETRY.
    19. "Characterization of human serum amyloid A protein isoforms separated by two-dimensional electrophoresis by liquid chromatography/electrospray ionization tandem mass spectrometry."
      Ducret A., Bruun C.F., Bures E.J., Marhaug G., Husby G., Aebersold R.
      Electrophoresis 17:866-876(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE (VARIOUS FORMS), METHYLATION AT ASN-101.
    20. "A protein AA-variant derived from a novel serum AA protein, SAA1 delta, in an individual from Papua New Guinea."
      Westermark P., Sletten K., Westermark G.T., Raynes J., McAdam K.P.
      Biochem. Biophys. Res. Commun. 223:320-323(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF ALLELE SAA1.4.
    21. "Revised nomenclature for serum amyloid A (SAA). Nomenclature Committee of the International Society of Amyloidosis. Part 2."
      Sipe J.
      Amyloid 6:67-70(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLYMORPHISM, NOMENCLATURE OF ALLELES.
    22. "Detection of novel truncated forms of human serum amyloid A protein in human plasma."
      Kiernan U.A., Tubbs K.A., Nedelkov D., Niederkofler E.E., Nelson R.W.
      FEBS Lett. 537:166-170(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY.
    23. "A novel polymorphism of human serum amyloid A protein, SAA1 gamma, is characterized by alanines at both residues 52 and 57."
      Baba S., Takahashi T., Kasama T., Fujie M., Shirasawa H.
      Arch. Biochem. Biophys. 303:361-366(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF ALLELE SAA1.3.
    24. "Structural mechanism of serum amyloid A-mediated inflammatory amyloidosis."
      Lu J., Yu Y., Zhu I., Cheng Y., Sun P.D.
      Proc. Natl. Acad. Sci. U.S.A. 111:5189-5194(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 19-122, SUBUNIT, MUTAGENESIS OF ARG-19; ARG-33; ARG-37; ARG-65; ARG-80 AND HIS-89.

    Entry informationi

    Entry nameiSAA1_HUMAN
    AccessioniPrimary (citable) accession number: P0DJI8
    Secondary accession number(s): P02735
    , P02736, P02737, Q16730, Q16834, Q16835, Q16879, Q3KRB3, Q6FG67, Q96QN0, Q9UCK9, Q9UCL0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2012
    Last sequence update: July 11, 2012
    Last modified: October 1, 2014
    This is version 24 of the entry and version 1 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 11
      Human chromosome 11: 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