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Protein

Serum amyloid A-1 protein

Gene

SAA1

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

Functioni

Major acute phase protein.

GO - Molecular functioni

  1. chemoattractant activity Source: GO_Central
  2. G-protein coupled receptor binding Source: UniProtKB
  3. heparin binding Source: UniProtKB-KW

GO - Biological processi

  1. activation of MAPK activity Source: CACAO
  2. acute-phase response Source: UniProtKB
  3. innate immune response Source: Reactome
  4. lymphocyte chemotaxis Source: UniProtKB
  5. macrophage chemotaxis Source: UniProtKB
  6. negative regulation of inflammatory response Source: UniProtKB
  7. neutrophil chemotaxis Source: UniProtKB
  8. platelet activation Source: UniProtKB
  9. positive chemotaxis Source: GOC
  10. positive regulation of cell adhesion Source: UniProtKB
  11. positive regulation of cytokine secretion Source: UniProtKB
  12. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
  13. positive regulation of interleukin-1 secretion Source: UniProtKB
  14. receptor-mediated endocytosis Source: Reactome
  15. regulation of protein secretion Source: UniProtKB
Complete GO annotation...

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_163773. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
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 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:10513. SAA1.

Subcellular locationi

  1. Secreted 1 Publication

GO - Cellular componenti

  1. cytoplasmic microtubule Source: CACAO
  2. endocytic vesicle lumen Source: Reactome
  3. extracellular region Source: UniProtKB
  4. extracellular space Source: GO_Central
  5. extracellular vesicular exosome Source: UniProtKB
  6. high-density lipoprotein particle Source: UniProtKB-KW
Complete GO annotation...

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.

Elevated serum SAA1 protein levels may be associated with lung cancer.

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.

Chemistry

DrugBankiDB00062. Human Serum Albumin.
DB00064. Serum albumin iodonated.

Polymorphism and mutation databases

BioMutaiSAA1.
DMDMi395406826.

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.
ExpressionAtlasiP0DJI8. baseline.
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 – 4527Combined sources
Helixi51 – 6515Combined sources
Helixi67 – 8620Combined sources
Helixi91 – 10515Combined sources
Helixi110 – 1134Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP0DJI8.
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

        10         20         30         40         50
MKLLTGLVFC SLVLGVSSRS FFSFLGEAFD GARDMWRAYS DMREANYIGS
60 70 80 90 100
DKYFHARGNY DAAKRGPGGV WAAEAISDAR ENIQRFFGHG AEDSLADQAA
110 120
NEWGRSGKDP NHFRPAGLPE KY
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:
EMBLi
GenBanki
DDBJi
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 and mutation databases

BioMutaiSAA1.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Chemistry

DrugBankiDB00062. Human Serum Albumin.
DB00064. Serum albumin iodonated.

Polymorphism and mutation databases

BioMutaiSAA1.
DMDMi395406826.

2D gel databases

UCD-2DPAGEP02735.

Proteomic databases

PeptideAtlasiP02735.
PRIDEiP0DJI8.

Protocols and materials databases

DNASUi6288.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6288.
GeneCardsiGC11P018287.
H-InvDBHIX0009484.
HGNCiHGNC:10513. SAA1.
MIMi104750. gene.
neXtProtiNX_P0DJI8.
Orphaneti85445. Secondary amyloidosis.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG26520.
HOVERGENiHBG016327.
InParanoidiP0DJI8.
KOiK17310.
OrthoDBiEOG7QVM4V.
PhylomeDBiP0DJI8.
TreeFamiTF332544.

Enzyme and pathway databases

ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_163679. Scavenging by Class B Receptors.
REACT_163773. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
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

ChiTaRSiSAA1. human.
GeneWikiiSerum_amyloid_A1.
GenomeRNAii6288.
NextBioi24415.
PMAP-CutDBQ6FG67.
PROiP0DJI8.
SOURCEiSearch...

Gene expression databases

BgeeiP0DJI8.
CleanExiHS_SAA1.
ExpressionAtlasiP0DJI8. baseline.
GenevestigatoriP02735.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  25. "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: April 29, 2015
This is version 30 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.