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P06702

- S10A9_HUMAN

UniProt

P06702 - S10A9_HUMAN

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Protein

Protein S100-A9

Gene
S100A9, CAGB, CFAG, MRP14
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

S100A9 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis, adhesion, can increase the bactericidal activity of neutrophils by promoting phagocytosis via activation of SYK, PI3K/AKT, and ERK1/2 and can induce degranulation of neutrophils by a MAPK-dependent mechanism. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve proinfammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its proinflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the proinflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn2+ which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread.17 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi20 – 201Zinc Inferred
Metal bindingi30 – 301Zinc Inferred
Metal bindingi91 – 911Zinc Inferred
Metal bindingi95 – 951Zinc Inferred

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi23 – 36141; low affinityAdd
BLAST
Calcium bindingi67 – 78122; high affinity InferredAdd
BLAST

GO - Molecular functioni

  1. antioxidant activity Source: UniProtKB-KW
  2. arachidonic acid binding Source: UniProtKB
  3. calcium ion binding Source: UniProtKB
  4. microtubule binding Source: UniProtKB
  5. protein binding Source: IntAct
  6. RAGE receptor binding Source: UniProtKB
  7. signal transducer activity Source: ProtInc
  8. Toll-like receptor 4 binding Source: UniProtKB
  9. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. actin cytoskeleton reorganization Source: Ensembl
  2. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  3. autophagy Source: UniProtKB
  4. cell-cell signaling Source: ProtInc
  5. chemokine production Source: UniProtKB
  6. chronic inflammatory response Source: Ensembl
  7. cytokine production Source: UniProtKB
  8. defense response to bacterium Source: UniProtKB
  9. defense response to fungus Source: UniProtKB
  10. inflammatory response Source: ProtInc
  11. innate immune response Source: UniProtKB-KW
  12. leukocyte migration involved in inflammatory response Source: UniProtKB
  13. neutrophil aggregation Source: UniProtKB
  14. neutrophil chemotaxis Source: UniProtKB
  15. positive regulation of cell growth Source: UniProtKB
  16. positive regulation of inflammatory response Source: UniProtKB
  17. positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  18. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  19. regulation of cytoskeleton organization Source: UniProtKB
  20. regulation of integrin biosynthetic process Source: Ensembl
  21. response to ethanol Source: Ensembl
  22. response to lipopolysaccharide Source: Ensembl
  23. response to zinc ion Source: Ensembl
  24. sequestering of zinc ion Source: UniProtKB
  25. signal transduction Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Antioxidant

Keywords - Biological processi

Apoptosis, Autophagy, Chemotaxis, Immunity, Inflammatory response, Innate immunity

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Protein S100-A9
Alternative name(s):
Calgranulin-B
Calprotectin L1H subunit
Leukocyte L1 complex heavy chain
Migration inhibitory factor-related protein 14
Short name:
MRP-14
Short name:
p14
S100 calcium-binding protein A9
Gene namesi
Name:S100A9
Synonyms:CAGB, CFAG, MRP14
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:10499. S100A9.

Subcellular locationi

Secreted. Cytoplasm. Cytoplasmcytoskeleton. Cell membrane; Peripheral membrane protein
Note: Predominantly localized in the cytoplasm. Upon elevation of the intracellular calcium level, translocated from the cytoplasm to the cytoskeleton and the cell membrane. Upon neutrophil activation or endothelial adhesion of monocytes, is secreted via a microtubule-mediated, alternative pathway.6 Publications

GO - Cellular componenti

  1. cytoskeleton Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. extracellular region Source: UniProtKB
  4. extracellular space Source: UniProt
  5. extracellular vesicular exosome Source: UniProt
  6. nucleus Source: UniProt
  7. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi36 – 361E → Q: Loss of resistance to bacterial invasion; when associated with Q-78. 1 Publication
Mutagenesisi63 – 631M → A: Loss of antifungal activity. 1 Publication
Mutagenesisi78 – 781E → Q: Loss of resistance to bacterial invasion; when associated with Q-36. 1 Publication
Mutagenesisi81 – 811M → A: No effect on antifungal activity. 1 Publication
Mutagenesisi83 – 831M → A: Loss of antifungal activity. 1 Publication

Organism-specific databases

PharmGKBiPA34911.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 114113Protein S100-A9PRO_0000143997Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21Blocked amino end (Thr)
Modified residuei105 – 1051Pros-methylhistidine By similarity
Modified residuei113 – 1131Phosphothreonine; by MAPK146 Publications

Post-translational modificationi

Phosphorylated. Phosphorylation inhibits activation of tubulin polymerization.3 Publications

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiP06702.
PaxDbiP06702.
PeptideAtlasiP06702.
PRIDEiP06702.

2D gel databases

OGPiP06702.
SWISS-2DPAGEP06702.
UCD-2DPAGEP06702.

PTM databases

PhosphoSiteiP06702.

Expressioni

Tissue specificityi

Calprotectin (S100A8/9) is predominantly expressed in myeloid cells. Except for inflammatory conditions, the expression is restricted to a specific stage of myeloid differentiation since both proteins are expressed in circulating neutrophils and monocytes but are absent in normal tissue macrophages and lymphocytes. Under chronic inflammatory conditions, such as psoriasis and malignant disorders, also expressed in the epidermis. Found in high concentrations at local sites of inflammation or in the serum of patients with inflammatory diseases such as rheumatoid, cystic fibrosis, inflammatory bowel disease, Crohn's disease, giant cell arteritis, cystic fibrosis, Sjogren's syndrome, systemic lupus erythematosus, and progressive systemic sclerosis. Involved in the formation and deposition of amyloids in the aging prostate known as corpora amylacea inclusions. Strongly up-regulated in many tumors, including gastric, esophageal, colon, pancreatic, bladder, ovarian, thyroid, breast and skin cancers.5 Publications

Gene expression databases

BgeeiP06702.
CleanExiHS_S100A9.
GenevestigatoriP06702.

Organism-specific databases

HPAiCAB009441.
HPA004193.

Interactioni

Subunit structurei

Homodimer. Preferentially exists as a heterodimer or heterotetramer with S100A8 known as calprotectin (S100A8/A9). S100A9 interacts with ATP2A2 By similarity. S100A9 interacts with AGER, and with the heterodimeric complex formed by TLR4 and LY96 in the presence of calcium and/or zinc ions. S100A9 binds quinoline-3-carboxamides in the presence of calcium and/or zinc ions. S100A9 interacts with beta-APP40 (beta-amyloid protein 40) peptide of APP. Calprotectin (S100A8/9) interacts with CEACAM3 and tubulin filaments in a calcium-dependent manner. Heterotetrameric calprotectin (S100A8/A9) interacts with ANXA6 and associates with tubulin filaments in activated monocytes. Calprotectin (S100A8/9) interacts with NCF2/P67PHOX, RAC1, RAC2, CYBA and CYBB.14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARRB1P494072EBI-1055001,EBI-743313
ARRB2P321212EBI-1055001,EBI-714559
S100A8P051093EBI-1055001,EBI-355281

Protein-protein interaction databases

BioGridi112188. 79 interactions.
DIPiDIP-1166N.
IntActiP06702. 19 interactions.
MINTiMINT-5002390.
STRINGi9606.ENSP00000357727.

Structurei

Secondary structure

1
114
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2317
Beta strandi25 – 284
Helixi34 – 4411
Turni45 – 495
Helixi50 – 534
Helixi56 – 6611
Beta strandi71 – 744
Helixi76 – 9419
Turni95 – 973

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IRJX-ray2.10A/B/C/D/E/F/G/H2-114[»]
1XK4X-ray1.80C/D/G/H/K/L2-114[»]
4GGFX-ray1.60C/L/T/V1-114[»]
ProteinModelPortaliP06702.
SMRiP06702. Positions 4-112.

Miscellaneous databases

EvolutionaryTraceiP06702.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 4736EF-hand 1Add
BLAST
Domaini54 – 8936EF-hand 2Add
BLAST

Sequence similaritiesi

Belongs to the S-100 family.
Contains 2 EF-hand domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG47012.
HOGENOMiHOG000246968.
HOVERGENiHBG001479.
InParanoidiP06702.
OMAiHEKMHEN.
OrthoDBiEOG73807B.
PhylomeDBiP06702.
TreeFamiTF332727.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR028475. S100-A9.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]
PANTHERiPTHR11639:SF53. PTHR11639:SF53. 1 hit.
PfamiPF01023. S_100. 1 hit.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P06702-1 [UniParc]FASTAAdd to Basket

« Hide

MTCKMSQLER NIETIINTFH QYSVKLGHPD TLNQGEFKEL VRKDLQNFLK    50
KENKNEKVIE HIMEDLDTNA DKQLSFEEFI MLMARLTWAS HEKMHEGDEG 100
PGHHHKPGLG EGTP 114
Length:114
Mass (Da):13,242
Last modified:January 1, 1988 - v1
Checksum:iC3BE19729E14C078
GO

Mass spectrometryi

Molecular mass is 13115 Da from positions 2 - 114. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201H → R.1 Publication
VAR_013008

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61S → H AA sequence 1 Publication
Sequence conflicti25 – 251K → F AA sequence 1 Publication
Sequence conflicti28 – 281H → L AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06233 mRNA. Translation: CAA29579.1.
M21064 Genomic DNA. Translation: AAA36326.1.
M26311 mRNA. Translation: AAA68480.1.
AF237581 Genomic DNA. Translation: AAF62536.1.
AF237582 Genomic DNA. Translation: AAF62537.1.
CR542207 mRNA. Translation: CAG47003.1.
CR542224 mRNA. Translation: CAG47020.1.
AL591704 Genomic DNA. Translation: CAI19494.1.
CH471121 Genomic DNA. Translation: EAW53333.1.
CH471121 Genomic DNA. Translation: EAW53334.1.
BC047681 mRNA. Translation: AAH47681.1.
CCDSiCCDS1036.1.
PIRiB31848.
RefSeqiNP_002956.1. NM_002965.3.
UniGeneiHs.112405.

Genome annotation databases

EnsembliENST00000368738; ENSP00000357727; ENSG00000163220.
GeneIDi6280.
KEGGihsa:6280.
UCSCiuc001fbq.3. human.

Polymorphism databases

DMDMi115444.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06233 mRNA. Translation: CAA29579.1 .
M21064 Genomic DNA. Translation: AAA36326.1 .
M26311 mRNA. Translation: AAA68480.1 .
AF237581 Genomic DNA. Translation: AAF62536.1 .
AF237582 Genomic DNA. Translation: AAF62537.1 .
CR542207 mRNA. Translation: CAG47003.1 .
CR542224 mRNA. Translation: CAG47020.1 .
AL591704 Genomic DNA. Translation: CAI19494.1 .
CH471121 Genomic DNA. Translation: EAW53333.1 .
CH471121 Genomic DNA. Translation: EAW53334.1 .
BC047681 mRNA. Translation: AAH47681.1 .
CCDSi CCDS1036.1.
PIRi B31848.
RefSeqi NP_002956.1. NM_002965.3.
UniGenei Hs.112405.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IRJ X-ray 2.10 A/B/C/D/E/F/G/H 2-114 [» ]
1XK4 X-ray 1.80 C/D/G/H/K/L 2-114 [» ]
4GGF X-ray 1.60 C/L/T/V 1-114 [» ]
ProteinModelPortali P06702.
SMRi P06702. Positions 4-112.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112188. 79 interactions.
DIPi DIP-1166N.
IntActi P06702. 19 interactions.
MINTi MINT-5002390.
STRINGi 9606.ENSP00000357727.

PTM databases

PhosphoSitei P06702.

Polymorphism databases

DMDMi 115444.

2D gel databases

OGPi P06702.
SWISS-2DPAGE P06702.
UCD-2DPAGE P06702.

Proteomic databases

MaxQBi P06702.
PaxDbi P06702.
PeptideAtlasi P06702.
PRIDEi P06702.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368738 ; ENSP00000357727 ; ENSG00000163220 .
GeneIDi 6280.
KEGGi hsa:6280.
UCSCi uc001fbq.3. human.

Organism-specific databases

CTDi 6280.
GeneCardsi GC01P153330.
HGNCi HGNC:10499. S100A9.
HPAi CAB009441.
HPA004193.
MIMi 123886. gene.
neXtProti NX_P06702.
PharmGKBi PA34911.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG47012.
HOGENOMi HOG000246968.
HOVERGENi HBG001479.
InParanoidi P06702.
OMAi HEKMHEN.
OrthoDBi EOG73807B.
PhylomeDBi P06702.
TreeFami TF332727.

Miscellaneous databases

ChiTaRSi S100A9. human.
EvolutionaryTracei P06702.
GeneWikii S100A9.
GenomeRNAii 6280.
NextBioi 24377.
PROi P06702.
SOURCEi Search...

Gene expression databases

Bgeei P06702.
CleanExi HS_S100A9.
Genevestigatori P06702.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
InterProi IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR028475. S100-A9.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view ]
PANTHERi PTHR11639:SF53. PTHR11639:SF53. 1 hit.
Pfami PF01023. S_100. 1 hit.
[Graphical view ]
PROSITEi PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Two calcium-binding proteins in infiltrate macrophages of rheumatoid arthritis."
    Odink K., Cerletti N., Bruggen J., Clerc R.G., Tarcsay L., Zwaldo G., Gerhards G., Schlegel R., Sorg C.
    Nature 330:80-82(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "Cloning and expression of two human genes encoding calcium-binding proteins that are regulated during myeloid differentiation."
    Lagasse E., Clerc R.G.
    Mol. Cell. Biol. 8:2402-2410(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
  3. "A protein containing the cystic fibrosis antigen is an inhibitor of protein kinases."
    Murao S., Collart F.R., Huberman E.
    J. Biol. Chem. 264:8356-8360(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], BLOCKAGE OF N-TERMINUS.
  4. "Human gene for migration inhibitory factor-related protein 14 (MRP14), variant allele."
    Wang M., Xu X., Cai Y., Xu H., Han Y., Xu Z., Wu M.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-20.
  5. "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].
  6. "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].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Lung.
  9. "Ionomycin-regulated phosphorylation of the myeloid calcium-binding protein p14."
    Edgeworth J., Freemont P., Hogg N.
    Nature 342:189-192(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 84-114, PHOSPHORYLATION AT THR-113.
  10. "Amino acid sequences of 60B8 antigens induced in HL-60 cells by 1,25-dihydroxyvitamin D3. The antigens are identical with macrophage-related protein-14 and -8."
    Tobe T., Murakami K., Tomita M., Nozawa R.
    Chem. Pharm. Bull. 37:1576-1580(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, BLOCKAGE OF N-TERMINUS.
  11. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
    Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
    Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 11-19; 26-37 AND 94-107.
    Tissue: Keratinocyte.
  12. "In vitro antimicrobial activity of the human neutrophil cytosolic S-100 protein complex, calprotectin, against Capnocytophaga sputigena."
    Miyasaki K.T., Bodeau A.L., Murthy A.R., Lehrer R.I.
    J. Dent. Res. 72:517-523(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 5-34, SUBCELLULAR LOCATION, IDENTIFICATION IN THE CALPROTECTIN COMPLEX, FUNCTION, TISSUE SPECIFICITY.
  13. "Myeloid-related protein (MRP) 8 and MRP14, calcium-binding proteins of the S100 family, are secreted by activated monocytes via a novel, tubulin-dependent pathway."
    Rammes A., Roth J., Goebeler M., Klempt M., Hartmann M., Sorg C.
    J. Biol. Chem. 272:9496-9502(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY.
  14. "The microbial receptor CEACAM3 is linked to the calprotectin complex in granulocytes."
    Streichert T., Ebrahimnejad A., Ganzer S., Flayeh R., Wagener C., Bruemmer J.
    Biochem. Biophys. Res. Commun. 289:191-197(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CEACAM3.
  15. "Proinflammatory activities of S100: proteins S100A8, S100A9, and S100A8/A9 induce neutrophil chemotaxis and adhesion."
    Ryckman C., Vandal K., Rouleau P., Talbot M., Tessier P.A.
    J. Immunol. 170:3233-3242(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "MRP8 and MRP14 control microtubule reorganization during transendothelial migration of phagocytes."
    Vogl T., Ludwig S., Goebeler M., Strey A., Thorey I.S., Reichelt R., Foell D., Gerke V., Manitz M.P., Nacken W., Werner S., Sorg C., Roth J.
    Blood 104:4260-4268(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TUBULIN, PHOSPHORYLATION AT THR-113.
  17. "Myeloid-related proteins 8 and 14 induce a specific inflammatory response in human microvascular endothelial cells."
    Viemann D., Strey A., Janning A., Jurk K., Klimmek K., Vogl T., Hirono K., Ichida F., Foell D., Kehrel B., Gerke V., Sorg C., Roth J.
    Blood 105:2955-2962(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
  18. "The arachidonic acid-binding protein S100A8/A9 promotes NADPH oxidase activation by interaction with p67phox and Rac-2."
    Kerkhoff C., Nacken W., Benedyk M., Dagher M.C., Sopalla C., Doussiere J.
    FASEB J. 19:467-469(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NCF2/P67PHOX; RAC1 AND RAC2.
  19. "Myeloid-related protein-14 is a p38 MAPK substrate in human neutrophils."
    Lominadze G., Rane M.J., Merchant M., Cai J., Ward R.A., McLeish K.R.
    J. Immunol. 174:7257-7267(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-113.
  20. "Regulation of S100A8/A9 (calprotectin) binding to tumor cells by zinc ion and its implication for apoptosis-inducing activity."
    Nakatani Y., Yamazaki M., Chazin W.J., Yui S.
    Mediators Inflamm. 2005:280-292(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INHIBITION BY ZINC IONS, SUBUNIT.
  21. "Interaction between S100A8/A9 and annexin A6 is involved in the calcium-induced cell surface exposition of S100A8/A9."
    Bode G., Lueken A., Kerkhoff C., Roth J., Ludwig S., Nacken W.
    J. Biol. Chem. 283:31776-31784(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ANXA6.
  22. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  23. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  24. Cited for: REVIEW.
  25. "A novel p53 target gene, S100A9, induces p53-dependent cellular apoptosis and mediates the p53 apoptosis pathway."
    Li C., Chen H., Ding F., Zhang Y., Luo A., Wang M., Liu Z.
    Biochem. J. 422:363-372(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  26. "S100A8/A9: a Janus-faced molecule in cancer therapy and tumorgenesis."
    Ghavami S., Chitayat S., Hashemi M., Eshraghi M., Chazin W.J., Halayko A.J., Kerkhoff C.
    Eur. J. Pharmacol. 625:73-83(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  27. "Substitution of methionine 63 or 83 in S100A9 and cysteine 42 in S100A8 abrogate the antifungal activities of S100A8/A9: potential role for oxidative regulation."
    Sroussi H.Y., Koehler G.A., Agabian N., Villines D., Palefsky J.M.
    FEMS Immunol. Med. Microbiol. 55:55-61(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF MET-63; MET-81 AND MET-83, INHIBITION BY ZINC IONS.
  28. "Calprotectin S100A9 calcium-binding loops I and II are essential for keratinocyte resistance to bacterial invasion."
    Champaiboon C., Sappington K.J., Guenther B.D., Ross K.F., Herzberg M.C.
    J. Biol. Chem. 284:7078-7090(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF GLU-36 AND GLU-78.
  29. "The endogenous Toll-like receptor 4 agonist S100A8/S100A9 (calprotectin) as innate amplifier of infection, autoimmunity, and cancer."
    Ehrchen J.M., Sunderkoetter C., Foell D., Vogl T., Roth J.
    J. Leukoc. Biol. 86:557-566(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  30. "Identification of human S100A9 as a novel target for treatment of autoimmune disease via binding to quinoline-3-carboxamides."
    Bjoerk P., Bjoerk A., Vogl T., Stenstroem M., Liberg D., Olsson A., Roth J., Ivars F., Leanderson T.
    PLoS Biol. 7:E97-E97(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH TLR4; LY96 AND AGER, QUINOLINE-3-CARBOXAMIDE BINDING.
  31. "S100A8/A9 induces autophagy and apoptosis via ROS-mediated cross-talk between mitochondria and lysosomes that involves BNIP3."
    Ghavami S., Eshragi M., Ande S.R., Chazin W.J., Klonisch T., Halayko A.J., McNeill K.D., Hashemi M., Kerkhoff C., Los M.
    Cell Res. 20:314-331(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  32. "S100 Calgranulins in inflammatory arthritis."
    Perera C., McNeil H.P., Geczy C.L.
    Immunol. Cell Biol. 88:41-49(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  33. "Induction of neutrophil degranulation by S100A9 via a MAPK-dependent mechanism."
    Simard J.C., Girard D., Tessier P.A.
    J. Leukoc. Biol. 87:905-914(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  34. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  35. "Inflammation-associated S100 proteins: new mechanisms that regulate function."
    Goyette J., Geczy C.L.
    Amino Acids 41:821-842(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  36. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  37. "Damage-associated molecular pattern S100A9 increases bactericidal activity of human neutrophils by enhancing phagocytosis."
    Simard J.C., Simon M.M., Tessier P.A., Girard D.
    J. Immunol. 186:3622-3631(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  38. Cited for: REVIEW.
  39. "Induction of nuclear factor-kappaB responses by the S100A9 protein is Toll-like receptor-4-dependent."
    Riva M., Kaellberg E., Bjoerk P., Hancz D., Vogl T., Roth J., Ivars F., Leanderson T.
    Immunology 137:172-182(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  40. "Dynamic mobility of immunological cells expressing S100A8 and S100A9 in vivo: a variety of functional roles of the two proteins as regulators in acute inflammatory reaction."
    Koike A., Arai S., Yamada S., Nagae A., Saita N., Itoh H., Uemoto S., Totani M., Ikemoto M.
    Inflammation 35:409-419(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  41. "Pro-inflammatory S100A8 and S100A9 proteins: self-assembly into multifunctional native and amyloid complexes."
    Vogl T., Gharibyan A.L., Morozova-Roche L.A.
    Int. J. Mol. Sci. 13:2893-2917(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  42. "S100A8 and S100A9: new insights into their roles in malignancy."
    Srikrishna G.
    J. Innate Immun. 4:31-40(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  43. "Molecular interface of S100A8 with cytochrome b and NADPH oxidase activation."
    Berthier S., Nguyen M.V., Baillet A., Hograindleur M.A., Paclet M.H., Polack B., Morel F.
    PLoS ONE 7:E40277-E40277(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CYBA AND CYBB.
  44. "MRP14 (S100A9) protein interacts with Alzheimer beta-amyloid peptide and induces its fibrillization."
    Zhang C., Liu Y., Gilthorpe J., van der Maarel J.R.
    PLoS ONE 7:E32953-E32953(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APP.
  45. "Constitutive neutrophil apoptosis: regulation by cell concentration via S100 A8/9 and the MEK-ERK pathway."
    Atallah M., Krispin A., Trahtemberg U., Ben-Hamron S., Grau A., Verbovetski I., Mevorach D.
    PLoS ONE 7:E29333-E29333(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  46. "The crystal structure of human MRP14 (S100A9), a Ca(2+)-dependent regulator protein in inflammatory process."
    Itou H., Yao M., Fujita I., Watanabe N., Suzuki M., Nishihira J., Tanaka I.
    J. Mol. Biol. 316:265-276(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, MASS SPECTROMETRY, SUBUNIT.
  47. "The crystal structure of the human (S100A8/S100A9)2 heterotetramer, calprotectin, illustrates how conformational changes of interacting alpha-helices can determine specific association of two EF-hand proteins."
    Korndoerfer I.P., Brueckner F., Skerra A.
    J. Mol. Biol. 370:887-898(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 4-114 IN COMPLEX WITH S100A8, SUBUNIT, ZINC-BINDING.

Entry informationi

Entry nameiS10A9_HUMAN
AccessioniPrimary (citable) accession number: P06702
Secondary accession number(s): D3DV36
, Q6FGA1, Q9NYM0, Q9UCJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: September 3, 2014
This is version 168 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 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

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