Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P05109

- S10A8_HUMAN

UniProt

P05109 - S10A8_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Protein S100-A8

Gene

S100A8

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

Functioni

S100A8 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 and adhesion. 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.11 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi17 – 171ZincCurated
Metal bindingi27 – 271ZincCurated
Metal bindingi83 – 831ZincCurated
Metal bindingi87 – 871ZincCurated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi20 – 33141; low affinityAdd
BLAST
Calcium bindingi59 – 70122; high affinityAdd
BLAST

GO - Molecular functioni

  1. arachidonic acid binding Source: UniProtKB
  2. calcium ion binding Source: UniProtKB
  3. microtubule binding Source: UniProtKB
  4. RAGE receptor binding Source: UniProtKB
  5. Toll-like receptor 4 binding Source: UniProtKB
  6. zinc ion binding Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Antimicrobial

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-A8
Alternative name(s):
Calgranulin-A
Calprotectin L1L subunit
Cystic fibrosis antigen
Short name:
CFAG
Leukocyte L1 complex light chain
Migration inhibitory factor-related protein 8
Short name:
MRP-8
Short name:
p8
S100 calcium-binding protein A8
Urinary stone protein band A
Cleaved into the following chain:
Gene namesi
Name:S100A8
Synonyms:CAGA, CFAG, MRP8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:10498. S100A8.

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.

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: UniProtKB
  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
Mutagenesisi42 – 421C → A: Loss of antifungal activity. 1 Publication

Organism-specific databases

PharmGKBiPA34910.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9393Protein S100-A8PRO_0000143993Add
BLAST
Initiator methioninei1 – 11Removed; alternateBy similarity
Chaini2 – 9392Protein S100-A8, N-terminally processedPRO_0000421773Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421S-nitrosocysteine1 Publication

Keywords - PTMi

S-nitrosylation

Proteomic databases

MaxQBiP05109.
PaxDbiP05109.
PeptideAtlasiP05109.
PRIDEiP05109.

2D gel databases

SWISS-2DPAGEP05109.

PTM databases

PhosphoSiteiP05109.

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.2 Publications

Gene expression databases

BgeeiP05109.
CleanExiHS_S100A8.
GenevestigatoriP05109.

Organism-specific databases

HPAiCAB002791.
HPA024372.

Interactioni

Subunit structurei

Homodimer. Preferentially exists as a heterodimer or heterotetramer with S100A9 known as calprotectin (S100A8/A9). S100A8 interacts with AGER, ATP2A2 and with the heterodimeric complex formed by TLR4 and LY96 (By similarity). 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. S100A8 and calprotectin (S100A8/9) interact with NCF2/P67PHOX, RAC1 and RAC2. Calprotectin (S100A8/9) interacts with CYBA and CYBB.By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
S100A9P067023EBI-355281,EBI-1055001

Protein-protein interaction databases

BioGridi112187. 43 interactions.
DIPiDIP-1165N.
IntActiP05109. 31 interactions.
MINTiMINT-1151603.
STRINGi9606.ENSP00000357721.

Structurei

Secondary structure

1
93
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2017
Beta strandi22 – 254
Helixi31 – 4111
Helixi44 – 474
Helixi51 – 588
Beta strandi63 – 664
Helixi68 – 8619

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MR8X-ray1.90A/B1-93[»]
1XK4X-ray1.80A/B/E/F/I/J1-93[»]
4GGFX-ray1.60A/K/S/U1-93[»]
ProteinModelPortaliP05109.
SMRiP05109. Positions 1-90.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05109.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 4736EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini46 – 8136EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the S-100 family.Curated
Contains 2 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG39611.
GeneTreeiENSGT00730000111352.
HOVERGENiHBG001479.
InParanoidiP05109.
OMAiDTWFKEL.
OrthoDBiEOG76HQ48.
PhylomeDBiP05109.
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.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
IPR028474. S100A8.
[Graphical view]
PANTHERiPTHR11639:SF5. PTHR11639:SF5. 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.

P05109-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG
60 70 80 90
ADVWFKELDI NTDGAVNFQE FLILVIKMGV AAHKKSHEES HKE
Length:93
Mass (Da):10,835
Last modified:January 1, 1988 - v1
Checksum:i78F589140B9CE166
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 9314VAAHK…ESHKE → WQPTKKAMKKATKSS in CAA68390. (PubMed:3561500)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00278 mRNA. Translation: CAA68390.1.
X06234 mRNA. Translation: CAA29580.1.
M21005 Genomic DNA. Translation: AAA36327.1.
AK291328 mRNA. Translation: BAF84017.1.
CR407674 mRNA. Translation: CAG28602.1.
BT007378 mRNA. Translation: AAP36042.1.
AL591704 Genomic DNA. Translation: CAI19497.1.
CH471121 Genomic DNA. Translation: EAW53330.1.
CH471121 Genomic DNA. Translation: EAW53331.1.
BC005928 mRNA. Translation: AAH05928.1.
CCDSiCCDS1038.1.
PIRiA31848. BCHUCF.
RefSeqiNP_002955.2. NM_002964.4.
UniGeneiHs.416073.

Genome annotation databases

EnsembliENST00000368732; ENSP00000357721; ENSG00000143546.
ENST00000368733; ENSP00000357722; ENSG00000143546.
GeneIDi6279.
KEGGihsa:6279.
UCSCiuc001fbs.3. human.

Polymorphism databases

DMDMi115442.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00278 mRNA. Translation: CAA68390.1 .
X06234 mRNA. Translation: CAA29580.1 .
M21005 Genomic DNA. Translation: AAA36327.1 .
AK291328 mRNA. Translation: BAF84017.1 .
CR407674 mRNA. Translation: CAG28602.1 .
BT007378 mRNA. Translation: AAP36042.1 .
AL591704 Genomic DNA. Translation: CAI19497.1 .
CH471121 Genomic DNA. Translation: EAW53330.1 .
CH471121 Genomic DNA. Translation: EAW53331.1 .
BC005928 mRNA. Translation: AAH05928.1 .
CCDSi CCDS1038.1.
PIRi A31848. BCHUCF.
RefSeqi NP_002955.2. NM_002964.4.
UniGenei Hs.416073.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MR8 X-ray 1.90 A/B 1-93 [» ]
1XK4 X-ray 1.80 A/B/E/F/I/J 1-93 [» ]
4GGF X-ray 1.60 A/K/S/U 1-93 [» ]
ProteinModelPortali P05109.
SMRi P05109. Positions 1-90.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112187. 43 interactions.
DIPi DIP-1165N.
IntActi P05109. 31 interactions.
MINTi MINT-1151603.
STRINGi 9606.ENSP00000357721.

PTM databases

PhosphoSitei P05109.

Polymorphism databases

DMDMi 115442.

2D gel databases

SWISS-2DPAGE P05109.

Proteomic databases

MaxQBi P05109.
PaxDbi P05109.
PeptideAtlasi P05109.
PRIDEi P05109.

Protocols and materials databases

DNASUi 6279.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368732 ; ENSP00000357721 ; ENSG00000143546 .
ENST00000368733 ; ENSP00000357722 ; ENSG00000143546 .
GeneIDi 6279.
KEGGi hsa:6279.
UCSCi uc001fbs.3. human.

Organism-specific databases

CTDi 6279.
GeneCardsi GC01M153362.
HGNCi HGNC:10498. S100A8.
HPAi CAB002791.
HPA024372.
MIMi 123885. gene.
neXtProti NX_P05109.
PharmGKBi PA34910.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG39611.
GeneTreei ENSGT00730000111352.
HOVERGENi HBG001479.
InParanoidi P05109.
OMAi DTWFKEL.
OrthoDBi EOG76HQ48.
PhylomeDBi P05109.
TreeFami TF332727.

Miscellaneous databases

ChiTaRSi S100A8. human.
EvolutionaryTracei P05109.
GeneWikii S100_calcium_binding_protein_A8.
GenomeRNAii 6279.
NextBioi 24373.
PROi P05109.
SOURCEi Search...

Gene expression databases

Bgeei P05109.
CleanExi HS_S100A8.
Genevestigatori P05109.

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.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
IPR028474. S100A8.
[Graphical view ]
PANTHERi PTHR11639:SF5. PTHR11639:SF5. 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. "A clue to the basic defect in cystic fibrosis from cloning the CF antigen gene."
    Dorin J.R., Novak M., Hill R.E., Brock D.J.H., Secher D.S., van Heyningen V.
    Nature 326:614-617(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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].
  3. "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].
  4. "The calcium-binding protein MRP-8 is produced by human pulmonary tumor cells."
    Schaefer T., Sachse G.E., Gassen H.G.
    Biol. Chem. Hoppe-Seyler 372:1-4(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-30.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Tongue.
  6. "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].
  7. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  8. "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].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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.
  11. "Host-parasite interaction in human onchocerciasis: identification and sequence analysis of a novel human calgranulin."
    Marti T., Erttmann K.D., Gallin M.Y.
    Biochem. Biophys. Res. Commun. 221:454-458(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-19; 24-35 AND 63-89.
  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 1-27.
  13. "Translocation of a small cytosolic calcium-binding protein (MRP-8) to plasma membrane correlates with human neutrophil activation."
    Lemarchand P., Vaglio M., Mauel J., Markert M.
    J. Biol. Chem. 267:19379-19382(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-25.
    Tissue: Neutrophil.
  14. "Calprotectin-like protein is related to soluble organic matrix in calcium oxalate urinary stone."
    Umekawa T., Kurita T.
    Biochem. Mol. Biol. Int. 34:309-313(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-20.
  15. "Isolation of an ascitic oncodevelopmental protein exhibiting high sequence homology with calcium-binding protein MRP8."
    Nakai M., Ishikawa M., Hamada Y., Sugano S.
    Biol. Chem. Hoppe-Seyler 375:789-792(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-20.
    Tissue: Ascites.
  16. "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 38-47 AND 50-56.
    Tissue: Keratinocyte.
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  21. "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, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  22. "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.
  23. "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.
  24. "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.
  25. Cited for: S-NITROSYLATION AT CYS-42.
  26. Cited for: REVIEW.
  27. "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.
  28. "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, MUTAGENESIS OF CYS-42.
  29. "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.
  30. "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.
  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. "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.
  34. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. Cited for: REVIEW.
  36. "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, SUBCELLULAR LOCATION.
  37. "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.
  38. "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.
  39. "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.
  40. "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.
  41. "The structure of human MRP8, a member of the S100 calcium-binding protein family, by MAD phasing at 1.9 A resolution."
    Ishikawa K., Nakagawa A., Tanaka I., Suzuki M., Nishihira J.
    Acta Crystallogr. D 56:559-566(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  42. "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) IN COMPLEX WITH S100A9, SUBUNIT, ZINC-BINDING.

Entry informationi

Entry nameiS10A8_HUMAN
AccessioniPrimary (citable) accession number: P05109
Secondary accession number(s): A8K5L3
, D3DV37, Q5SY70, Q9UC84, Q9UC92, Q9UCJ0, Q9UCM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 1, 1988
Last modified: October 29, 2014
This is version 161 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

Miscellaneous

Binds two calcium ions per molecule with an affinity similar to that of the S100 proteins.

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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3