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UniProtKB - P06702 (S10A9_HUMAN)

Protein

Protein S100-A9

Gene

S100A9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 proinflammatory, 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. Has transnitrosylase activity; in oxidatively-modified low-densitity lipoprotein (LDL(ox))-induced S-nitrosylation of GAPDH on 'Cys-247' proposed to transfer the NO moiety from NOS2/iNOS to GAPDH via its own S-nitrosylated Cys-3. The iNOS-S100A8/A9 transnitrosylase complex is proposed to also direct selective inflammatory stimulus-dependent S-nitrosylation of multiple targets such as ANXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif.18 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi20ZincCurated1
Metal bindingi30ZincCurated1
Metal bindingi91ZincCurated1
Metal bindingi95ZincCurated1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi23 – 361; low affinityAdd BLAST14
Calcium bindingi67 – 782; high affinityCuratedAdd BLAST12

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAntimicrobial, Antioxidant
Biological processApoptosis, Autophagy, Chemotaxis, Immunity, Inflammatory response, Innate immunity
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-5686938 Regulation of TLR by endogenous ligand
R-HSA-6798695 Neutrophil degranulation
R-HSA-6799990 Metal sequestration by antimicrobial proteins

SIGNOR Signaling Network Open Resource

More...SIGNORi		P06702

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:S100A9
Synonyms:CAGB, CFAG, MRP14
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000163220.10

Human Gene Nomenclature Database

More...HGNCi		HGNC:10499 S100A9

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		123886 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P06702

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi3C → A: Disrupts interaction with NOS2 and inhibits LDL(ox)-induced GAPDH S-nitrosylation; no effect on interaction with S100A8. 1 Publication1
Mutagenesisi36E → Q: Loss of resistance to bacterial invasion; when associated with Q-78. 1 Publication1
Mutagenesisi63M → A: Loss of antifungal activity. 1 Publication1
Mutagenesisi78E → Q: Loss of resistance to bacterial invasion; when associated with Q-36. 1 Publication1
Mutagenesisi81M → A: No effect on antifungal activity. 1 Publication1
Mutagenesisi83M → A: Loss of antifungal activity. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		6280

Open Targets

More...OpenTargetsi		ENSG00000163220

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA34911

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		S100A9

Domain mapping of disease mutations (DMDM)

More...DMDMi		115444

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001439971 – 114Protein S100-A9Add BLAST114

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2Blocked amino end (Thr)1
Modified residuei3S-nitrosocysteine; transient1 Publication1
Modified residuei105Pros-methylhistidineBy similarity1
Modified residuei113Phosphothreonine; by MAPK14Combined sources3 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated. Phosphorylation inhibits activation of tubulin polymerization.3 Publications
S-nitrosylation of Cys-3 is implicated in LDL(ox)-induced S-nitrosylation of GAPDH at 'Cys-247' through a transnitrosylase mechanism involving a iNOS-S100A8/9 complex (PubMed:25417112).1 Publication

Keywords - PTMi

Methylation, Phosphoprotein, S-nitrosylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P06702

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P06702

MaxQB - The MaxQuant DataBase

More...MaxQBi		P06702

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P06702

PeptideAtlas

More...PeptideAtlasi		P06702

PRoteomics IDEntifications database

More...PRIDEi		P06702

ProteomicsDB human proteome resource

More...ProteomicsDBi		51910

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P06702

2D gel databases

USC-OGP 2-DE database

More...OGPi		P06702

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P06702

University College Dublin 2-DE Proteome Database

More...UCD-2DPAGEi		P06702

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P06702

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P06702

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P06702

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000163220 Expressed in 181 organ(s), highest expression level in ectocervix

CleanEx database of gene expression profiles

More...CleanExi		HS_S100A9

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P06702 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB009441
HPA004193

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 amyloid-beta protein 40. 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. Calprotectin (S100A8/9) interacts with NOS2 to form the iNOS-S100A8/A9 transnitrosylase complex; induced by LDL(ox) (PubMed:25417112).By similarity1 Publication15 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		112188, 119 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-37 Calprotectin heterotetramer
CPX-39 Calprotectin heterodimer
CPX-48 S100A9 complex
CPX-52 iNOS-S100A8/A9 complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P06702

Database of interacting proteins

More...DIPi		DIP-1166N

Protein interaction database and analysis system

More...IntActi		P06702, 29 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000357727

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1114
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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[»]
4XJKX-ray1.76B/D/F/H/J1-114[»]
5I8NNMR-A/B1-114[»]
5W1FX-ray2.60B/D/F/H1-114[»]
6DS2X-ray2.10B/D/F/H1-114[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P06702

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P06702

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P06702

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini12 – 47EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini54 – 89EF-hand 2PROSITE-ProRule annotationAdd BLAST36

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the S-100 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG410J1XC Eukaryota
ENOG4111C30 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000161606

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000246968

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG001479

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P06702

KEGG Orthology (KO)

More...KOi		K21128

Identification of Orthologs from Complete Genome Data

More...OMAi		HEKMHEN

Database of Orthologous Groups

More...OrthoDBi		1521098at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P06702

TreeFam database of animal gene trees

More...TreeFami		TF332727

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
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

The PANTHER Classification System

More...PANTHERi		PTHR11639:SF79 PTHR11639:SF79, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01023 S_100, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00054 EFh, 1 hit
SM01394 S_100, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47473 SSF47473, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00018 EF_HAND_1, 1 hit
PS50222 EF_HAND_2, 1 hit
PS00303 S100_CABP, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P06702-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTCKMSQLER NIETIINTFH QYSVKLGHPD TLNQGEFKEL VRKDLQNFLK 
        60         70         80         90        100
KENKNEKVIE HIMEDLDTNA DKQLSFEEFI MLMARLTWAS HEKMHEGDEG 
       110 
PGHHHKPGLG EGTP
Length:114
Mass (Da):13,242
Last modified:January 1, 1988 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC3BE19729E14C078
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti6S → H AA sequence (PubMed:8423249).Curated1
Sequence conflicti25K → F AA sequence (PubMed:8423249).Curated1
Sequence conflicti28H → L AA sequence (PubMed:8423249).Curated1

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_01300820H → R1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
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 No translation available.
CH471121 Genomic DNA Translation: EAW53333.1
CH471121 Genomic DNA Translation: EAW53334.1
BC047681 mRNA Translation: AAH47681.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS1036.1

Protein sequence database of the Protein Information Resource

More...PIRi		B31848

NCBI Reference Sequences

More...RefSeqi		NP_002956.1, NM_002965.3

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.112405

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000368738; ENSP00000357727; ENSG00000163220

Database of genes from NCBI RefSeq genomes

More...GeneIDi		6280

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:6280

UCSC genome browser

More...UCSCi		uc001fbq.3 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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 No translation available.
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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4XJKX-ray1.76B/D/F/H/J1-114[»]
5I8NNMR-A/B1-114[»]
5W1FX-ray2.60B/D/F/H1-114[»]
6DS2X-ray2.10B/D/F/H1-114[»]
ProteinModelPortaliP06702
SMRiP06702
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112188, 119 interactors
ComplexPortaliCPX-37 Calprotectin heterotetramer
CPX-39 Calprotectin heterodimer
CPX-48 S100A9 complex
CPX-52 iNOS-S100A8/A9 complex
CORUMiP06702
DIPiDIP-1166N
IntActiP06702, 29 interactors
STRINGi9606.ENSP00000357727

PTM databases

iPTMnetiP06702
PhosphoSitePlusiP06702
SwissPalmiP06702

Polymorphism and mutation databases

BioMutaiS100A9
DMDMi115444

2D gel databases

OGPiP06702
SWISS-2DPAGEiP06702
UCD-2DPAGEiP06702

Proteomic databases

EPDiP06702
jPOSTiP06702
MaxQBiP06702
PaxDbiP06702
PeptideAtlasiP06702
PRIDEiP06702
ProteomicsDBi51910
TopDownProteomicsiP06702

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		6280
DisGeNETi6280
EuPathDBiHostDB:ENSG00000163220.10

GeneCards: human genes, protein and diseases

More...GeneCardsi		S100A9
HGNCiHGNC:10499 S100A9
HPAiCAB009441
HPA004193
MIMi123886 gene
neXtProtiNX_P06702
OpenTargetsiENSG00000163220
PharmGKBiPA34911

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG410J1XC Eukaryota
ENOG4111C30 LUCA
GeneTreeiENSGT00940000161606
HOGENOMiHOG000246968
HOVERGENiHBG001479
InParanoidiP06702
KOiK21128
OMAiHEKMHEN
OrthoDBi1521098at2759
PhylomeDBiP06702
TreeFamiTF332727

Enzyme and pathway databases

ReactomeiR-HSA-5686938 Regulation of TLR by endogenous ligand
R-HSA-6798695 Neutrophil degranulation
R-HSA-6799990 Metal sequestration by antimicrobial proteins
SIGNORiP06702

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		S100A9 human
EvolutionaryTraceiP06702

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		S100A9

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		6280

Protein Ontology

More...PROi		PR:P06702

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000163220 Expressed in 181 organ(s), highest expression level in ectocervix
CleanExiHS_S100A9
GenevisibleiP06702 HS

Family and domain databases

InterProiView protein in InterPro
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
PANTHERiPTHR11639:SF79 PTHR11639:SF79, 1 hit
PfamiView protein in Pfam
PF01023 S_100, 1 hit
SMARTiView protein in SMART
SM00054 EFh, 1 hit
SM01394 S_100, 1 hit
SUPFAMiSSF47473 SSF47473, 1 hit
PROSITEiView protein in PROSITE
PS00018 EF_HAND_1, 1 hit
PS50222 EF_HAND_2, 1 hit
PS00303 S100_CABP, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiS10A9_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P06702
Secondary accession number(s): D3DV36
, Q6FGA1, Q9NYM0, Q9UCJ1
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: January 16, 2019
This is version 212 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
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