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Protein

Protein S100-A7

Gene

S100A7

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

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi18 – 181Zinc
Metal bindingi25 – 251Zinc
Metal bindingi87 – 871Zinc
Metal bindingi91 – 911Zinc

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi63 – 74122; high affinityAdd
BLAST

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • RAGE receptor binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • angiogenesis Source: UniProtKB
  • defense response to Gram-negative bacterium Source: UniProtKB
  • epidermis development Source: ProtInc
  • innate immune response Source: UniProtKB
  • keratinocyte differentiation Source: UniProtKB
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of granulocyte chemotaxis Source: UniProtKB
  • positive regulation of monocyte chemotaxis Source: UniProtKB
  • positive regulation of T cell chemotaxis Source: UniProtKB
  • response to lipopolysaccharide Source: UniProtKB
  • response to reactive oxygen species Source: UniProtKB
  • sequestering of metal ion Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Protein S100-A7
Alternative name(s):
Psoriasin
S100 calcium-binding protein A7
Gene namesi
Name:S100A7
Synonyms:PSOR1, S100A7C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:10497. S100A7.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34909.

Polymorphism and mutation databases

BioMutaiS100A7.
DMDMi172046820.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 101100Protein S100-A7PRO_0000143990Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Disulfide bondi47 ↔ 96

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

EPDiP31151.
MaxQBiP31151.
PaxDbiP31151.
PeptideAtlasiP31151.
PRIDEiP31151.
TopDownProteomicsiP31151.

2D gel databases

UCD-2DPAGEP31151.

PTM databases

iPTMnetiP31151.
PhosphoSiteiP31151.

Expressioni

Tissue specificityi

Fetal ear, skin, and tongue and human cell lines. Highly up-regulated in psoriatic epidermis. Also highly expressed in the urine of bladder squamous cell carcinoma (SCC) bearing patients.1 Publication

Gene expression databases

BgeeiP31151.
CleanExiHS_S100A7.
GenevisibleiP31151. HS.

Organism-specific databases

HPAiCAB001453.
CAB033766.
HPA006997.

Interactioni

Subunit structurei

Interacts with RANBP9.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RANBP9Q96S593EBI-357520,EBI-636085

GO - Molecular functioni

  • RAGE receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112186. 45 interactions.
IntActiP31151. 14 interactions.
MINTiMINT-1156620.
STRINGi9606.ENSP00000357711.

Structurei

Secondary structure

1
101
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1915Combined sources
Helixi29 – 3911Combined sources
Helixi41 – 499Combined sources
Helixi54 – 563Combined sources
Helixi58 – 625Combined sources
Beta strandi67 – 704Combined sources
Helixi72 – 8918Combined sources
Turni90 – 923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PSRX-ray1.05A/B2-101[»]
2PSRX-ray2.05A2-101[»]
2WNDX-ray1.60A2-97[»]
2WORX-ray1.70A2-101[»]
2WOSX-ray1.70A2-101[»]
3PSRX-ray2.50A/B2-101[»]
4AQJX-ray1.60A1-101[»]
ProteinModelPortaliP31151.
SMRiP31151. Positions 2-101.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31151.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 4836EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini50 – 8536EF-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

eggNOGiENOG410JEQ8. Eukaryota.
ENOG41114XT. LUCA.
GeneTreeiENSGT00390000017320.
HOGENOMiHOG000154231.
HOVERGENiHBG095357.
InParanoidiP31151.
OMAiSHGAPAC.
OrthoDBiEOG7RZ5SH.
PhylomeDBiP31151.
TreeFamiTF341148.

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.
IPR028477. S100A7.
[Graphical view]
PANTHERiPTHR11639:SF64. PTHR11639:SF64. 1 hit.
PfamiPF01023. S_100. 1 hit.
[Graphical view]
SMARTiSM01394. S_100. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
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.

P31151-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNTQAERSI IGMIDMFHKY TRRDDKIEKP SLLTMMKENF PNFLSACDKK
60 70 80 90 100
GTNYLADVFE KKDKNEDKKI DFSEFLSLLG DIATDYHKQS HGAAPCSGGS

Q
Length:101
Mass (Da):11,471
Last modified:February 26, 2008 - v4
Checksum:i02C4CE39BF140971
GO

Mass spectrometryi

Molecular mass is 11365±0.7 Da from positions 2 - 101. Determined by ESI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti28 – 281E → D.4 Publications
Corresponds to variant rs3014837 [ dbSNP | Ensembl ].
VAR_039118

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86757 mRNA. Translation: AAA60210.1.
CR542164 mRNA. Translation: CAG46961.1.
AL591704 Genomic DNA. Translation: CAI19502.1.
BC034687 mRNA. Translation: AAH34687.1.
AJ012825 Genomic DNA. Translation: CAC20409.1.
BR000043 Genomic DNA. Translation: FAA00017.1.
CCDSiCCDS1039.1.
PIRiA54327.
RefSeqiNP_002954.2. NM_002963.3.
UniGeneiHs.112408.

Genome annotation databases

EnsembliENST00000368722; ENSP00000357711; ENSG00000143556.
ENST00000368723; ENSP00000357712; ENSG00000143556.
GeneIDi6278.
KEGGihsa:6278.
UCSCiuc001fbv.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86757 mRNA. Translation: AAA60210.1.
CR542164 mRNA. Translation: CAG46961.1.
AL591704 Genomic DNA. Translation: CAI19502.1.
BC034687 mRNA. Translation: AAH34687.1.
AJ012825 Genomic DNA. Translation: CAC20409.1.
BR000043 Genomic DNA. Translation: FAA00017.1.
CCDSiCCDS1039.1.
PIRiA54327.
RefSeqiNP_002954.2. NM_002963.3.
UniGeneiHs.112408.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PSRX-ray1.05A/B2-101[»]
2PSRX-ray2.05A2-101[»]
2WNDX-ray1.60A2-97[»]
2WORX-ray1.70A2-101[»]
2WOSX-ray1.70A2-101[»]
3PSRX-ray2.50A/B2-101[»]
4AQJX-ray1.60A1-101[»]
ProteinModelPortaliP31151.
SMRiP31151. Positions 2-101.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112186. 45 interactions.
IntActiP31151. 14 interactions.
MINTiMINT-1156620.
STRINGi9606.ENSP00000357711.

PTM databases

iPTMnetiP31151.
PhosphoSiteiP31151.

Polymorphism and mutation databases

BioMutaiS100A7.
DMDMi172046820.

2D gel databases

UCD-2DPAGEP31151.

Proteomic databases

EPDiP31151.
MaxQBiP31151.
PaxDbiP31151.
PeptideAtlasiP31151.
PRIDEiP31151.
TopDownProteomicsiP31151.

Protocols and materials databases

DNASUi6278.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368722; ENSP00000357711; ENSG00000143556.
ENST00000368723; ENSP00000357712; ENSG00000143556.
GeneIDi6278.
KEGGihsa:6278.
UCSCiuc001fbv.2. human.

Organism-specific databases

CTDi6278.
GeneCardsiS100A7.
H-InvDBHIX0200006.
HGNCiHGNC:10497. S100A7.
HPAiCAB001453.
CAB033766.
HPA006997.
MIMi600353. gene.
neXtProtiNX_P31151.
PharmGKBiPA34909.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410JEQ8. Eukaryota.
ENOG41114XT. LUCA.
GeneTreeiENSGT00390000017320.
HOGENOMiHOG000154231.
HOVERGENiHBG095357.
InParanoidiP31151.
OMAiSHGAPAC.
OrthoDBiEOG7RZ5SH.
PhylomeDBiP31151.
TreeFamiTF341148.

Miscellaneous databases

EvolutionaryTraceiP31151.
GeneWikiiS100A7.
GenomeRNAii6278.
PROiP31151.
SOURCEiSearch...

Gene expression databases

BgeeiP31151.
CleanExiHS_S100A7.
GenevisibleiP31151. HS.

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.
IPR028477. S100A7.
[Graphical view]
PANTHERiPTHR11639:SF64. PTHR11639:SF64. 1 hit.
PfamiPF01023. S_100. 1 hit.
[Graphical view]
SMARTiSM01394. S_100. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, occurrence, and expression of a novel partially secreted protein 'psoriasin' that is highly up-regulated in psoriatic skin."
    Madsen P., Rasmussen H.H., Leffers H., Honore B., Dejgaard K., Olsen E., Kiil J., Walbum E., Andersen A.H., Basse B., Lauridsen J.B., Ratz G.P., Celis A., Vandekerckhove J., Celis J.E.
    J. Invest. Dermatol. 97:701-712(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-28.
    Tissue: Keratinocyte.
  2. "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], VARIANT ASP-28.
  3. "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].
  4. "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], VARIANT ASP-28.
    Tissue: Skin.
  5. "Genomic organization of human psoriasin (S100A7) gene."
    Glaeser R., Harder J., Christophers E., Schroeder J.M.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89, VARIANT ASP-28.
  6. "Amino acid sequence analysis of human S100A7 (psoriasin) by tandem mass spectrometry."
    Burgisser D.M., Siegenthaler G., Kuster T., Hellman U., Hunziker P., Birchler N., Heizmann C.W.
    Biochem. Biophys. Res. Commun. 217:257-263(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-101, MASS SPECTROMETRY, ACETYLATION AT SER-2.
    Tissue: Psoriatic skin.
  7. "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 9-19; 38-48; 50-61; 69-87 AND 89-101.
    Tissue: Keratinocyte.
  8. "Bladder squamous cell carcinomas express psoriasin and externalize it to the urine."
    Celis J.E., Rasmussen H.H., Vorum H., Madsen P., Honore B., Wolf H., Orntoft T.F.
    J. Urol. 155:2105-2112(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  9. "RanBPM interacts with psoriasin in vitro and their expression correlates with specific clinical features in vivo in breast cancer."
    Emberley E.D., Gietz R.D., Campbell J.D., Hayglass K.T., Murphy L.C., Watson P.H.
    BMC Cancer 2:28-28(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RANBP9.
  10. "Genomic and phylogenetic analysis of the S100A7 (psoriasin) gene duplications within the region of the S100 gene cluster on human chromosome 1q21."
    Kulski J.K., Lim C.P., Dunn D.S., Bellgard M.
    J. Mol. Evol. 56:397-406(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOMIC ORGANIZATION.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "EF-hands at atomic resolution: the structure of human psoriasin (S100A7) solved by MAD phasing."
    Brodersen D.E., Etzerodt M., Madsen P., Celis J.E., Thoegersen H.C., Nyborg J., Kjeldgaard M.
    Structure 6:477-489(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS).
  13. "Zinc-binding site of an S100 protein revealed. Two crystal structures of Ca2+-bound human psoriasin (S100A7) in the Zn2+-loaded and Zn2+-free states."
    Brodersen D.E., Nyborg J., Kjeldgaard M.
    Biochemistry 38:1695-1704(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).

Entry informationi

Entry nameiS10A7_HUMAN
AccessioniPrimary (citable) accession number: P31151
Secondary accession number(s): Q5SY67, Q6FGE3, Q9H1E2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: February 26, 2008
Last modified: June 8, 2016
This is version 166 of the entry and version 4 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

Similar proteinsi

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