P31151 (S10A7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein S100-A7

Alternative name(s):
Psoriasin
S100 calcium-binding protein A7

Gene names

Name:	S100A7
Synonyms:	PSOR1, S100A7C

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	101 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Subunit structure	Interacts with RANBP9. Ref.9
Subcellular location	Cytoplasm. Secreted. Note: Secreted by a non-classical secretory pathway. Ref.8
Tissue specificity	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. Ref.8
Sequence similarities	Belongs to the S-101 family. Contains 2 EF-hand domains.
Mass spectrometry	Molecular mass is 11365±0.7 Da from positions 2 - 101. Determined by ESI. Ref.6

Ontologies

Keywords
Cellular component	Cytoplasm Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	Calcium Metal-binding Zinc
PTM	Acetylation Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	angiogenesis Non-traceable author statement. Source: UniProtKB defense response to Gram-negative bacterium Inferred from mutant phenotype. Source: UniProtKB innate immune response Non-traceable author statement. Source: UniProtKB keratinocyte differentiation Non-traceable author statement. Source: UniProtKB positive regulation of ERK1 and ERK2 cascade Inferred from direct assay. Source: UniProtKB positive regulation of T cell chemotaxis Inferred from direct assay. Source: UniProtKB positive regulation of granulocyte chemotaxis Inferred from direct assay. Source: UniProtKB positive regulation of monocyte chemotaxis Inferred from direct assay. Source: UniProtKB response to lipopolysaccharide Inferred from expression pattern. Source: UniProtKB response to reactive oxygen species Inferred from direct assay. Source: UniProtKB sequestering of metal ion Inferred from direct assay. Source: UniProtKB
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB endoplasmic reticulum Inferred from direct assay. Source: UniProtKB extracellular region Inferred from direct assay. Source: UniProtKB focal adhesion Non-traceable author statement. Source: UniProtKB nucleus Inferred from direct assay. Source: UniProtKB
Molecular function	RAGE receptor binding Inferred from physical interaction. Source: UniProtKB calcium ion binding Inferred from direct assay. Source: UniProtKB zinc ion binding Non-traceable author statement Ref.12. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RANBP9	Q96S59	3	EBI-357520,EBI-636085

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 101

100

Protein S100-A7

PRO_0000143990

Regions

Domain

13 – 48

36

EF-hand 1

Domain

50 – 85

36

EF-hand 2

Calcium binding

63 – 74

12

2; high affinity

Sites

Metal binding

18

1

Zinc

Metal binding

25

1

Zinc

Metal binding

87

1

Zinc

Metal binding

91

1

Zinc

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.6

Disulfide bond

47 ↔ 96

Natural variations

Natural variant

28

1

E → D. Ref.1 Ref.2 Ref.4 Ref.5
Corresponds to variant rs3014837 [ dbSNP | Ensembl ].

VAR_039118

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

101

Helix Strand Turn

Details...

Helix

5 – 19

15

Helix

29 – 39

11

Helix

41 – 49

9

Helix

54 – 56

3

Helix

58 – 62

5

Helix

72 – 89

18

Turn

90 – 92

3

Sequences

	Sequence		Length	Mass (Da)
	P31151 [UniParc]. Last modified February 26, 2008. Version 4. Checksum: 02C4CE39BF140971	FASTA	101	11,471
	10 20 30 40 50 60 MSNTQAERSI IGMIDMFHKY TRRDDKIEKP SLLTMMKENF PNFLSACDKK GTNYLADVFE 70 80 90 100 KKDKNEDKKI DFSEFLSLLG DIATDYHKQS HGAAPCSGGS Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1940442] [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: 16710414] [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: 15489334] [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: 8526920] [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: 1286667] [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: 8618345] [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: 12421467] [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: 12664160] [Abstract] Cited for: GENOMIC ORGANIZATION.
[11]	"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: 9562557] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS).
[12]	"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: 10026247] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00219806.

PIR

A54327.

RefSeq

NP_002954.2. NM_002963.3.

UniGene

Hs.112408.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PSR	X-ray	1.05	A/B	2-101	[»]
2PSR	X-ray	2.05	A	2-101	[»]
2WND	X-ray	1.60	A	2-97	[»]
2WOR	X-ray	1.70	A	2-101	[»]
2WOS	X-ray	1.70	A	2-101	[»]
3PSR	X-ray	2.50	A/B	2-101	[»]

ProteinModelPortal

P31151.

SMR

P31151. Positions 2-101.

ModBase

Search...

Protein-protein interaction databases

IntAct

P31151. 6 interactions.

MINT

MINT-1156620.

STRING

P31151.

PTM databases

PhosphoSite

P31151.

Polymorphism databases

DMDM

172046820.

2D gel databases

Aarhus/Ghent-2DPAGE

3002. IEF.

UCD-2DPAGE

P31151.

Proteomic databases

PeptideAtlas

P31151.

PRIDE

P31151.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368722; ENSP00000357711; ENSG00000143556.
ENST00000368723; ENSP00000357712; ENSG00000143556.

GeneID

6278.

KEGG

hsa:6278.

UCSC

uc001fbv.1. human.

Organism-specific databases

CTD

6278.

GeneCards

GC01M153430.

HGNC

HGNC:10497. S100A7.

HPA

CAB001453.
HPA006997.

MIM

600353. gene.

neXtProt

NX_P31151.

PharmGKB

PA34909.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG21615.

GeneTree

ENSGT00390000017320.

HOGENOM

HBG506094.

HOVERGEN

HBG095357.

InParanoid

P31151.

OMA

ACDKKGT.

OrthoDB

EOG49GKJ6.

PhylomeDB

P31151.

Gene expression databases

ArrayExpress

P31151.

Bgee

P31151.

CleanEx

HS_S100A7.

Genevestigator

P31151.

GermOnline

ENSG00000143556. Homo sapiens.

Family and domain databases

InterPro

IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]

Gene3D

G3DSA:1.10.238.10. EF-Hand_type. 1 hit.

Pfam

PF01023. S_100. 1 hit.
[Graphical view]

PROSITE

PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

24369.

SOURCE

Search...

Entry information

Entry name

S10A7_HUMAN

Accession

Primary (citable) accession number: P31151
Secondary accession number(s): Q5SY67, Q6FGE3, Q9H1E2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	February 26, 2008
Last modified:	January 25, 2012
This is version 123 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.