Protein S100-P - Homo sapiens (Human)

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P25815 (S100P_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 123. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Protein S100-P

Alternative name(s):
Migration-inducing gene 9 protein
Short name=MIG9
Protein S100-E
S100 calcium-binding protein P

Gene names

Name:	S100P
Synonyms:	S100E

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	95 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May stimulate cell proliferation in an autocrine manner via activation of the receptor for activated glycation end products (RAGE). Ref.10
Subunit structure	Homodimer and heterodimer with S100A1. Interacts with S100PBP and S100Z. Interacts with CACYBP in a calcium-dependent manner. Dimeric form binds to and may activate EZR/Ezrin by unmasking its F-actin binding sites. Ref.7 Ref.9 Ref.11
Subcellular location	Nucleus. Cytoplasm. Note: Colocalizes with S100PBP in the nucleus. Ref.11
Tissue specificity	Detected in all of the tissues except brain, testis and small intestine, expression level is higher in placenta, heart, lung, skeletal muscle, spleen and leukocyte. Up-regulated in various pancreatic ductal adenocarcinomas and pancreatic intraepithelial neoplasias. Ref.8 Ref.11
Miscellaneous	This protein binds two calcium ions.
Sequence similarities	Belongs to the S-100 family. Contains 2 EF-hand domains.
Sequence caution	The sequence AAS00487.1 differs from that shown. Reason: Sequencing error in Met-1 codon.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Domain	Repeat
Ligand	Calcium Metal-binding
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	endothelial cell migration Inferred from mutant phenotype PubMed 15313892. Source: UniProtKB response to organic substance Inferred from expression pattern PubMed 17486081. Source: UniProtKB
Cellular_component	cytoplasm Traceable author statement Ref.11. Source: HGNC nucleus Inferred from direct assay Ref.11. Source: HGNC
Molecular_function	calcium ion binding Traceable author statement Ref.1. Source: ProtInc magnesium ion binding Traceable author statement Ref.11. Source: HGNC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AGER	Q15109	2	EBI-743700,EBI-1646426
Cacybp	Q9CXW3	2	EBI-743700,EBI-767146	From a different organism.
S100A1	P23297	7	EBI-743700,EBI-743686

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 95

Protein S100-P

PRO_0000144032

Regions

Domain

12 – 47

EF-hand 1

Domain

49 – 84

EF-hand 2

Calcium binding

19 – 32

1; low affinity

Calcium binding

62 – 73

2; high affinity

Experimental info

Sequence conflict

I → M in AAS00487. Ref.4

Sequence conflict

E → T AA sequence Ref.6

Sequence conflict

F → E AA sequence Ref.6

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P25815 [UniParc].

Last modified December 1, 1992. Version 2.
Checksum: 786E6E3F3EACC6C1
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FASTA

10,400

        10         20         30         40         50         60 
MTELETAMGM IIDVFSRYSG SEGSTQTLTK GELKVLMEKE LPGFLQSGKD KDAVDKLLKD 

        70         80         90 
LDANGDAQVD FSEFIVFVAA ITSACHKYFE KAGLK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"S100P, a novel Ca(2+)-binding protein from human placenta. cDNA cloning, recombinant protein expression and Ca2+ binding properties." Becker T., Gerke V., Kube E., Weber K. Eur. J. Biochem. 207:541-547(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	"Cloning, expression and characterization of a novel human calcium-binding S100 gene." Jin G., Wang S., Chen J. Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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 (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Identification of a human migration-inducing gene 9 (MIG9)." Kim J.W. Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"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: Placenta.
[6]	"Purification and characterization of a new member of the S-100 protein family from human placenta." Emoto Y., Kobayashi R., Akatsuka H., Hidaka H. Biochem. Biophys. Res. Commun. 182:1246-1253(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-91. Tissue: Placenta.
[7]	"Ca2+-dependent binding and activation of dormant ezrin by dimeric S100P." Koltzscher M., Neumann C., Konig S., Gerke V. Mol. Biol. Cell 14:2372-2384(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EZR.
[8]	"Characterization of the tissue-specific expression of the s100P gene which encodes an EF-hand Ca2+-binding protein." Jin G., Wang S., Hu X., Jing Z., Chen J., Ying K., Xie Y., Mao Y. Mol. Biol. Rep. 30:243-248(2003) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[9]	"Heterodimeric interaction and interfaces of S100A1 and S100P." Wang G., Zhang S., Fernig D.G., Spiller D., Martin-Fernandez M., Zhang H., Ding Y., Rao Z., Rudland P.S., Barraclough R. Biochem. J. 382:375-383(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, INTERACTION WITH S100A1.
[10]	"S100P stimulates cell proliferation and survival via receptor for activated glycation end products (RAGE)." Arumugam T., Simeone D.M., Schmidt A.M., Logsdon C.D. J. Biol. Chem. 279:5059-5065(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Expression of S100P and its novel binding partner S100PBPR in early pancreatic cancer." Dowen S.E., Crnogorac-Jurcevic T., Gangeswaran R., Hansen M., Eloranta J.J., Bhakta V., Brentnall T.A., Luettges J., Kloeppel G., Lemoine N.R. Am. J. Pathol. 166:81-92(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH S100PBP, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"The crystal structure at 2A resolution of the Ca2+ -binding protein S100P." Zhang H., Wang G., Ding Y., Wang Z., Barraclough R., Rudland P.S., Fernig D.G., Rao Z. J. Mol. Biol. 325:785-794(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[14]	"NMR structure of the Apo-S100P protein." Lee Y.C., Volk D.E., Thiviyanathan V., Kleerekoper Q., Gribenko A.V., Zhang S., Gorenstein D.G., Makhatadze G.I., Luxon B.A. J. Biomol. NMR 29:399-402(2004) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X65614 mRNA. Translation: CAA46566.1.
AF539739 mRNA. Translation: AAO41114.1.
BT007289 mRNA. Translation: AAP35953.1.
AY423724 mRNA. Translation: AAS00487.1. Sequence problems.
BC006819 mRNA. Translation: AAH06819.1.

IPI

IPI00017526.

PIR

S24146.

RefSeq

NP_005971.1. NM_005980.2.

UniGene

Hs.2962.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1J55	X-ray	2.00	A	1-95	[»]
1OZO	NMR	-	A/B	1-95	[»]

ProteinModelPortal

P25815.

ModBase

Search...

Protein-protein interaction databases

IntAct

P25815. 5 interactions.

MINT

MINT-239013.

STRING

9606.ENSP00000296370.

PTM databases

PhosphoSite

P25815.

Polymorphism databases

DMDM

134142.

Proteomic databases

PaxDb

P25815.

PeptideAtlas

P25815.

PRIDE

P25815.

Protocols and materials databases

DNASU

6286.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000296370; ENSP00000296370; ENSG00000163993.

GeneID

6286.

KEGG

hsa:6286.

UCSC

uc003gjl.3. human.

Organism-specific databases

CTD

6286.

GeneCards

GC04P006696.

HGNC

HGNC:10504. S100P.

HPA

CAB012900.
HPA019502.

MIM

600614. gene.

neXtProt

NX_P25815.

PharmGKB

PA34913.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG78209.

HOGENOM

HOG000246968.

HOVERGEN

HBG001479.

InParanoid

P25815.

OMA

NGDSEVD.

OrthoDB

EOG4GQQ6N.

PhylomeDB

P25815.

Gene expression databases

Bgee

P25815.

CleanEx

HS_S100P.

Genevestigator

P25815.

GermOnline

ENSG00000163993. Homo sapiens.

Family and domain databases

Gene3D

1.10.238.10. 1 hit.

InterPro

IPR011992. EF-hand-like_dom.
IPR002048. EF_hand_dom.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]

Pfam

PF01023. S_100. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Other

DrugBank

DB01003. Cromoglicate.

EvolutionaryTrace

P25815.

GenomeRNAi

6286.

NextBio

24409.

SOURCE

Search...

Entry information

Entry name

S100P_HUMAN

Accession

Primary (citable) accession number: P25815
Secondary accession number(s): Q5J7W2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	December 1, 1992
Last modified:	May 1, 2013
This is version 123 of the entry and version 2 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.

Relevant documents

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents