Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P04271 (S100B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein S100-B
Alternative name(s):
S-100 protein beta chain
S-100 protein subunit beta
S100 calcium-binding protein B
Gene names
Name:S100B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length92 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity. Ref.10 Ref.11

Subunit structure

Dimer of either two alpha chains, or two beta chains, or one alpha and one beta chain. The S100B dimer binds two molecules of STK38. Interacts with CACYBP in a calcium-dependent manner. Interacts with ATAD3A; this interaction probably occurs in the cytosol prior to ATAD3A mitochondrial targeting. Interacts with S100A6. The S100B dimer interacts with two molecules of CAPZA1. Interacts with AGER. Interacts with PPP5C (via TPR repeats); the interaction is calcium-dependent and modulates PPP5C activity. Ref.8 Ref.9 Ref.10 Ref.11

Subcellular location

Cytoplasm. Nucleus Ref.8.

Tissue specificity

Although predominant among the water-soluble brain proteins, S100 is also found in a variety of other tissues.

Miscellaneous

In addition to metal-ion binding, this protein is involved with the regulation of protein phosphorylation in brain tissue.

Sequence similarities

Belongs to the S-101 family.

Contains 2 EF-hand domains.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
   LigandCalcium
Metal-binding
Zinc
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processastrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

axonogenesis

Traceable author statement PubMed 8202493. Source: ProtInc

cell proliferation

Traceable author statement PubMed 8202493. Source: ProtInc

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

central nervous system development

Traceable author statement PubMed 8202493. Source: ProtInc

innate immune response

Traceable author statement. Source: Reactome

learning or memory

Inferred from sequence or structural similarity. Source: UniProtKB

long-term synaptic potentiation

Inferred from electronic annotation. Source: Ensembl

memory

Inferred from electronic annotation. Source: Ensembl

negative regulation of skeletal muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from direct assay PubMed 15033494. Source: UniProtKB

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of cell shape

Inferred from electronic annotation. Source: Ensembl

regulation of neuronal synaptic plasticity

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to methylmercury

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 10913138. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from electronic annotation. Source: Ensembl

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 10913138. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 12118070PubMed 15033494. Source: UniProtKB

ruffle

Inferred from direct assay PubMed 10913138. Source: UniProtKB

   Molecular_functionRAGE receptor binding

Inferred from physical interaction PubMed 15033494. Source: UniProtKB

S100 protein binding

Inferred from physical interaction PubMed 10913138Ref.12. Source: UniProtKB

calcium ion binding

Non-traceable author statement Ref.12. Source: UniProtKB

calcium-dependent protein binding

Inferred from direct assay PubMed 10913138. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 10913138PubMed 17660747. Source: IntAct

protein homodimerization activity

Inferred from direct assay PubMed 10913138. Source: UniProtKB

tau protein binding

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 9291Protein S100-B
PRO_0000143966

Regions

Domain13 – 4836EF-hand 1
Domain49 – 8436EF-hand 2
Calcium binding19 – 32141; low affinity
Calcium binding62 – 73122; high affinity

Amino acid modifications

Modified residue21Blocked amino end (Ser) Ref.6
Modified residue21N-acetylserine By similarity

Secondary structure

.................. 92
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04271 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 43815AC212A3AD6B

FASTA9210,713
        10         20         30         40         50         60 
MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET 

        70         80         90 
LDNDGDGECD FQEFMAFVAM VTTACHEFFE HE 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of the human S100 beta gene."
Allore R.J., Friend W.C., O'Hanlon D., Neilson K.M., Baumal R., Dunn R.J., Marks A.
J. Biol. Chem. 265:15537-15543(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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 (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"The DNA sequence of human chromosome 21."
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. expand/collapse author list , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: Skin.
[6]"Characterization of human brain S100 protein fraction: amino acid sequence of S100 beta."
Jensen R., Marshak D.R., Anderson C., Lukas T.J., Watterson D.M.
J. Neurochem. 45:700-705(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-92.
[7]"Purification, characterization and ion binding properties of human brain S100b protein."
Baudier J., Glasser N., Haglid K., Gerard D.
Biochim. Biophys. Acta 790:164-173(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: METAL ION-BINDING PROPERTIES.
[8]"Demonstration of heterodimer formation between S100B and S100A6 in the yeast two-hybrid system and human melanoma."
Yang Q., O'Hanlon D., Heizmann C.W., Marks A.
Exp. Cell Res. 246:501-509(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH S100A6.
[9]"The 1.5 A crystal structure of human receptor for advanced glycation endproducts (RAGE) ectodomains reveals unique features determining ligand binding."
Park H., Adsit F.G., Boyington J.C.
J. Biol. Chem. 285:40762-40770(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AGER.
[10]"The calcium-dependent interaction between S100B and the mitochondrial AAA ATPase ATAD3A and the role of this complex in the cytoplasmic processing of ATAD3A."
Gilquin B., Cannon B.R., Hubstenberger A., Moulouel B., Falk E., Merle N., Assard N., Kieffer S., Rousseau D., Wilder P.T., Weber D.J., Baudier J.
Mol. Cell. Biol. 30:2724-2736(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ATAD3A.
[11]"S100 proteins modulate protein phosphatase 5 function: a link between CA2+ signal transduction and protein dephosphorylation."
Yamaguchi F., Umeda Y., Shimamoto S., Tsuchiya M., Tokumitsu H., Tokuda M., Kobayashi R.
J. Biol. Chem. 287:13787-13798(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PPP5C.
[12]"A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form."
Smith S.P., Shaw G.S.
Structure 6:211-222(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[13]"A novel S100 target conformation is revealed by the solution structure of the Ca2+-S100B-TRTK-12 complex."
McClintock K.A., Shaw G.S.
J. Biol. Chem. 278:6251-6257(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR IN COMPLEX WITH CAPZA1 AND CALCIUM.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M59488, M59487 Genomic DNA. Translation: AAA60367.1.
CR542123 mRNA. Translation: CAG46920.1.
AP000339 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09267.1.
CH471079 Genomic DNA. Translation: EAX09268.1.
CH471079 Genomic DNA. Translation: EAX09269.1.
CH471079 Genomic DNA. Translation: EAX09270.1.
BC001766 mRNA. Translation: AAH01766.1.
PIRBCHUIB. A38364.
RefSeqNP_006263.1. NM_006272.2.
UniGeneHs.422181.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MQ1NMR-A/B2-92[»]
1UWONMR-A/B2-92[»]
2H61X-ray1.90A/B/C/D/E/F/G/H1-92[»]
2M49NMR-B/D2-92[»]
2PRUNMR-A/B2-92[»]
3CZTX-ray1.40X1-92[»]
3D0YX-ray1.50A/B1-92[»]
3D10X-ray1.65A/B1-92[»]
3HCMX-ray2.00A/B1-92[»]
ProteinModelPortalP04271.
SMRP04271. Positions 1-91.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112193. 17 interactions.
IntActP04271. 11 interactions.
MINTMINT-192546.
STRING9606.ENSP00000291700.

Chemistry

BindingDBP04271.
ChEMBLCHEMBL4300.

PTM databases

PhosphoSiteP04271.

Polymorphism databases

DMDM134138.

Proteomic databases

PaxDbP04271.
PeptideAtlasP04271.
PRIDEP04271.

Protocols and materials databases

DNASU6285.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000291700; ENSP00000291700; ENSG00000160307.
ENST00000397648; ENSP00000380769; ENSG00000160307.
GeneID6285.
KEGGhsa:6285.
UCSCuc002zju.1. human.

Organism-specific databases

CTD6285.
GeneCardsGC21M048018.
HGNCHGNC:10500. S100B.
HPACAB000073.
CAB006825.
HPA015768.
MIM176990. gene.
neXtProtNX_P04271.
PharmGKBPA34912.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41158.
HOVERGENHBG001479.
OMAGDAECDF.
OrthoDBEOG7R833W.
PhylomeDBP04271.
TreeFamTF332727.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP04271.
BgeeP04271.
CleanExHS_S100B.
GenevestigatorP04271.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR028481. S100-B.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]
PANTHERPTHR11639:SF17. PTHR11639:SF17. 1 hit.
PfamPF01023. S_100. 1 hit.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSS100B. human.
EvolutionaryTraceP04271.
GeneWikiS100B.
GenomeRNAi6285.
NextBio24405.
PROP04271.
SOURCESearch...

Entry information

Entry nameS100B_HUMAN
AccessionPrimary (citable) accession number: P04271
Secondary accession number(s): D3DSN6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM