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P04631 (S100B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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.8 Ref.9

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.7 Ref.8 Ref.9

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Tissue specificity

Although predominant among the water-soluble brain proteins, S100 is also found in a variety of other tissues. Ref.3

Induction

Up-regulated in periinfarct ventricular myocardium. Ref.8

Sequence similarities

Belongs to the S-100 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 expression pattern PubMed 19147496. Source: RGD

cellular response to hypoxia

Inferred from expression pattern Ref.8. Source: RGD

learning or memory

Inferred from sequence or structural similarity. Source: UniProtKB

long-term synaptic potentiation

Inferred from expression pattern PubMed 21546003. Source: RGD

memory

Inferred from electronic annotation. Source: Ensembl

negative regulation of skeletal muscle cell differentiation

Inferred from mutant phenotype PubMed 20069545. Source: RGD

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

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 17639288. Source: RGD

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 2229184. Source: RGD

positive regulation of synaptic transmission

Inferred from mutant phenotype PubMed 12428274. Source: RGD

regulation of cell shape

Inferred from mutant phenotype PubMed 2229184. Source: RGD

regulation of neuronal synaptic plasticity

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from expression pattern PubMed 16112204. Source: RGD

response to methylmercury

Inferred from expression pattern PubMed 21783483. Source: RGD

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 21098642. Source: RGD

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

ruffle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionRAGE receptor binding

Inferred from physical interaction Ref.8. Source: RGD

calcium ion binding

Inferred from direct assay PubMed 18949447. Source: RGD

protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 18949447. Source: RGD

receptor binding

Inferred from physical interaction PubMed 18445708. Source: RGD

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...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AgerQ634953EBI-2696631,EBI-6479195

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 9291Protein S100-B
PRO_0000143969

Regions

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

Amino acid modifications

Modified residue21N-acetylserine By similarity

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P04631 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 43815AC212BEC7D0

FASTA9210,744
        10         20         30         40         50         60 
MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET 

        70         80         90 
LDEDGDGECD FQEFMAFVSM VTTACHEFFE HE 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and the complete nucleotide sequence of cDNA to mRNA for S-100 protein of rat brain."
Kuwano R., Usui H., Maeda T., Fukui T., Yamanari N., Ohtsuka E., Ikehara M., Takahashi Y.
Nucleic Acids Res. 12:7455-7465(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning and nucleotide sequences of cDNA and genomic DNA for alpha and beta subunits of S100 protein."
Kuwano R., Usui H., Maeda T., Araki K., Kurihara T., Yamakuni T., Ohtsuka E., Ikehara M., Takahashi Y.
Taniguchi Symp. Brain Sci. 19:243-255(1987)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Structure and expression of rat S-100 beta subunit gene."
Maeda T., Usui H., Araki K., Kuwano R., Takahashi Y., Suzuki Y.
Brain Res. Mol. Brain Res. 10:193-202(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
[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].
Tissue: Heart.
[5]"Reduction in S100 protein beta subunit mRNA in C6 rat glioma cells following treatment with anti-microtubular drugs."
Dunn R., Landry C., O'Hanlon D., Dunn J., Allore R., Brown I., Marks A.
J. Biol. Chem. 262:3562-3566(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-92.
[6]Lubec G., Afjehi-Sadat L., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 7-21 AND 35-56, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain and Spinal cord.
[7]"CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand proteins of the S100 family."
Filipek A., Jastrzebska B., Nowotny M., Kuznicki J.
J. Biol. Chem. 277:28848-28852(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CACYBP.
[8]"S100B interaction with the receptor for advanced glycation end products (RAGE): a novel receptor-mediated mechanism for myocyte apoptosis postinfarction."
Tsoporis J.N., Izhar S., Leong-Poi H., Desjardins J.F., Huttunen H.J., Parker T.G.
Circ. Res. 106:93-101(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH AGER, INDUCTION.
[9]"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.
[10]"Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy."
Drohat A.C., Amburgey J.C., Abildgaard F., Starich M.R., Baldisseri D.M., Weber D.J.
Biochemistry 35:11577-11588(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[11]"Solution structure of calcium-bound rat S100B(betabeta) as determined by nuclear magnetic resonance spectroscopy."
Drohat A.C., Baldisseri D.M., Rustandi R.R., Weber D.J.
Biochemistry 37:2729-2740(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[12]"The use of dipolar couplings for determining the solution structure of rat apo-S100B."
Drohat A.C., Tjandra N., Baldisseri D.M., Weber D.J.
Protein Sci. 8:800-809(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[13]"Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12."
Inman K.G., Yang R., Rustandi R.R., Miller K.E., Baldisseri D.M., Weber D.J.
J. Mol. Biol. 324:1003-1014(2002) [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
X01090 mRNA. Translation: CAA25567.1.
M54919 mRNA. Translation: AAA42096.1.
S53527 Genomic DNA. No translation available.
S53522 Genomic DNA. No translation available.
BC087026 mRNA. Translation: AAH87026.1.
M15705 mRNA. No translation available.
PIRA26557. A60046.
RefSeqNP_037323.1. NM_013191.1.
XP_006256344.1. XM_006256282.1.
UniGeneRn.8937.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B4CNMR-A/B1-92[»]
1DT7NMR-A/B1-92[»]
1MWNNMR-A/B1-92[»]
1QLKNMR-A/B1-92[»]
1SYMNMR-A/B1-92[»]
1XYDNMR-A/B1-92[»]
2K7ONMR-A/B2-92[»]
ProteinModelPortalP04631.
SMRP04631. Positions 1-91.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247770. 1 interaction.
IntActP04631. 2 interactions.
STRING10116.ENSRNOP00000001743.

PTM databases

PhosphoSiteP04631.

Proteomic databases

PaxDbP04631.
PRIDEP04631.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000001743; ENSRNOP00000001743; ENSRNOG00000001295.
GeneID25742.
KEGGrno:25742.
UCSCRGD:3615. rat.

Organism-specific databases

CTD6285.
RGD3615. S100b.

Phylogenomic databases

eggNOGNOG41158.
GeneTreeENSGT00740000114986.
HOGENOMHOG000246968.
HOVERGENHBG001479.
InParanoidP04631.
OMAGDAECDF.
OrthoDBEOG7R833W.
PhylomeDBP04631.
TreeFamTF332727.

Gene expression databases

GenevestigatorP04631.

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

EvolutionaryTraceP04631.
NextBio607903.
PROP04631.

Entry information

Entry nameS100B_RAT
AccessionPrimary (citable) accession number: P04631
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references