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Protein S100-B (S-100 protein beta chain) (S-100 protein subunit beta) (S100 calcium-binding protein B)

 S100B_RAT               Reviewed;          92 AA.
P04631;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
13-FEB-2019, entry version 177.
RecName: Full=Protein S100-B;
AltName: Full=S-100 protein beta chain;
AltName: Full=S-100 protein subunit beta;
AltName: Full=S100 calcium-binding protein B;
Name=S100b;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6093041; DOI=10.1093/nar/12.19.7455;
Kuwano R., Usui H., Maeda T., Fukui T., Yamanari N., Ohtsuka E.,
Ikehara M., Takahashi Y.;
"Molecular cloning and the complete nucleotide sequence of cDNA to
mRNA for S-100 protein of rat brain.";
Nucleic Acids Res. 12:7455-7465(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Kuwano R., Usui H., Maeda T., Araki K., Kurihara T., Yamakuni T.,
Ohtsuka E., Ikehara M., Takahashi Y.;
"Molecular cloning and nucleotide sequences of cDNA and genomic DNA
for alpha and beta subunits of S100 protein.";
Taniguchi Symp. Brain Sci. 19:243-255(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
PubMed=1653388; DOI=10.1016/0169-328X(91)90061-2;
Maeda T., Usui H., Araki K., Kuwano R., Takahashi Y., Suzuki Y.;
"Structure and expression of rat S-100 beta subunit gene.";
Brain Res. Mol. Brain Res. 10:193-202(1991).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-92.
PubMed=3818655;
Dunn R., Landry C., O'Hanlon D., Dunn J., Allore R., Brown I.,
Marks A.;
"Reduction in S100 protein beta subunit mRNA in C6 rat glioma cells
following treatment with anti-microtubular drugs.";
J. Biol. Chem. 262:3562-3566(1987).
[6]
PROTEIN SEQUENCE OF 7-21 AND 35-56, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
Lubec G., Afjehi-Sadat L., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[7]
INTERACTION WITH CACYBP.
PubMed=12042313; DOI=10.1074/jbc.M203602200;
Filipek A., Jastrzebska B., Nowotny M., Kuznicki J.;
"CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand
proteins of the S100 family.";
J. Biol. Chem. 277:28848-28852(2002).
[8]
FUNCTION, INTERACTION WITH AGER, AND INDUCTION.
PubMed=19910580; DOI=10.1161/CIRCRESAHA.109.195834;
Tsoporis J.N., Izhar S., Leong-Poi H., Desjardins J.F., Huttunen H.J.,
Parker T.G.;
"S100B interaction with the receptor for advanced glycation end
products (RAGE): a novel receptor-mediated mechanism for myocyte
apoptosis postinfarction.";
Circ. Res. 106:93-101(2010).
[9]
FUNCTION, AND INTERACTION WITH ATAD3A.
PubMed=20351179; DOI=10.1128/MCB.01468-09;
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.;
"The calcium-dependent interaction between S100B and the mitochondrial
AAA ATPase ATAD3A and the role of this complex in the cytoplasmic
processing of ATAD3A.";
Mol. Cell. Biol. 30:2724-2736(2010).
[10]
STRUCTURE BY NMR.
PubMed=8794737; DOI=10.1021/bi9612226;
Drohat A.C., Amburgey J.C., Abildgaard F., Starich M.R.,
Baldisseri D.M., Weber D.J.;
"Solution structure of rat apo-S100B(beta beta) as determined by NMR
spectroscopy.";
Biochemistry 35:11577-11588(1996).
[11]
STRUCTURE BY NMR.
PubMed=9485423; DOI=10.1021/bi972635p;
Drohat A.C., Baldisseri D.M., Rustandi R.R., Weber D.J.;
"Solution structure of calcium-bound rat S100B(betabeta) as determined
by nuclear magnetic resonance spectroscopy.";
Biochemistry 37:2729-2740(1998).
[12]
STRUCTURE BY NMR.
PubMed=10211826; DOI=10.1110/ps.8.4.800;
Drohat A.C., Tjandra N., Baldisseri D.M., Weber D.J.;
"The use of dipolar couplings for determining the solution structure
of rat apo-S100B.";
Protein Sci. 8:800-809(1999).
[13]
STRUCTURE BY NMR IN COMPLEX WITH CAPZA1 AND CALCIUM.
PubMed=12470955; DOI=10.1016/S0022-2836(02)01152-X;
Inman K.G., Yang R., Rustandi R.R., Miller K.E., Baldisseri D.M.,
Weber D.J.;
"Solution NMR structure of S100B bound to the high-affinity target
peptide TRTK-12.";
J. Mol. Biol. 324:1003-1014(2002).
-!- 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. {ECO:0000269|PubMed:19910580,
ECO:0000269|PubMed:20351179}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:12042313, ECO:0000269|PubMed:12470955,
ECO:0000269|PubMed:19910580, ECO:0000269|PubMed:20351179}.
-!- INTERACTION:
Q63495:Ager; NbExp=3; IntAct=EBI-2696631, EBI-6479195;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Although predominant among the water-soluble
brain proteins, S100 is also found in a variety of other tissues.
{ECO:0000269|PubMed:1653388}.
-!- INDUCTION: Up-regulated in periinfarct ventricular myocardium.
{ECO:0000269|PubMed:19910580}.
-!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; X01090; CAA25567.1; -; mRNA.
EMBL; M54919; AAA42096.1; -; mRNA.
EMBL; S53527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; S53522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC087026; AAH87026.1; -; mRNA.
EMBL; M15705; -; NOT_ANNOTATED_CDS; mRNA.
PIR; A60046; A26557.
RefSeq; NP_037323.1; NM_013191.1.
RefSeq; XP_008771090.1; XM_008772868.1.
RefSeq; XP_017457057.1; XM_017601568.1.
UniGene; Rn.8937; -.
PDB; 1B4C; NMR; -; A/B=1-92.
PDB; 1DT7; NMR; -; A/B=1-92.
PDB; 1MWN; NMR; -; A/B=1-92.
PDB; 1QLK; NMR; -; A/B=1-92.
PDB; 1SYM; NMR; -; A/B=1-92.
PDB; 1XYD; NMR; -; A/B=1-92.
PDB; 2K7O; NMR; -; A/B=2-92.
PDBsum; 1B4C; -.
PDBsum; 1DT7; -.
PDBsum; 1MWN; -.
PDBsum; 1QLK; -.
PDBsum; 1SYM; -.
PDBsum; 1XYD; -.
PDBsum; 2K7O; -.
ProteinModelPortal; P04631; -.
SMR; P04631; -.
BioGrid; 247770; 2.
IntAct; P04631; 2.
STRING; 10116.ENSRNOP00000001743; -.
BindingDB; P04631; -.
ChEMBL; CHEMBL3763006; -.
iPTMnet; P04631; -.
PhosphoSitePlus; P04631; -.
SwissPalm; P04631; -.
PaxDb; P04631; -.
PRIDE; P04631; -.
Ensembl; ENSRNOT00000001743; ENSRNOP00000001743; ENSRNOG00000001295.
GeneID; 25742; -.
KEGG; rno:25742; -.
UCSC; RGD:3615; rat.
CTD; 6285; -.
RGD; 3615; S100b.
eggNOG; ENOG410IYFX; Eukaryota.
eggNOG; ENOG41127J0; LUCA.
GeneTree; ENSGT00940000161997; -.
HOGENOM; HOG000246968; -.
HOVERGEN; HBG001479; -.
InParanoid; P04631; -.
OMA; CCHEFFE; -.
OrthoDB; 1574989at2759; -.
PhylomeDB; P04631; -.
TreeFam; TF332727; -.
Reactome; R-RNO-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-RNO-879415; Advanced glycosylation endproduct receptor signaling.
Reactome; R-RNO-933542; TRAF6 mediated NF-kB activation.
EvolutionaryTrace; P04631; -.
PRO; PR:P04631; -.
Proteomes; UP000002494; Chromosome 20.
Bgee; ENSRNOG00000001295; Expressed in 9 organ(s), highest expression level in Ammon's horn.
Genevisible; P04631; RN.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0001726; C:ruffle; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; IDA:RGD.
GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0050786; F:RAGE receptor binding; IPI:RGD.
GO; GO:0044548; F:S100 protein binding; IEA:Ensembl.
GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
GO; GO:0048156; F:tau protein binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:RGD.
GO; GO:0048708; P:astrocyte differentiation; IEP:RGD.
GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
GO; GO:0007611; P:learning or memory; ISS:UniProtKB.
GO; GO:0060291; P:long-term synaptic potentiation; IEP:RGD.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:2001015; P:negative regulation of skeletal muscle cell differentiation; IMP:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0031643; P:positive regulation of myelination; IMP:RGD.
GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:RGD.
GO; GO:0008360; P:regulation of cell shape; IMP:RGD.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0051597; P:response to methylmercury; IEP:RGD.
CDD; cd05027; S-100B; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR028481; S100-B.
InterPro; IPR001751; S100/CaBP-9k_CS.
InterPro; IPR013787; S100_Ca-bd_sub.
PANTHER; PTHR11639:SF17; PTHR11639:SF17; 1.
Pfam; PF00036; EF-hand_1; 1.
Pfam; PF01023; S_100; 1.
SMART; SM00054; EFh; 1.
SMART; SM01394; S_100; 1.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 1.
PROSITE; PS50222; EF_HAND_2; 1.
PROSITE; PS00303; S100_CABP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Calcium; Complete proteome; Cytoplasm;
Direct protein sequencing; Metal-binding; Nucleus; Reference proteome;
Repeat; Zinc.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P02638}.
CHAIN 2 92 Protein S100-B.
/FTId=PRO_0000143969.
DOMAIN 13 48 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 49 84 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 19 32 1; low affinity.
CA_BIND 62 73 2; high affinity.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P02638}.
HELIX 3 18 {ECO:0000244|PDB:1B4C}.
STRAND 21 23 {ECO:0000244|PDB:1SYM}.
STRAND 25 29 {ECO:0000244|PDB:1DT7}.
HELIX 30 40 {ECO:0000244|PDB:1B4C}.
HELIX 41 43 {ECO:0000244|PDB:1QLK}.
HELIX 44 47 {ECO:0000244|PDB:1B4C}.
HELIX 51 62 {ECO:0000244|PDB:1B4C}.
STRAND 66 69 {ECO:0000244|PDB:1B4C}.
HELIX 71 84 {ECO:0000244|PDB:1B4C}.
STRAND 85 87 {ECO:0000244|PDB:1B4C}.
TURN 88 90 {ECO:0000244|PDB:1XYD}.
SEQUENCE 92 AA; 10744 MW; 43815AC212BEC7D0 CRC64;
MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET
LDEDGDGECD FQEFMAFVSM VTTACHEFFE HE


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Kits Elisa; taq POLYMERASE

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Pathways :
WP1566: Citrate cycle (TCA cycle)
WP210: Cytoplasmic Ribosomal Proteins
WP2218: sGC
WP2292: Chemokine signaling pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1616: ABC transporters
WP1644: DNA replication
WP1654: gamma-Hexachlorocyclohexane degradation
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1693: Purine metabolism
WP1694: Pyrimidine metabolism
WP2272: Pathogenic Escherichia coli infection
WP731: Sterol regulatory element binding protein related
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1613: 1,4-Dichlorobenzene degradation
WP1614: 1- and 2-Methylnaphthalene degradation
WP1624: Bacterial secretion system

Related Genes :
[S100B] Protein S100-B (S-100 protein beta chain) (S-100 protein subunit beta) (S100 calcium-binding protein B)
[S100b] Protein S100-B (S-100 protein beta chain) (S-100 protein subunit beta) (S100 calcium-binding protein B)
[S100B] Protein S100-B (S-100 protein beta chain) (S-100 protein subunit beta) (S100 calcium-binding protein B)
[S100b] Protein S100-B (S-100 protein beta chain) (S-100 protein subunit beta) (S100 calcium-binding protein B)
[S100A1 S100A] Protein S100-A1 (S-100 protein alpha chain) (S-100 protein subunit alpha) (S100 calcium-binding protein A1)
[S100a1] Protein S100-A1 (S-100 protein alpha chain) (S-100 protein subunit alpha) (S100 calcium-binding protein A1)
[S100A12] Protein S100-A12 (CGRP) (Calcium-binding protein in amniotic fluid 1) (CAAF1) (Calgranulin-C) (CAGC) (Extracellular newly identified RAGE-binding protein) (EN-RAGE) (Migration inhibitory factor-related protein 6) (MRP-6) (p6) (Neutrophil S100 protein) (S100 calcium-binding protein A12) [Cleaved into: Calcitermin]
[S100A9 CAGB CFAG MRP14] Protein S100-A9 (Calgranulin-B) (Calprotectin L1H subunit) (Leukocyte L1 complex heavy chain) (Migration inhibitory factor-related protein 14) (MRP-14) (p14) (S100 calcium-binding protein A9)
[S100a8 Caga Mrp8] Protein S100-A8 (Calgranulin-A) (Chemotactic cytokine CP-10) (Leukocyte L1 complex light chain) (Migration inhibitory factor-related protein 8) (MRP-8) (p8) (Pro-inflammatory S100 cytokine) (S100 calcium-binding protein A8)
[S100A2 S100L] Protein S100-A2 (CAN19) (Protein S-100L) (S100 calcium-binding protein A2)
[S100a9 Cagb Mrp14] Protein S100-A9 (Calgranulin-B) (Leukocyte L1 complex heavy chain) (Migration inhibitory factor-related protein 14) (MRP-14) (p14) (S100 calcium-binding protein A9)
[S100A8 CAGA CFAG MRP8] Protein S100-A8 (Calgranulin-A) (Calprotectin L1L subunit) (Cystic fibrosis antigen) (CFAG) (Leukocyte L1 complex light chain) (Migration inhibitory factor-related protein 8) (MRP-8) (p8) (S100 calcium-binding protein A8) (Urinary stone protein band A)
[S100a9 Mrp14] Protein S100-A9 (Calgranulin-B) (Migration inhibitory factor-related protein 14) (MRP-14) (p14) (Myeloid-related protein 14) (S100 calcium-binding protein A9)
[S100A1] Protein S100-A1 (S-100 protein alpha chain) (S-100 protein subunit alpha) (S100 calcium-binding protein A1)
[S100A14 S100A15] Protein S100-A14 (S100 calcium-binding protein A14) (S114)
[S100a8 Mrp8] Protein S100-A8 (Calgranulin-A) (Migration inhibitory factor-related protein 8) (MRP-8) (p8) (S100 calcium-binding protein A8)
[S100A9 MRP14] Protein S100-A9 (Calgranulin-B) (Migration inhibitory factor-related protein 14) (MRP-14) (p14) (S100 calcium-binding protein A9)
[S100A12 CAAF1] Protein S100-A12 (Calcium-binding protein in amniotic fluid 1) (CAAF1) (Calgranulin-C) (CAGC) (Cornea-associated antigen) (CO-AG) (Extracellular newly identified RAGE-binding protein) (EN-RAGE) (RAGE-binding protein) (S100 calcium-binding protein A12)
[S100A9] Protein S100-A9 (BEE22) (Calgranulin-B) (Neutrophil cytosolic 23 kDa protein) (p23) (S100 calcium-binding protein A9)
[S100A5 S100D] Protein S100-A5 (Protein S-100D) (S100 calcium-binding protein A5)
[S100a1] Protein S100-A1 (S-100 protein alpha chain) (S-100 protein subunit alpha) (S100 calcium-binding protein A1)
[S100A12] Protein S100-A12 (Calgranulin-C) (CAGC) (Extracellular newly identified RAGE-binding protein) (EN-RAGE) (S100 calcium-binding protein A12)
[S100A8] Protein S100-A8 (BEE11) (Calgranulin-A) (Neutrophil cytosolic 7 kDa protein) (P7) (S100 calcium-binding protein A8)
[CACYBP S100A6BP SIP PNAS-107] Calcyclin-binding protein (CacyBP) (hCacyBP) (S100A6-binding protein) (Siah-interacting protein)
[S100a5 S100d] Protein S100-A5 (Protein S-100D) (S100 calcium-binding protein A5)
[S100PBP S100PBPR] S100P-binding protein (S100P-binding protein Riken)
[S100a14 Gm1020 S100a15] Protein S100-A14 (S100 calcium-binding protein A14) (S114)
[S100A12] Protein S100-A12 (Calgranulin-C) (CAGC) (Extracellular newly identified RAGE-binding protein) (EN-RAGE) (S100 calcium-binding protein A12)
[S100A9] Protein S100 (S100 calcium-binding protein)
[S100B] Protein S100-B (S-100 protein beta chain) (S-100 protein subunit beta) (S100 calcium-binding protein B)

Bibliography :
[20047785] Can early serum levels of S100B protein predict the prognosis of patients with out-of-hospital cardiac arrest?