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

 S100B_HUMAN             Reviewed;          92 AA.
P04271; D3DSN6;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 188.
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;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2394738;
Allore R.J., Friend W.C., O'Hanlon D., Neilson K.M., Baumal R.,
Dunn R.J., Marks A.;
"Cloning and expression of the human S100 beta gene.";
J. Biol. Chem. 265:15537-15543(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
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., 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.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
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).
[6]
PROTEIN SEQUENCE OF 2-92.
PubMed=4031854; DOI=10.1111/j.1471-4159.1985.tb04048.x;
Jensen R., Marshak D.R., Anderson C., Lukas T.J., Watterson D.M.;
"Characterization of human brain S100 protein fraction: amino acid
sequence of S100 beta.";
J. Neurochem. 45:700-705(1985).
[7]
METAL ION-BINDING PROPERTIES.
PubMed=6487634; DOI=10.1016/0167-4838(84)90220-6;
Baudier J., Glasser N., Haglid K., Gerard D.;
"Purification, characterization and ion binding properties of human
brain S100b protein.";
Biochim. Biophys. Acta 790:164-173(1984).
[8]
SUBCELLULAR LOCATION, AND INTERACTION WITH S100A6.
PubMed=9925766; DOI=10.1006/excr.1998.4314;
Yang Q., O'Hanlon D., Heizmann C.W., Marks A.;
"Demonstration of heterodimer formation between S100B and S100A6 in
the yeast two-hybrid system and human melanoma.";
Exp. Cell Res. 246:501-509(1999).
[9]
INTERACTION WITH AGER.
PubMed=20943659; DOI=10.1074/jbc.M110.169276;
Park H., Adsit F.G., Boyington J.C.;
"The 1.5 A crystal structure of human receptor for advanced glycation
endproducts (RAGE) ectodomains reveals unique features determining
ligand binding.";
J. Biol. Chem. 285:40762-40770(2010).
[10]
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).
[11]
FUNCTION, AND INTERACTION WITH PPP5C.
PubMed=22399290; DOI=10.1074/jbc.M111.329771;
Yamaguchi F., Umeda Y., Shimamoto S., Tsuchiya M., Tokumitsu H.,
Tokuda M., Kobayashi R.;
"S100 proteins modulate protein phosphatase 5 function: a link between
CA2+ signal transduction and protein dephosphorylation.";
J. Biol. Chem. 287:13787-13798(2012).
[12]
STRUCTURE BY NMR.
PubMed=9519411; DOI=10.1016/S0969-2126(98)00022-7;
Smith S.P., Shaw G.S.;
"A novel calcium-sensitive switch revealed by the structure of human
S100B in the calcium-bound form.";
Structure 6:211-222(1998).
[13]
STRUCTURE BY NMR IN COMPLEX WITH CAPZA1 AND CALCIUM.
PubMed=12480931; DOI=10.1074/jbc.M210622200;
McClintock K.A., Shaw G.S.;
"A novel S100 target conformation is revealed by the solution
structure of the Ca2+-S100B-TRTK-12 complex.";
J. Biol. Chem. 278:6251-6257(2003).
-!- 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:20351179,
ECO:0000269|PubMed:22399290}.
-!- 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:12480931, ECO:0000269|PubMed:20351179,
ECO:0000269|PubMed:20943659, ECO:0000269|PubMed:22399290,
ECO:0000269|PubMed:9925766}.
-!- INTERACTION:
Self; NbExp=18; IntAct=EBI-458391, EBI-458391;
Q15109:AGER; NbExp=5; IntAct=EBI-458391, EBI-1646426;
Q00987:MDM2; NbExp=2; IntAct=EBI-458391, EBI-389668;
P23297:S100A1; NbExp=17; IntAct=EBI-458391, EBI-743686;
Q5T7Y6:S100A1; NbExp=5; IntAct=EBI-458391, EBI-11746600;
P31949:S100A11; NbExp=5; IntAct=EBI-458391, EBI-701862;
P29034:S100A2; NbExp=7; IntAct=EBI-458391, EBI-752230;
P26447:S100A4; NbExp=7; IntAct=EBI-458391, EBI-717058;
P06703:S100A6; NbExp=5; IntAct=EBI-458391, EBI-352877;
P25815:S100P; NbExp=6; IntAct=EBI-458391, EBI-743700;
Q9NZD8:SPG21; NbExp=5; IntAct=EBI-458391, EBI-742688;
P04637:TP53; NbExp=2; IntAct=EBI-458391, EBI-366083;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9925766}.
Nucleus {ECO:0000269|PubMed:9925766}.
-!- 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.
-!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/S100BID42195ch21q22.html";
-----------------------------------------------------------------------
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EMBL; M59488; AAA60367.1; -; Genomic_DNA.
EMBL; M59487; AAA60367.1; JOINED; Genomic_DNA.
EMBL; CR542123; CAG46920.1; -; mRNA.
EMBL; AP000339; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471079; EAX09267.1; -; Genomic_DNA.
EMBL; CH471079; EAX09268.1; -; Genomic_DNA.
EMBL; CH471079; EAX09269.1; -; Genomic_DNA.
EMBL; CH471079; EAX09270.1; -; Genomic_DNA.
EMBL; BC001766; AAH01766.1; -; mRNA.
CCDS; CCDS13736.1; -.
PIR; A38364; BCHUIB.
RefSeq; NP_006263.1; NM_006272.2.
RefSeq; XP_016883913.1; XM_017028424.1.
UniGene; Hs.422181; -.
PDB; 1MQ1; NMR; -; A/B=2-92.
PDB; 1UWO; NMR; -; A/B=2-92.
PDB; 2H61; X-ray; 1.90 A; A/B/C/D/E/F/G/H=1-92.
PDB; 2M49; NMR; -; B/D=2-92.
PDB; 2PRU; NMR; -; A/B=2-92.
PDB; 3CZT; X-ray; 1.40 A; X=1-92.
PDB; 3D0Y; X-ray; 1.50 A; A/B=1-92.
PDB; 3D10; X-ray; 1.65 A; A/B=1-92.
PDB; 3HCM; X-ray; 2.00 A; A/B=1-92.
PDB; 4XYN; X-ray; 2.55 A; A/B/C/D=1-92.
PDB; 5CSF; X-ray; 2.40 A; A/B=1-92.
PDB; 5CSI; X-ray; 2.13 A; A/B=1-92.
PDB; 5CSJ; X-ray; 2.70 A; A/B=1-92.
PDB; 5CSN; X-ray; 2.95 A; A/B=1-92.
PDB; 5D7F; X-ray; 1.30 A; A/B=1-92.
PDBsum; 1MQ1; -.
PDBsum; 1UWO; -.
PDBsum; 2H61; -.
PDBsum; 2M49; -.
PDBsum; 2PRU; -.
PDBsum; 3CZT; -.
PDBsum; 3D0Y; -.
PDBsum; 3D10; -.
PDBsum; 3HCM; -.
PDBsum; 4XYN; -.
PDBsum; 5CSF; -.
PDBsum; 5CSI; -.
PDBsum; 5CSJ; -.
PDBsum; 5CSN; -.
PDBsum; 5D7F; -.
ProteinModelPortal; P04271; -.
SMR; P04271; -.
BioGrid; 112193; 31.
IntAct; P04271; 20.
MINT; MINT-192546; -.
STRING; 9606.ENSP00000291700; -.
BindingDB; P04271; -.
ChEMBL; CHEMBL4300; -.
DrugBank; DB06941; (Z)-2-[2-(4-methylpiperazin-1-yl)benzyl]diazenecarbothioamide.
DrugBank; DB07004; 2-[(5-hex-1-yn-1-ylfuran-2-yl)carbonyl]-N-methylhydrazinecarbothioamide.
DrugBank; DB01373; Calcium.
DrugBank; DB04464; N-Formylmethionine.
DrugBank; DB00768; Olopatadine.
DrugBank; DB05343; ONO-2506.
TCDB; 8.A.81.1.4; the s100 calcium-binding protein (s100) family.
iPTMnet; P04271; -.
PhosphoSitePlus; P04271; -.
BioMuta; S100B; -.
DMDM; 134138; -.
EPD; P04271; -.
PaxDb; P04271; -.
PeptideAtlas; P04271; -.
PRIDE; P04271; -.
TopDownProteomics; P04271; -.
DNASU; 6285; -.
Ensembl; ENST00000291700; ENSP00000291700; ENSG00000160307.
Ensembl; ENST00000397648; ENSP00000380769; ENSG00000160307.
GeneID; 6285; -.
KEGG; hsa:6285; -.
UCSC; uc002zju.2; human.
CTD; 6285; -.
DisGeNET; 6285; -.
EuPathDB; HostDB:ENSG00000160307.9; -.
GeneCards; S100B; -.
HGNC; HGNC:10500; S100B.
HPA; CAB000073; -.
HPA; CAB078196; -.
HPA; HPA015768; -.
MIM; 176990; gene.
neXtProt; NX_P04271; -.
OpenTargets; ENSG00000160307; -.
PharmGKB; PA34912; -.
eggNOG; ENOG410IYFX; Eukaryota.
eggNOG; ENOG41127J0; LUCA.
GeneTree; ENSGT00760000119034; -.
HOVERGEN; HBG001479; -.
InParanoid; P04271; -.
OMA; CCHEFFE; -.
PhylomeDB; P04271; -.
TreeFam; TF332727; -.
Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
Reactome; R-HSA-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-HSA-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-HSA-879415; Advanced glycosylation endproduct receptor signaling.
Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
ChiTaRS; S100B; human.
EvolutionaryTrace; P04271; -.
GeneWiki; S100B; -.
GenomeRNAi; 6285; -.
PRO; PR:P04271; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000160307; -.
CleanEx; HS_S100B; -.
ExpressionAtlas; P04271; baseline and differential.
Genevisible; P04271; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0001726; C:ruffle; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
GO; GO:0048306; F:calcium-dependent protein binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0050786; F:RAGE receptor binding; IPI:UniProtKB.
GO; GO:0044548; F:S100 protein binding; IPI:UniProtKB.
GO; GO:0048156; F:tau protein binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0048708; P:astrocyte differentiation; IEA:Ensembl.
GO; GO:0007409; P:axonogenesis; TAS:ProtInc.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
GO; GO:0045087; P:innate immune response; TAS:Reactome.
GO; GO:0007611; P:learning or memory; ISS:UniProtKB.
GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:2001015; P:negative regulation of skeletal muscle cell differentiation; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0031643; P:positive regulation of myelination; IEA:Ensembl.
GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0051597; P:response to methylmercury; IEA:Ensembl.
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,
ECO:0000269|PubMed:4031854}.
CHAIN 2 92 Protein S100-B.
/FTId=PRO_0000143966.
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 Blocked amino end (Ser); alternate.
{ECO:0000269|PubMed:4031854}.
MOD_RES 2 2 N-acetylserine; alternate.
{ECO:0000250|UniProtKB:P02638}.
HELIX 3 19 {ECO:0000244|PDB:5D7F}.
STRAND 21 24 {ECO:0000244|PDB:5D7F}.
HELIX 30 40 {ECO:0000244|PDB:5D7F}.
TURN 42 44 {ECO:0000244|PDB:5D7F}.
STRAND 47 49 {ECO:0000244|PDB:2PRU}.
HELIX 51 61 {ECO:0000244|PDB:5D7F}.
STRAND 65 69 {ECO:0000244|PDB:5D7F}.
HELIX 71 85 {ECO:0000244|PDB:5D7F}.
HELIX 86 88 {ECO:0000244|PDB:5D7F}.
TURN 89 91 {ECO:0000244|PDB:2PRU}.
SEQUENCE 92 AA; 10713 MW; 43815AC212A3AD6B CRC64;
MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET
LDNDGDGECD FQEFMAFVAM VTTACHEFFE HE


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