S100B_HUMAN
ID S100B_HUMAN Reviewed; 92 AA.
AC P04271; D3DSN6;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Protein S100-B;
DE AltName: Full=S-100 protein beta chain;
DE AltName: Full=S-100 protein subunit beta;
DE AltName: Full=S100 calcium-binding protein B;
GN Name=S100B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2394738; DOI=10.1016/s0021-9258(18)55430-2;
RA Allore R.J., Friend W.C., O'Hanlon D., Neilson K.M., Baumal R., Dunn R.J.,
RA Marks A.;
RT "Cloning and expression of the human S100 beta gene.";
RL J. Biol. Chem. 265:15537-15543(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-92.
RX PubMed=4031854; DOI=10.1111/j.1471-4159.1985.tb04048.x;
RA Jensen R., Marshak D.R., Anderson C., Lukas T.J., Watterson D.M.;
RT "Characterization of human brain S100 protein fraction: amino acid sequence
RT of S100 beta.";
RL J. Neurochem. 45:700-705(1985).
RN [7]
RP METAL ION-BINDING PROPERTIES.
RX PubMed=6487634; DOI=10.1016/0167-4838(84)90220-6;
RA Baudier J., Glasser N., Haglid K., Gerard D.;
RT "Purification, characterization and ion binding properties of human brain
RT S100b protein.";
RL Biochim. Biophys. Acta 790:164-173(1984).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH S100A6.
RX PubMed=9925766; DOI=10.1006/excr.1998.4314;
RA Yang Q., O'Hanlon D., Heizmann C.W., Marks A.;
RT "Demonstration of heterodimer formation between S100B and S100A6 in the
RT yeast two-hybrid system and human melanoma.";
RL Exp. Cell Res. 246:501-509(1999).
RN [9]
RP INTERACTION WITH AGER.
RX PubMed=20943659; DOI=10.1074/jbc.m110.169276;
RA Park H., Adsit F.G., Boyington J.C.;
RT "The 1.5 A crystal structure of human receptor for advanced glycation
RT endproducts (RAGE) ectodomains reveals unique features determining ligand
RT binding.";
RL J. Biol. Chem. 285:40762-40770(2010).
RN [10]
RP FUNCTION, AND INTERACTION WITH ATAD3A.
RX PubMed=20351179; DOI=10.1128/mcb.01468-09;
RA Gilquin B., Cannon B.R., Hubstenberger A., Moulouel B., Falk E., Merle N.,
RA Assard N., Kieffer S., Rousseau D., Wilder P.T., Weber D.J., Baudier J.;
RT "The calcium-dependent interaction between S100B and the mitochondrial AAA
RT ATPase ATAD3A and the role of this complex in the cytoplasmic processing of
RT ATAD3A.";
RL Mol. Cell. Biol. 30:2724-2736(2010).
RN [11]
RP FUNCTION, AND INTERACTION WITH PPP5C.
RX PubMed=22399290; DOI=10.1074/jbc.m111.329771;
RA Yamaguchi F., Umeda Y., Shimamoto S., Tsuchiya M., Tokumitsu H., Tokuda M.,
RA Kobayashi R.;
RT "S100 proteins modulate protein phosphatase 5 function: a link between CA2+
RT signal transduction and protein dephosphorylation.";
RL J. Biol. Chem. 287:13787-13798(2012).
RN [12]
RP INTERACTION WITH TPPP.
RX PubMed=33831707; DOI=10.1016/j.ceca.2021.102404;
RA Doi S., Fujioka N., Ohtsuka S., Kondo R., Yamamoto M., Denda M., Magari M.,
RA Kanayama N., Hatano N., Morishita R., Hasegawa T., Tokumitsu H.;
RT "Regulation of the tubulin polymerization-promoting protein by Ca2+/S100
RT proteins.";
RL Cell Calcium 96:102404-102404(2021).
RN [13]
RP STRUCTURE BY NMR.
RX PubMed=9519411; DOI=10.1016/s0969-2126(98)00022-7;
RA Smith S.P., Shaw G.S.;
RT "A novel calcium-sensitive switch revealed by the structure of human S100B
RT in the calcium-bound form.";
RL Structure 6:211-222(1998).
RN [14]
RP STRUCTURE BY NMR IN COMPLEX WITH CAPZA1 AND CALCIUM.
RX PubMed=12480931; DOI=10.1074/jbc.m210622200;
RA McClintock K.A., Shaw G.S.;
RT "A novel S100 target conformation is revealed by the solution structure of
RT the Ca2+-S100B-TRTK-12 complex.";
RL J. Biol. Chem. 278:6251-6257(2003).
CC -!- FUNCTION: Weakly binds calcium but binds zinc very tightly-distinct
CC binding sites with different affinities exist for both ions on each
CC monomer. Physiological concentrations of potassium ion antagonize the
CC binding of both divalent cations, especially affecting high-affinity
CC calcium-binding sites. Binds to and initiates the activation of STK38
CC by releasing autoinhibitory intramolecular interactions within the
CC kinase. Interaction with AGER after myocardial infarction may play a
CC role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling.
CC Could assist ATAD3A cytoplasmic processing, preventing aggregation and
CC favoring mitochondrial localization. May mediate calcium-dependent
CC regulation on many physiological processes by interacting with other
CC proteins, such as TPR-containing proteins, and modulating their
CC activity. {ECO:0000269|PubMed:20351179, ECO:0000269|PubMed:22399290}.
CC -!- SUBUNIT: Dimer of either two alpha chains, or two beta chains, or one
CC alpha and one beta chain. The S100B dimer binds two molecules of STK38.
CC Interacts with CACYBP in a calcium-dependent manner. Interacts with
CC ATAD3A; this interaction probably occurs in the cytosol prior to ATAD3A
CC mitochondrial targeting. Interacts with S100A6. The S100B dimer
CC interacts with two molecules of CAPZA1. Interacts with AGER. Interacts
CC with PPP5C (via TPR repeats); the interaction is calcium-dependent and
CC modulates PPP5C activity. Interacts with TPPP; this interaction
CC inhibits TPPP dimerization (PubMed:33831707).
CC {ECO:0000269|PubMed:12480931, ECO:0000269|PubMed:20351179,
CC ECO:0000269|PubMed:20943659, ECO:0000269|PubMed:22399290,
CC ECO:0000269|PubMed:33831707, ECO:0000269|PubMed:9925766}.
CC -!- INTERACTION:
CC P04271; P01023: A2M; NbExp=3; IntAct=EBI-458391, EBI-640741;
CC P04271; Q15109: AGER; NbExp=5; IntAct=EBI-458391, EBI-1646426;
CC P04271; Q06481-5: APLP2; NbExp=3; IntAct=EBI-458391, EBI-25646567;
CC P04271; P05067: APP; NbExp=3; IntAct=EBI-458391, EBI-77613;
CC P04271; Q13867: BLMH; NbExp=3; IntAct=EBI-458391, EBI-718504;
CC P04271; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-458391, EBI-1383687;
CC P04271; P27824-2: CANX; NbExp=3; IntAct=EBI-458391, EBI-25890990;
CC P04271; P52907: CAPZA1; NbExp=3; IntAct=EBI-458391, EBI-355586;
CC P04271; Q86YQ8-2: CPNE8; NbExp=3; IntAct=EBI-458391, EBI-25891175;
CC P04271; Q9UGL9: CRCT1; NbExp=3; IntAct=EBI-458391, EBI-713677;
CC P04271; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-458391, EBI-9087876;
CC P04271; O75553-5: DAB1; NbExp=3; IntAct=EBI-458391, EBI-12133006;
CC P04271; O14576-2: DYNC1I1; NbExp=3; IntAct=EBI-458391, EBI-25840445;
CC P04271; P21860: ERBB3; NbExp=3; IntAct=EBI-458391, EBI-720706;
CC P04271; P0DMV8: HSPA1A; NbExp=3; IntAct=EBI-458391, EBI-11052499;
CC P04271; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-458391, EBI-739832;
CC P04271; Q07954-2: LRP1; NbExp=3; IntAct=EBI-458391, EBI-25833471;
CC P04271; Q00987: MDM2; NbExp=2; IntAct=EBI-458391, EBI-389668;
CC P04271; O15151: MDM4; NbExp=3; IntAct=EBI-458391, EBI-398437;
CC P04271; P35579: MYH9; NbExp=2; IntAct=EBI-458391, EBI-350338;
CC P04271; P41271-2: NBL1; NbExp=3; IntAct=EBI-458391, EBI-12135485;
CC P04271; Q15843: NEDD8; NbExp=3; IntAct=EBI-458391, EBI-716247;
CC P04271; P62136: PPP1CA; NbExp=3; IntAct=EBI-458391, EBI-357253;
CC P04271; P17612: PRKACA; NbExp=3; IntAct=EBI-458391, EBI-476586;
CC P04271; P63000: RAC1; NbExp=3; IntAct=EBI-458391, EBI-413628;
CC P04271; Q15418: RPS6KA1; NbExp=2; IntAct=EBI-458391, EBI-963034;
CC P04271; P23297: S100A1; NbExp=25; IntAct=EBI-458391, EBI-743686;
CC P04271; Q5T7Y6: S100A1; NbExp=5; IntAct=EBI-458391, EBI-11746600;
CC P04271; P31949: S100A11; NbExp=5; IntAct=EBI-458391, EBI-701862;
CC P04271; P29034: S100A2; NbExp=9; IntAct=EBI-458391, EBI-752230;
CC P04271; P26447: S100A4; NbExp=8; IntAct=EBI-458391, EBI-717058;
CC P04271; P06703: S100A6; NbExp=6; IntAct=EBI-458391, EBI-352877;
CC P04271; P06702: S100A9; NbExp=3; IntAct=EBI-458391, EBI-1055001;
CC P04271; P04271: S100B; NbExp=23; IntAct=EBI-458391, EBI-458391;
CC P04271; P25815: S100P; NbExp=7; IntAct=EBI-458391, EBI-743700;
CC P04271; Q8WXG8: S100Z; NbExp=3; IntAct=EBI-458391, EBI-12198403;
CC P04271; O00560: SDCBP; NbExp=3; IntAct=EBI-458391, EBI-727004;
CC P04271; Q92599-3: SEPTIN8; NbExp=3; IntAct=EBI-458391, EBI-25891137;
CC P04271; Q9NZD8: SPG21; NbExp=7; IntAct=EBI-458391, EBI-742688;
CC P04271; P04637: TP53; NbExp=3; IntAct=EBI-458391, EBI-366083;
CC P04271; Q9Y4K3: TRAF6; NbExp=3; IntAct=EBI-458391, EBI-359276;
CC P04271; P13051-2: UNG; NbExp=3; IntAct=EBI-458391, EBI-25834258;
CC P04271; A0A024RC47: ZNF24; NbExp=3; IntAct=EBI-458391, EBI-25830832;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9925766}. Nucleus
CC {ECO:0000269|PubMed:9925766}.
CC -!- TISSUE SPECIFICITY: Although predominant among the water-soluble brain
CC proteins, S100 is also found in a variety of other tissues.
CC -!- MISCELLANEOUS: In addition to metal-ion binding, this protein is
CC involved with the regulation of protein phosphorylation in brain
CC tissue.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/S100BID42195ch21q22.html";
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DR EMBL; M59488; AAA60367.1; -; Genomic_DNA.
DR EMBL; M59487; AAA60367.1; JOINED; Genomic_DNA.
DR EMBL; CR542123; CAG46920.1; -; mRNA.
DR EMBL; AP000339; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX09267.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09268.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09269.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09270.1; -; Genomic_DNA.
DR EMBL; BC001766; AAH01766.1; -; mRNA.
DR CCDS; CCDS13736.1; -.
DR PIR; A38364; BCHUIB.
DR RefSeq; NP_006263.1; NM_006272.2.
DR RefSeq; XP_016883913.1; XM_017028424.1.
DR PDB; 1MQ1; NMR; -; A/B=2-92.
DR PDB; 1UWO; NMR; -; A/B=2-92.
DR PDB; 2H61; X-ray; 1.90 A; A/B/C/D/E/F/G/H=1-92.
DR PDB; 2M49; NMR; -; B/D=2-92.
DR PDB; 2PRU; NMR; -; A/B=2-92.
DR PDB; 3CZT; X-ray; 1.40 A; X=1-92.
DR PDB; 3D0Y; X-ray; 1.50 A; A/B=1-92.
DR PDB; 3D10; X-ray; 1.65 A; A/B=1-92.
DR PDB; 3HCM; X-ray; 2.00 A; A/B=1-92.
DR PDB; 4XYN; X-ray; 2.55 A; A/B/C/D=1-92.
DR PDB; 5CSF; X-ray; 2.40 A; A/B=1-92.
DR PDB; 5CSI; X-ray; 2.13 A; A/B=1-92.
DR PDB; 5CSJ; X-ray; 2.70 A; A/B=1-92.
DR PDB; 5CSN; X-ray; 2.95 A; A/B=1-92.
DR PDB; 5D7F; X-ray; 1.30 A; A/B=1-92.
DR PDBsum; 1MQ1; -.
DR PDBsum; 1UWO; -.
DR PDBsum; 2H61; -.
DR PDBsum; 2M49; -.
DR PDBsum; 2PRU; -.
DR PDBsum; 3CZT; -.
DR PDBsum; 3D0Y; -.
DR PDBsum; 3D10; -.
DR PDBsum; 3HCM; -.
DR PDBsum; 4XYN; -.
DR PDBsum; 5CSF; -.
DR PDBsum; 5CSI; -.
DR PDBsum; 5CSJ; -.
DR PDBsum; 5CSN; -.
DR PDBsum; 5D7F; -.
DR AlphaFoldDB; P04271; -.
DR BMRB; P04271; -.
DR SMR; P04271; -.
DR BioGRID; 112193; 178.
DR IntAct; P04271; 54.
DR MINT; P04271; -.
DR STRING; 9606.ENSP00000291700; -.
DR BindingDB; P04271; -.
DR ChEMBL; CHEMBL4300; -.
DR DrugBank; DB06941; (Z)-2-[2-(4-methylpiperazin-1-yl)benzyl]diazenecarbothioamide.
DR DrugBank; DB07004; 2-[(5-hex-1-yn-1-ylfuran-2-yl)carbonyl]-N-methylhydrazinecarbothioamide.
DR DrugBank; DB05343; Arundic acid.
DR DrugBank; DB01373; Calcium.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR DrugBank; DB04464; N-Formylmethionine.
DR DrugBank; DB00768; Olopatadine.
DR DrugCentral; P04271; -.
DR TCDB; 8.A.81.1.4; the s100 calcium-binding protein (s100) family.
DR iPTMnet; P04271; -.
DR PhosphoSitePlus; P04271; -.
DR BioMuta; S100B; -.
DR DMDM; 134138; -.
DR CPTAC; CPTAC-1454; -.
DR CPTAC; CPTAC-1455; -.
DR EPD; P04271; -.
DR jPOST; P04271; -.
DR MassIVE; P04271; -.
DR PaxDb; P04271; -.
DR PeptideAtlas; P04271; -.
DR PRIDE; P04271; -.
DR ProteomicsDB; 51695; -.
DR TopDownProteomics; P04271; -.
DR ABCD; P04271; 1 sequenced antibody.
DR Antibodypedia; 3474; 1771 antibodies from 45 providers.
DR DNASU; 6285; -.
DR Ensembl; ENST00000291700.9; ENSP00000291700.4; ENSG00000160307.10.
DR Ensembl; ENST00000397648.1; ENSP00000380769.1; ENSG00000160307.10.
DR GeneID; 6285; -.
DR KEGG; hsa:6285; -.
DR MANE-Select; ENST00000291700.9; ENSP00000291700.4; NM_006272.3; NP_006263.1.
DR UCSC; uc002zju.2; human.
DR CTD; 6285; -.
DR DisGeNET; 6285; -.
DR GeneCards; S100B; -.
DR HGNC; HGNC:10500; S100B.
DR HPA; ENSG00000160307; Group enriched (brain, choroid plexus).
DR MIM; 176990; gene.
DR neXtProt; NX_P04271; -.
DR OpenTargets; ENSG00000160307; -.
DR PharmGKB; PA34912; -.
DR VEuPathDB; HostDB:ENSG00000160307; -.
DR eggNOG; ENOG502S4HJ; Eukaryota.
DR GeneTree; ENSGT00940000161997; -.
DR HOGENOM; CLU_138624_2_0_1; -.
DR InParanoid; P04271; -.
DR OMA; VTMVTIC; -.
DR OrthoDB; 1574989at2759; -.
DR PhylomeDB; P04271; -.
DR TreeFam; TF332727; -.
DR PathwayCommons; P04271; -.
DR Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-HSA-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-HSA-879415; Advanced glycosylation endproduct receptor signaling.
DR Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
DR SignaLink; P04271; -.
DR SIGNOR; P04271; -.
DR BioGRID-ORCS; 6285; 12 hits in 1077 CRISPR screens.
DR ChiTaRS; S100B; human.
DR EvolutionaryTrace; P04271; -.
DR GeneWiki; S100B; -.
DR GenomeRNAi; 6285; -.
DR Pharos; P04271; Tchem.
DR PRO; PR:P04271; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P04271; protein.
DR Bgee; ENSG00000160307; Expressed in C1 segment of cervical spinal cord and 159 other tissues.
DR ExpressionAtlas; P04271; baseline and differential.
DR Genevisible; P04271; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0048306; F:calcium-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0050786; F:RAGE receptor binding; IPI:UniProtKB.
DR GO; GO:0044548; F:S100 protein binding; IPI:UniProtKB.
DR GO; GO:0048156; F:tau protein binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; TAS:ProtInc.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:0007611; P:learning or memory; ISS:UniProtKB.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IEA:Ensembl.
DR CDD; cd05027; S-100B; 1.
DR DisProt; DP01738; -.
DR IDEAL; IID00410; -.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028481; S100-B.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF01023; S_100; 1.
DR SMART; SM00054; EFh; 1.
DR SMART; SM01394; S_100; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00303; S100_CABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Cytoplasm; Direct protein sequencing;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02638,
FT ECO:0000269|PubMed:4031854"
FT CHAIN 2..92
FT /note="Protein S100-B"
FT /id="PRO_0000143966"
FT DOMAIN 13..48
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 49..84
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000305"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000305"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="Blocked amino end (Ser); alternate"
FT /evidence="ECO:0000269|PubMed:4031854"
FT MOD_RES 2
FT /note="N-acetylserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02638"
FT HELIX 3..19
FT /evidence="ECO:0007829|PDB:5D7F"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:5D7F"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:5D7F"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:5D7F"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2PRU"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:5D7F"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:5D7F"
FT HELIX 71..85
FT /evidence="ECO:0007829|PDB:5D7F"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:5D7F"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:2PRU"
SQ SEQUENCE 92 AA; 10713 MW; 43815AC212A3AD6B CRC64;
MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET
LDNDGDGECD FQEFMAFVAM VTTACHEFFE HE
