S100B_MOUSE
ID S100B_MOUSE Reviewed; 92 AA.
AC P50114;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BALB/cJ;
RX PubMed=8376406; DOI=10.1016/s0021-9258(20)80754-6;
RA Jiang H., Shah S., Hilt D.C.;
RT "Organization, sequence, and expression of the murine S100 beta gene.
RT Transcriptional regulation by cell type-specific cis-acting regulatory
RT elements.";
RL J. Biol. Chem. 268:20502-20511(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Although predominant among the water-soluble brain
CC proteins, S100 is also found in a variety of other tissues.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; L22144; AAA03075.1; -; Unassigned_DNA.
DR EMBL; BC061178; AAH61178.1; -; mRNA.
DR CCDS; CCDS35943.1; -.
DR PIR; A48015; A48015.
DR RefSeq; NP_033141.1; NM_009115.3.
DR AlphaFoldDB; P50114; -.
DR BMRB; P50114; -.
DR SMR; P50114; -.
DR BioGRID; 203058; 5.
DR IntAct; P50114; 1.
DR STRING; 10090.ENSMUSP00000047968; -.
DR PhosphoSitePlus; P50114; -.
DR PaxDb; P50114; -.
DR PeptideAtlas; P50114; -.
DR PRIDE; P50114; -.
DR ProteomicsDB; 255430; -.
DR ABCD; P50114; 1 sequenced antibody.
DR DNASU; 20203; -.
DR Ensembl; ENSMUST00000036387; ENSMUSP00000047968; ENSMUSG00000033208.
DR GeneID; 20203; -.
DR KEGG; mmu:20203; -.
DR UCSC; uc007fuc.2; mouse.
DR CTD; 6285; -.
DR MGI; MGI:98217; S100b.
DR VEuPathDB; HostDB:ENSMUSG00000033208; -.
DR eggNOG; ENOG502S4HJ; Eukaryota.
DR GeneTree; ENSGT00940000161997; -.
DR HOGENOM; CLU_138624_2_0_1; -.
DR InParanoid; P50114; -.
DR OMA; VTMVTIC; -.
DR OrthoDB; 1574989at2759; -.
DR PhylomeDB; P50114; -.
DR TreeFam; TF332727; -.
DR Reactome; R-MMU-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-MMU-879415; Advanced glycosylation endproduct receptor signaling.
DR Reactome; R-MMU-933542; TRAF6 mediated NF-kB activation.
DR BioGRID-ORCS; 20203; 5 hits in 76 CRISPR screens.
DR ChiTaRS; S100b; mouse.
DR PRO; PR:P50114; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P50114; protein.
DR Bgee; ENSMUSG00000033208; Expressed in vestibular membrane of cochlear duct and 158 other tissues.
DR ExpressionAtlas; P50114; baseline and differential.
DR Genevisible; P50114; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0050786; F:RAGE receptor binding; ISO:MGI.
DR GO; GO:0044548; F:S100 protein binding; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0048156; F:tau protein binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; NAS:UniProtKB.
DR GO; GO:0006112; P:energy reserve metabolic process; NAS:UniProtKB.
DR GO; GO:0007611; P:learning or memory; IMP:UniProtKB.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:2001015; P:negative regulation of skeletal muscle cell differentiation; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0031643; P:positive regulation of myelination; ISO:MGI.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
DR GO; GO:0001817; P:regulation of cytokine production; NAS:UniProtKB.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; NAS:UniProtKB.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:MGI.
DR CDD; cd05027; S-100B; 1.
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 Acetylation; Calcium; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02638"
FT CHAIN 2..92
FT /note="Protein S100-B"
FT /id="PRO_0000143967"
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="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P02638"
SQ SEQUENCE 92 AA; 10728 MW; 43815AC212A81DD0 CRC64;
MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET
LDEDGDGECD FQEFMAFVAM VTTACHEFFE HE
