(data stored in ACNUC27670 zone)


ID   BOVIN1_153_PE7                       STANDARD;      PRT;   92 AA.
AC   BOVIN1_153_PE7; P02638; A4IFR6; Q3ZBY1;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Protein S100-B;AltName: Full=S-100 protein beta
DE   chain;AltName: Full=S-100 protein subunit beta;AltName: Full=S100
DE   calcium-binding protein B; (BOVIN1_153.PE7).
GN   Name=S100B;
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BOVIN1_153.PE7.
CC       Bos taurus chromosome 1 Btau_4.0 partial sequence 148948934..149948933
CC       annotated by Ensembl
CC   -!- FUNCTION: Weakly binds calcium but binds zinc very tightly-
CC       distinct binding sites with different affinities exist for both
CC       ions on each monomer. Physiological concentrations of potassium
CC       ion antagonize the binding of both divalent cations, especially
CC       affecting high-affinity calcium-binding sites. Binds to and
CC       initiates the activation of STK38 by releasing autoinhibitory
CC       intramolecular interactions within the kinase. Interaction with
CC       AGER after myocardial infarction may play a role in myocyte
CC       apoptosis by activating ERK1/2 and p53/TP53 signaling (By
CC       similarity).
CC   -!- SUBUNIT: Dimer of either two alpha chains, or two beta chains, or
CC       one alpha and one beta chain. The S100B dimer interacts with two
CC       molecules of CAPZA1. Interacts with AGER (By similarity). The
CC       S100B dimer interacts with two molecules of STK38.
CC       Q15208:STK38 (xeno); NbExp=3; IntAct=EBI-458452, EBI-458376;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- TISSUE SPECIFICITY: Although predominant among the water-soluble
CC       brain proteins, S100 is also found in a variety of other tissues.
CC   -!- SIMILARITY: Belongs to the S-101 family.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -!- GENE_FAMILY: HOG000246968 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Bos_taurus;ENSBTAG00000004777;ENSBTAT00000006275;ENSBTAP00000006275.
DR   EMBL; BC103041; - ;
DR   EMBL; BC134727; - ;
DR   EMBL; DQ195377; - ;
DR   UniProtKB/Swiss-Prot; P02638; A4IFR6; Q3ZBY1; -.
DR   EMBL; DQ195377; ABA39829.1; -; mRNA.
DR   EMBL; BC103041; AAI03042.1; -; mRNA.
DR   EMBL; BC134727; AAI34728.1; -; mRNA.
DR   IPI; IPI00712739; -.
DR   PIR; A91254; BCBOIB.
DR   RefSeq; NP_001029727.1; NM_001034555.2.
DR   UniGene; Bt.49610; -.
DR   PDB; 1CFP; NMR; -; A/B=1-92.
DR   PDB; 1MHO; X-ray; 2.00 A; A=2-88.
DR   PDB; 1PSB; NMR; -; A/B=2-92.
DR   PDB; 3CR2; X-ray; 1.88 A; A=1-92.
DR   PDB; 3CR4; X-ray; 2.15 A; X=1-92.
DR   PDB; 3CR5; X-ray; 1.85 A; X=1-92.
DR   PDB; 3GK1; X-ray; 2.10 A; A=1-92.
DR   PDB; 3GK2; X-ray; 1.98 A; A=1-92.
DR   PDB; 3GK4; X-ray; 1.90 A; X=1-92.
DR   PDB; 3IQO; X-ray; 1.50 A; A/B=1-92.
DR   PDB; 3IQQ; X-ray; 2.01 A; A=1-92.
DR   PDB; 3LK0; X-ray; 2.04 A; A/B/C/D=1-90.
DR   PDB; 3LK1; X-ray; 1.79 A; A=1-90.
DR   PDB; 3LLE; X-ray; 1.85 A; A/B=1-92.
DR   PDBsum; 1CFP; -.
DR   PDBsum; 1MHO; -.
DR   PDBsum; 1PSB; -.
DR   PDBsum; 3CR2; -.
DR   PDBsum; 3CR4; -.
DR   PDBsum; 3CR5; -.
DR   PDBsum; 3GK1; -.
DR   PDBsum; 3GK2; -.
DR   PDBsum; 3GK4; -.
DR   PDBsum; 3IQO; -.
DR   PDBsum; 3IQQ; -.
DR   PDBsum; 3LK0; -.
DR   PDBsum; 3LK1; -.
DR   PDBsum; 3LLE; -.
DR   ProteinModelPortal; P02638; -.
DR   SMR; P02638; 1-92.
DR   IntAct; P02638; 1.
DR   MINT; MINT-1210691; -.
DR   STRING; P02638; -.
DR   Ensembl; ENSBTAT00000006275; ENSBTAP00000006275; ENSBTAG00000004777.
DR   GeneID; 525716; -.
DR   KEGG; bta:525716; -.
DR   CTD; 6285; -.
DR   eggNOG; maNOG21158; -.
DR   GeneTree; ENSGT00600000084162; -.
DR   InParanoid; P02638; -.
DR   OrthoDB; EOG4BZN47; -.
DR   PhylomeDB; P02638; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0019210; F:kinase inhibitor activity; NAS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0048154; F:S100 beta binding; ISS:UniProtKB.
DR   GO; GO:0048156; F:tau protein binding; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0048143; P:astrocyte activation; NAS:UniProtKB.
DR   GO; GO:0007409; P:axonogenesis; NAS:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; NAS:UniProtKB.
DR   GO; GO:0045917; P:positive regulation of complement activation; NAS:UniProtKB.
DR   GO; GO:0006417; P:regulation of translation; NAS:UniProtKB.
DR   InterPro; IPR018248; EF-hand.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR001751; S100/CaBP-9k_CS.
DR   InterPro; IPR013787; S100_Ca-bd_sub.
DR   Gene3D; G3DSA:; EF-Hand_type; 1.
DR   Pfam; PF00036; efhand; 1.
DR   Pfam; PF01023; S_100; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS00303; S100_CABP; 1.
KW   ENSBTAG00000004777fold_1320000031; ENSBTAP00000006275fold_1320000031;
KW   BC103041; BC134727; DQ195377;
KW   3D-structure; Acetylation; Calcium; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Metal-binding; Nucleus; Reference proteome;
KW   Repeat; Zinc.

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