UniProt Accession

 S100B_RAT; P04631 

Genbank Protein ID

 X01090; M54919; S53527; S53522; BC087026; M15705 

Genbank Nucleotide ID

 CAA25567.1; AAA42096.1; AAH87026.1 

Protein Name

 Protein S100-B 

Protein Synonyms/Alias

 S-100 protein beta chain; S-100 protein subunit beta; S100 calcium-binding protein B 

Gene Name

 S100b 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Rattus norvegicus (Rat) 

NCBI Taxa ID

 10116 

Lysine Modification

Position	Peptide	Type	References
49	SHFLEEIKEQEVVDK	acetylation	[1]

Reference

 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 

Functional Description

 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. 

Sequence Annotation

 DOMAIN 13 48 EF-hand 1.
 DOMAIN 49 84 EF-hand 2.
 MOD_RES 2 2 N-acetylserine (By similarity).  

Keyword

 3D-structure; Acetylation; Calcium; Complete proteome; Cytoplasm; Direct protein sequencing; Metal-binding; Nucleus; Reference proteome; Repeat; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 92 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0005615; C:extracellular space; IDA:RGD.
 GO:0043025; C:neuronal cell body; IEA:Compara.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0001726; C:ruffle; IEA:Compara.
 GO:0005509; F:calcium ion binding; IDA:RGD.
 GO:0042803; F:protein homodimerization activity; IDA:RGD.
 GO:0048156; F:tau protein binding; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; ISS:UniProtKB.
 GO:0048708; P:astrocyte differentiation; IEP:RGD.
 GO:0071456; P:cellular response to hypoxia; IEP:RGD.
 GO:0007611; P:learning or memory; ISS:UniProtKB.
 GO:0060291; P:long-term synaptic potentiation; IEP:RGD.
 GO:0007613; P:memory; IEA:Compara.
 GO:2001015; P:negative regulation of skeletal muscle cell differentiation; IMP:RGD.
 GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
 GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IEA:Compara.
 GO:0008360; P:regulation of cell shape; IMP:RGD.
 GO:0048168; P:regulation of neuronal synaptic plasticity; IEA:Compara.
 GO:0051384; P:response to glucocorticoid stimulus; IEP:RGD.
 GO:0051597; P:response to methylmercury; IEP:RGD. 

Interpro

 IPR011992; EF-hand-like_dom.
 IPR018247; EF_Hand_1_Ca_BS.
 IPR002048; EF_hand_dom.
 IPR001751; S100/CaBP-9k_CS.
 IPR013787; S100_Ca-bd_sub. 

Pfam

 PF01023; S_100 

SMART

  

PROSITE

 PS00018; EF_HAND_1
 PS50222; EF_HAND_2
 PS00303; S100_CABP 

PRINTS