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Protein

Protein S100-B

Gene

S100B

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi19 – 32141; low affinityAdd
BLAST
Calcium bindingi62 – 73122; high affinityAdd
BLAST

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • kinase inhibitor activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • S100 protein binding Source: UniProtKB
  • tau protein binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • astrocyte activation Source: UniProtKB
  • axonogenesis Source: UniProtKB
  • learning or memory Source: UniProtKB
  • memory Source: Ensembl
  • negative regulation of monocyte chemotactic protein-1 production Source: GO_Central
  • negative regulation of phosphorylation Source: GOC
  • phosphorylation Source: UniProtKB
  • positive regulation of complement activation Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  • regulation of neuronal synaptic plasticity Source: Ensembl
  • regulation of translation Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-BTA-1251985. Nuclear signaling by ERBB4.
R-BTA-1810476. RIP-mediated NFkB activation via ZBP1.
R-BTA-3134963. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
R-BTA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-BTA-879415. Advanced glycosylation endproduct receptor signaling.
R-BTA-933542. TRAF6 mediated NF-kB activation.
SABIO-RKP02638.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein S100-B
Alternative name(s):
S-100 protein beta chain
S-100 protein subunit beta
S100 calcium-binding protein B
Gene namesi
Name:S100B
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • neuronal cell body Source: Ensembl
  • nucleus Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: Ensembl
  • ruffle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 9291Protein S100-BPRO_0000143965Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP02638.

PTM databases

iPTMnetiP02638.

Expressioni

Tissue specificityi

Although predominant among the water-soluble brain proteins, S100 is also found in a variety of other tissues.

Interactioni

Subunit structurei

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 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CacybpQ9CXW34EBI-458452,EBI-767146From a different organism.
KCNH1O952593EBI-458452,EBI-2909270From a different organism.
STK38Q152083EBI-458452,EBI-458376From a different organism.

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • S100 protein binding Source: UniProtKB
  • tau protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi182329. 3 interactions.
IntActiP02638. 3 interactions.
MINTiMINT-1210691.
STRINGi9913.ENSBTAP00000006275.

Structurei

Secondary structure

1
92
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1917Combined sources
Beta strandi21 – 244Combined sources
Beta strandi25 – 295Combined sources
Helixi30 – 4011Combined sources
Turni42 – 443Combined sources
Helixi48 – 503Combined sources
Helixi51 – 6111Combined sources
Beta strandi66 – 694Combined sources
Helixi71 – 8818Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CFPNMR-A/B1-92[»]
1MHOX-ray2.00A2-89[»]
1PSBNMR-A/B2-92[»]
3CR2X-ray1.88A1-92[»]
3CR4X-ray2.15X1-92[»]
3CR5X-ray1.85X1-92[»]
3GK1X-ray2.10A1-92[»]
3GK2X-ray1.98A1-92[»]
3GK4X-ray1.90X1-92[»]
3IQOX-ray1.50A/B1-92[»]
3IQQX-ray2.01A1-92[»]
3LK0X-ray2.04A/B/C/D1-90[»]
3LK1X-ray1.79A1-90[»]
3LLEX-ray1.85A/B1-92[»]
3RLZX-ray2.01A/B1-92[»]
3RM1X-ray1.24A1-92[»]
4FQOX-ray1.65A1-89[»]
4PDZX-ray1.73A/B1-92[»]
4PE0X-ray1.08A/X1-92[»]
4PE1X-ray1.58A/B1-92[»]
4PE4X-ray2.18A/X1-92[»]
4PE7X-ray1.65A1-92[»]
5DKNX-ray1.53A1-92[»]
5DKQX-ray1.59A1-92[»]
5DKRX-ray1.74A/B1-92[»]
ProteinModelPortaliP02638.
SMRiP02638. Positions 1-92.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02638.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 4836EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini49 – 8436EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the S-100 family.Curated
Contains 2 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IYFX. Eukaryota.
ENOG41127J0. LUCA.
GeneTreeiENSGT00760000119034.
HOGENOMiHOG000246968.
HOVERGENiHBG001479.
InParanoidiP02638.
OMAiGDAECDF.
OrthoDBiEOG7R833W.
TreeFamiTF332727.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR028481. S100-B.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]
PANTHERiPTHR11639:SF17. PTHR11639:SF17. 1 hit.
PfamiPF00036. EF-hand_1. 1 hit.
PF01023. S_100. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 1 hit.
SM01394. S_100. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02638-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSELEKAVVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE
60 70 80 90
QEVVDKVMET LDSDGDGECD FQEFMAFVAM ITTACHEFFE HE
Length:92
Mass (Da):10,668
Last modified:January 23, 2007 - v2
Checksum:i589BF1DAA0AF6DA7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ195377 mRNA. Translation: ABA39829.1.
BC103041 mRNA. Translation: AAI03042.1.
BC134727 mRNA. Translation: AAI34728.1.
PIRiA91254. BCBOIB.
RefSeqiNP_001029727.1. NM_001034555.3.
UniGeneiBt.49610.

Genome annotation databases

EnsembliENSBTAT00000006275; ENSBTAP00000006275; ENSBTAG00000004777.
GeneIDi525716.
KEGGibta:525716.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ195377 mRNA. Translation: ABA39829.1.
BC103041 mRNA. Translation: AAI03042.1.
BC134727 mRNA. Translation: AAI34728.1.
PIRiA91254. BCBOIB.
RefSeqiNP_001029727.1. NM_001034555.3.
UniGeneiBt.49610.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CFPNMR-A/B1-92[»]
1MHOX-ray2.00A2-89[»]
1PSBNMR-A/B2-92[»]
3CR2X-ray1.88A1-92[»]
3CR4X-ray2.15X1-92[»]
3CR5X-ray1.85X1-92[»]
3GK1X-ray2.10A1-92[»]
3GK2X-ray1.98A1-92[»]
3GK4X-ray1.90X1-92[»]
3IQOX-ray1.50A/B1-92[»]
3IQQX-ray2.01A1-92[»]
3LK0X-ray2.04A/B/C/D1-90[»]
3LK1X-ray1.79A1-90[»]
3LLEX-ray1.85A/B1-92[»]
3RLZX-ray2.01A/B1-92[»]
3RM1X-ray1.24A1-92[»]
4FQOX-ray1.65A1-89[»]
4PDZX-ray1.73A/B1-92[»]
4PE0X-ray1.08A/X1-92[»]
4PE1X-ray1.58A/B1-92[»]
4PE4X-ray2.18A/X1-92[»]
4PE7X-ray1.65A1-92[»]
5DKNX-ray1.53A1-92[»]
5DKQX-ray1.59A1-92[»]
5DKRX-ray1.74A/B1-92[»]
ProteinModelPortaliP02638.
SMRiP02638. Positions 1-92.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi182329. 3 interactions.
IntActiP02638. 3 interactions.
MINTiMINT-1210691.
STRINGi9913.ENSBTAP00000006275.

PTM databases

iPTMnetiP02638.

Proteomic databases

PaxDbiP02638.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000006275; ENSBTAP00000006275; ENSBTAG00000004777.
GeneIDi525716.
KEGGibta:525716.

Organism-specific databases

CTDi6285.

Phylogenomic databases

eggNOGiENOG410IYFX. Eukaryota.
ENOG41127J0. LUCA.
GeneTreeiENSGT00760000119034.
HOGENOMiHOG000246968.
HOVERGENiHBG001479.
InParanoidiP02638.
OMAiGDAECDF.
OrthoDBiEOG7R833W.
TreeFamiTF332727.

Enzyme and pathway databases

ReactomeiR-BTA-1251985. Nuclear signaling by ERBB4.
R-BTA-1810476. RIP-mediated NFkB activation via ZBP1.
R-BTA-3134963. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
R-BTA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-BTA-879415. Advanced glycosylation endproduct receptor signaling.
R-BTA-933542. TRAF6 mediated NF-kB activation.
SABIO-RKP02638.

Miscellaneous databases

EvolutionaryTraceiP02638.
PROiP02638.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR028481. S100-B.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]
PANTHERiPTHR11639:SF17. PTHR11639:SF17. 1 hit.
PfamiPF00036. EF-hand_1. 1 hit.
PF01023. S_100. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 1 hit.
SM01394. S_100. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, molecular and biochemical characterization of S100B from bovine retina."
    Burczynska B.B., Duda T., Venkataraman V., Sharma R.K.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal pons and Hypothalamus.
  3. "The amino-acid sequence of S-100 protein (PAP I-b protein) and its relation to the calcium-binding proteins."
    Isobe T., Okuyama T.
    Eur. J. Biochem. 89:379-388(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-92.
  4. "The amino-acid sequence of the alpha subunit in bovine brain S-100a protein."
    Isobe T., Okuyama T.
    Eur. J. Biochem. 116:79-86(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 1-5.
  5. "Structural characterization of the calcium binding protein s100 from adipose tissue."
    Marshak D.R., Umekawa H., Watterson D.M., Hidaka H.
    Arch. Biochem. Biophys. 240:777-780(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-92.
  6. "Ions binding to S100 proteins: structural changes induced by calcium and zinc on S100a and S100b proteins."
    Baudier J., Gerard D.
    Biochemistry 22:3360-3369(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: METAL ION-BINDING PROPERTIES.
  7. "Spectral studies on the cadmium-ion-binding properties of bovine brain S-100b protein."
    Donato H. Jr., Mani R.S., Kay C.M.
    Biochem. J. 276:13-18(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: CADMIUM-BINDING STUDIES.
  8. "The solution structure of the bovine S100B protein dimer in the calcium-free state."
    Kilby P.M., van Eldik L.J., Roberts G.C.K.
    Structure 4:1041-1052(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  9. "Structure of the Ca2+/S100B/NDR kinase peptide complex: insights into S100 target specificity and activation of the kinase."
    Bhattacharya S., Large E., Heizmann C.W., Hemmings B.A., Chazin W.J.
    Biochemistry 42:14416-14426(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, FUNCTION, INTERACTION WITH STK38.

Entry informationi

Entry nameiS100B_BOVIN
AccessioniPrimary (citable) accession number: P02638
Secondary accession number(s): A4IFR6, Q3ZBY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.