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Protein

Protein S100-B

Gene

S100B

Organism
Homo sapiens (Human)
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.2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi19 – 321; low affinityAdd BLAST14
Calcium bindingi62 – 732; high affinityAdd BLAST12

GO - Molecular functioni

  • calcium-dependent protein binding Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: UniProtKB
  • RAGE receptor binding Source: UniProtKB
  • S100 protein binding Source: UniProtKB
  • tau protein binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000160307-MONOMER.
ReactomeiR-HSA-1251985. Nuclear signaling by ERBB4.
R-HSA-1810476. RIP-mediated NFkB activation via ZBP1.
R-HSA-3134963. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
R-HSA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-HSA-879415. Advanced glycosylation endproduct receptor signaling.
R-HSA-933542. TRAF6 mediated NF-kB activation.

Protein family/group databases

TCDBi8.A.81.1.4. the s100 calcium-binding protein (s100) family.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 21

Organism-specific databases

HGNCiHGNC:10500. S100B.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: Ensembl
  • intracellular membrane-bounded organelle Source: HPA
  • neuronal cell body Source: Ensembl
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi6285.
OpenTargetsiENSG00000160307.
PharmGKBiPA34912.

Chemistry databases

ChEMBLiCHEMBL4300.
DrugBankiDB00768. Olopatadine.

Polymorphism and mutation databases

BioMutaiS100B.
DMDMi134138.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity1 Publication
ChainiPRO_00001439662 – 92Protein S100-BAdd BLAST91

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2Blocked amino end (Ser); alternate1 Publication1
Modified residuei2N-acetylserine; alternateBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP04271.
PaxDbiP04271.
PeptideAtlasiP04271.
PRIDEiP04271.
TopDownProteomicsiP04271.

PTM databases

PhosphoSitePlusiP04271.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000160307.
CleanExiHS_S100B.
ExpressionAtlasiP04271. baseline and differential.
GenevisibleiP04271. HS.

Organism-specific databases

HPAiCAB000073.
HPA015768.

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.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself18EBI-458391,EBI-458391
AGERQ151095EBI-458391,EBI-1646426
MDM2Q009872EBI-458391,EBI-389668
S100A1P2329713EBI-458391,EBI-743686
S100A1Q5T7Y69EBI-458391,EBI-11746600
S100A11P319495EBI-458391,EBI-701862
S100A2P290347EBI-458391,EBI-752230
S100A4P264477EBI-458391,EBI-717058
S100A6P067035EBI-458391,EBI-352877
S100PP258156EBI-458391,EBI-743700
SPG21Q9NZD85EBI-458391,EBI-742688
TP53P046372EBI-458391,EBI-366083

GO - Molecular functioni

  • calcium-dependent protein binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: UniProtKB
  • RAGE receptor binding Source: UniProtKB
  • S100 protein binding Source: UniProtKB
  • tau protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112193. 30 interactors.
IntActiP04271. 20 interactors.
MINTiMINT-192546.
STRINGi9606.ENSP00000291700.

Chemistry databases

BindingDBiP04271.

Structurei

Secondary structure

192
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 19Combined sources17
Beta strandi21 – 24Combined sources4
Helixi30 – 40Combined sources11
Turni42 – 44Combined sources3
Beta strandi47 – 49Combined sources3
Helixi51 – 61Combined sources11
Beta strandi65 – 69Combined sources5
Helixi71 – 85Combined sources15
Helixi86 – 88Combined sources3
Turni89 – 91Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MQ1NMR-A/B2-92[»]
1UWONMR-A/B2-92[»]
2H61X-ray1.90A/B/C/D/E/F/G/H1-92[»]
2M49NMR-B/D2-92[»]
2PRUNMR-A/B2-92[»]
3CZTX-ray1.40X1-92[»]
3D0YX-ray1.50A/B1-92[»]
3D10X-ray1.65A/B1-92[»]
3HCMX-ray2.00A/B1-92[»]
4XYNX-ray2.55A/B/C/D1-92[»]
5CSFX-ray2.40A/B1-92[»]
5CSIX-ray2.13A/B1-92[»]
5CSJX-ray2.70A/B1-92[»]
5CSNX-ray2.95A/B1-92[»]
5D7FX-ray1.30A/B1-92[»]
ProteinModelPortaliP04271.
SMRiP04271.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04271.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 48EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini49 – 84EF-hand 2PROSITE-ProRule annotationAdd BLAST36

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.
HOVERGENiHBG001479.
InParanoidiP04271.
OMAiCCHEFFE.
PhylomeDBiP04271.
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.

P04271-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE
60 70 80 90
QEVVDKVMET LDNDGDGECD FQEFMAFVAM VTTACHEFFE HE
Length:92
Mass (Da):10,713
Last modified:January 23, 2007 - v2
Checksum:i43815AC212A3AD6B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59488, M59487 Genomic DNA. Translation: AAA60367.1.
CR542123 mRNA. Translation: CAG46920.1.
AP000339 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09267.1.
CH471079 Genomic DNA. Translation: EAX09268.1.
CH471079 Genomic DNA. Translation: EAX09269.1.
CH471079 Genomic DNA. Translation: EAX09270.1.
BC001766 mRNA. Translation: AAH01766.1.
CCDSiCCDS13736.1.
PIRiA38364. BCHUIB.
RefSeqiNP_006263.1. NM_006272.2.
XP_016883913.1. XM_017028424.1.
UniGeneiHs.422181.

Genome annotation databases

EnsembliENST00000291700; ENSP00000291700; ENSG00000160307.
ENST00000397648; ENSP00000380769; ENSG00000160307.
GeneIDi6285.
KEGGihsa:6285.
UCSCiuc002zju.2. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59488, M59487 Genomic DNA. Translation: AAA60367.1.
CR542123 mRNA. Translation: CAG46920.1.
AP000339 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09267.1.
CH471079 Genomic DNA. Translation: EAX09268.1.
CH471079 Genomic DNA. Translation: EAX09269.1.
CH471079 Genomic DNA. Translation: EAX09270.1.
BC001766 mRNA. Translation: AAH01766.1.
CCDSiCCDS13736.1.
PIRiA38364. BCHUIB.
RefSeqiNP_006263.1. NM_006272.2.
XP_016883913.1. XM_017028424.1.
UniGeneiHs.422181.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MQ1NMR-A/B2-92[»]
1UWONMR-A/B2-92[»]
2H61X-ray1.90A/B/C/D/E/F/G/H1-92[»]
2M49NMR-B/D2-92[»]
2PRUNMR-A/B2-92[»]
3CZTX-ray1.40X1-92[»]
3D0YX-ray1.50A/B1-92[»]
3D10X-ray1.65A/B1-92[»]
3HCMX-ray2.00A/B1-92[»]
4XYNX-ray2.55A/B/C/D1-92[»]
5CSFX-ray2.40A/B1-92[»]
5CSIX-ray2.13A/B1-92[»]
5CSJX-ray2.70A/B1-92[»]
5CSNX-ray2.95A/B1-92[»]
5D7FX-ray1.30A/B1-92[»]
ProteinModelPortaliP04271.
SMRiP04271.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112193. 30 interactors.
IntActiP04271. 20 interactors.
MINTiMINT-192546.
STRINGi9606.ENSP00000291700.

Chemistry databases

BindingDBiP04271.
ChEMBLiCHEMBL4300.
DrugBankiDB00768. Olopatadine.

Protein family/group databases

TCDBi8.A.81.1.4. the s100 calcium-binding protein (s100) family.

PTM databases

PhosphoSitePlusiP04271.

Polymorphism and mutation databases

BioMutaiS100B.
DMDMi134138.

Proteomic databases

EPDiP04271.
PaxDbiP04271.
PeptideAtlasiP04271.
PRIDEiP04271.
TopDownProteomicsiP04271.

Protocols and materials databases

DNASUi6285.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000291700; ENSP00000291700; ENSG00000160307.
ENST00000397648; ENSP00000380769; ENSG00000160307.
GeneIDi6285.
KEGGihsa:6285.
UCSCiuc002zju.2. human.

Organism-specific databases

CTDi6285.
DisGeNETi6285.
GeneCardsiS100B.
HGNCiHGNC:10500. S100B.
HPAiCAB000073.
HPA015768.
MIMi176990. gene.
neXtProtiNX_P04271.
OpenTargetsiENSG00000160307.
PharmGKBiPA34912.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IYFX. Eukaryota.
ENOG41127J0. LUCA.
GeneTreeiENSGT00760000119034.
HOVERGENiHBG001479.
InParanoidiP04271.
OMAiCCHEFFE.
PhylomeDBiP04271.
TreeFamiTF332727.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000160307-MONOMER.
ReactomeiR-HSA-1251985. Nuclear signaling by ERBB4.
R-HSA-1810476. RIP-mediated NFkB activation via ZBP1.
R-HSA-3134963. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
R-HSA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-HSA-879415. Advanced glycosylation endproduct receptor signaling.
R-HSA-933542. TRAF6 mediated NF-kB activation.

Miscellaneous databases

ChiTaRSiS100B. human.
EvolutionaryTraceiP04271.
GeneWikiiS100B.
GenomeRNAii6285.
PROiP04271.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000160307.
CleanExiHS_S100B.
ExpressionAtlasiP04271. baseline and differential.
GenevisibleiP04271. HS.

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...

Entry informationi

Entry nameiS100B_HUMAN
AccessioniPrimary (citable) accession number: P04271
Secondary accession number(s): D3DSN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 180 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

In addition to metal-ion binding, this protein is involved with the regulation of protein phosphorylation in brain tissue.

Keywords - Technical termi

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

Documents

  1. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.