Protein S100-B - Bos taurus (Bovine)

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Reviewed, UniProtKB/Swiss-Prot P02638 (S100B_BOVIN)

Last modified March 2, 2010. Version 98. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Protein S100-B

Alternative name(s):
S100 calcium-binding protein B
S-100 protein subunit beta
S-100 protein beta chain

Gene names

Name:

S100B

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length	92 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	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 By similarity. Ref.9
Subunit structure	Dimer of either two alpha chains, or two beta chains, or one alpha and one beta chain. The S100B dimer interacts with two molecules of CAPZA1. Interacts with AGER By similarity. The S100B dimer interacts with two molecules of STK38. Ref.9
Subcellular location	Cytoplasm. Nucleus.
Tissue specificity	Although predominant among the water-soluble brain proteins, S100 is also found in a variety of other tissues.
Sequence similarities	Belongs to the S-101 family. Contains 2 EF-hand domains.

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Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Domain	Repeat
Ligand	Calcium Metal-binding Zinc
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	astrocyte activation Non-traceable author statement. Source: UniProtKB axonogenesis Non-traceable author statement. Source: UniProtKB phosphorylation Non-traceable author statement. Source: UniProtKB positive regulation of complement activation Non-traceable author statement. Source: UniProtKB regulation of translation Non-traceable author statement. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	S100 beta binding Inferred from sequence or structural similarity. Source: UniProtKB calcium ion binding Inferred from direct assay. Source: UniProtKB kinase inhibitor activity Non-traceable author statement. Source: UniProtKB protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB tau protein binding Inferred from physical interaction. Source: UniProtKB zinc ion binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3 Ref.5

Chain

2 – 92

Protein S100-B

PRO_0000143965

Regions

Domain

13 – 48

EF-hand 1

Domain

49 – 84

EF-hand 2

Calcium binding

19 – 32

1; low affinity

Calcium binding

62 – 73

2; high affinity

Amino acid modifications

Modified residue

N-acetylserine Ref.5

Secondary structure

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P02638-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 589BF1DAA0AF6DA7
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FASTA

10,668

        10         20         30         40         50         60 
MSELEKAVVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET 

        70         80         90 
LDSDGDGECD FQEFMAFVAM ITTACHEFFE HE

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 710399] [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: 7250124] [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: 4026304] [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: 6615778] [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: 2039467] [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: 8805590] [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: 14661952] [Abstract] Cited for: STRUCTURE BY NMR, FUNCTION, INTERACTION WITH STK38.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

DQ195377 mRNA. Translation: ABA39829.1.
BC103041 mRNA. Translation: AAI03042.1.
BC134727 mRNA. Translation: AAI34728.1.

IPI

IPI00712739.

PIR

BCBOIB. A91254.

RefSeq

NP_001029727.1.

UniGene

Bt.49610

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CFP	NMR	-	A/B	1-92	[»]
1MHO	X-ray	2.00	A	2-88	[»]
1PSB	NMR	-	A/B	2-92	[»]
3CR2	X-ray	1.88	A	1-92	[»]
3CR4	X-ray	2.15	X	1-92	[»]
3CR5	X-ray	1.85	X	1-92	[»]
3GK1	X-ray	2.10	A	1-92	[»]
3GK2	X-ray	1.98	A	1-92	[»]
3GK4	X-ray	1.90	X	1-92	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P02638. 1 interaction.

STRING

P02638.

Genome annotation databases

Ensembl

ENSBTAT00000006275; ENSBTAP00000006275; ENSBTAG00000004777; Bos taurus. [Genome view]

GeneID

525716.

KEGG

bta:525716.

Organism-specific databases

CTD

525716.

Phylogenomic databases

eggNOG

maNOG21158.

HOVERGEN

HBG001479.

InParanoid

P02638.

OMA

GDAECDF.

OrthoDB

EOG94TRVH.

PhylomeDB

P02638.

Family and domain databases

InterPro

IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca_bd_sub.
[Graphical view]

Gene3D

G3DSA:1.10.238.10. EF-Hand_type. 1 hit.

Pfam

PF01023. S_100. 1 hit.
[Graphical view]

PROSITE

PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

S100B_BOVIN

Accession

Primary (citable) accession number: P02638
Secondary accession number(s): A4IFR6, Q3ZBY1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	March 2, 2010
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families