P04271 (S100B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein S100-B

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

Gene names

Name:

S100B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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

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. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. Ref.10
Subunit structure	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 By similarity. Interacts with CACYBP in a calcium-dependent manner By similarity. 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. Ref.8 Ref.9 Ref.10
Subcellular location	Cytoplasm. Nucleus Ref.8.
Tissue specificity	Although predominant among the water-soluble brain proteins, S100 is also found in a variety of other tissues.
Miscellaneous	In addition to metal-ion binding, this protein is involved with the regulation of protein phosphorylation in brain tissue.
Sequence similarities	Belongs to the S-101 family. Contains 2 EF-hand domains.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Domain	Repeat
Ligand	Calcium Metal-binding Zinc
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	astrocyte differentiation Inferred from electronic annotation. Source: Compara axonogenesis Traceable author statement PubMed 8202493. Source: ProtInc cell proliferation Traceable author statement PubMed 8202493. Source: ProtInc cellular response to hypoxia Inferred from electronic annotation. Source: Compara central nervous system development Traceable author statement PubMed 8202493. Source: ProtInc innate immune response Traceable author statement. Source: Reactome learning or memory Inferred from sequence or structural similarity. Source: UniProtKB long-term synaptic potentiation Inferred from electronic annotation. Source: Compara memory Inferred from electronic annotation. Source: Compara negative regulation of skeletal muscle cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from direct assay PubMed 15033494. Source: UniProtKB positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara regulation of cell shape Inferred from electronic annotation. Source: Compara regulation of neuronal synaptic plasticity Inferred from electronic annotation. Source: Compara response to glucocorticoid stimulus Inferred from electronic annotation. Source: Compara response to methylmercury Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular region Traceable author statement. Source: Reactome extracellular space Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay PubMed 10913138. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay PubMed 12118070PubMed 15033494. Source: UniProtKB ruffle Inferred from direct assay PubMed 10913138. Source: UniProtKB
Molecular_function	calcium ion binding Non-traceable author statement Ref.11. Source: UniProtKB calcium-dependent protein binding Inferred from direct assay PubMed 10913138. Source: UniProtKB protein homodimerization activity Inferred from direct assay PubMed 10913138. Source: UniProtKB tau protein binding Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		4	EBI-458391,EBI-458391
S100A1	P23297	5	EBI-458391,EBI-743686
S100A11	P31949	5	EBI-458391,EBI-701862
S100A6	P06703	5	EBI-458391,EBI-352877

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 92

91

Protein S100-B

PRO_0000143966

Regions

Domain

13 – 48

36

EF-hand 1

Domain

49 – 84

36

EF-hand 2

Calcium binding

19 – 32

14

1; low affinity

Calcium binding

62 – 73

12

2; high affinity

Amino acid modifications

Modified residue

2

1

Blocked amino end (Ser) Ref.6

Modified residue

2

1

N-acetylserine By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

92

Helix Strand Turn

Details...

Helix

3 – 19

17

Beta strand

22 – 24

3

Helix

30 – 40

11

Turn

42 – 44

3

Beta strand

47 – 49

3

Helix

51 – 61

11

Beta strand

65 – 69

5

Helix

71 – 88

18

Turn

89 – 91

3

Sequences

	Sequence		Length	Mass (Da)
	P04271 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 43815AC212A3AD6B	FASTA	92	10,713
	10 20 30 40 50 60 MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET 70 80 90 LDNDGDGECD FQEFMAFVAM VTTACHEFFE HE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of the human S100 beta gene." Allore R.J., Friend W.C., O'Hanlon D., Neilson K.M., Baumal R., Dunn R.J., Marks A. J. Biol. Chem. 265:15537-15543(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The DNA sequence of human chromosome 21." Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L. Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[6]	"Characterization of human brain S100 protein fraction: amino acid sequence of S100 beta." Jensen R., Marshak D.R., Anderson C., Lukas T.J., Watterson D.M. J. Neurochem. 45:700-705(1985) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-92.
[7]	"Purification, characterization and ion binding properties of human brain S100b protein." Baudier J., Glasser N., Haglid K., Gerard D. Biochim. Biophys. Acta 790:164-173(1984) [PubMed] [Europe PMC] [Abstract] Cited for: METAL ION-BINDING PROPERTIES.
[8]	"Demonstration of heterodimer formation between S100B and S100A6 in the yeast two-hybrid system and human melanoma." Yang Q., O'Hanlon D., Heizmann C.W., Marks A. Exp. Cell Res. 246:501-509(1999) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH S100A6.
[9]	"The 1.5 A crystal structure of human receptor for advanced glycation endproducts (RAGE) ectodomains reveals unique features determining ligand binding." Park H., Adsit F.G., Boyington J.C. J. Biol. Chem. 285:40762-40770(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AGER.
[10]	"The calcium-dependent interaction between S100B and the mitochondrial AAA ATPase ATAD3A and the role of this complex in the cytoplasmic processing of ATAD3A." Gilquin B., Cannon B.R., Hubstenberger A., Moulouel B., Falk E., Merle N., Assard N., Kieffer S., Rousseau D., Wilder P.T., Weber D.J., Baudier J. Mol. Cell. Biol. 30:2724-2736(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ATAD3A.
[11]	"A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form." Smith S.P., Shaw G.S. Structure 6:211-222(1998) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[12]	"A novel S100 target conformation is revealed by the solution structure of the Ca2+-S100B-TRTK-12 complex." McClintock K.A., Shaw G.S. J. Biol. Chem. 278:6251-6257(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR IN COMPLEX WITH CAPZA1 AND CALCIUM.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00299399.

PIR

BCHUIB. A38364.

RefSeq

NP_006263.1. NM_006272.2.

UniGene

Hs.422181.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MQ1	NMR	-	A/B	2-92	[»]
1UWO	NMR	-	A/B	2-92	[»]
2H61	X-ray	1.90	A/B/C/D/E/F/G/H	1-92	[»]
2PRU	NMR	-	A/B	2-92	[»]
3CZT	X-ray	1.40	X	1-92	[»]
3D0Y	X-ray	1.50	A/B	1-92	[»]
3D10	X-ray	1.65	A/B	1-92	[»]
3HCM	X-ray	2.00	A/B	1-92	[»]

ProteinModelPortal

P04271.

ModBase

Search...

Protein-protein interaction databases

IntAct

P04271. 4 interactions.

MINT

MINT-192546.

STRING

9606.ENSP00000291700.

PTM databases

PhosphoSite

P04271.

Polymorphism databases

DMDM

134138.

Proteomic databases

PaxDb

P04271.

PeptideAtlas

P04271.

PRIDE

P04271.

Protocols and materials databases

DNASU

6285.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000291700; ENSP00000291700; ENSG00000160307.
ENST00000397648; ENSP00000380769; ENSG00000160307.

GeneID

6285.

KEGG

hsa:6285.

UCSC

uc002zju.1. human.

Organism-specific databases

CTD

6285.

GeneCards

GC21M048018.

HGNC

HGNC:10500. S100B.

HPA

CAB000073.
CAB006825.
HPA015768.

MIM

176990. gene.

neXtProt

NX_P04271.

PharmGKB

PA34912.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG41158.

HOVERGEN

HBG001479.

OMA

SDGDGEC.

OrthoDB

EOG4BZN47.

PhylomeDB

P04271.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P04271.

Bgee

P04271.

CleanEx

HS_S100B.

Genevestigator

P04271.

GermOnline

ENSG00000160307. Homo sapiens.

Family and domain databases

Gene3D

1.10.238.10. 1 hit.

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.
[Graphical view]

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...

Other

BindingDB

P04271.

ChEMBL

CHEMBL4300.

ChiTaRS

S100B. human.

EvolutionaryTrace

P04271.

GenomeRNAi

6285.

NextBio

24405.

SOURCE

Search...

Entry information

Entry name

S100B_HUMAN

Accession

Primary (citable) accession number: P04271
Secondary accession number(s): D3DSN6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 145 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.