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P33764

- S10A3_HUMAN

UniProt

P33764 - S10A3_HUMAN

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Protein

Protein S100-A3

Gene

S100A3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Binds both calcium and zinc. May be involved in calcium-dependent cuticle cell differentiation, hair shaft and hair cuticular barrier formation.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi83 – 831Zinc
Metal bindingi86 – 861Zinc
Metal bindingi87 – 871Zinc
Metal bindingi93 – 931Zinc

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi20 – 33141; low affinitySequence AnalysisAdd
BLAST
Calcium bindingi63 – 74122; high affinitySequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Protein S100-A3
Alternative name(s):
Protein S-100E
S100 calcium-binding protein A3
Gene namesi
Name:S100A3
Synonyms:S100E
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:10493. S100A3.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleolus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi30 – 301C → A: Abolishes calcium binding; when associated with Ala-68. 1 Publication
Mutagenesisi68 – 681C → A: Abolishes calcium binding; when associated with Ala-30. 1 Publication
Mutagenesisi81 – 811C → A: Increases affinity for calcium; when associated with Ala-99. 1 Publication
Mutagenesisi99 – 991C → A: Increases affinity for calcium; when associated with Ala-81. 1 Publication

Organism-specific databases

PharmGKBiPA34905.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 101100Protein S100-A3PRO_0000143972Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Disulfide bondi30 ↔ 681 Publication
Modified residuei51 – 511Citrulline; by PAD31 Publication
Disulfide bondi81 ↔ 991 Publication

Post-translational modificationi

More than half of the arginine residues undergo citrullination by PAD1 and PAD2. Arg-51 is specifically citrullinated by PAD3 and promotes tetramerization.1 Publication

Keywords - PTMi

Acetylation, Citrullination, Disulfide bond

Proteomic databases

MaxQBiP33764.
PaxDbiP33764.
PeptideAtlasiP33764.
PRIDEiP33764.

Expressioni

Tissue specificityi

Skin specific, specifically expressed at the inner endocuticle of hair fibers.1 Publication

Gene expression databases

BgeeiP33764.
CleanExiHS_S100A3.
GenevestigatoriP33764.

Organism-specific databases

HPAiHPA042674.

Interactioni

Subunit structurei

Homodimer and homotetramer for the citrullinated form.1 Publication

Protein-protein interaction databases

BioGridi112182. 9 interactions.
MINTiMINT-4714713.
STRINGi9606.ENSP00000357701.

Structurei

Secondary structure

1
101
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2017Combined sources
Beta strandi22 – 243Combined sources
Beta strandi28 – 303Combined sources
Helixi31 – 4111Combined sources
Turni42 – 443Combined sources
Turni49 – 513Combined sources
Helixi52 – 6413Combined sources
Turni65 – 673Combined sources
Beta strandi68 – 714Combined sources
Helixi72 – 8615Combined sources
Helixi88 – 903Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KSOX-ray1.70A/B1-101[»]
3NSIX-ray2.15A/B1-101[»]
3NSKX-ray1.55A/B1-101[»]
3NSLX-ray1.50A/B/C/D/E/F2-101[»]
3NSOX-ray1.45A/B1-101[»]
ProteinModelPortaliP33764.
SMRiP33764. Positions 2-94.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33764.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 4736EF-hand 1Add
BLAST
Domaini50 – 8536EF-hand 2Add
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG40471.
GeneTreeiENSGT00760000119034.
HOGENOMiHOG000246968.
HOVERGENiHBG001479.
InParanoidiP33764.
OMAiCEVDFAE.
OrthoDBiEOG779P19.
PhylomeDBiP33764.
TreeFamiTF332727.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
IPR028488. S100A3.
[Graphical view]
PANTHERiPTHR11639:SF12. PTHR11639:SF12. 1 hit.
PfamiPF01023. S_100. 1 hit.
[Graphical view]
PROSITEiPS00303. S100_CABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P33764-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARPLEQAVA AIVCTFQEYA GRCGDKYKLC QAELKELLQK ELATWTPTEF
60 70 80 90 100
RECDYNKFMS VLDTNKDCEV DFVEYVRSLA CLCLYCHEYF KDCPSEPPCS

Q
Length:101
Mass (Da):11,713
Last modified:February 1, 1994 - v1
Checksum:iABCAF4B7E5F2E0A1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31R → K.
Corresponds to variant rs36022742 [ dbSNP | Ensembl ].
VAR_061047

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18948 mRNA. Translation: CAA79471.1.
Z18950 Genomic DNA. Translation: CAA79473.1.
BT006955 mRNA. Translation: AAP35601.1.
CR542163 mRNA. Translation: CAG46960.1.
CR542185 mRNA. Translation: CAG46982.1.
BX470102 Genomic DNA. Translation: CAI14755.1.
CH471121 Genomic DNA. Translation: EAW53306.1.
CH471121 Genomic DNA. Translation: EAW53307.1.
BC012893 mRNA. Translation: AAH12893.1.
CCDSiCCDS1043.1.
PIRiC48219.
S70326.
RefSeqiNP_002951.1. NM_002960.1.
UniGeneiHs.557609.

Genome annotation databases

EnsembliENST00000368712; ENSP00000357701; ENSG00000188015.
ENST00000368713; ENSP00000357702; ENSG00000188015.
GeneIDi6274.
KEGGihsa:6274.
UCSCiuc001fca.1. human.

Polymorphism databases

DMDMi464729.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18948 mRNA. Translation: CAA79471.1 .
Z18950 Genomic DNA. Translation: CAA79473.1 .
BT006955 mRNA. Translation: AAP35601.1 .
CR542163 mRNA. Translation: CAG46960.1 .
CR542185 mRNA. Translation: CAG46982.1 .
BX470102 Genomic DNA. Translation: CAI14755.1 .
CH471121 Genomic DNA. Translation: EAW53306.1 .
CH471121 Genomic DNA. Translation: EAW53307.1 .
BC012893 mRNA. Translation: AAH12893.1 .
CCDSi CCDS1043.1.
PIRi C48219.
S70326.
RefSeqi NP_002951.1. NM_002960.1.
UniGenei Hs.557609.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KSO X-ray 1.70 A/B 1-101 [» ]
3NSI X-ray 2.15 A/B 1-101 [» ]
3NSK X-ray 1.55 A/B 1-101 [» ]
3NSL X-ray 1.50 A/B/C/D/E/F 2-101 [» ]
3NSO X-ray 1.45 A/B 1-101 [» ]
ProteinModelPortali P33764.
SMRi P33764. Positions 2-94.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112182. 9 interactions.
MINTi MINT-4714713.
STRINGi 9606.ENSP00000357701.

Polymorphism databases

DMDMi 464729.

Proteomic databases

MaxQBi P33764.
PaxDbi P33764.
PeptideAtlasi P33764.
PRIDEi P33764.

Protocols and materials databases

DNASUi 6274.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368712 ; ENSP00000357701 ; ENSG00000188015 .
ENST00000368713 ; ENSP00000357702 ; ENSG00000188015 .
GeneIDi 6274.
KEGGi hsa:6274.
UCSCi uc001fca.1. human.

Organism-specific databases

CTDi 6274.
GeneCardsi GC01M153519.
H-InvDB HIX0116376.
HGNCi HGNC:10493. S100A3.
HPAi HPA042674.
MIMi 176992. gene.
neXtProti NX_P33764.
PharmGKBi PA34905.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG40471.
GeneTreei ENSGT00760000119034.
HOGENOMi HOG000246968.
HOVERGENi HBG001479.
InParanoidi P33764.
OMAi CEVDFAE.
OrthoDBi EOG779P19.
PhylomeDBi P33764.
TreeFami TF332727.

Miscellaneous databases

EvolutionaryTracei P33764.
GeneWikii S100A3.
GenomeRNAii 6274.
NextBioi 24351.
PROi P33764.
SOURCEi Search...

Gene expression databases

Bgeei P33764.
CleanExi HS_S100A3.
Genevestigatori P33764.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
InterProi IPR011992. EF-hand-dom_pair.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
IPR028488. S100A3.
[Graphical view ]
PANTHERi PTHR11639:SF12. PTHR11639:SF12. 1 hit.
Pfami PF01023. S_100. 1 hit.
[Graphical view ]
PROSITEi PS00303. S100_CABP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Six S100 genes are clustered on human chromosome 1q21: identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E."
    Engelkamp D., Schaefer B.W., Mattei M.-G., Erne P., Heizmann C.W.
    Proc. Natl. Acad. Sci. U.S.A. 90:6547-6551(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Lung.
  7. "Probing the structure of the human Ca2+- and Zn2+-binding protein S100A3: spectroscopic investigations of its transition metal ion complexes, and three-dimensional structural model."
    Fritz G., Heizmann C.W., Kroneck P.M.H.
    Biochim. Biophys. Acta 1448:264-276(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "Characterization of the cysteine-rich calcium-binding S100A3 protein from human hair cuticles."
    Kizawa K., Troxler H., Kleinert P., Inoue T., Toyoda M., Morohashi M., Heizmann C.W.
    Biochem. Biophys. Res. Commun. 299:857-862(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, TISSUE SPECIFICITY.
  9. "Specific citrullination causes assembly of a globular S100A3 homotetramer: a putative Ca2+ modulator matures human hair cuticle."
    Kizawa K., Takahara H., Troxler H., Kleinert P., Mochida U., Heizmann C.W.
    J. Biol. Chem. 283:5004-5013(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, CITRULLINATION AT ARG-51, SUBCELLULAR LOCATION.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  11. "Refined crystal structures of human Ca(2+)/Zn(2+)-binding S100A3 protein characterized by two disulfide bridges."
    Unno M., Kawasaki T., Takahara H., Heizmann C.W., Kizawa K.
    J. Mol. Biol. 408:477-490(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS), DISULFIDE BONDS, ZINC-BINDING SITES, MUTAGENESIS OF CYS-30; CYS-68; CSY-81 AND CYS-99.

Entry informationi

Entry nameiS10A3_HUMAN
AccessioniPrimary (citable) accession number: P33764
Secondary accession number(s): D3DV51, Q6FGE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: November 26, 2014
This is version 139 of the entry and version 1 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3