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Q99584 (S10AD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein S100-A13
Alternative name(s):
S100 calcium-binding protein A13
Gene names
Name:S100A13
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length98 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway. Binds two calcium ions per subunit. Binds one copper ion. Binding of one copper ion does not interfere with calcium binding. Required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine By similarity. Ref.7 Ref.8

Subunit structure

Homodimer. Part of a copper-dependent multiprotein complex containing S100A13, FGF1 and SYT1. Interacts with FGF1 and SYT1 By similarity. Ref.10 Ref.11 Ref.12 Ref.13

Subcellular location

Cytoplasm. Secreted. Note: Secretion is mediated by exposure to stress and requires copper ions.

Tissue specificity

Expressed in heart and skeletal muscle.

Sequence similarities

Belongs to the S-100 family.

Contains 1 EF-hand domain.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
Secreted
   DomainRepeat
   LigandCalcium
Copper
Lipid-binding
Metal-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcytokine secretion

Inferred from mutant phenotype Ref.8. Source: UniProtKB

interleukin-1 alpha secretion

Inferred from direct assay Ref.7. Source: UniProtKB

mast cell degranulation

Non-traceable author statement PubMed 10051426. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from direct assay PubMed 15033494. Source: UniProtKB

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of cell shape

Inferred from electronic annotation. Source: Ensembl

response to copper ion

Inferred from electronic annotation. Source: Ensembl

response to electrical stimulus

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 15821778. Source: UniProtKB

cytosol

Inferred from direct assay Ref.7. Source: UniProtKB

extracellular space

Inferred from direct assay Ref.7. Source: UniProtKB

mast cell granule

Non-traceable author statement PubMed 10051426. Source: GOC

nucleus

Inferred from direct assay PubMed 12118070PubMed 15033494. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 10722710. Source: UniProtKB

   Molecular_functionRAGE receptor binding

Inferred from physical interaction PubMed 15033494. Source: UniProtKB

calcium ion binding

Inferred from direct assay Ref.10Ref.11. Source: UniProtKB

copper ion binding

Inferred from direct assay Ref.7Ref.10. Source: UniProtKB

fibroblast growth factor binding

Inferred from physical interaction PubMed 11432880. Source: UniProtKB

lipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.7Ref.13. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.7Ref.10. Source: UniProtKB

zinc ion binding

Inferred from direct assay PubMed 12118070. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9898Protein S100-A13
PRO_0000144019

Regions

Domain18 – 5336EF-hand
Calcium binding24 – 37141
Calcium binding64 – 75122

Secondary structure

.................. 98
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q99584 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 1D1BE57F3CD49E81

FASTA9811,471
        10         20         30         40         50         60 
MAAEPLTELE ESIETVVTTF FTFARQEGRK DSLSVNEFKE LVTQQLPHLL KDVGSLDEKM 

        70         80         90 
KSLDVNQDSE LKFNEYWRLI GELAKEIRKK KDLKIRKK 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the human and mouse cDNAs coding for S100A13, a new member of the S100 protein family."
Wicki R., Schaefer B.W., Erne P., Heizmann C.W.
Biochem. Biophys. Res. Commun. 227:594-599(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
[3]"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 (OCT-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. expand/collapse author list , 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]"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: Eye and Skin.
[6]Wen G.B., Yang J., Cao R.X., Liu J.H., Peng Z.L.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-98.
Tissue: Thyroid.
[7]"S100A13 mediates the copper-dependent stress-induced release of IL-1alpha from both human U937 and murine NIH 3T3 cells."
Mandinova A., Soldi R., Graziani I., Bagala C., Bellum S., Landriscina M., Tarantini F., Prudovsky I., Maciag T.
J. Cell Sci. 116:2687-2696(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Effect of human S100A13 gene silencing on FGF-1 transportation in human endothelial cells."
Cao R., Yan B., Yang H., Zu X., Wen G., Zhong J.
J. Formos. Med. Assoc. 109:632-640(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Structural interplay between calcium(II) and copper(II) binding to S100A13 protein."
Arnesano F., Banci L., Bertini I., Fantoni A., Tenori L., Viezzoli M.S.
Angew. Chem. Int. Ed. 44:6341-6344(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR IN COMPLEX WITH CALCIUM IONS, COPPER-BINDING, SUBUNIT.
[11]"Crystal structure study on human S100A13 at 2.0 A resolution."
Li M., Zhang P.F., Pan X.W., Chang W.R.
Biochem. Biophys. Res. Commun. 356:616-621(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, SUBUNIT.
[12]"Structure of calcium-bound human S100A13 at pH 7.5 at 1.8 A resolution."
Imai F.L., Nagata K., Yonezawa N., Nakano M., Tanokura M.
Acta Crystallogr. F 64:70-76(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, SUBUNIT.
[13]"S100A13-C2A binary complex structure-a key component in the acidic fibroblast growth factor for the non-classical pathway."
Mohan S.K., Rani S.G., Kumar S.M., Yu C.
Biochem. Biophys. Res. Commun. 380:514-519(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR IN COMPLEX WITH SYT1, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X99920 mRNA. Translation: CAA68188.1.
CR542149 mRNA. Translation: CAG46946.1.
BT006724 mRNA. Translation: AAP35370.1.
BX470102 Genomic DNA. Translation: CAI14760.1.
BC000632 mRNA. Translation: AAH00632.1.
BC068064 mRNA. Translation: AAH68064.1.
BC070291 mRNA. Translation: AAH70291.1.
AY987392 mRNA. Translation: AAX89402.1.
CCDSCCDS30874.1.
PIRJC5064.
RefSeqNP_001019381.1. NM_001024210.1.
NP_001019382.1. NM_001024211.1.
NP_001019383.1. NM_001024212.1.
NP_001019384.1. NM_001024213.1.
NP_005970.1. NM_005979.2.
XP_005245491.1. XM_005245434.2.
UniGeneHs.516505.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YURNMR-A/B1-98[»]
1YUSNMR-A/B1-98[»]
1YUTNMR-A/B1-98[»]
1YUUNMR-A/B1-98[»]
2EGDX-ray1.80A/B1-98[»]
2H2KX-ray2.00A/B1-98[»]
2K8MNMR-B/C1-98[»]
2KI4NMR-B/C1-98[»]
2KI6NMR-C/D1-98[»]
2KOTNMR-A/B1-98[»]
2L5XNMR-B/C1-98[»]
2LE9NMR-B/C2-98[»]
ProteinModelPortalQ99584.
SMRQ99584. Positions 6-96.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112192. 13 interactions.
IntActQ99584. 4 interactions.
MINTMINT-4537584.
STRING9606.ENSP00000344822.

Chemistry

DrugBankDB01025. Amlexanox.

PTM databases

PhosphoSiteQ99584.

Polymorphism databases

DMDM2493416.

Proteomic databases

MaxQBQ99584.
PaxDbQ99584.
PeptideAtlasQ99584.
PRIDEQ99584.

Protocols and materials databases

DNASU6284.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000339556; ENSP00000344822; ENSG00000189171.
ENST00000368699; ENSP00000357688; ENSG00000189171.
ENST00000392622; ENSP00000376398; ENSG00000189171.
ENST00000392623; ENSP00000376399; ENSG00000189171.
ENST00000440685; ENSP00000392767; ENSG00000189171.
GeneID6284.
KEGGhsa:6284.
UCSCuc001fcf.4. human.

Organism-specific databases

CTD6284.
GeneCardsGC01M153591.
HGNCHGNC:10490. S100A13.
HPACAB025494.
HPA019592.
MIM601989. gene.
neXtProtNX_Q99584.
PharmGKBPA34902.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41858.
HOGENOMHOG000246968.
HOVERGENHBG001479.
InParanoidQ99584.
OMAKFANAMA.
OrthoDBEOG71P2D8.
PhylomeDBQ99584.
TreeFamTF332727.

Gene expression databases

BgeeQ99584.
CleanExHS_S100A13.
GenevestigatorQ99584.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR013787. S100_Ca-bd_sub.
IPR028487. S100A13.
[Graphical view]
PANTHERPTHR11639:SF57. PTHR11639:SF57. 1 hit.
PfamPF01023. S_100. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSS100A13. human.
EvolutionaryTraceQ99584.
GeneWikiS100A13.
GenomeRNAi6284.
NextBio24393.
PROQ99584.
SOURCESearch...

Entry information

Entry nameS10AD_HUMAN
AccessionPrimary (citable) accession number: Q99584
Secondary accession number(s): Q52PI9, Q6FGF8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM