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Q99584 (S10AD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Protein S100-A13
Alternative name(s):
S100 calcium-binding protein A13
Gene names
Name:S100A13
OrganismHomo sapiens (Human)
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 2 EF-hand domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9898Protein S100-A13
PRO_0000144019

Regions

Domain18 – 5336EF-hand 1
Calcium binding24 – 37141
Calcium binding64 – 75122

Amino acid modifications

Modified residue321Phosphoserine By similarity

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: 8878558] [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: 16710414] [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: 15489334] [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: 12746488] [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: 20863990] [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: 21269460] [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: 16145699] [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: 17374362] [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: 18259052] [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: 19284995] [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.
IPIIPI00016179.
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.
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[»]
ProteinModelPortalQ99584.
SMRQ99584. Positions 5-90.
ModBaseSearch...

Protein-protein interaction databases

IntActQ99584. 4 interactions.
STRINGQ99584.

PTM databases

PhosphoSiteQ99584.

Polymorphism databases

DMDM2493416.

Proteomic databases

PeptideAtlasQ99584.
PRIDEQ99584.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000339556; ENSP00000344822; ENSG00000189171.
ENST00000368699; ENSP00000357688; ENSG00000189171.
ENST00000392622; ENSP00000376398; ENSG00000189171.
ENST00000392623; ENSP00000376399; ENSG00000189171.
ENST00000440685; ENSP00000392767; ENSG00000189171.
GeneID6284.
KEGGhsa:6284.
NMPDRfig|9606.3.peg.2109.
UCSCuc001fcf.2. human.

Organism-specific databases

CTD6284.
GeneCardsGC01M153591.
H-InvDBHIX0001084.
HGNCHGNC:10490. S100A13.
HPACAB025494.
HPA019592.
MIM601989. gene.
neXtProtNX_Q99584.
PharmGKBPA34902.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG21774.
GeneTreeENSGT00530000063972.
HOGENOMHBG716817.
HOVERGENHBG001479.
InParanoidQ99584.
OMAFTFAGRE.
OrthoDBEOG4G1MJ0.
PhylomeDBQ99584.

Gene expression databases

ArrayExpressQ99584.
BgeeQ99584.
CleanExHS_S100A13.
GenevestigatorQ99584.
GermOnlineENSG00000189171. Homo sapiens.

Family and domain databases

InterProIPR011992. EF-hand-like_dom.
IPR013787. S100_Ca-bd_sub.
[Graphical view]
Gene3DG3DSA:1.10.238.10. EF-Hand_type. 1 hit.
PfamPF01023. S_100. 1 hit.
[Graphical view]
PROSITEPS00018. EF_HAND_1. False negative.
PS50222. EF_HAND_2. False negative.
PS00303. S100_CABP. False negative.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB01025. Amlexanox.
NextBio24393.
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: January 25, 2012
This is version 102 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

Human chromosome 1

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families