Q99584 (S10AD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein S100-A13

Alternative name(s):
S100 calcium-binding protein A13

Gene names

Name:

S100A13

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	98 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Protein transport Transport
Cellular component	Cytoplasm Secreted
Domain	Repeat
Ligand	Calcium Copper Lipid-binding Metal-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 cascade Inferred from direct assay PubMed 15033494. Source: UniProtKB positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara regulation of cell shape Inferred from electronic annotation. Source: Compara response to copper ion Inferred from electronic annotation. Source: Compara response to electrical stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Inferred from direct assay Ref.7. Source: UniProtKB extracellular space Inferred from direct assay Ref.7. Source: UniProtKB nucleus Inferred from direct assay PubMed 12118070PubMed 15033494. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay PubMed 10722710. Source: UniProtKB
Molecular_function	calcium ion binding Inferred from direct assay Ref.10Ref.11. Source: UniProtKB copper ion binding Inferred from direct assay Ref.7Ref.10. Source: UniProtKB lipid binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from direct assay PubMed 12118070. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 98

98

Protein S100-A13

PRO_0000144019

Regions

Domain

18 – 53

36

EF-hand

Calcium binding

24 – 37

14

1

Calcium binding

64 – 75

12

2

Amino acid modifications

Modified residue

32

1

Phosphoserine By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

98

Helix Strand Turn

Details...

Helix

1 – 3

3

Helix

8 – 24

17

Beta strand

26 – 28

3

Beta strand

32 – 34

3

Helix

35 – 45

11

Turn

47 – 52

6

Beta strand

53 – 55

3

Helix

56 – 63

8

Beta strand

67 – 72

6

Helix

73 – 88

16

Helix

93 – 95

3

Sequences

	Sequence		Length	Mass (Da)
	Q99584 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 1D1BE57F3CD49E81	FASTA	98	11,471
	10 20 30 40 50 60 MAAEPLTELE ESIETVVTTF FTFARQEGRK DSLSVNEFKE LVTQQLPHLL KDVGSLDEKM 70 80 90 KSLDVNQDSE LKFNEYWRLI GELAKEIRKK KDLKIRKK

References

	« Hide 'large scale' referencesShow '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. , 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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00016179.

PIR

JC5064.

RefSeq

NP_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.

UniGene

Hs.516505.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YUR	NMR	-	A/B	1-98	[»]
1YUS	NMR	-	A/B	1-98	[»]
1YUT	NMR	-	A/B	1-98	[»]
1YUU	NMR	-	A/B	1-98	[»]
2EGD	X-ray	1.80	A/B	1-98	[»]
2H2K	X-ray	2.00	A/B	1-98	[»]
2K8M	NMR	-	B/C	1-98	[»]
2KI4	NMR	-	B/C	1-98	[»]
2KI6	NMR	-	C/D	1-98	[»]
2KOT	NMR	-	A/B	1-98	[»]
2L5X	NMR	-	B/C	1-98	[»]
2LE9	NMR	-	B/C	2-98	[»]

ProteinModelPortal

Q99584.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q99584. 4 interactions.

MINT

MINT-4537584.

STRING

9606.ENSP00000344822.

PTM databases

PhosphoSite

Q99584.

Polymorphism databases

DMDM

2493416.

Proteomic databases

PaxDb

Q99584.

PeptideAtlas

Q99584.

PRIDE

Q99584.

Protocols and materials databases

DNASU

6284.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000339556; ENSP00000344822; ENSG00000189171.
ENST00000368699; ENSP00000357688; ENSG00000189171.
ENST00000392622; ENSP00000376398; ENSG00000189171.
ENST00000392623; ENSP00000376399; ENSG00000189171.
ENST00000440685; ENSP00000392767; ENSG00000189171.

GeneID

6284.

KEGG

hsa:6284.

UCSC

uc001fcf.4. human.

Organism-specific databases

CTD

6284.

GeneCards

GC01M153591.

HGNC

HGNC:10490. S100A13.

HPA

CAB025494.
HPA019592.

MIM

601989. gene.

neXtProt

NX_Q99584.

PharmGKB

PA34902.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG41858.

HOGENOM

HOG000246968.

HOVERGEN

HBG001479.

InParanoid

Q99584.

OMA

FTFAGRE.

OrthoDB

EOG4G1MJ0.

PhylomeDB

Q99584.

Gene expression databases

ArrayExpress

Q99584.

Bgee

Q99584.

CleanEx

HS_S100A13.

Genevestigator

Q99584.

GermOnline

ENSG00000189171. Homo sapiens.

Family and domain databases

Gene3D

1.10.238.10. 1 hit.

InterPro

IPR011992. EF-hand-like_dom.
IPR013787. S100_Ca-bd_sub.
[Graphical view]

Pfam

PF01023. S_100. 1 hit.
[Graphical view]

PROSITE

PS00018. EF_HAND_1. False negative.
PS50222. EF_HAND_2. False negative.
PS00303. S100_CABP. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

S100A13. human.

DrugBank

DB01025. Amlexanox.

EvolutionaryTrace

Q99584.

GenomeRNAi

6284.

NextBio

24393.

SOURCE

Search...

Entry information

Entry name

S10AD_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 118 of the entry and version 1 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.