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Q99584

- S10AD_HUMAN

UniProt

Q99584 - S10AD_HUMAN

Protein

Protein S100-A13

Gene

S100A13

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

    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.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi24 – 37141Add
    BLAST
    Calcium bindingi64 – 75122Add
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. copper ion binding Source: UniProtKB
    3. fibroblast growth factor binding Source: UniProtKB
    4. lipid binding Source: UniProtKB-KW
    5. protein binding Source: UniProtKB
    6. protein homodimerization activity Source: UniProtKB
    7. RAGE receptor binding Source: UniProtKB
    8. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cytokine secretion Source: UniProtKB
    2. interleukin-1 alpha secretion Source: UniProtKB
    3. mast cell degranulation Source: UniProtKB
    4. positive regulation of cell proliferation Source: Ensembl
    5. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    6. regulation of cell shape Source: Ensembl
    7. response to copper ion Source: Ensembl
    8. response to electrical stimulus Source: Ensembl

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    Calcium, Copper, Lipid-binding, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein S100-A13
    Alternative name(s):
    S100 calcium-binding protein A13
    Gene namesi
    Name:S100A13
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10490. S100A13.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. extracellular space Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. mast cell granule Source: GOC
    6. nucleus Source: UniProtKB
    7. perinuclear region of cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34902.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9898Protein S100-A13PRO_0000144019Add
    BLAST

    Proteomic databases

    MaxQBiQ99584.
    PaxDbiQ99584.
    PeptideAtlasiQ99584.
    PRIDEiQ99584.

    PTM databases

    PhosphoSiteiQ99584.

    Expressioni

    Tissue specificityi

    Expressed in heart and skeletal muscle.

    Gene expression databases

    BgeeiQ99584.
    CleanExiHS_S100A13.
    GenevestigatoriQ99584.

    Organism-specific databases

    HPAiCAB025494.
    HPA019592.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi112192. 13 interactions.
    IntActiQ99584. 4 interactions.
    MINTiMINT-4537584.
    STRINGi9606.ENSP00000344822.

    Structurei

    Secondary structure

    98
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1 – 33
    Helixi8 – 2417
    Beta strandi26 – 283
    Beta strandi32 – 343
    Helixi35 – 4511
    Turni47 – 526
    Beta strandi53 – 553
    Helixi56 – 638
    Beta strandi67 – 726
    Helixi73 – 8816
    Helixi93 – 953

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ99584.
    SMRiQ99584. Positions 6-96.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99584.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 5336EF-handAdd
    BLAST

    Sequence similaritiesi

    Belongs to the S-100 family.Curated
    Contains 1 EF-hand domain.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG41858.
    HOGENOMiHOG000246968.
    HOVERGENiHBG001479.
    InParanoidiQ99584.
    OMAiKFANAMA.
    OrthoDBiEOG71P2D8.
    PhylomeDBiQ99584.
    TreeFamiTF332727.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR013787. S100_Ca-bd_sub.
    IPR028487. S100A13.
    [Graphical view]
    PANTHERiPTHR11639:SF57. PTHR11639:SF57. 1 hit.
    PfamiPF01023. S_100. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q99584-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAEPLTELE ESIETVVTTF FTFARQEGRK DSLSVNEFKE LVTQQLPHLL   50
    KDVGSLDEKM KSLDVNQDSE LKFNEYWRLI GELAKEIRKK KDLKIRKK 98
    Length:98
    Mass (Da):11,471
    Last modified:May 1, 1997 - v1
    Checksum:i1D1BE57F3CD49E81
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS30874.1.
    PIRiJC5064.
    RefSeqiNP_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.
    UniGeneiHs.516505.

    Genome annotation databases

    EnsembliENST00000339556; ENSP00000344822; ENSG00000189171.
    ENST00000368699; ENSP00000357688; ENSG00000189171.
    ENST00000392622; ENSP00000376398; ENSG00000189171.
    ENST00000392623; ENSP00000376399; ENSG00000189171.
    ENST00000440685; ENSP00000392767; ENSG00000189171.
    GeneIDi6284.
    KEGGihsa:6284.
    UCSCiuc001fcf.4. human.

    Polymorphism databases

    DMDMi2493416.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS30874.1.
    PIRi JC5064.
    RefSeqi 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.
    XP_005245491.1. XM_005245434.2.
    UniGenei Hs.516505.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali Q99584.
    SMRi Q99584. Positions 6-96.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112192. 13 interactions.
    IntActi Q99584. 4 interactions.
    MINTi MINT-4537584.
    STRINGi 9606.ENSP00000344822.

    Chemistry

    DrugBanki DB01025. Amlexanox.

    PTM databases

    PhosphoSitei Q99584.

    Polymorphism databases

    DMDMi 2493416.

    Proteomic databases

    MaxQBi Q99584.
    PaxDbi Q99584.
    PeptideAtlasi Q99584.
    PRIDEi Q99584.

    Protocols and materials databases

    DNASUi 6284.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000339556 ; ENSP00000344822 ; ENSG00000189171 .
    ENST00000368699 ; ENSP00000357688 ; ENSG00000189171 .
    ENST00000392622 ; ENSP00000376398 ; ENSG00000189171 .
    ENST00000392623 ; ENSP00000376399 ; ENSG00000189171 .
    ENST00000440685 ; ENSP00000392767 ; ENSG00000189171 .
    GeneIDi 6284.
    KEGGi hsa:6284.
    UCSCi uc001fcf.4. human.

    Organism-specific databases

    CTDi 6284.
    GeneCardsi GC01M153591.
    HGNCi HGNC:10490. S100A13.
    HPAi CAB025494.
    HPA019592.
    MIMi 601989. gene.
    neXtProti NX_Q99584.
    PharmGKBi PA34902.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG41858.
    HOGENOMi HOG000246968.
    HOVERGENi HBG001479.
    InParanoidi Q99584.
    OMAi KFANAMA.
    OrthoDBi EOG71P2D8.
    PhylomeDBi Q99584.
    TreeFami TF332727.

    Miscellaneous databases

    ChiTaRSi S100A13. human.
    EvolutionaryTracei Q99584.
    GeneWikii S100A13.
    GenomeRNAii 6284.
    NextBioi 24393.
    PROi Q99584.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q99584.
    CleanExi HS_S100A13.
    Genevestigatori Q99584.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR013787. S100_Ca-bd_sub.
    IPR028487. S100A13.
    [Graphical view ]
    PANTHERi PTHR11639:SF57. PTHR11639:SF57. 1 hit.
    Pfami PF01023. S_100. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiS10AD_HUMAN
    AccessioniPrimary (citable) accession number: Q99584
    Secondary accession number(s): Q52PI9, Q6FGF8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 132 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3