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Q9HCY8

- S10AE_HUMAN

UniProt

Q9HCY8 - S10AE_HUMAN

Protein

Protein S100-A14

Gene

S100A14

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

    Modulates P53/TP53 protein levels, and thereby plays a role in the regulation of cell survival and apoptosis. Depending on the context, it can promote cell proliferation or apoptosis. Plays a role in the regulation of cell migration by modulating the levels of MMP2, a matrix protease that is under transcriptional control of P53/TP53. Does not bind calcium.3 Publications

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. chemokine receptor binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. calcium ion homeostasis Source: UniProtKB
    3. defense response to bacterium Source: UniProtKB
    4. positive regulation of granulocyte chemotaxis Source: UniProtKB
    5. positive regulation of monocyte chemotaxis Source: UniProtKB
    6. response to lipopolysaccharide Source: UniProtKB
    7. toll-like receptor 4 signaling pathway Source: UniProtKB

    Keywords - Biological processi

    Apoptosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein S100-A14
    Alternative name(s):
    S100 calcium-binding protein A14
    Short name:
    S114
    Gene namesi
    Name:S100A14
    Synonyms:S100A15
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:18901. S100A14.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. perinuclear region of cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134905502.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 104104Protein S100-A14PRO_0000144021Add
    BLAST

    Proteomic databases

    MaxQBiQ9HCY8.
    PaxDbiQ9HCY8.
    PeptideAtlasiQ9HCY8.
    PRIDEiQ9HCY8.

    PTM databases

    PhosphoSiteiQ9HCY8.

    Expressioni

    Tissue specificityi

    Expressed at highest levels in colon and at moderate levels in thymus, kidney, liver, small intestine, and lung. Low expression in heart and no expression is seen in brain, skeletal muscle, spleen, placenta and peripheral blood leukocytes.1 Publication

    Gene expression databases

    BgeeiQ9HCY8.
    CleanExiHS_S100A14.
    GenevestigatoriQ9HCY8.

    Organism-specific databases

    HPAiHPA027613.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with AGER.2 Publications

    Protein-protein interaction databases

    BioGridi121504. 5 interactions.
    IntActiQ9HCY8. 3 interactions.
    MINTiMINT-5002007.
    STRINGi9606.ENSP00000340463.

    Structurei

    Secondary structure

    1
    104
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 114
    Helixi19 – 3214
    Turni34 – 396
    Helixi43 – 5311
    Turni55 – 573
    Helixi60 – 623
    Helixi65 – 717
    Helixi81 – 9414
    Beta strandi98 – 1003

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2M0RNMR-A/B1-104[»]
    ProteinModelPortaliQ9HCY8.
    SMRiQ9HCY8. Positions 1-104.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 6135EF-handAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG46731.
    HOGENOMiHOG000246968.
    HOVERGENiHBG001479.
    InParanoidiQ9HCY8.
    OMAiYPARNLA.
    OrthoDBiEOG715Q6C.
    PhylomeDBiQ9HCY8.
    TreeFamiTF332727.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR013787. S100_Ca-bd_sub.
    IPR028493. S100A14.
    [Graphical view]
    PANTHERiPTHR11639:SF4. PTHR11639:SF4. 1 hit.
    PfamiPF01023. S_100. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9HCY8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGQCRSANAE DAQEFSDVER AIETLIKNFH QYSVEGGKET LTPSELRDLV    50
    TQQLPHLMPS NCGLEEKIAN LGSCNDSKLE FRSFWELIGE AAKSVKLERP 100
    VRGH 104
    Length:104
    Mass (Da):11,662
    Last modified:March 1, 2001 - v1
    Checksum:i97EF31A46B388E79
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY007220 mRNA. Translation: AAG01893.1.
    AF426828 Genomic DNA. Translation: AAM19206.1.
    BX470102 Genomic DNA. Translation: CAI14759.1.
    BC005019 mRNA. Translation: AAH05019.1.
    CCDSiCCDS1046.1.
    RefSeqiNP_065723.1. NM_020672.2.
    XP_005245419.1. XM_005245362.1.
    XP_006711531.1. XM_006711468.1.
    UniGeneiHs.288998.

    Genome annotation databases

    EnsembliENST00000344616; ENSP00000340463; ENSG00000189334.
    ENST00000368701; ENSP00000357690; ENSG00000189334.
    ENST00000368702; ENSP00000357691; ENSG00000189334.
    ENST00000476873; ENSP00000420296; ENSG00000189334.
    GeneIDi57402.
    KEGGihsa:57402.
    UCSCiuc001fce.3. human.

    Polymorphism databases

    DMDMi20178118.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY007220 mRNA. Translation: AAG01893.1 .
    AF426828 Genomic DNA. Translation: AAM19206.1 .
    BX470102 Genomic DNA. Translation: CAI14759.1 .
    BC005019 mRNA. Translation: AAH05019.1 .
    CCDSi CCDS1046.1.
    RefSeqi NP_065723.1. NM_020672.2.
    XP_005245419.1. XM_005245362.1.
    XP_006711531.1. XM_006711468.1.
    UniGenei Hs.288998.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2M0R NMR - A/B 1-104 [» ]
    ProteinModelPortali Q9HCY8.
    SMRi Q9HCY8. Positions 1-104.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121504. 5 interactions.
    IntActi Q9HCY8. 3 interactions.
    MINTi MINT-5002007.
    STRINGi 9606.ENSP00000340463.

    PTM databases

    PhosphoSitei Q9HCY8.

    Polymorphism databases

    DMDMi 20178118.

    Proteomic databases

    MaxQBi Q9HCY8.
    PaxDbi Q9HCY8.
    PeptideAtlasi Q9HCY8.
    PRIDEi Q9HCY8.

    Protocols and materials databases

    DNASUi 57402.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000344616 ; ENSP00000340463 ; ENSG00000189334 .
    ENST00000368701 ; ENSP00000357690 ; ENSG00000189334 .
    ENST00000368702 ; ENSP00000357691 ; ENSG00000189334 .
    ENST00000476873 ; ENSP00000420296 ; ENSG00000189334 .
    GeneIDi 57402.
    KEGGi hsa:57402.
    UCSCi uc001fce.3. human.

    Organism-specific databases

    CTDi 57402.
    GeneCardsi GC01M153586.
    HGNCi HGNC:18901. S100A14.
    HPAi HPA027613.
    MIMi 607986. gene.
    neXtProti NX_Q9HCY8.
    PharmGKBi PA134905502.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG46731.
    HOGENOMi HOG000246968.
    HOVERGENi HBG001479.
    InParanoidi Q9HCY8.
    OMAi YPARNLA.
    OrthoDBi EOG715Q6C.
    PhylomeDBi Q9HCY8.
    TreeFami TF332727.

    Miscellaneous databases

    ChiTaRSi S100A14. human.
    GenomeRNAii 57402.
    NextBioi 63504.
    PROi Q9HCY8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9HCY8.
    CleanExi HS_S100A14.
    Genevestigatori Q9HCY8.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR013787. S100_Ca-bd_sub.
    IPR028493. S100A14.
    [Graphical view ]
    PANTHERi PTHR11639:SF4. PTHR11639:SF4. 1 hit.
    Pfami PF01023. S_100. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of the human S100A14 gene encoding a novel member of the S100 family."
      Pietas A., Schluns K., Marenholz I., Schafer B.W., Heizmann C.W., Petersen I.
      Genomics 79:513-522(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "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].
    3. "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: Pancreas.
    4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. "S100A14 stimulates cell proliferation and induces cell apoptosis at different concentrations via receptor for advanced glycation end products (RAGE)."
      Jin Q., Chen H., Luo A., Ding F., Liu Z.
      PLoS ONE 6:E19375-E19375(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AGER.
    6. "Involvement of S100A14 protein in cell invasion by affecting expression and function of matrix metalloproteinase (MMP)-2 via p53-dependent transcriptional regulation."
      Chen H., Yuan Y., Zhang C., Luo A., Ding F., Ma J., Yang S., Tian Y., Tong T., Zhan Q., Liu Z.
      J. Biol. Chem. 287:17109-17119(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "S100A14 inhibits proliferation of oral carcinoma derived cells through G1-arrest."
      Sapkota D., Costea D.E., Blo M., Bruland O., Lorens J.B., Vasstrand E.N., Ibrahim S.O.
      Oral Oncol. 48:219-225(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. Cited for: STRUCTURE BY NMR, ABSENCE OF CALCIUM BINDING, SUBUNIT.

    Entry informationi

    Entry nameiS10AE_HUMAN
    AccessioniPrimary (citable) accession number: Q9HCY8
    Secondary accession number(s): Q5RHT0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 16, 2002
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 110 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

    Caution

    Part of the residues that are essential for calcium binding are not conserved, resulting in loss of calcium binding at physiological calcium concentrations.1 Publication

    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