Full text data of S100A14
S100A14
(S100A15)
[Confidence: low (only semi-automatic identification from reviews)]
Protein S100-A14 (S100 calcium-binding protein A14; S114)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Protein S100-A14 (S100 calcium-binding protein A14; S114)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9HCY8
ID S10AE_HUMAN Reviewed; 104 AA.
AC Q9HCY8; Q5RHT0;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=Protein S100-A14;
DE AltName: Full=S100 calcium-binding protein A14;
DE Short=S114;
GN Name=S100A14; Synonyms=S100A15;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=11944983; DOI=10.1006/geno.2002.6744;
RA Pietas A., Schluns K., Marenholz I., Schafer B.W., Heizmann C.W.,
RA Petersen I.;
RT "Molecular cloning and characterization of the human S100A14 gene
RT encoding a novel member of the S100 family.";
RL Genomics 79:513-522(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [5]
RP FUNCTION, AND INTERACTION WITH AGER.
RX PubMed=21559403; DOI=10.1371/journal.pone.0019375;
RA Jin Q., Chen H., Luo A., Ding F., Liu Z.;
RT "S100A14 stimulates cell proliferation and induces cell apoptosis at
RT different concentrations via receptor for advanced glycation end
RT products (RAGE).";
RL PLoS ONE 6:E19375-E19375(2011).
RN [6]
RP FUNCTION.
RX PubMed=22451655; DOI=10.1074/jbc.M111.326975;
RA Chen H., Yuan Y., Zhang C., Luo A., Ding F., Ma J., Yang S., Tian Y.,
RA Tong T., Zhan Q., Liu Z.;
RT "Involvement of S100A14 protein in cell invasion by affecting
RT expression and function of matrix metalloproteinase (MMP)-2 via p53-
RT dependent transcriptional regulation.";
RL J. Biol. Chem. 287:17109-17119(2012).
RN [7]
RP FUNCTION.
RX PubMed=22032898; DOI=10.1016/j.oraloncology.2011.10.001;
RA Sapkota D., Costea D.E., Blo M., Bruland O., Lorens J.B.,
RA Vasstrand E.N., Ibrahim S.O.;
RT "S100A14 inhibits proliferation of oral carcinoma derived cells
RT through G1-arrest.";
RL Oral Oncol. 48:219-225(2012).
RN [8]
RP STRUCTURE BY NMR, ABSENCE OF CALCIUM BINDING, AND SUBUNIT.
RX PubMed=23197251; DOI=10.1007/s00775-012-0963-3;
RA Bertini I., Borsi V., Cerofolini L., Das Gupta S., Fragai M.,
RA Luchinat C.;
RT "Solution structure and dynamics of human S100A14.";
RL J. Biol. Inorg. Chem. 18:183-194(2013).
CC -!- FUNCTION: Modulates P53/TP53 protein levels, and thereby plays a
CC role in the regulation of cell survival and apoptosis. Depending
CC on the context, it can promote cell proliferation or apoptosis.
CC Plays a role in the regulation of cell migration by modulating the
CC levels of MMP2, a matrix protease that is under transcriptional
CC control of P53/TP53. Does not bind calcium.
CC -!- SUBUNIT: Homodimer. Interacts with AGER.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in colon and at
CC moderate levels in thymus, kidney, liver, small intestine, and
CC lung. Low expression in heart and no expression is seen in brain,
CC skeletal muscle, spleen, placenta and peripheral blood leukocytes.
CC -!- SIMILARITY: Belongs to the S-100 family.
CC -!- SIMILARITY: Contains 1 EF-hand domain.
CC -!- CAUTION: Part of the residues that are essential for calcium
CC binding are not conserved, resulting in loss of calcium binding at
CC physiological calcium concentrations (PubMed:23197251).
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AY007220; AAG01893.1; -; mRNA.
DR EMBL; AF426828; AAM19206.1; -; Genomic_DNA.
DR EMBL; BX470102; CAI14759.1; -; Genomic_DNA.
DR EMBL; BC005019; AAH05019.1; -; mRNA.
DR RefSeq; NP_065723.1; NM_020672.2.
DR RefSeq; XP_005245419.1; XM_005245362.1.
DR UniGene; Hs.288998; -.
DR PDB; 2M0R; NMR; -; A/B=1-104.
DR PDBsum; 2M0R; -.
DR ProteinModelPortal; Q9HCY8; -.
DR SMR; Q9HCY8; 1-104.
DR IntAct; Q9HCY8; 2.
DR MINT; MINT-5002007; -.
DR STRING; 9606.ENSP00000340463; -.
DR PhosphoSite; Q9HCY8; -.
DR DMDM; 20178118; -.
DR PaxDb; Q9HCY8; -.
DR PeptideAtlas; Q9HCY8; -.
DR PRIDE; Q9HCY8; -.
DR DNASU; 57402; -.
DR Ensembl; ENST00000344616; ENSP00000340463; ENSG00000189334.
DR Ensembl; ENST00000368701; ENSP00000357690; ENSG00000189334.
DR Ensembl; ENST00000368702; ENSP00000357691; ENSG00000189334.
DR Ensembl; ENST00000476873; ENSP00000420296; ENSG00000189334.
DR GeneID; 57402; -.
DR KEGG; hsa:57402; -.
DR UCSC; uc001fce.3; human.
DR CTD; 57402; -.
DR GeneCards; GC01M153586; -.
DR HGNC; HGNC:18901; S100A14.
DR HPA; HPA027613; -.
DR MIM; 607986; gene.
DR neXtProt; NX_Q9HCY8; -.
DR PharmGKB; PA134905502; -.
DR eggNOG; NOG46731; -.
DR HOGENOM; HOG000246968; -.
DR HOVERGEN; HBG001479; -.
DR InParanoid; Q9HCY8; -.
DR OMA; IANLGNC; -.
DR OrthoDB; EOG715Q6C; -.
DR PhylomeDB; Q9HCY8; -.
DR ChiTaRS; S100A14; human.
DR GenomeRNAi; 57402; -.
DR NextBio; 63504; -.
DR PRO; PR:Q9HCY8; -.
DR Bgee; Q9HCY8; -.
DR CleanEx; HS_S100A14; -.
DR Genevestigator; Q9HCY8; -.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR GO; GO:0042379; F:chemokine receptor binding; IMP:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0055074; P:calcium ion homeostasis; NAS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IEP:UniProtKB.
DR GO; GO:0071624; P:positive regulation of granulocyte chemotaxis; IDA:UniProtKB.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IDA:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:UniProtKB.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IDA:UniProtKB.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR InterPro; IPR028493; S100A14.
DR PANTHER; PTHR11639:SF4; PTHR11639:SF4; 1.
DR Pfam; PF01023; S_100; 1.
DR PROSITE; PS50222; EF_HAND_2; FALSE_NEG.
DR PROSITE; PS00303; S100_CABP; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Complete proteome; Cytoplasm;
KW Reference proteome.
FT CHAIN 1 104 Protein S100-A14.
FT /FTId=PRO_0000144021.
FT DOMAIN 27 61 EF-hand.
FT STRAND 8 11
FT HELIX 19 32
FT TURN 34 39
FT HELIX 43 53
FT TURN 55 57
FT HELIX 60 62
FT HELIX 65 71
FT HELIX 81 94
FT STRAND 98 100
SQ SEQUENCE 104 AA; 11662 MW; 97EF31A46B388E79 CRC64;
MGQCRSANAE DAQEFSDVER AIETLIKNFH QYSVEGGKET LTPSELRDLV TQQLPHLMPS
NCGLEEKIAN LGSCNDSKLE FRSFWELIGE AAKSVKLERP VRGH
//
ID S10AE_HUMAN Reviewed; 104 AA.
AC Q9HCY8; Q5RHT0;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=Protein S100-A14;
DE AltName: Full=S100 calcium-binding protein A14;
DE Short=S114;
GN Name=S100A14; Synonyms=S100A15;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=11944983; DOI=10.1006/geno.2002.6744;
RA Pietas A., Schluns K., Marenholz I., Schafer B.W., Heizmann C.W.,
RA Petersen I.;
RT "Molecular cloning and characterization of the human S100A14 gene
RT encoding a novel member of the S100 family.";
RL Genomics 79:513-522(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [5]
RP FUNCTION, AND INTERACTION WITH AGER.
RX PubMed=21559403; DOI=10.1371/journal.pone.0019375;
RA Jin Q., Chen H., Luo A., Ding F., Liu Z.;
RT "S100A14 stimulates cell proliferation and induces cell apoptosis at
RT different concentrations via receptor for advanced glycation end
RT products (RAGE).";
RL PLoS ONE 6:E19375-E19375(2011).
RN [6]
RP FUNCTION.
RX PubMed=22451655; DOI=10.1074/jbc.M111.326975;
RA Chen H., Yuan Y., Zhang C., Luo A., Ding F., Ma J., Yang S., Tian Y.,
RA Tong T., Zhan Q., Liu Z.;
RT "Involvement of S100A14 protein in cell invasion by affecting
RT expression and function of matrix metalloproteinase (MMP)-2 via p53-
RT dependent transcriptional regulation.";
RL J. Biol. Chem. 287:17109-17119(2012).
RN [7]
RP FUNCTION.
RX PubMed=22032898; DOI=10.1016/j.oraloncology.2011.10.001;
RA Sapkota D., Costea D.E., Blo M., Bruland O., Lorens J.B.,
RA Vasstrand E.N., Ibrahim S.O.;
RT "S100A14 inhibits proliferation of oral carcinoma derived cells
RT through G1-arrest.";
RL Oral Oncol. 48:219-225(2012).
RN [8]
RP STRUCTURE BY NMR, ABSENCE OF CALCIUM BINDING, AND SUBUNIT.
RX PubMed=23197251; DOI=10.1007/s00775-012-0963-3;
RA Bertini I., Borsi V., Cerofolini L., Das Gupta S., Fragai M.,
RA Luchinat C.;
RT "Solution structure and dynamics of human S100A14.";
RL J. Biol. Inorg. Chem. 18:183-194(2013).
CC -!- FUNCTION: Modulates P53/TP53 protein levels, and thereby plays a
CC role in the regulation of cell survival and apoptosis. Depending
CC on the context, it can promote cell proliferation or apoptosis.
CC Plays a role in the regulation of cell migration by modulating the
CC levels of MMP2, a matrix protease that is under transcriptional
CC control of P53/TP53. Does not bind calcium.
CC -!- SUBUNIT: Homodimer. Interacts with AGER.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in colon and at
CC moderate levels in thymus, kidney, liver, small intestine, and
CC lung. Low expression in heart and no expression is seen in brain,
CC skeletal muscle, spleen, placenta and peripheral blood leukocytes.
CC -!- SIMILARITY: Belongs to the S-100 family.
CC -!- SIMILARITY: Contains 1 EF-hand domain.
CC -!- CAUTION: Part of the residues that are essential for calcium
CC binding are not conserved, resulting in loss of calcium binding at
CC physiological calcium concentrations (PubMed:23197251).
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AY007220; AAG01893.1; -; mRNA.
DR EMBL; AF426828; AAM19206.1; -; Genomic_DNA.
DR EMBL; BX470102; CAI14759.1; -; Genomic_DNA.
DR EMBL; BC005019; AAH05019.1; -; mRNA.
DR RefSeq; NP_065723.1; NM_020672.2.
DR RefSeq; XP_005245419.1; XM_005245362.1.
DR UniGene; Hs.288998; -.
DR PDB; 2M0R; NMR; -; A/B=1-104.
DR PDBsum; 2M0R; -.
DR ProteinModelPortal; Q9HCY8; -.
DR SMR; Q9HCY8; 1-104.
DR IntAct; Q9HCY8; 2.
DR MINT; MINT-5002007; -.
DR STRING; 9606.ENSP00000340463; -.
DR PhosphoSite; Q9HCY8; -.
DR DMDM; 20178118; -.
DR PaxDb; Q9HCY8; -.
DR PeptideAtlas; Q9HCY8; -.
DR PRIDE; Q9HCY8; -.
DR DNASU; 57402; -.
DR Ensembl; ENST00000344616; ENSP00000340463; ENSG00000189334.
DR Ensembl; ENST00000368701; ENSP00000357690; ENSG00000189334.
DR Ensembl; ENST00000368702; ENSP00000357691; ENSG00000189334.
DR Ensembl; ENST00000476873; ENSP00000420296; ENSG00000189334.
DR GeneID; 57402; -.
DR KEGG; hsa:57402; -.
DR UCSC; uc001fce.3; human.
DR CTD; 57402; -.
DR GeneCards; GC01M153586; -.
DR HGNC; HGNC:18901; S100A14.
DR HPA; HPA027613; -.
DR MIM; 607986; gene.
DR neXtProt; NX_Q9HCY8; -.
DR PharmGKB; PA134905502; -.
DR eggNOG; NOG46731; -.
DR HOGENOM; HOG000246968; -.
DR HOVERGEN; HBG001479; -.
DR InParanoid; Q9HCY8; -.
DR OMA; IANLGNC; -.
DR OrthoDB; EOG715Q6C; -.
DR PhylomeDB; Q9HCY8; -.
DR ChiTaRS; S100A14; human.
DR GenomeRNAi; 57402; -.
DR NextBio; 63504; -.
DR PRO; PR:Q9HCY8; -.
DR Bgee; Q9HCY8; -.
DR CleanEx; HS_S100A14; -.
DR Genevestigator; Q9HCY8; -.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR GO; GO:0042379; F:chemokine receptor binding; IMP:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0055074; P:calcium ion homeostasis; NAS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IEP:UniProtKB.
DR GO; GO:0071624; P:positive regulation of granulocyte chemotaxis; IDA:UniProtKB.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IDA:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:UniProtKB.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IDA:UniProtKB.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR InterPro; IPR028493; S100A14.
DR PANTHER; PTHR11639:SF4; PTHR11639:SF4; 1.
DR Pfam; PF01023; S_100; 1.
DR PROSITE; PS50222; EF_HAND_2; FALSE_NEG.
DR PROSITE; PS00303; S100_CABP; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Complete proteome; Cytoplasm;
KW Reference proteome.
FT CHAIN 1 104 Protein S100-A14.
FT /FTId=PRO_0000144021.
FT DOMAIN 27 61 EF-hand.
FT STRAND 8 11
FT HELIX 19 32
FT TURN 34 39
FT HELIX 43 53
FT TURN 55 57
FT HELIX 60 62
FT HELIX 65 71
FT HELIX 81 94
FT STRAND 98 100
SQ SEQUENCE 104 AA; 11662 MW; 97EF31A46B388E79 CRC64;
MGQCRSANAE DAQEFSDVER AIETLIKNFH QYSVEGGKET LTPSELRDLV TQQLPHLMPS
NCGLEEKIAN LGSCNDSKLE FRSFWELIGE AAKSVKLERP VRGH
//
MIM
607986
*RECORD*
*FIELD* NO
607986
*FIELD* TI
*607986 S100 CALCIUM-BINDING PROTEIN A14; S100A14
;;BCMP84
*FIELD* TX
DESCRIPTION
read more
S100A14 is a member of a subfamily of proteins related by Ca(2+)-binding
motifs to the EF-hand Ca(2+)-binding protein superfamily.
CLONING
By analyzing a human lung cancer cell line subtractive cDNA library,
Pietas et al. (2002) identified and characterized S100A14, which encodes
a deduced 104-amino acid protein with a calculated molecular mass of
11,662 Da. It contains 2 EF-hand Ca(2+)-binding domains, a
myristoylation motif, a glycosylation site, and several potential
protein kinase phosphorylation sites. Pietas et al. (2002) also cloned
the mouse homolog. S100A14 shares 38% amino acid sequence identity with
human S100A13 (601989) and 97% similarity with mouse S100a14. Northern
blot analysis detected expression of an approximately 1.1-kb transcript
at highest levels in colon and at moderate levels in thymus, kidney,
liver, small intestine, and lung. Low expression of an approximately
1.35-kb transcript was detected in heart and no expression was seen in
brain, skeletal muscle, spleen, placenta, and peripheral blood
leukocytes. S100A14 was found to be overexpressed in ovary, breast, and
uterus tumors and underexpressed in kidney, rectum, and colon tumors.
Transfection experiments indicated localization to the cytoplasm,
particularly in the perinuclear region.
Using a proteomics approach to identify genes upregulated in breast
cancer, followed by database analysis and PCR of a breast carcinoma cell
line, Adam et al. (2003) cloned S100A14, which they called BCMP84.
BCMP84 expression in normal tissue was restricted to stratified squamous
epithelium of skin, cervix, and tonsil. Weak staining was seen in normal
breast ductal tissue, but strong immunoreactivity was detected in 10 of
58 (17%) breast cancer tissues. BCMP84 was expressed in the plasma
membrane of transiently transfected breast carcinoma cells.
GENE FUNCTION
By yeast 2-hybrid analysis, Adam et al. (2003) found that BCMP84
interacted with nucleobindin (NUCB1; 601323).
GENE STRUCTURE
Pietas et al. (2002) determined that the S100A14 gene contains 4 exons.
Exon 1 is untranslated.
MAPPING
By fluorescence in situ hybridization, Pietas et al. (2002) mapped the
S100A14 gene to chromosome 1q21 in a cluster with at least 15 other S100
genes.
MOLECULAR GENETICS
Chen et al. (2009) identified 4 SNPs in the S100A14 gene that were in
linkage disequilibrium among Han Chinese individuals. One SNP, 461G-A
(dbSNP rs11548103) in the 5-prime untranslated region, was shown to
diminish a binding site for the transcription factor P53 (TP53; 191170),
and was associated with decreased expression of S100A14 in vitro and in
vivo. A study of S100A14 RNA levels in surgically removed normal
esophageal tissues showed that individuals with the 461GG genotype had
significantly higher S100A14 RNA levels compared to those with at least
one 461A allele. A case-control study of 1,021 Han Chinese patients with
squamous cell esophageal carcinoma (133239) and 1,253 control subjects
found a significant association between the 461A allele and increased
susceptibility to esophageal cancer among smokers (odds ratio of 2.01
and 2.10 for the 461GA or 461AA genotypes, respectively, compared to the
461GG genotype). Chen et al. (2009) suggested that S100A14 may function
as a cancer suppressor in the P53 pathway and play a role in esophageal
carcinogenesis.
*FIELD* RF
1. Adam, P. J.; Boyd, R.; Tyson, K. L.; Fletcher, G. C.; Stamps, A.;
Hudson, L.; Poyser, H. R.; Redpath, N.; Griffiths, M.; Steers, G.;
Harris, A. L.; Patel, S.; Berry, J.; Loader, J. A.; Townsend, R. R.;
Daviet, L.; Legrain, P.; Parekh, R.; Terrett, J. A.: Comprehensive
proteomic analysis of breast cancer cell membranes reveals unique
proteins with potential roles in clinical cancer. J. Biol. Chem. 278:
6482-6489, 2003.
2. Chen, H.; Yu, D.; Luo, A.; Tan, W.; Zhang, C.; Zhao, D.; Yang,
M.; Liu, J.; Lin, D.; Liu, Z.: Functional role of S100A14 genetic
variants and their association with esophageal squamous cell carcinoma. Cancer
Res. 69: 3451-3457, 2009.
3. Pietas, A.; Schluns, K.; Marenholz, I.; Schafer, B. W.; Heizmann,
C. W.; Petersen, I.: Molecular cloning and characterization of the
human S100A14 gene encoding a novel member of the S100 family. Genomics 79:
513-522, 2002.
*FIELD* CN
Cassandra L. Kniffin - updated: 12/15/2009
Patricia A. Hartz - updated: 6/30/2005
*FIELD* CD
Carol A. Bocchini: 7/25/2003
*FIELD* ED
carol: 12/23/2009
ckniffin: 12/15/2009
mgross: 7/19/2005
terry: 6/30/2005
tkritzer: 7/28/2003
carol: 7/28/2003
*RECORD*
*FIELD* NO
607986
*FIELD* TI
*607986 S100 CALCIUM-BINDING PROTEIN A14; S100A14
;;BCMP84
*FIELD* TX
DESCRIPTION
read more
S100A14 is a member of a subfamily of proteins related by Ca(2+)-binding
motifs to the EF-hand Ca(2+)-binding protein superfamily.
CLONING
By analyzing a human lung cancer cell line subtractive cDNA library,
Pietas et al. (2002) identified and characterized S100A14, which encodes
a deduced 104-amino acid protein with a calculated molecular mass of
11,662 Da. It contains 2 EF-hand Ca(2+)-binding domains, a
myristoylation motif, a glycosylation site, and several potential
protein kinase phosphorylation sites. Pietas et al. (2002) also cloned
the mouse homolog. S100A14 shares 38% amino acid sequence identity with
human S100A13 (601989) and 97% similarity with mouse S100a14. Northern
blot analysis detected expression of an approximately 1.1-kb transcript
at highest levels in colon and at moderate levels in thymus, kidney,
liver, small intestine, and lung. Low expression of an approximately
1.35-kb transcript was detected in heart and no expression was seen in
brain, skeletal muscle, spleen, placenta, and peripheral blood
leukocytes. S100A14 was found to be overexpressed in ovary, breast, and
uterus tumors and underexpressed in kidney, rectum, and colon tumors.
Transfection experiments indicated localization to the cytoplasm,
particularly in the perinuclear region.
Using a proteomics approach to identify genes upregulated in breast
cancer, followed by database analysis and PCR of a breast carcinoma cell
line, Adam et al. (2003) cloned S100A14, which they called BCMP84.
BCMP84 expression in normal tissue was restricted to stratified squamous
epithelium of skin, cervix, and tonsil. Weak staining was seen in normal
breast ductal tissue, but strong immunoreactivity was detected in 10 of
58 (17%) breast cancer tissues. BCMP84 was expressed in the plasma
membrane of transiently transfected breast carcinoma cells.
GENE FUNCTION
By yeast 2-hybrid analysis, Adam et al. (2003) found that BCMP84
interacted with nucleobindin (NUCB1; 601323).
GENE STRUCTURE
Pietas et al. (2002) determined that the S100A14 gene contains 4 exons.
Exon 1 is untranslated.
MAPPING
By fluorescence in situ hybridization, Pietas et al. (2002) mapped the
S100A14 gene to chromosome 1q21 in a cluster with at least 15 other S100
genes.
MOLECULAR GENETICS
Chen et al. (2009) identified 4 SNPs in the S100A14 gene that were in
linkage disequilibrium among Han Chinese individuals. One SNP, 461G-A
(dbSNP rs11548103) in the 5-prime untranslated region, was shown to
diminish a binding site for the transcription factor P53 (TP53; 191170),
and was associated with decreased expression of S100A14 in vitro and in
vivo. A study of S100A14 RNA levels in surgically removed normal
esophageal tissues showed that individuals with the 461GG genotype had
significantly higher S100A14 RNA levels compared to those with at least
one 461A allele. A case-control study of 1,021 Han Chinese patients with
squamous cell esophageal carcinoma (133239) and 1,253 control subjects
found a significant association between the 461A allele and increased
susceptibility to esophageal cancer among smokers (odds ratio of 2.01
and 2.10 for the 461GA or 461AA genotypes, respectively, compared to the
461GG genotype). Chen et al. (2009) suggested that S100A14 may function
as a cancer suppressor in the P53 pathway and play a role in esophageal
carcinogenesis.
*FIELD* RF
1. Adam, P. J.; Boyd, R.; Tyson, K. L.; Fletcher, G. C.; Stamps, A.;
Hudson, L.; Poyser, H. R.; Redpath, N.; Griffiths, M.; Steers, G.;
Harris, A. L.; Patel, S.; Berry, J.; Loader, J. A.; Townsend, R. R.;
Daviet, L.; Legrain, P.; Parekh, R.; Terrett, J. A.: Comprehensive
proteomic analysis of breast cancer cell membranes reveals unique
proteins with potential roles in clinical cancer. J. Biol. Chem. 278:
6482-6489, 2003.
2. Chen, H.; Yu, D.; Luo, A.; Tan, W.; Zhang, C.; Zhao, D.; Yang,
M.; Liu, J.; Lin, D.; Liu, Z.: Functional role of S100A14 genetic
variants and their association with esophageal squamous cell carcinoma. Cancer
Res. 69: 3451-3457, 2009.
3. Pietas, A.; Schluns, K.; Marenholz, I.; Schafer, B. W.; Heizmann,
C. W.; Petersen, I.: Molecular cloning and characterization of the
human S100A14 gene encoding a novel member of the S100 family. Genomics 79:
513-522, 2002.
*FIELD* CN
Cassandra L. Kniffin - updated: 12/15/2009
Patricia A. Hartz - updated: 6/30/2005
*FIELD* CD
Carol A. Bocchini: 7/25/2003
*FIELD* ED
carol: 12/23/2009
ckniffin: 12/15/2009
mgross: 7/19/2005
terry: 6/30/2005
tkritzer: 7/28/2003
carol: 7/28/2003