ID   S10AE_HUMAN             Reviewed;         104 AA.
AC   Q9HCY8; Q5RHT0;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 177.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP   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 encoding
RT   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., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., 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., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., 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., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., 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 project:
RT   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., Buerckstuemmer T.,
RA   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 products
RT   (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 expression
RT   and function of matrix metalloproteinase (MMP)-2 via p53-dependent
RT   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., Vasstrand E.N.,
RA   Ibrahim S.O.;
RT   "S100A14 inhibits proliferation of oral carcinoma derived cells through G1-
RT   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., 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 role
CC       in the regulation of cell survival and apoptosis. Depending on the
CC       context, it can promote cell proliferation or apoptosis. Plays a role
CC       in the regulation of cell migration by modulating the levels of MMP2, a
CC       matrix protease that is under transcriptional control of P53/TP53. Does
CC       not bind calcium. {ECO:0000269|PubMed:21559403,
CC       ECO:0000269|PubMed:22032898, ECO:0000269|PubMed:22451655}.
CC   -!- SUBUNIT: Homodimer. Interacts with AGER. {ECO:0000269|PubMed:21559403,
CC       ECO:0000269|PubMed:23197251}.
CC   -!- INTERACTION:
CC       Q9HCY8; P43360: MAGEA6; NbExp=3; IntAct=EBI-751842, EBI-1045155;
CC       Q9HCY8; Q99584: S100A13; NbExp=5; IntAct=EBI-751842, EBI-721909;
CC       Q9HCY8; Q96FQ6: S100A16; NbExp=11; IntAct=EBI-751842, EBI-751850;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11944983}.
CC   -!- TISSUE SPECIFICITY: Expressed at highest levels in colon and at
CC       moderate levels in thymus, kidney, liver, small intestine, and lung.
CC       Low expression in heart and no expression is seen in brain, skeletal
CC       muscle, spleen, placenta and peripheral blood leukocytes.
CC       {ECO:0000269|PubMed:11944983}.
CC   -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
CC   -!- CAUTION: Part of the residues that are essential for calcium binding
CC       are not conserved, resulting in loss of calcium binding at
CC       physiological calcium concentrations. {ECO:0000305|PubMed:23197251}.
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DR   EMBL; AY007220; AAG01893.1; -; mRNA.
DR   EMBL; AF426828; AAM19206.1; -; Genomic_DNA.
DR   EMBL; BX470102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC005019; AAH05019.1; -; mRNA.
DR   CCDS; CCDS1046.1; -.
DR   RefSeq; NP_065723.1; NM_020672.2.
DR   RefSeq; XP_005245419.1; XM_005245362.1.
DR   RefSeq; XP_016857364.1; XM_017001875.1.
DR   PDB; 2M0R; NMR; -; A/B=1-104.
DR   PDBsum; 2M0R; -.
DR   AlphaFoldDB; Q9HCY8; -.
DR   BMRB; Q9HCY8; -.
DR   SMR; Q9HCY8; -.
DR   BioGRID; 121504; 66.
DR   IntAct; Q9HCY8; 23.
DR   MINT; Q9HCY8; -.
DR   STRING; 9606.ENSP00000357691; -.
DR   GlyGen; Q9HCY8; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9HCY8; -.
DR   PhosphoSitePlus; Q9HCY8; -.
DR   SwissPalm; Q9HCY8; -.
DR   BioMuta; S100A14; -.
DR   DMDM; 20178118; -.
DR   EPD; Q9HCY8; -.
DR   jPOST; Q9HCY8; -.
DR   MassIVE; Q9HCY8; -.
DR   MaxQB; Q9HCY8; -.
DR   PaxDb; 9606-ENSP00000357691; -.
DR   PeptideAtlas; Q9HCY8; -.
DR   PRIDE; Q9HCY8; -.
DR   ProteomicsDB; 81807; -.
DR   TopDownProteomics; Q9HCY8; -.
DR   Antibodypedia; 34129; 170 antibodies from 23 providers.
DR   DNASU; 57402; -.
DR   Ensembl; ENST00000344616.4; ENSP00000340463.2; ENSG00000189334.9.
DR   Ensembl; ENST00000368701.5; ENSP00000357690.1; ENSG00000189334.9.
DR   Ensembl; ENST00000368702.5; ENSP00000357691.1; ENSG00000189334.9.
DR   Ensembl; ENST00000476873.5; ENSP00000420296.1; ENSG00000189334.9.
DR   GeneID; 57402; -.
DR   KEGG; hsa:57402; -.
DR   MANE-Select; ENST00000344616.4; ENSP00000340463.2; NM_020672.3; NP_065723.1.
DR   UCSC; uc001fce.4; human.
DR   AGR; HGNC:18901; -.
DR   CTD; 57402; -.
DR   DisGeNET; 57402; -.
DR   GeneCards; S100A14; -.
DR   HGNC; HGNC:18901; S100A14.
DR   HPA; ENSG00000189334; Group enriched (esophagus, vagina).
DR   MIM; 607986; gene.
DR   neXtProt; NX_Q9HCY8; -.
DR   OpenTargets; ENSG00000189334; -.
DR   PharmGKB; PA134905502; -.
DR   VEuPathDB; HostDB:ENSG00000189334; -.
DR   eggNOG; ENOG502SB9V; Eukaryota.
DR   GeneTree; ENSGT00940000161706; -.
DR   HOGENOM; CLU_138624_3_0_1; -.
DR   InParanoid; Q9HCY8; -.
DR   OMA; NFHQYSA; -.
DR   OrthoDB; 3954907at2759; -.
DR   PhylomeDB; Q9HCY8; -.
DR   TreeFam; TF332727; -.
DR   PathwayCommons; Q9HCY8; -.
DR   SignaLink; Q9HCY8; -.
DR   BioGRID-ORCS; 57402; 16 hits in 1155 CRISPR screens.
DR   ChiTaRS; S100A14; human.
DR   GenomeRNAi; 57402; -.
DR   Pharos; Q9HCY8; Tbio.
DR   PRO; PR:Q9HCY8; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9HCY8; Protein.
DR   Bgee; ENSG00000189334; Expressed in lower esophagus mucosa and 138 other cell types or tissues.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
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   CDD; cd05022; S-100A13; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR013787; S100_Ca-bd_sub.
DR   PANTHER; PTHR11639:SF4; PROTEIN S100-A14; 1.
DR   PANTHER; PTHR11639; S100 CALCIUM-BINDING PROTEIN; 1.
DR   Pfam; PF01023; S_100; 1.
DR   SMART; SM01394; S_100; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   Genevisible; Q9HCY8; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Apoptosis; Cytoplasm; Reference proteome.
FT   CHAIN           1..104
FT                   /note="Protein S100-A14"
FT                   /id="PRO_0000144021"
FT   DOMAIN          27..61
FT                   /note="EF-hand"
FT   STRAND          8..11
FT                   /evidence="ECO:0007829|PDB:2M0R"
FT   HELIX           19..32
FT                   /evidence="ECO:0007829|PDB:2M0R"
FT   TURN            34..39
FT                   /evidence="ECO:0007829|PDB:2M0R"
FT   HELIX           43..53
FT                   /evidence="ECO:0007829|PDB:2M0R"
FT   TURN            55..57
FT                   /evidence="ECO:0007829|PDB:2M0R"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:2M0R"
FT   HELIX           65..71
FT                   /evidence="ECO:0007829|PDB:2M0R"
FT   HELIX           81..94
FT                   /evidence="ECO:0007829|PDB:2M0R"
FT   STRAND          98..100
FT                   /evidence="ECO:0007829|PDB:2M0R"
SQ   SEQUENCE   104 AA;  11662 MW;  97EF31A46B388E79 CRC64;
     MGQCRSANAE DAQEFSDVER AIETLIKNFH QYSVEGGKET LTPSELRDLV TQQLPHLMPS
     NCGLEEKIAN LGSCNDSKLE FRSFWELIGE AAKSVKLERP VRGH
//