S10AG_HUMAN
ID S10AG_HUMAN Reviewed; 103 AA.
AC Q96FQ6; A8K439; D3DV52; Q5RHS6;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Protein S100-A16;
DE AltName: Full=Aging-associated gene 13 protein;
DE AltName: Full=Protein S100-F;
DE AltName: Full=S100 calcium-binding protein A16;
GN Name=S100A16 {ECO:0000312|HGNC:HGNC:20441}; Synonyms=S100F; ORFNames=AAG13;
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], AND TISSUE SPECIFICITY.
RX PubMed=14684152; DOI=10.1016/j.bbrc.2003.11.115;
RA Marenholz I., Heizmann C.W.;
RT "S100A16, a ubiquitously expressed EF-hand protein which is up-regulated in
RT tumors.";
RL Biochem. Biophys. Res. Commun. 313:237-244(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Keratinocyte;
RA Morita K.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim J.W.;
RT "Identification of a human aging related gene.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Cervix;
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 [8]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, CALCIUM-BINDING, AND TISSUE SPECIFICITY.
RX PubMed=17030513; DOI=10.1074/jbc.m605798200;
RA Sturchler E., Cox J.A., Durussel I., Weibel M., Heizmann C.W.;
RT "S100A16, a novel calcium-binding protein of the EF-hand superfamily.";
RL J. Biol. Chem. 281:38905-38917(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), STRUCTURE BY NMR, SUBUNIT, AND
RP CALCIUM-BINDING DOMAIN.
RX PubMed=21046186; DOI=10.1007/s00775-010-0721-3;
RA Babini E., Bertini I., Borsi V., Calderone V., Hu X., Luchinat C.,
RA Parigi G.;
RT "Structural characterization of human S100A16, a low-affinity calcium
RT binder.";
RL J. Biol. Inorg. Chem. 16:243-256(2011).
CC -!- FUNCTION: Calcium-binding protein. Binds one calcium ion per monomer
CC (PubMed:17030513). Can promote differentiation of adipocytes (in vitro)
CC (By similarity). Overexpression in preadipocytes increases their
CC proliferation, enhances adipogenesis and reduces insulin-stimulated
CC glucose uptake (By similarity). {ECO:0000250|UniProtKB:Q9D708,
CC ECO:0000269|PubMed:17030513}.
CC -!- SUBUNIT: Homodimer (PubMed:17030513, PubMed:21046186). Interacts with
CC TP53 (By similarity). {ECO:0000250|UniProtKB:Q9D708,
CC ECO:0000269|PubMed:17030513, ECO:0000269|PubMed:21046186}.
CC -!- INTERACTION:
CC Q96FQ6; Q9HCY8: S100A14; NbExp=11; IntAct=EBI-751850, EBI-751842;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:17030513}.
CC Cytoplasm {ECO:0000269|PubMed:17030513}. Note=Primarily nucleolar. A
CC high intracellular calcium level induces nucleolar exit and
CC nucleocytoplasmic transport, whereas a low intracellular calcium level
CC leads to nuclear translocation and accumulation within specific region
CC of nucleoli (PubMed:17030513).
CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:14684152). Highly expressed in
CC esophagus, adipose tissues and colon. Expressed at lower level in lung,
CC brain, pancreas and skeletal muscle. Expression is up-regulated in
CC tumors of bladder, lung, thyroid gland, pancreas and ovary
CC (PubMed:14684152). Expressed in astrocytes (PubMed:17030513).
CC {ECO:0000269|PubMed:14684152, ECO:0000269|PubMed:17030513}.
CC -!- DOMAIN: S100A16 proteins, but not other S100 proteins, have only one
CC functional Ca(2+) binding site per monomer. Upon Ca(2+) binding,
CC undergoes conformational changes leading to the exposure of hydrophobic
CC patches which could be implicated in the Ca(2+) -dependent nuclear
CC export. Binds Zn(2+). Ca(2+) and Zn(2+) do not bind to the same site.
CC Does not bind Cu(2+). {ECO:0000269|PubMed:17030513}.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; AJ585980; CAE51865.1; -; Genomic_DNA.
DR EMBL; AY221961; AAP46152.1; -; mRNA.
DR EMBL; AY762098; AAW88319.1; -; mRNA.
DR EMBL; AK290804; BAF83493.1; -; mRNA.
DR EMBL; BX470102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53303.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53304.1; -; Genomic_DNA.
DR EMBL; BC010541; AAH10541.1; -; mRNA.
DR EMBL; BC019099; AAH19099.1; -; mRNA.
DR EMBL; BC095462; AAH95462.1; -; mRNA.
DR CCDS; CCDS1045.1; -.
DR RefSeq; NP_001303936.1; NM_001317007.1.
DR RefSeq; NP_001303937.1; NM_001317008.1.
DR RefSeq; NP_525127.1; NM_080388.2.
DR PDB; 2L50; NMR; -; A/B=2-103.
DR PDB; 2L51; NMR; -; A/B=2-103.
DR PDB; 3NXA; X-ray; 2.10 A; A/B/C/D=3-102.
DR PDBsum; 2L50; -.
DR PDBsum; 2L51; -.
DR PDBsum; 3NXA; -.
DR AlphaFoldDB; Q96FQ6; -.
DR BMRB; Q96FQ6; -.
DR SMR; Q96FQ6; -.
DR BioGRID; 126627; 58.
DR IntAct; Q96FQ6; 15.
DR MINT; Q96FQ6; -.
DR STRING; 9606.ENSP00000357693; -.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR TCDB; 8.A.81.1.3; the s100 calcium-binding protein (s100) family.
DR iPTMnet; Q96FQ6; -.
DR MetOSite; Q96FQ6; -.
DR PhosphoSitePlus; Q96FQ6; -.
DR SwissPalm; Q96FQ6; -.
DR BioMuta; S100A16; -.
DR DMDM; 20178113; -.
DR SWISS-2DPAGE; Q96FQ6; -.
DR EPD; Q96FQ6; -.
DR jPOST; Q96FQ6; -.
DR MassIVE; Q96FQ6; -.
DR MaxQB; Q96FQ6; -.
DR PaxDb; Q96FQ6; -.
DR PeptideAtlas; Q96FQ6; -.
DR PRIDE; Q96FQ6; -.
DR ProteomicsDB; 76549; -.
DR TopDownProteomics; Q96FQ6; -.
DR Antibodypedia; 47029; 197 antibodies from 29 providers.
DR DNASU; 140576; -.
DR Ensembl; ENST00000368703.6; ENSP00000357692.1; ENSG00000188643.11.
DR Ensembl; ENST00000368704.5; ENSP00000357693.1; ENSG00000188643.11.
DR Ensembl; ENST00000368705.2; ENSP00000357694.1; ENSG00000188643.11.
DR Ensembl; ENST00000368706.9; ENSP00000357695.3; ENSG00000188643.11.
DR GeneID; 140576; -.
DR KEGG; hsa:140576; -.
DR MANE-Select; ENST00000368706.9; ENSP00000357695.3; NM_080388.3; NP_525127.1.
DR UCSC; uc001fcc.5; human.
DR CTD; 140576; -.
DR DisGeNET; 140576; -.
DR GeneCards; S100A16; -.
DR HGNC; HGNC:20441; S100A16.
DR HPA; ENSG00000188643; Tissue enhanced (esophagus).
DR MIM; 617437; gene.
DR neXtProt; NX_Q96FQ6; -.
DR OpenTargets; ENSG00000188643; -.
DR PharmGKB; PA134931606; -.
DR VEuPathDB; HostDB:ENSG00000188643; -.
DR eggNOG; ENOG502S6F9; Eukaryota.
DR GeneTree; ENSGT00390000000920; -.
DR HOGENOM; CLU_138624_3_1_1; -.
DR InParanoid; Q96FQ6; -.
DR OMA; DCYTDLE; -.
DR OrthoDB; 1506806at2759; -.
DR PhylomeDB; Q96FQ6; -.
DR TreeFam; TF332727; -.
DR PathwayCommons; Q96FQ6; -.
DR SignaLink; Q96FQ6; -.
DR BioGRID-ORCS; 140576; 9 hits in 1077 CRISPR screens.
DR ChiTaRS; S100A16; human.
DR EvolutionaryTrace; Q96FQ6; -.
DR GeneWiki; S100A16; -.
DR GenomeRNAi; 140576; -.
DR Pharos; Q96FQ6; Tbio.
DR PRO; PR:Q96FQ6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96FQ6; protein.
DR Bgee; ENSG00000188643; Expressed in lower esophagus mucosa and 177 other tissues.
DR Genevisible; Q96FQ6; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR DisProt; DP02652; -.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028485; S100-A16.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR PANTHER; PTHR11639:SF76; PTHR11639:SF76; 1.
DR Pfam; PF01023; S_100; 1.
DR SMART; SM01394; S_100; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00303; S100_CABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..103
FT /note="Protein S100-A16"
FT /id="PRO_0000144023"
FT DOMAIN 12..47
FT /note="EF-hand 1; degenerate"
FT /evidence="ECO:0000305|PubMed:14684152"
FT DOMAIN 54..89
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000303|PubMed:17030513"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000303|PubMed:17030513"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000303|PubMed:17030513"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000303|PubMed:17030513"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000303|PubMed:17030513"
FT HELIX 7..21
FT /evidence="ECO:0007829|PDB:3NXA"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:2L50"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:3NXA"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:3NXA"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2L50"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:3NXA"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:2L51"
FT HELIX 76..87
FT /evidence="ECO:0007829|PDB:3NXA"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:3NXA"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:3NXA"
SQ SEQUENCE 103 AA; 11801 MW; 7D00C08F85697A6C CRC64;
MSDCYTELEK AVIVLVENFY KYVSKYSLVK NKISKSSFRE MLQKELNHML SDTGNRKAAD
KLIQNLDANH DGRISFDEYW TLIGGITGPI AKLIHEQEQQ SSS
