ID S10A6_HUMAN Reviewed; 90 AA. AC P06703; D3DV39; Q5RHS4; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 02-SEP-2026, entry version 230. DE RecName: Full=Protein S100-A6; DE AltName: Full=Calcyclin; DE AltName: Full=Growth factor-inducible protein 2A9; DE AltName: Full=MLN 4; DE AltName: Full=Prolactin receptor-associated protein; DE Short=PRA; DE AltName: Full=S100 calcium-binding protein A6; GN Name=S100A6; Synonyms=CACY; 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 [MRNA]. RC TISSUE=Fibroblast; RX PubMed=3755724; DOI=10.1016/s0021-9258(18)67137-6; RA Calabretta B., Battini R., Kaczmarek L., de Riel J.K., Baserga R.; RT "Molecular cloning of the cDNA for a growth factor-inducible gene with RT strong homology to S-100, a calcium-binding protein."; RL J. Biol. Chem. 261:12628-12632(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3036810; DOI=10.1016/s0021-9258(18)47567-9; RA Ferrari S., Calabretta B., Deriel J.K., Battini R., Ghezzo F., Lauret E., RA Griffin C., Emanuel B.S., Gurrieri F., Baserga R.; RT "Structural and functional analysis of a growth-regulated gene, the human RT calcyclin."; RL J. Biol. Chem. 262:8325-8332(1987). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2448309; DOI=10.1016/s0021-9258(18)69220-8; RA Murphy L.C., Murphy L.J., Tsuyuki D., Duckworth M.L., Shiu R.P.C.; RT "Cloning and characterization of a cDNA encoding a highly conserved, RT putative calcium binding protein, identified by an anti-prolactin receptor RT antiserum."; RL J. Biol. Chem. 263:2397-2401(1988). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Wu J., Liu W., Zhou Y., Zhao Z., Peng X., Yuan J., Qiang B.; RT "Cloning of human calcyclin and calcyclin binding protein (CacyBP)."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [6] 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 [7] 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Placenta; 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 [9] RP PROTEIN SEQUENCE OF 27-31 AND 48-89. RC TISSUE=Platelet; RX PubMed=1482346; DOI=10.1016/0006-291x(92)90216-8; RA Tomida Y., Terasawa M., Kobayashi R., Hidaka H.; RT "Calcyclin and calvasculin exist in human platelets."; RL Biochem. Biophys. Res. Commun. 189:1310-1316(1992). RN [10] RP PROTEIN SEQUENCE OF 57-74. RX PubMed=2775283; DOI=10.1016/0006-291x(89)92166-9; RA Gabius H.J., Bardosi A., Gabius S., Hellmann K.P., Karas M., Kratzin H.; RT "Identification of a cell cycle-dependent gene product as a sialic acid- RT binding protein."; RL Biochem. Biophys. Res. Commun. 163:506-512(1989). RN [11] RP INTERACTION WITH SUGT1. RX PubMed=12746458; DOI=10.1074/jbc.m211518200; RA Nowotny M., Spiechowicz M., Jastrzebska B., Filipek A., Kitagawa K., RA Kuznicki J.; RT "Calcium-regulated interaction of Sgt1 with S100A6 (calcyclin) and other RT S100 proteins."; RL J. Biol. Chem. 278:26923-26928(2003). RN [12] RP SUBCELLULAR LOCATION. RX PubMed=12601007; DOI=10.1074/jbc.m212669200; RA Tomas A., Moss S.E.; RT "Calcium- and cell cycle-dependent association of annexin 11 with the RT nuclear envelope."; RL J. Biol. Chem. 278:20210-20216(2003). RN [13] RP INTERACTION WITH ANXA2; ANXA11 AND TROPOMYOSIN, AND SUBCELLULAR LOCATION. RX PubMed=19724273; DOI=10.1038/sj.bjc.6605289; RA Nedjadi T., Kitteringham N., Campbell F., Jenkins R.E., Park B.K., RA Navarro P., Ashcroft F., Tepikin A., Neoptolemos J.P., Costello E.; RT "S100A6 binds to annexin 2 in pancreatic cancer cells and promotes RT pancreatic cancer cell motility."; RL Br. J. Cancer 101:1145-1154(2009). RN [14] RP INTERACTION WITH TP53. RX PubMed=19819244; DOI=10.1016/j.jmb.2009.10.002; RA van Dieck J., Teufel D.P., Jaulent A.M., Fernandez-Fernandez M.R., RA Rutherford T.J., Wyslouch-Cieszynska A., Fersht A.R.; RT "Posttranslational modifications affect the interaction of S100 proteins RT with tumor suppressor p53."; RL J. Mol. Biol. 394:922-930(2009). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-40, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [16] RP INTERACTION WITH FKBP4. RX PubMed=20188096; DOI=10.1016/j.febslet.2010.02.055; RA Shimamoto S., Kubota Y., Tokumitsu H., Kobayashi R.; RT "S100 proteins regulate the interaction of Hsp90 with cyclophilin 40 and RT FKBP52 through their tetratricopeptide repeats."; RL FEBS Lett. 584:1119-1125(2010). RN [17] 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 [18] RP FUNCTION, INTERACTION WITH PPP5C, AND SUBCELLULAR LOCATION. RX PubMed=22399290; DOI=10.1074/jbc.m111.329771; RA Yamaguchi F., Umeda Y., Shimamoto S., Tsuchiya M., Tokumitsu H., Tokuda M., RA Kobayashi R.; RT "S100 proteins modulate protein phosphatase 5 function: a link between CA2+ RT signal transduction and protein dephosphorylation."; RL J. Biol. Chem. 287:13787-13798(2012). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [22] RP INTERACTION WITH ANXA11. RX PubMed=28469040; DOI=10.1126/scitranslmed.aad9157; RA Smith B.N., Topp S.D., Fallini C., Shibata H., Chen H.J., Troakes C., RA King A., Ticozzi N., Kenna K.P., Soragia-Gkazi A., Miller J.W., Sato A., RA Dias D.M., Jeon M., Vance C., Wong C.H., de Majo M., Kattuah W., RA Mitchell J.C., Scotter E.L., Parkin N.W., Sapp P.C., Nolan M., Nestor P.J., RA Simpson M., Weale M., Lek M., Baas F., Vianney de Jong J.M., RA Ten Asbroek A.L.M.A., Redondo A.G., Esteban-Perez J., Tiloca C., Verde F., RA Duga S., Leigh N., Pall H., Morrison K.E., Al-Chalabi A., Shaw P.J., RA Kirby J., Turner M.R., Talbot K., Hardiman O., Glass J.D., RA De Belleroche J., Maki M., Moss S.E., Miller C., Gellera C., Ratti A., RA Al-Sarraj S., Brown R.H. Jr., Silani V., Landers J.E., Shaw C.E.; RT "Mutations in the vesicular trafficking protein annexin A11 are associated RT with amyotrophic lateral sclerosis."; RL Sci. Transl. Med. 9:0-0(2017). RN [23] RP INTERACTION WITH TPPP. RX PubMed=33831707; DOI=10.1016/j.ceca.2021.102404; RA Doi S., Fujioka N., Ohtsuka S., Kondo R., Yamamoto M., Denda M., Magari M., RA Kanayama N., Hatano N., Morishita R., Hasegawa T., Tokumitsu H.; RT "Regulation of the tubulin polymerization-promoting protein by Ca2+/S100 RT proteins."; RL Cell Calcium 96:102404-102404(2021). RN [24] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH TOXOPLASMA GONDII SAG1 RP (MICROBIAL INFECTION). RX PubMed=34950858; DOI=10.1016/j.isci.2021.103514; RA Zhou L.J., Peng J., Chen M., Yao L.J., Zou W.H., He C.Y., Peng H.J.; RT "Toxoplasma gondii SAG1 targeting host cell S100A6 for parasite invasion RT and host immunity."; RL IScience 24:103514-103514(2021). RN [25] RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS), SUBUNIT, AND CALCIUM-BINDING. RX PubMed=11937060; DOI=10.1016/s0969-2126(02)00740-2; RA Otterbein L.R., Kordowska J., Witte-Hoffmann C., Wang C.-L.A., RA Dominguez R.; RT "Crystal structures of S100A6 in the Ca(2+)-free and Ca(2+)-bound states: RT the calcium sensor mechanism of S100 proteins revealed at atomic RT resolution."; RL Structure 10:557-567(2002). CC -!- FUNCTION: May function as calcium sensor and modulator, contributing to CC cellular calcium signaling. May function by interacting with other CC proteins, such as TPR-containing proteins, and indirectly play a role CC in many physiological processes such as the reorganization of the actin CC cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium CC binding is cooperative. {ECO:0000269|PubMed:22399290}. CC -!- FUNCTION: (Microbial infection) Facilitates attachment and invasion of CC Toxoplasma gondii parasites. {ECO:0000269|PubMed:34950858}. CC -!- SUBUNIT: Homodimer; head to tail assembly of 2 subunits. Interacts with CC CACYBP in a calcium-dependent manner. Interacts with ANXA2 and ANXA11 CC (via N-terminus). Interacts with SUGT1. Interacts with TP53; has higher CC affinity for TP53 that is phosphorylated on its N-terminal domain, and CC lower affinity for TP53 that is phosphorylated on its C-terminal CC domain. Interacts with tropomyosin. Interacts with FKBP4. Interacts CC with PPP5C (via TPR repeats); the interaction is calcium-dependent and CC modulates PPP5C activity. Interacts with TPPP; this interaction CC inhibits TPPP dimerization (PubMed:33831707). CC {ECO:0000269|PubMed:11937060, ECO:0000269|PubMed:12746458, CC ECO:0000269|PubMed:19724273, ECO:0000269|PubMed:19819244, CC ECO:0000269|PubMed:20188096, ECO:0000269|PubMed:22399290, CC ECO:0000269|PubMed:28469040, ECO:0000269|PubMed:33831707}. CC -!- SUBUNIT: (Microbial infection) Interacts with Toxoplasma gondii SAG1. CC {ECO:0000269|PubMed:34950858}. CC -!- INTERACTION: CC P06703; Q9HB71: CACYBP; NbExp=3; IntAct=EBI-352877, EBI-1047302; CC P06703; O95684: CEP43; NbExp=2; IntAct=EBI-352877, EBI-1266334; CC P06703; B3EWG3: FAM25A; NbExp=3; IntAct=EBI-352877, EBI-14240149; CC P06703; Q02790: FKBP4; NbExp=3; IntAct=EBI-352877, EBI-1047444; CC P06703; P52292: KPNA2; NbExp=3; IntAct=EBI-352877, EBI-349938; CC P06703; Q00987: MDM2; NbExp=2; IntAct=EBI-352877, EBI-389668; CC P06703; P35579: MYH9; NbExp=2; IntAct=EBI-352877, EBI-350338; CC P06703; P50542: PEX5; NbExp=3; IntAct=EBI-352877, EBI-597835; CC P06703; P04271: S100B; NbExp=6; IntAct=EBI-352877, EBI-458391; CC P06703; P04637: TP53; NbExp=3; IntAct=EBI-352877, EBI-366083; CC P06703; Q8TD43: TRPM4; NbExp=2; IntAct=EBI-352877, EBI-11723041; CC P06703; P61960: UFM1; NbExp=2; IntAct=EBI-352877, EBI-1045061; CC P06703; P26882: PPID; Xeno; NbExp=3; IntAct=EBI-352877, EBI-6477155; CC -!- SUBCELLULAR LOCATION: Nucleus envelope. Cytoplasm. Cell membrane; CC Peripheral membrane protein; Cytoplasmic side. CC -!- INDUCTION: Preferentially expressed when quiescent fibroblasts are CC stimulated to proliferate. It is inducible by growth factors and CC overexpressed in acute myeloid leukemias. CC -!- PTM: The N-terminus is blocked. CC -!- MISCELLANEOUS: This protein co-purified with the prolactin receptor. CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M14300; AAA35886.1; -; mRNA. DR EMBL; J02763; AAA51905.1; -; Genomic_DNA. DR EMBL; M18981; AAA51906.1; -; mRNA. DR EMBL; AY034480; AAK59702.1; -; Genomic_DNA. DR EMBL; BT006965; AAP35611.1; -; mRNA. DR EMBL; BX470102; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471121; EAW53318.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53320.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53321.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53322.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53323.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53324.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53325.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53326.1; -; Genomic_DNA. DR EMBL; BC001431; AAH01431.1; -; mRNA. DR EMBL; BC009017; AAH09017.1; -; mRNA. DR CCDS; CCDS1040.1; -. DR PIR; A28363; BCHUY. DR RefSeq; NP_055439.1; NM_014624.4. DR RefSeq; XP_016857522.1; XM_017002033.2. DR RefSeq; XP_054194088.1; XM_054338113.1. DR PDB; 1K8U; X-ray; 1.15 A; A=1-90. DR PDB; 1K96; X-ray; 1.44 A; A=1-90. DR PDB; 1K9K; X-ray; 1.76 A; A/B=1-90. DR PDB; 1K9P; X-ray; 1.90 A; A=1-90. DR PDB; 2M1K; NMR; -; B/D=1-90. DR PDB; 4YBH; X-ray; 2.40 A; B=1-90. DR AlphaFoldDB; P06703; -. DR BMRB; P06703; -. DR SMR; P06703; -. DR BioGRID; 112185; 287. DR CORUM; P06703; -. DR FunCoup; P06703; 409. DR IntAct; P06703; 169. DR MINT; P06703; -. DR NDEx; IQUERY-CP-S100A6; 3 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000357709; -. DR BindingDB; P06703; -. DR ChEMBL; CHEMBL6066977; -. DR DrugBank; DB11093; Calcium citrate. DR DrugBank; DB11348; Calcium Phosphate. DR DrugBank; DB14481; Calcium phosphate dihydrate. DR GlyGen; P06703; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P06703; -. DR MetOSite; P06703; -. DR PhosphoSitePlus; P06703; -. DR SwissPalm; P06703; -. DR BioMuta; S100A6; -. DR DMDM; 116509; -. DR jPOST; P06703; -. DR MassIVE; P06703; -. DR PaxDb; 9606-ENSP00000357709; -. DR PeptideAtlas; P06703; -. DR ProteomicsDB; 51911; -. DR Pumba; P06703; -. DR TopDownProteomics; P06703; -. DR Antibodypedia; 1680; 559 antibodies from 43 providers. DR CPTC; P06703; 3 antibodies. DR DNASU; 6277; -. DR Ensembl; ENST00000368719.9; ENSP00000357708.3; ENSG00000197956.11. DR Ensembl; ENST00000368720.6; ENSP00000357709.1; ENSG00000197956.11. DR Ensembl; ENST00000496817.5; ENSP00000473589.1; ENSG00000197956.11. DR Ensembl; ENST00000896466.1; ENSP00000566525.1; ENSG00000197956.11. DR Ensembl; ENST00000896467.1; ENSP00000566526.1; ENSG00000197956.11. DR Ensembl; ENST00000896468.1; ENSP00000566527.1; ENSG00000197956.11. DR Ensembl; ENST00000896469.1; ENSP00000566528.1; ENSG00000197956.11. DR Ensembl; ENST00000896470.1; ENSP00000566529.1; ENSG00000197956.11. DR Ensembl; ENST00000896471.1; ENSP00000566530.1; ENSG00000197956.11. DR Ensembl; ENST00000896472.1; ENSP00000566531.1; ENSG00000197956.11. DR Ensembl; ENST00000896473.1; ENSP00000566532.1; ENSG00000197956.11. DR Ensembl; ENST00000925440.1; ENSP00000595499.1; ENSG00000197956.11. DR Ensembl; ENST00000925441.1; ENSP00000595500.1; ENSG00000197956.11. DR Ensembl; ENST00000925442.1; ENSP00000595501.1; ENSG00000197956.11. DR Ensembl; ENST00000925443.1; ENSP00000595502.1; ENSG00000197956.11. DR GeneID; 6277; -. DR KEGG; hsa:6277; -. DR MANE-Select; ENST00000368719.9; ENSP00000357708.3; NM_014624.4; NP_055439.1. DR UCSC; uc001fbw.2; human. DR AGR; HGNC:10496; -. DR ClinPGx; PA34908; -. DR CTD; 6277; -. DR DisGeNET; 6277; -. DR GeneCards; S100A6; -. DR HGNC; HGNC:10496; S100A6. DR HPA; ENSG00000197956; Low tissue specificity. DR MIM; 114110; gene. DR OpenTargets; ENSG00000197956; -. DR VEuPathDB; HostDB:ENSG00000197956; -. DR eggNOG; ENOG502S6IN; Eukaryota. DR GeneTree; ENSGT00940000161896; -. DR InParanoid; P06703; -. DR OMA; LVVICHK; -. DR OrthoDB; 8881129at2759; -. DR PAN-GO; P06703; 5 GO annotations based on evolutionary models. DR PhylomeDB; P06703; -. DR PathwayCommons; P06703; -. DR SignaLink; P06703; -. DR SIGNOR; P06703; -. DR Agora; ENSG00000197956; Agora Nominated Target for Alzheimer's Disease. DR BioGRID-ORCS; 6277; 19 hits in 1158 CRISPR screens. DR ChiTaRS; S100A6; human. DR EvolutionaryTrace; P06703; -. DR GeneWiki; S100A6; -. DR GenomeRNAi; 6277; -. DR Pharos; P06703; Tbio. DR PRO; PR:P06703; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P06703; protein. DR Bgee; ENSG00000197956; Expressed in calcaneal tendon and 197 other cell types or tissues. DR ExpressionAtlas; P06703; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0031012; C:extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL. DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0001726; C:ruffle; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB. DR GO; GO:0048306; F:calcium-dependent protein binding; IDA:UniProtKB. DR GO; GO:0015075; F:monoatomic ion transmembrane transporter activity; IEA:Ensembl. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0044548; F:S100 protein binding; IPI:UniProtKB. DR GO; GO:0005523; F:tropomyosin binding; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl. DR GO; GO:0007409; P:axonogenesis; NAS:UniProtKB. DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; NAS:UniProtKB. DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB. DR CDD; cd05029; S-100A6; 1. DR FunFam; 1.10.238.10:FF:000044; Protein S100; 1. DR Gene3D; 1.10.238.10; EF-hand; 1. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR002048; EF_hand_dom. DR InterPro; IPR034118; S-100A6. DR InterPro; IPR001751; S100/CaBP7/8-like_CS. DR InterPro; IPR013787; S100_Ca-bd_sub. DR PANTHER; PTHR11639:SF80; PROTEIN S100-A6; 1. DR PANTHER; PTHR11639; S100 CALCIUM-BINDING PROTEIN; 1. DR Pfam; PF01023; S_100; 1. DR SMART; SM00054; EFh; 1. DR SMART; SM01394; S_100; 1. DR SUPFAM; SSF47473; EF-hand; 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; Acetylation; Calcium; Cell membrane; Cytoplasm; KW Direct protein sequencing; Membrane; Metal-binding; Nucleus; KW Phosphoprotein; Proteomics identification; Reference proteome; Repeat. FT CHAIN 1..90 FT /note="Protein S100-A6" FT /id="PRO_0000143984" FT DOMAIN 12..47 FT /note="EF-hand 1" FT /evidence="ECO:0000305" FT DOMAIN 48..83 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 28 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 33 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 61 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 63 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 65 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 67 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 72 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT MOD_RES 40 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 46 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 47 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P14069" FT MOD_RES 47 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P14069" FT VARIANT 27 FT /note="H -> R (in dbSNP:rs11974)" FT /id="VAR_011982" FT VARIANT 69 FT /note="N -> S (in dbSNP:rs1802581)" FT /id="VAR_011983" FT VARIANT 83 FT /note="I -> T (in dbSNP:rs1802582)" FT /id="VAR_011984" FT VARIANT 90 FT /note="G -> D (in dbSNP:rs2228293)" FT /id="VAR_029281" FT HELIX 4..20 FT /evidence="ECO:0007829|PDB:1K8U" FT STRAND 22..24 FT /evidence="ECO:0007829|PDB:1K8U" FT STRAND 28..30 FT /evidence="ECO:0007829|PDB:1K8U" FT HELIX 31..41 FT /evidence="ECO:0007829|PDB:1K8U" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:1K8U" FT HELIX 51..62 FT /evidence="ECO:0007829|PDB:1K8U" FT TURN 63..65 FT /evidence="ECO:0007829|PDB:1K8U" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:1K8U" FT HELIX 70..84 FT /evidence="ECO:0007829|PDB:1K8U" FT HELIX 86..88 FT /evidence="ECO:0007829|PDB:1K8U" SQ SEQUENCE 90 AA; 10180 MW; 860CBB1416ACBCA1 CRC64; MACPLDQAIG LLVAIFHKYS GREGDKHTLS KKELKELIQK ELTIGSKLQD AEIARLMEDL DRNKDQEVNF QEYVTFLGAL ALIYNEALKG //