S10A6_HUMAN
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 03-AUG-2022, entry version 211.
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 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 -!- 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 -!- INTERACTION:
CC P06703; Q9HB71: CACYBP; NbExp=2; IntAct=EBI-352877, EBI-1047302;
CC P06703; O95684: CEP43; NbExp=2; IntAct=EBI-352877, EBI-1266334;
CC P06703; B3EWG5: FAM25C; 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; 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}.
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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_014624.3.
DR RefSeq; XP_016857522.1; XM_017002033.1.
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 PDBsum; 1K8U; -.
DR PDBsum; 1K96; -.
DR PDBsum; 1K9K; -.
DR PDBsum; 1K9P; -.
DR PDBsum; 2M1K; -.
DR PDBsum; 4YBH; -.
DR AlphaFoldDB; P06703; -.
DR BMRB; P06703; -.
DR SMR; P06703; -.
DR BioGRID; 112185; 222.
DR CORUM; P06703; -.
DR IntAct; P06703; 44.
DR MINT; P06703; -.
DR STRING; 9606.ENSP00000357709; -.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR iPTMnet; P06703; -.
DR MetOSite; P06703; -.
DR PhosphoSitePlus; P06703; -.
DR SwissPalm; P06703; -.
DR BioMuta; S100A6; -.
DR DMDM; 116509; -.
DR DOSAC-COBS-2DPAGE; P06703; -.
DR EPD; P06703; -.
DR jPOST; P06703; -.
DR MassIVE; P06703; -.
DR MaxQB; P06703; -.
DR PaxDb; P06703; -.
DR PeptideAtlas; P06703; -.
DR PRIDE; P06703; -.
DR ProteomicsDB; 51911; -.
DR TopDownProteomics; P06703; -.
DR Antibodypedia; 1680; 536 antibodies from 40 providers.
DR CPTC; P06703; 3 antibodies.
DR DNASU; 6277; -.
DR Ensembl; ENST00000368719.9; ENSP00000357708.3; ENSG00000197956.10.
DR Ensembl; ENST00000368720.6; ENSP00000357709.1; ENSG00000197956.10.
DR Ensembl; ENST00000496817.5; ENSP00000473589.1; ENSG00000197956.10.
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 CTD; 6277; -.
DR DisGeNET; 6277; -.
DR GeneCards; S100A6; -.
DR HGNC; HGNC:10496; S100A6.
DR HPA; ENSG00000197956; Low tissue specificity.
DR MIM; 114110; gene.
DR neXtProt; NX_P06703; -.
DR OpenTargets; ENSG00000197956; -.
DR PharmGKB; PA34908; -.
DR VEuPathDB; HostDB:ENSG00000197956; -.
DR eggNOG; ENOG502S6IN; Eukaryota.
DR GeneTree; ENSGT00940000161896; -.
DR InParanoid; P06703; -.
DR OMA; LVVICHK; -.
DR OrthoDB; 1581517at2759; -.
DR PhylomeDB; P06703; -.
DR TreeFam; TF332727; -.
DR PathwayCommons; P06703; -.
DR SignaLink; P06703; -.
DR SIGNOR; P06703; -.
DR BioGRID-ORCS; 6277; 19 hits in 1080 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 195 other tissues.
DR ExpressionAtlas; P06703; baseline and differential.
DR Genevisible; P06703; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
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: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 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 Pfam; PF01023; S_100; 1.
DR SMART; SM00054; EFh; 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; Acetylation; Calcium; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; 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
