ID S10A1_HUMAN Reviewed; 94 AA. AC P23297; B2R5D9; Q5T7Y3; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 214. DE RecName: Full=Protein S100-A1; DE AltName: Full=S-100 protein alpha chain; DE AltName: Full=S-100 protein subunit alpha; DE AltName: Full=S100 calcium-binding protein A1; GN Name=S100A1; Synonyms=S100A; 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], AND TISSUE SPECIFICITY. RC TISSUE=Heart; RX PubMed=1384693; DOI=10.1021/bi00157a012; RA Engelkamp D., Schaefer B.W., Erne P., Heizmann C.W.; RT "S100 alpha, CAPL, and CACY: molecular cloning and expression analysis of RT three calcium-binding proteins from human heart."; RL Biochemistry 31:10258-10264(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Caudate nucleus; 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 [3] 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 (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., RA Nomura N.; RT "Human protein factory for converting the transcriptome into an in vitro- RT expressed proteome."; RL Nat. Methods 5:1011-1017(2008). 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., 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=Skin; 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. RX PubMed=11717446; DOI=10.1073/pnas.241393598; RA Most P., Bernotat J., Ehlermann P., Pleger S.T., Reppel M., Boerries M., RA Niroomand F., Pieske B., Janssen P.M., Eschenhagen T., Karczewski P., RA Smith G.L., Koch W.J., Katus H.A., Remppis A.; RT "S100A1: a regulator of myocardial contractility."; RL Proc. Natl. Acad. Sci. U.S.A. 98:13889-13894(2001). RN [9] RP INTERACTION WITH CACYBP. RX PubMed=12042313; DOI=10.1074/jbc.m203602200; RA Filipek A., Jastrzebska B., Nowotny M., Kuznicki J.; RT "CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand RT proteins of the S100 family."; RL J. Biol. Chem. 277:28848-28852(2002). RN [10] RP FUNCTION, INTERACTION WITH ATP2A2 AND PLN, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=12804600; DOI=10.1016/s0006-291x(03)00987-2; RA Kiewitz R., Acklin C., Schaefer B.W., Maco B., Uhrik B., Wuytack F., RA Erne P., Heizmann C.W.; RT "Ca2+ -dependent interaction of S100A1 with the sarcoplasmic reticulum Ca2+ RT -ATPase2a and phospholamban in the human heart."; RL Biochem. Biophys. Res. Commun. 306:550-557(2003). RN [11] RP INTERACTION WITH S100P, AND SUBCELLULAR LOCATION. RX PubMed=15171681; DOI=10.1042/bj20040142; RA Wang G., Zhang S., Fernig D.G., Spiller D., Martin-Fernandez M., Zhang H., RA Ding Y., Rao Z., Rudland P.S., Barraclough R.; RT "Heterodimeric interaction and interfaces of S100A1 and S100P."; RL Biochem. J. 382:375-383(2004). RN [12] RP GLUTATHIONYLATION. RX PubMed=15885104; DOI=10.1111/j.1742-4658.2005.04680.x; RA Goch G., Vdovenko S., Kozlowska H., Bierzynski A.; RT "Affinity of S100A1 protein for calcium increases dramatically upon RT glutathionylation."; RL FEBS J. 272:2557-2565(2005). RN [13] RP INTERACTION WITH RYR1 AND RYR2. RX PubMed=18650434; DOI=10.1074/jbc.m804432200; RA Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F., RA Weber D.J.; RT "S100A1 and calmodulin compete for the same binding site on ryanodine RT receptor."; RL J. Biol. Chem. 283:26676-26683(2008). RN [14] 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 [15] 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 [16] RP FUNCTION, AND INTERACTION WITH PPP5C. 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 [17] RP STRUCTURE BY NMR, AND SUBUNIT. RX PubMed=21296671; DOI=10.1016/j.jsb.2011.01.011; RA Nowakowski M., Jaremko L., Jaremko M., Zhukov I., Belczyk A., RA Bierzynski A., Ejchart A.; RT "Solution NMR structure and dynamics of human apo-S100A1 protein."; RL J. Struct. Biol. 174:391-399(2011). RN [18] RP STRUCTURE BY NMR OF 2-94, AND S-NITROSYLATION AT CYS-86. RX PubMed=22989881; DOI=10.1074/jbc.m112.418392; RA Lenarcic Zivkovic M., Zareba-Koziol M., Zhukova L., Poznanski J., RA Zhukov I., Wyslouch-Cieszynska A.; RT "Post-translational S-nitrosylation is an endogenous factor fine tuning the RT properties of human S100A1 protein."; RL J. Biol. Chem. 287:40457-40470(2012). RN [19] RP STRUCTURE BY NMR OF 2-94 IN COMPLEX WITH CALCIUM, AND FUNCTION. RX PubMed=23351007; DOI=10.1021/bi3015407; RA Nowakowski M., Ruszczynska-Bartnik K., Budzinska M., Jaremko L., RA Jaremko M., Zdanowski K., Bierzynski A., Ejchart A.; RT "Impact of calcium binding and thionylation of S100A1 protein on its RT nuclear magnetic resonance-derived structure and backbone dynamics."; RL Biochemistry 52:1149-1159(2013). RN [20] {ECO:0007744|PDB:5K89} RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH CALCIUM. RX PubMed=28368280; DOI=10.1107/s2053230x17003983; RA Melville Z., Aligholizadeh E., McKnight L.E., Weber D.J., Pozharski E., RA Weber D.J.; RT "X-ray crystal structure of human calcium-bound S100A1."; RL Acta Crystallogr. F 73:215-221(2017). CC -!- FUNCTION: Small calcium binding protein that plays important roles in CC several biological processes such as Ca(2+) homeostasis, chondrocyte CC biology and cardiomyocyte regulation (PubMed:12804600). In response to CC an increase in intracellular Ca(2+) levels, binds calcium which CC triggers conformational changes (PubMed:23351007). These changes allow CC interactions with specific target proteins and modulate their activity CC (PubMed:22399290). Regulates a network in cardiomyocytes controlling CC sarcoplasmic reticulum Ca(2+) cycling and mitochondrial function CC through interaction with the ryanodine receptors RYR1 and RYR2, CC sarcoplasmic reticulum Ca(2+)-ATPase/ATP2A2 and mitochondrial F1-ATPase CC (PubMed:12804600). Facilitates diastolic Ca(2+) dissociation and CC myofilament mechanics in order to improve relaxation during diastole CC (PubMed:11717446). {ECO:0000269|PubMed:11717446, CC ECO:0000269|PubMed:12804600, ECO:0000269|PubMed:22399290, CC ECO:0000269|PubMed:23351007}. CC -!- SUBUNIT: Dimer of either two alpha chains, or two beta chains, or one CC alpha and one beta chain (PubMed:21296671). Also forms heterodimers CC with S100P (PubMed:15171681). Interacts with AGER (By similarity). CC Interacts with CAPZA1 (By similarity). Interacts with FKBP4 CC (PubMed:20188096). Interacts with RYR1 and RYR2 (PubMed:18650434). CC Interacts with CACYBP in a calcium-dependent manner (PubMed:12042313). CC Interacts with PPP5C (via TPR repeats); the interaction is calcium- CC dependent and modulates PPP5C activity (PubMed:22399290). Interacts CC with ATP2A2 and PLN in a Ca(2+)-dependent manner (PubMed:12804600). CC Interacts with mitochondrial F1-ATPase subunits ATP5F1A and ATP5F1B; CC these interactions increase F1-ATPase activity (By similarity). CC {ECO:0000250|UniProtKB:P35467, ECO:0000250|UniProtKB:P56565, CC ECO:0000269|PubMed:12042313, ECO:0000269|PubMed:15171681, CC ECO:0000269|PubMed:18650434, ECO:0000269|PubMed:20188096, CC ECO:0000269|PubMed:21296671, ECO:0000269|PubMed:22399290}. CC -!- INTERACTION: CC P23297; Q00994: BEX3; NbExp=3; IntAct=EBI-743686, EBI-741753; CC P23297; P52907: CAPZA1; NbExp=2; IntAct=EBI-743686, EBI-355586; CC P23297; Q00987: MDM2; NbExp=2; IntAct=EBI-743686, EBI-389668; CC P23297; O15151: MDM4; NbExp=2; IntAct=EBI-743686, EBI-398437; CC P23297; P35579: MYH9; NbExp=3; IntAct=EBI-743686, EBI-350338; CC P23297; Q96CV9: OPTN; NbExp=3; IntAct=EBI-743686, EBI-748974; CC P23297; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-743686, EBI-742388; CC P23297; P23297: S100A1; NbExp=9; IntAct=EBI-743686, EBI-743686; CC P23297; P29034: S100A2; NbExp=7; IntAct=EBI-743686, EBI-752230; CC P23297; P33764: S100A3; NbExp=3; IntAct=EBI-743686, EBI-1044747; CC P23297; P26447: S100A4; NbExp=4; IntAct=EBI-743686, EBI-717058; CC P23297; P04271: S100B; NbExp=25; IntAct=EBI-743686, EBI-458391; CC P23297; P25815: S100P; NbExp=11; IntAct=EBI-743686, EBI-743700; CC P23297; Q8WXG8: S100Z; NbExp=7; IntAct=EBI-743686, EBI-12198403; CC P23297; P32418: SLC8A1; NbExp=3; IntAct=EBI-743686, EBI-2682189; CC P23297; P04637: TP53; NbExp=3; IntAct=EBI-743686, EBI-366083; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15171681}. CC Sarcoplasmic reticulum {ECO:0000269|PubMed:12804600}. Mitochondrion CC {ECO:0000250|UniProtKB:P56565}. CC -!- TISSUE SPECIFICITY: Highly prevalent in heart (PubMed:12804600, CC PubMed:1384693). Also found in lesser quantities in skeletal muscle and CC brain (PubMed:1384693). {ECO:0000269|PubMed:12804600, CC ECO:0000269|PubMed:1384693}. CC -!- PTM: Glutathionylated; glutathionylation increases affinity to calcium CC about 10-fold. {ECO:0000269|PubMed:15885104}. CC -!- MISCELLANEOUS: Able to bind zinc in vitro; the binding sites are CC different from the calcium binding sites. The physiological relevance CC of zinc binding is unclear. Physiological concentrations of potassium CC antagonize the binding of both divalent cations, especially affecting CC the high-affinity calcium-binding sites. CC {ECO:0000250|UniProtKB:P02639}. CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44149/S100A1"; 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; X58079; CAA41107.1; -; mRNA. DR EMBL; AK312152; BAG35086.1; -; mRNA. DR EMBL; BT006938; AAP35584.1; -; mRNA. DR EMBL; AB451316; BAG70130.1; -; mRNA. DR EMBL; AB451446; BAG70260.1; -; mRNA. DR EMBL; AL162258; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471121; EAW53302.1; -; Genomic_DNA. DR EMBL; BC014392; AAH14392.1; -; mRNA. DR CCDS; CCDS1047.1; -. DR PIR; A44470; BCHUIA. DR RefSeq; NP_006262.1; NM_006271.1. DR PDB; 2L0P; NMR; -; A/B=1-94. DR PDB; 2LHL; NMR; -; A/B=2-94. DR PDB; 2LLS; NMR; -; A/B=2-94. DR PDB; 2LLT; NMR; -; A/B=2-94. DR PDB; 2LLU; NMR; -; A/B=2-94. DR PDB; 2LP2; NMR; -; A/B=2-94. DR PDB; 2LP3; NMR; -; A/B=2-94. DR PDB; 2LUX; NMR; -; A/B=2-94. DR PDB; 2M3W; NMR; -; A/B=2-94. DR PDB; 5K89; X-ray; 2.25 A; A/C/H=1-94. DR PDBsum; 2L0P; -. DR PDBsum; 2LHL; -. DR PDBsum; 2LLS; -. DR PDBsum; 2LLT; -. DR PDBsum; 2LLU; -. DR PDBsum; 2LP2; -. DR PDBsum; 2LP3; -. DR PDBsum; 2LUX; -. DR PDBsum; 2M3W; -. DR PDBsum; 5K89; -. DR AlphaFoldDB; P23297; -. DR BMRB; P23297; -. DR SMR; P23297; -. DR BioGRID; 112179; 33. DR IntAct; P23297; 24. DR MINT; P23297; -. DR STRING; 9606.ENSP00000292169; -. DR DrugBank; DB00768; Olopatadine. DR TCDB; 8.A.81.1.1; the s100 calcium-binding protein (s100) family. DR iPTMnet; P23297; -. DR PhosphoSitePlus; P23297; -. DR BioMuta; S100A1; -. DR DMDM; 134136; -. DR CPTAC; CPTAC-1452; -. DR EPD; P23297; -. DR jPOST; P23297; -. DR MassIVE; P23297; -. DR MaxQB; P23297; -. DR PaxDb; 9606-ENSP00000292169; -. DR PeptideAtlas; P23297; -. DR ProteomicsDB; 54079; -. DR Antibodypedia; 1674; 1268 antibodies from 44 providers. DR DNASU; 6271; -. DR Ensembl; ENST00000292169.6; ENSP00000292169.2; ENSG00000160678.12. DR GeneID; 6271; -. DR KEGG; hsa:6271; -. DR MANE-Select; ENST00000292169.6; ENSP00000292169.2; NM_006271.2; NP_006262.1. DR UCSC; uc001fck.1; human. DR AGR; HGNC:10486; -. DR CTD; 6271; -. DR DisGeNET; 6271; -. DR GeneCards; S100A1; -. DR HGNC; HGNC:10486; S100A1. DR HPA; ENSG00000160678; Tissue enhanced (heart muscle, skeletal muscle, tongue). DR MIM; 176940; gene. DR neXtProt; NX_P23297; -. DR OpenTargets; ENSG00000160678; -. DR PharmGKB; PA34898; -. DR VEuPathDB; HostDB:ENSG00000160678; -. DR eggNOG; ENOG502SSF0; Eukaryota. DR GeneTree; ENSGT00940000160475; -. DR HOGENOM; CLU_138624_2_1_1; -. DR InParanoid; P23297; -. DR OMA; ACNSFFW; -. DR OrthoDB; 4234580at2759; -. DR PhylomeDB; P23297; -. DR TreeFam; TF332727; -. DR PathwayCommons; P23297; -. DR Reactome; R-HSA-1236974; ER-Phagosome pathway. DR Reactome; R-HSA-166058; MyD88:MAL(TIRAP) cascade initiated on plasma membrane. DR Reactome; R-HSA-5602498; MyD88 deficiency (TLR2/4). DR Reactome; R-HSA-5603041; IRAK4 deficiency (TLR2/4). DR Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand. DR SignaLink; P23297; -. DR BioGRID-ORCS; 6271; 13 hits in 1158 CRISPR screens. DR ChiTaRS; S100A1; human. DR GeneWiki; S100_calcium-binding_protein_A1; -. DR GenomeRNAi; 6271; -. DR Pharos; P23297; Tbio. DR PRO; PR:P23297; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P23297; Protein. DR Bgee; ENSG00000160678; Expressed in apex of heart and 158 other cell types or tissues. DR ExpressionAtlas; P23297; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; NAS:UniProtKB. DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0051117; F:ATPase binding; IPI: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:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0044548; F:S100 protein binding; IPI:UniProtKB. DR GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB. DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IDA:BHF-UCL. DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IDA:BHF-UCL. DR GO; GO:0008016; P:regulation of heart contraction; NAS:UniProtKB. DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB. DR CDD; cd05025; S-100A1; 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; IPR028486; S100-A1. DR InterPro; IPR001751; S100/CaBP7/8-like_CS. DR InterPro; IPR013787; S100_Ca-bd_sub. DR PANTHER; PTHR11639:SF134; PROTEIN S100-A1-RELATED; 1. DR PANTHER; PTHR11639; S100 CALCIUM-BINDING PROTEIN; 1. DR Pfam; PF00036; EF-hand_1; 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. DR Genevisible; P23297; HS. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Cytoplasm; Glutathionylation; Metal-binding; KW Mitochondrion; Reference proteome; Repeat; S-nitrosylation; KW Sarcoplasmic reticulum. FT CHAIN 1..94 FT /note="Protein S100-A1" FT /id="PRO_0000143961" FT DOMAIN 13..48 FT /note="EF-hand 1" FT /evidence="ECO:0000305" FT DOMAIN 50..85 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 /ligand_note="low affinity" FT /evidence="ECO:0000269|PubMed:23351007, FT ECO:0000269|PubMed:28368280" FT BINDING 33 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /ligand_note="low affinity" FT /evidence="ECO:0000269|PubMed:23351007, FT ECO:0000269|PubMed:28368280" FT BINDING 63 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /ligand_note="high affinity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:23351007, ECO:0000269|PubMed:28368280" FT BINDING 65 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /ligand_note="high affinity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:23351007, ECO:0000269|PubMed:28368280" FT BINDING 67 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /ligand_note="high affinity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:23351007, ECO:0000269|PubMed:28368280" FT BINDING 69 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /ligand_note="high affinity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:23351007, ECO:0000269|PubMed:28368280" FT BINDING 74 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /ligand_note="high affinity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:23351007, ECO:0000269|PubMed:28368280" FT MOD_RES 86 FT /note="S-nitrosocysteine" FT /evidence="ECO:0000269|PubMed:22989881" FT HELIX 4..20 FT /evidence="ECO:0007829|PDB:5K89" FT STRAND 22..24 FT /evidence="ECO:0007829|PDB:5K89" FT STRAND 26..30 FT /evidence="ECO:0007829|PDB:2LHL" FT HELIX 31..41 FT /evidence="ECO:0007829|PDB:5K89" FT HELIX 45..48 FT /evidence="ECO:0007829|PDB:2L0P" FT HELIX 50..53 FT /evidence="ECO:0007829|PDB:2LUX" FT HELIX 54..62 FT /evidence="ECO:0007829|PDB:5K89" FT STRAND 67..71 FT /evidence="ECO:0007829|PDB:5K89" FT HELIX 72..89 FT /evidence="ECO:0007829|PDB:5K89" SQ SEQUENCE 94 AA; 10546 MW; AD5E53AF326B25D2 CRC64; MGSELETAME TLINVFHAHS GKEGDKYKLS KKELKELLQT ELSGFLDAQK DVDAVDKVMK ELDENGDGEV DFQEYVVLVA ALTVACNNFF WENS //