S10A1_HUMAN
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 03-AUG-2022, entry version 205.
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="http://atlasgeneticsoncology.org/Genes/S100A1ID44149ch1q21.html";
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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; 28.
DR IntAct; P23297; 23.
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; P23297; -.
DR PeptideAtlas; P23297; -.
DR PRIDE; P23297; -.
DR ProteomicsDB; 54079; -.
DR Antibodypedia; 1674; 1162 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 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; NEFFVDS; -.
DR OrthoDB; 1495576at2759; -.
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 1082 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 157 other tissues.
DR ExpressionAtlas; P23297; baseline and differential.
DR Genevisible; P23297; HS.
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 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 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; 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; 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
