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Protein S100-A1 (S-100 protein alpha chain) (S-100 protein subunit alpha) (S100 calcium-binding protein A1)

 S10A1_HUMAN             Reviewed;          94 AA.
P23297; B2R5D9; Q5T7Y3;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 172.
RecName: Full=Protein S100-A1;
AltName: Full=S-100 protein alpha chain;
AltName: Full=S-100 protein subunit alpha;
AltName: Full=S100 calcium-binding protein A1;
Name=S100A1; Synonyms=S100A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Heart;
PubMed=1384693; DOI=10.1021/bi00157a012;
Engelkamp D., Schaefer B.W., Erne P., Heizmann C.W.;
"S100 alpha, CAPL, and CACY: molecular cloning and expression analysis
of three calcium-binding proteins from human heart.";
Biochemistry 31:10258-10264(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Caudate nucleus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
INTERACTION WITH CACYBP.
PubMed=12042313; DOI=10.1074/jbc.M203602200;
Filipek A., Jastrzebska B., Nowotny M., Kuznicki J.;
"CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand
proteins of the S100 family.";
J. Biol. Chem. 277:28848-28852(2002).
[9]
INTERACTION WITH S100P, AND SUBCELLULAR LOCATION.
PubMed=15171681; DOI=10.1042/BJ20040142;
Wang G., Zhang S., Fernig D.G., Spiller D., Martin-Fernandez M.,
Zhang H., Ding Y., Rao Z., Rudland P.S., Barraclough R.;
"Heterodimeric interaction and interfaces of S100A1 and S100P.";
Biochem. J. 382:375-383(2004).
[10]
INTERACTION WITH RYR1 AND RYR2.
PubMed=18650434; DOI=10.1074/jbc.M804432200;
Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F.,
Weber D.J.;
"S100A1 and calmodulin compete for the same binding site on ryanodine
receptor.";
J. Biol. Chem. 283:26676-26683(2008).
[11]
INTERACTION WITH FKBP4.
PubMed=20188096; DOI=10.1016/j.febslet.2010.02.055;
Shimamoto S., Kubota Y., Tokumitsu H., Kobayashi R.;
"S100 proteins regulate the interaction of Hsp90 with cyclophilin 40
and FKBP52 through their tetratricopeptide repeats.";
FEBS Lett. 584:1119-1125(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
FUNCTION, AND INTERACTION WITH PPP5C.
PubMed=22399290; DOI=10.1074/jbc.M111.329771;
Yamaguchi F., Umeda Y., Shimamoto S., Tsuchiya M., Tokumitsu H.,
Tokuda M., Kobayashi R.;
"S100 proteins modulate protein phosphatase 5 function: a link between
CA2+ signal transduction and protein dephosphorylation.";
J. Biol. Chem. 287:13787-13798(2012).
[14]
STRUCTURE BY NMR, AND SUBUNIT.
PubMed=21296671; DOI=10.1016/j.jsb.2011.01.011;
Nowakowski M., Jaremko L., Jaremko M., Zhukov I., Belczyk A.,
Bierzynski A., Ejchart A.;
"Solution NMR structure and dynamics of human apo-S100A1 protein.";
J. Struct. Biol. 174:391-399(2011).
[15]
STRUCTURE BY NMR OF 2-94, AND S-NITROSYLATION AT CYS-86.
PubMed=22989881; DOI=10.1074/jbc.M112.418392;
Lenarcic Zivkovic M., Zareba-Koziol M., Zhukova L., Poznanski J.,
Zhukov I., Wyslouch-Cieszynska A.;
"Post-translational S-nitrosylation is an endogenous factor fine
tuning the properties of human S100A1 protein.";
J. Biol. Chem. 287:40457-40470(2012).
[16]
STRUCTURE BY NMR OF 2-94 IN COMPLEX WITH CALCIUM, AND FUNCTION.
PubMed=23351007; DOI=10.1021/bi3015407;
Nowakowski M., Ruszczynska-Bartnik K., Budzinska M., Jaremko L.,
Jaremko M., Zdanowski K., Bierzynski A., Ejchart A.;
"Impact of calcium binding and thionylation of S100A1 protein on its
nuclear magnetic resonance-derived structure and backbone dynamics.";
Biochemistry 52:1149-1159(2013).
-!- FUNCTION: Probably acts as a Ca(2+) signal transducer
(PubMed:22399290). In response to an increase in intracellular
Ca(2+) levels, binds calcium which triggers a conformational
change (PubMed:23351007). This conformational change allows
interaction of S1001A with specific target proteins, such as TPR-
containing proteins, and the modulation of their activity
(PubMed:22399290). {ECO:0000269|PubMed:22399290,
ECO:0000269|PubMed:23351007}.
-!- SUBUNIT: Dimer of either two alpha chains, or two beta chains, or
one alpha and one beta chain (PubMed:21296671). Also forms
heterodimers with S100P (PubMed:15171681). Interacts with AGER (By
similarity). Intreacts with CAPZA1 (By similarity). Interacts with
FKBP4 (PubMed:20188096). Interacts with RYR1 and RYR2
(PubMed:18650434). Interacts with CACYBP in a calcium-dependent
manner (PubMed:12042313). Interacts with PPP5C (via TPR repeats);
the interaction is calcium-dependent and modulates PPP5C activity
(PubMed:22399290). {ECO:0000250|UniProtKB:P35467,
ECO:0000269|PubMed:12042313, ECO:0000269|PubMed:15171681,
ECO:0000269|PubMed:18650434, ECO:0000269|PubMed:20188096,
ECO:0000269|PubMed:21296671, ECO:0000269|PubMed:22399290}.
-!- INTERACTION:
Self; NbExp=8; IntAct=EBI-743686, EBI-743686;
Q00987:MDM2; NbExp=2; IntAct=EBI-743686, EBI-389668;
Q9H8W4:PLEKHF2; NbExp=3; IntAct=EBI-743686, EBI-742388;
P29034:S100A2; NbExp=9; IntAct=EBI-743686, EBI-752230;
P26447:S100A4; NbExp=3; IntAct=EBI-743686, EBI-717058;
P04271:S100B; NbExp=17; IntAct=EBI-743686, EBI-458391;
P25815:S100P; NbExp=12; IntAct=EBI-743686, EBI-743700;
P04637:TP53; NbExp=2; IntAct=EBI-743686, EBI-366083;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15171681}.
-!- TISSUE SPECIFICITY: Highly prevalent in heart. Also found in
lesser quantities in skeletal muscle and brain.
{ECO:0000269|PubMed:1384693}.
-!- MISCELLANEOUS: Able to bind zinc in vitro; the binding sites are
different from the calcium binding sites. The physiological
relevance of zinc binding is unclear. Physiological concentrations
of potassium antagonize the binding of both divalent cations,
especially affecting the high-affinity calcium-binding sites.
{ECO:0000250|UniProtKB:P02639}.
-!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/S100A1ID44149ch1q21.html";
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EMBL; X58079; CAA41107.1; -; mRNA.
EMBL; AK312152; BAG35086.1; -; mRNA.
EMBL; BT006938; AAP35584.1; -; mRNA.
EMBL; AB451316; BAG70130.1; -; mRNA.
EMBL; AB451446; BAG70260.1; -; mRNA.
EMBL; AL162258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW53302.1; -; Genomic_DNA.
EMBL; BC014392; AAH14392.1; -; mRNA.
CCDS; CCDS1047.1; -.
PIR; A44470; BCHUIA.
RefSeq; NP_006262.1; NM_006271.1.
UniGene; Hs.515715; -.
PDB; 2L0P; NMR; -; A/B=1-94.
PDB; 2LHL; NMR; -; A/B=2-94.
PDB; 2LLS; NMR; -; A/B=2-94.
PDB; 2LLT; NMR; -; A/B=2-94.
PDB; 2LLU; NMR; -; A/B=2-94.
PDB; 2LP2; NMR; -; A/B=2-94.
PDB; 2LP3; NMR; -; A/B=2-94.
PDB; 2LUX; NMR; -; A/B=2-94.
PDB; 2M3W; NMR; -; A/B=2-94.
PDB; 5K89; X-ray; 2.25 A; A/C/H=1-94.
PDBsum; 2L0P; -.
PDBsum; 2LHL; -.
PDBsum; 2LLS; -.
PDBsum; 2LLT; -.
PDBsum; 2LLU; -.
PDBsum; 2LP2; -.
PDBsum; 2LP3; -.
PDBsum; 2LUX; -.
PDBsum; 2M3W; -.
PDBsum; 5K89; -.
ProteinModelPortal; P23297; -.
SMR; P23297; -.
BioGrid; 112179; 20.
IntAct; P23297; 12.
MINT; MINT-1543322; -.
STRING; 9606.ENSP00000292169; -.
DrugBank; DB00768; Olopatadine.
TCDB; 8.A.81.1.1; the s100 calcium-binding protein (s100) family.
iPTMnet; P23297; -.
PhosphoSitePlus; P23297; -.
BioMuta; S100A1; -.
DMDM; 134136; -.
MaxQB; P23297; -.
PaxDb; P23297; -.
PeptideAtlas; P23297; -.
PRIDE; P23297; -.
DNASU; 6271; -.
Ensembl; ENST00000292169; ENSP00000292169; ENSG00000160678.
GeneID; 6271; -.
KEGG; hsa:6271; -.
UCSC; uc001fck.1; human.
CTD; 6271; -.
DisGeNET; 6271; -.
EuPathDB; HostDB:ENSG00000160678.11; -.
GeneCards; S100A1; -.
HGNC; HGNC:10486; S100A1.
HPA; CAB002599; -.
HPA; HPA006462; -.
MIM; 176940; gene.
neXtProt; NX_P23297; -.
OpenTargets; ENSG00000160678; -.
PharmGKB; PA34898; -.
eggNOG; ENOG410IXZ2; Eukaryota.
eggNOG; ENOG4111987; LUCA.
GeneTree; ENSGT00760000119034; -.
HOGENOM; HOG000246968; -.
HOVERGEN; HBG001479; -.
InParanoid; P23297; -.
PhylomeDB; P23297; -.
TreeFam; TF332727; -.
Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
GeneWiki; S100_calcium-binding_protein_A1; -.
GenomeRNAi; 6271; -.
PRO; PR:P23297; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000160678; -.
CleanEx; HS_S100A1; -.
ExpressionAtlas; P23297; baseline and differential.
Genevisible; P23297; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0031430; C:M band; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; NAS:UniProtKB.
GO; GO:0016529; C:sarcoplasmic reticulum; IDA:UniProtKB.
GO; GO:0030018; C:Z disc; IEA:Ensembl.
GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0044548; F:S100 protein binding; IPI:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; IEA:Ensembl.
GO; GO:0008016; P:regulation of heart contraction; NAS:UniProtKB.
GO; GO:0021762; P:substantia nigra development; IEP:UniProtKB.
GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
CDD; cd05025; S-100A1; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR028486; S100-A1.
InterPro; IPR001751; S100/CaBP-9k_CS.
InterPro; IPR013787; S100_Ca-bd_sub.
PANTHER; PTHR11639:SF66; PTHR11639:SF66; 1.
Pfam; PF00036; EF-hand_1; 1.
Pfam; PF01023; S_100; 1.
SMART; SM00054; EFh; 1.
SMART; SM01394; S_100; 1.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 1.
PROSITE; PS50222; EF_HAND_2; 1.
PROSITE; PS00303; S100_CABP; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Cytoplasm; Metal-binding;
Reference proteome; Repeat; S-nitrosylation.
CHAIN 1 94 Protein S100-A1.
/FTId=PRO_0000143961.
DOMAIN 13 48 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 50 85 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 20 33 1; low affinity.
{ECO:0000269|PubMed:23351007}.
CA_BIND 63 74 2; high affinity.
{ECO:0000269|PubMed:23351007}.
MOD_RES 86 86 S-nitrosocysteine.
{ECO:0000269|PubMed:22989881}.
HELIX 4 20 {ECO:0000244|PDB:2L0P}.
STRAND 22 24 {ECO:0000244|PDB:2L0P}.
STRAND 26 30 {ECO:0000244|PDB:2LHL}.
HELIX 31 41 {ECO:0000244|PDB:2L0P}.
HELIX 45 48 {ECO:0000244|PDB:2L0P}.
HELIX 52 64 {ECO:0000244|PDB:2L0P}.
TURN 65 67 {ECO:0000244|PDB:2L0P}.
STRAND 68 70 {ECO:0000244|PDB:2LHL}.
HELIX 72 87 {ECO:0000244|PDB:2L0P}.
TURN 88 90 {ECO:0000244|PDB:2L0P}.
SEQUENCE 94 AA; 10546 MW; AD5E53AF326B25D2 CRC64;
MGSELETAME TLINVFHAHS GKEGDKYKLS KKELKELLQT ELSGFLDAQK DVDAVDKVMK
ELDENGDGEV DFQEYVVLVA ALTVACNNFF WENS


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20-272-190120 S100 - Mouse monoclonal [6G1] to S100; S100 calcium-binding protein A1; S-100 protein alpha subunit; S-100 protein alpha chain Monoclonal 0.1 mg
18-272-196435 S100 - Rabbit polyclonal to S100; S100 calcium-binding protein A1; S-100 protein alpha subunit; S-100 protein alpha chain Polyclonal 1 ml
18-272-196436 S100 prediluted - Rabbit polyclonal to S100 prediluted; S100 calcium-binding protein A1; S-100 protein alpha subunit; S-100 protein alpha chain Polyclonal 7 ml
20-272-190393 S100 alpha 6 - Mouse monoclonal [CACY - 100] to S100 alpha 6; S100 calcium-binding protein A6; Calcyclin; Prolactin receptor-associated protein; PRA; Growth factor-inducible protein 2A9; MLN 4 Monoclo 0.1 ml
10-663-45642 S100A1 Protein Human - S100 calcium-binding protein A1; S-100 protein alpha subunit; S-100 protein alpha chain N_A 0.01 mg
10-663-45642 S100A1 Protein Human - S100 calcium-binding protein A1; S-100 protein alpha subunit; S-100 protein alpha chain N_A 0.025 mg
10-663-45642 S100A1 Protein Human - S100 calcium-binding protein A1; S-100 protein alpha subunit; S-100 protein alpha chain N_A 0.005 mg
20-272-190119 S100 - Astrocyte Marker - Mouse monoclonal [4E3 ] to S100 - Astrocyte Marker; S100 calcium-binding protein A1; S-100 protein alpha subunit; S-100 protein alpha chain Monoclonal 0.1 mg
E0567h ELISA kit Homo sapiens,Human,Protein S100-B,S100 calcium-binding protein B,S-100 protein beta chain,S-100 protein subunit beta,S100B 96T
U0567h CLIA Homo sapiens,Human,Protein S100-B,S100 calcium-binding protein B,S-100 protein beta chain,S-100 protein subunit beta,S100B 96T
E0567h ELISA Homo sapiens,Human,Protein S100-B,S100 calcium-binding protein B,S-100 protein beta chain,S-100 protein subunit beta,S100B 96T
U0567Rb CLIA Oryctolagus cuniculus,Protein S100-B,Rabbit,S100 calcium-binding protein B,S-100 protein beta chain,S-100 protein subunit beta,S100B 96T
E0567Rb ELISA Oryctolagus cuniculus,Protein S100-B,Rabbit,S100 calcium-binding protein B,S-100 protein beta chain,S-100 protein subunit beta,S100B 96T
E0567Rb ELISA kit Oryctolagus cuniculus,Protein S100-B,Rabbit,S100 calcium-binding protein B,S-100 protein beta chain,S-100 protein subunit beta,S100B 96T
EIAAB36663 Homo sapiens,Human,Protein S100-A7A,S100 calcium-binding protein A15,S100 calcium-binding protein A7A,S100 calcium-binding protein A7-like 1,S100A15,S100A7A,S100A7L1
E0567r ELISA kit Protein S100-B,Rat,Rattus norvegicus,S100 calcium-binding protein B,S-100 protein beta chain,S-100 protein subunit beta,S100b 96T
U0567r CLIA Protein S100-B,Rat,Rattus norvegicus,S100 calcium-binding protein B,S-100 protein beta chain,S-100 protein subunit beta,S100b 96T
E0567m ELISA kit Mouse,Mus musculus,Protein S100-B,S100 calcium-binding protein B,S-100 protein beta chain,S-100 protein subunit beta,S100b 96T
E0567b ELISA kit Bos taurus,Bovine,Protein S100-B,S100 calcium-binding protein B,S-100 protein beta chain,S-100 protein subunit beta,S100B 96T


 

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