Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Protein S100-A14 (S100 calcium-binding protein A14) (S114)

 S10AE_HUMAN             Reviewed;         104 AA.
Q9HCY8; Q5RHT0;
16-APR-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
28-FEB-2018, entry version 141.
RecName: Full=Protein S100-A14;
AltName: Full=S100 calcium-binding protein A14;
Short=S114;
Name=S100A14; Synonyms=S100A15;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=11944983; DOI=10.1006/geno.2002.6744;
Pietas A., Schluns K., Marenholz I., Schafer B.W., Heizmann C.W.,
Petersen I.;
"Molecular cloning and characterization of the human S100A14 gene
encoding a novel member of the S100 family.";
Genomics 79:513-522(2002).
[2]
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
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).
[4]
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).
[5]
FUNCTION, AND INTERACTION WITH AGER.
PubMed=21559403; DOI=10.1371/journal.pone.0019375;
Jin Q., Chen H., Luo A., Ding F., Liu Z.;
"S100A14 stimulates cell proliferation and induces cell apoptosis at
different concentrations via receptor for advanced glycation end
products (RAGE).";
PLoS ONE 6:E19375-E19375(2011).
[6]
FUNCTION.
PubMed=22451655; DOI=10.1074/jbc.M111.326975;
Chen H., Yuan Y., Zhang C., Luo A., Ding F., Ma J., Yang S., Tian Y.,
Tong T., Zhan Q., Liu Z.;
"Involvement of S100A14 protein in cell invasion by affecting
expression and function of matrix metalloproteinase (MMP)-2 via p53-
dependent transcriptional regulation.";
J. Biol. Chem. 287:17109-17119(2012).
[7]
FUNCTION.
PubMed=22032898; DOI=10.1016/j.oraloncology.2011.10.001;
Sapkota D., Costea D.E., Blo M., Bruland O., Lorens J.B.,
Vasstrand E.N., Ibrahim S.O.;
"S100A14 inhibits proliferation of oral carcinoma derived cells
through G1-arrest.";
Oral Oncol. 48:219-225(2012).
[8]
STRUCTURE BY NMR, ABSENCE OF CALCIUM-BINDING, AND SUBUNIT.
PubMed=23197251; DOI=10.1007/s00775-012-0963-3;
Bertini I., Borsi V., Cerofolini L., Das Gupta S., Fragai M.,
Luchinat C.;
"Solution structure and dynamics of human S100A14.";
J. Biol. Inorg. Chem. 18:183-194(2013).
-!- FUNCTION: Modulates P53/TP53 protein levels, and thereby plays a
role in the regulation of cell survival and apoptosis. Depending
on the context, it can promote cell proliferation or apoptosis.
Plays a role in the regulation of cell migration by modulating the
levels of MMP2, a matrix protease that is under transcriptional
control of P53/TP53. Does not bind calcium.
{ECO:0000269|PubMed:21559403, ECO:0000269|PubMed:22032898,
ECO:0000269|PubMed:22451655}.
-!- SUBUNIT: Homodimer. Interacts with AGER.
{ECO:0000269|PubMed:21559403, ECO:0000269|PubMed:23197251}.
-!- INTERACTION:
Q8WYB5:KAT6B; NbExp=4; IntAct=EBI-751842, EBI-948029;
P43360:MAGEA6; NbExp=3; IntAct=EBI-751842, EBI-1045155;
Q96FQ6:S100A16; NbExp=8; IntAct=EBI-751842, EBI-751850;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11944983}.
-!- TISSUE SPECIFICITY: Expressed at highest levels in colon and at
moderate levels in thymus, kidney, liver, small intestine, and
lung. Low expression in heart and no expression is seen in brain,
skeletal muscle, spleen, placenta and peripheral blood leukocytes.
{ECO:0000269|PubMed:11944983}.
-!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
-!- CAUTION: Part of the residues that are essential for calcium
binding are not conserved, resulting in loss of calcium binding at
physiological calcium concentrations.
{ECO:0000305|PubMed:23197251}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY007220; AAG01893.1; -; mRNA.
EMBL; AF426828; AAM19206.1; -; Genomic_DNA.
EMBL; BX470102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC005019; AAH05019.1; -; mRNA.
CCDS; CCDS1046.1; -.
RefSeq; NP_065723.1; NM_020672.2.
RefSeq; XP_005245419.1; XM_005245362.1.
RefSeq; XP_016857364.1; XM_017001875.1.
UniGene; Hs.288998; -.
PDB; 2M0R; NMR; -; A/B=1-104.
PDBsum; 2M0R; -.
ProteinModelPortal; Q9HCY8; -.
SMR; Q9HCY8; -.
BioGrid; 121504; 22.
IntAct; Q9HCY8; 12.
MINT; Q9HCY8; -.
STRING; 9606.ENSP00000340463; -.
iPTMnet; Q9HCY8; -.
PhosphoSitePlus; Q9HCY8; -.
SwissPalm; Q9HCY8; -.
BioMuta; S100A14; -.
DMDM; 20178118; -.
EPD; Q9HCY8; -.
MaxQB; Q9HCY8; -.
PaxDb; Q9HCY8; -.
PeptideAtlas; Q9HCY8; -.
PRIDE; Q9HCY8; -.
TopDownProteomics; Q9HCY8; -.
DNASU; 57402; -.
Ensembl; ENST00000344616; ENSP00000340463; ENSG00000189334.
Ensembl; ENST00000368701; ENSP00000357690; ENSG00000189334.
Ensembl; ENST00000368702; ENSP00000357691; ENSG00000189334.
Ensembl; ENST00000476873; ENSP00000420296; ENSG00000189334.
GeneID; 57402; -.
KEGG; hsa:57402; -.
UCSC; uc001fce.4; human.
CTD; 57402; -.
DisGeNET; 57402; -.
EuPathDB; HostDB:ENSG00000189334.8; -.
GeneCards; S100A14; -.
HGNC; HGNC:18901; S100A14.
HPA; HPA027613; -.
MIM; 607986; gene.
neXtProt; NX_Q9HCY8; -.
OpenTargets; ENSG00000189334; -.
PharmGKB; PA134905502; -.
eggNOG; ENOG410IZKB; Eukaryota.
eggNOG; ENOG4111EF5; LUCA.
GeneTree; ENSGT00530000063972; -.
HOGENOM; HOG000246968; -.
HOVERGEN; HBG001479; -.
InParanoid; Q9HCY8; -.
OMA; NLGNCND; -.
OrthoDB; EOG091G0YGX; -.
PhylomeDB; Q9HCY8; -.
TreeFam; TF332727; -.
ChiTaRS; S100A14; human.
GenomeRNAi; 57402; -.
PRO; PR:Q9HCY8; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000189334; -.
CleanEx; HS_S100A14; -.
Genevisible; Q9HCY8; HS.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
GO; GO:0042379; F:chemokine receptor binding; IMP:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0055074; P:calcium ion homeostasis; NAS:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; IEP:UniProtKB.
GO; GO:0071624; P:positive regulation of granulocyte chemotaxis; IDA:UniProtKB.
GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IDA:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:UniProtKB.
GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IDA:UniProtKB.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR013787; S100_Ca-bd_sub.
InterPro; IPR028493; S100A14.
PANTHER; PTHR11639:SF4; PTHR11639:SF4; 1.
Pfam; PF01023; S_100; 1.
SMART; SM01394; S_100; 1.
SUPFAM; SSF47473; SSF47473; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Complete proteome; Cytoplasm;
Reference proteome.
CHAIN 1 104 Protein S100-A14.
/FTId=PRO_0000144021.
DOMAIN 27 61 EF-hand.
STRAND 8 11 {ECO:0000244|PDB:2M0R}.
HELIX 19 32 {ECO:0000244|PDB:2M0R}.
TURN 34 39 {ECO:0000244|PDB:2M0R}.
HELIX 43 53 {ECO:0000244|PDB:2M0R}.
TURN 55 57 {ECO:0000244|PDB:2M0R}.
HELIX 60 62 {ECO:0000244|PDB:2M0R}.
HELIX 65 71 {ECO:0000244|PDB:2M0R}.
HELIX 81 94 {ECO:0000244|PDB:2M0R}.
STRAND 98 100 {ECO:0000244|PDB:2M0R}.
SEQUENCE 104 AA; 11662 MW; 97EF31A46B388E79 CRC64;
MGQCRSANAE DAQEFSDVER AIETLIKNFH QYSVEGGKET LTPSELRDLV TQQLPHLMPS
NCGLEEKIAN LGSCNDSKLE FRSFWELIGE AAKSVKLERP VRGH


Related products :

Catalog number Product name Quantity
EIAAB36568 Gm1020,Mouse,Mus musculus,Protein S100-A14,S100 calcium-binding protein A14,S100a14,S100a15,S114
EIAAB36567 Homo sapiens,Human,Protein S100-A14,S100 calcium-binding protein A14,S100A14,S100A15,S114
10-288-22241F Protein S100-A14 - S100 calcium-binding protein A14; S114 0.05 mg
10-288-22241F Protein S100-A14 - S100 calcium-binding protein A14; S114 0.1 mg
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
32-213 S100 calcium binding protein A1 (S100-alpha_ S100A1), The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localiz 0.1 mL
EIAAB36572 Mouse,Mus musculus,Protein S100-A15A,Protein S100-A7A,S100 calcium-binding protein A15A,S100 calcium-binding protein A7A,S100a15,S100a15a,S100a7,S100a7a
EIAAB36554 Calgizzarin,Homo sapiens,Human,Metastatic lymph node gene 70 protein,MLN 70,MLN70,Protein S100-A11,Protein S100-C,S100 calcium-binding protein A11,S100A11,S100C
EIAAB36571 AAG13,Aging-associated gene 13 protein,Homo sapiens,Human,Protein S100-A16,Protein S100-F,S100 calcium-binding protein A16,S100A16,S100F
EIAAB36558 Calgizzarin,EMAP,Endothelial monocyte-activating polypeptide,Mouse,Mus musculus,Protein S100-A11,Protein S100-C,S100 calcium-binding protein A11,S100a11,S100c
EIAAB36557 Calgizzarin,Oryctolagus cuniculus,PCALG,Protein S100-A11,Protein S100-C,Rabbit,S100 calcium-binding protein A11,S100A11,S100C
32-201 S100 calcium binding protein A10 (S100A10_P11), The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in 0.1 mL
U2054h CLIA kit Homo sapiens,Human,Protein S100-E,Protein S100-P,S100 calcium-binding protein P,S100E,S100P 96T
U2054h CLIA Homo sapiens,Human,Protein S100-E,Protein S100-P,S100 calcium-binding protein P,S100E,S100P 96T
E2054h ELISA kit Homo sapiens,Human,Protein S100-E,Protein S100-P,S100 calcium-binding protein P,S100E,S100P 96T
E2054h ELISA Homo sapiens,Human,Protein S100-E,Protein S100-P,S100 calcium-binding protein P,S100E,S100P 96T
EIAAB36540 Metastasin,Nerve growth factor-induced protein 42A,P9K,Placental calcium-binding protein,Protein S100-A4,Rat,Rattus norvegicus,S100 calcium-binding protein A4,S100a4
10-663-45600 S100 calcium binding Protein A4 (S100A4) Human - S100 calcium-binding protein A4; Metastasin; Protein Mts1; Placental calcium-binding protein; Calvasculin N_A 0.01 mg
10-663-45600 S100 calcium binding Protein A4 (S100A4) Human - S100 calcium-binding protein A4; Metastasin; Protein Mts1; Placental calcium-binding protein; Calvasculin N_A 0.005 mg
10-663-45600 S100 calcium binding Protein A4 (S100A4) Human - S100 calcium-binding protein A4; Metastasin; Protein Mts1; Placental calcium-binding protein; Calvasculin N_A 0.002 mg
32-214 S100B (S100 calcium binding protein B) is a member of the S100 family of proteins containing 2 EF-hand calcium binding motifs. S100 proteins are localized in the cytoplasm and_or nucleus of a wide ran 0.1 mL
EIAAB36556 Calgizzarin,Pig,Protein S100-A11,Protein S100-C,S100 calcium-binding protein A11,S100A11,S100C,Sus scrofa
EIAAB36523 CABP,CABP9K,CALB3,Calbindin-D9k,Homo sapiens,Human,Protein S100-G,S100 calcium-binding protein G,S100D,S100G,Vitamin D-dependent calcium-binding protein, intestinal
EIAAB36524 Bos taurus,Bovine,CABP,CALB3,Calbindin-D9k,Protein S100-G,S100 calcium-binding protein G,S100D,S100G,Vitamin D-dependent calcium-binding protein, intestinal
EIAAB36525 CABP,Calb3,Calbindin-D9k,Mouse,Mus musculus,Protein S100-G,S100 calcium-binding protein G,S100d,S100g,Vitamin D-dependent calcium-binding protein, intestinal


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur