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14-3-3 protein sigma (Epithelial cell marker protein 1) (Stratifin)

 1433S_HUMAN             Reviewed;         248 AA.
P31947; Q6FH30; Q6FH51; Q96DH0;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
12-SEP-2018, entry version 199.
RecName: Full=14-3-3 protein sigma;
AltName: Full=Epithelial cell marker protein 1;
AltName: Full=Stratifin;
Name=SFN; Synonyms=HME1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Epithelium;
PubMed=1390337;
Prasad G.L., Valverius E.M., McDuffie E., Cooper H.L.;
"Complementary DNA cloning of a novel epithelial cell marker protein,
HME1, that may be down-regulated in neoplastic mammary cells.";
Cell Growth Differ. 3:507-513(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 19-25;
42-49; 118-122; 130-139; 149-159; 161-181; 196-199; 225-229 AND
231-239.
TISSUE=Keratinocyte;
PubMed=8515476; DOI=10.1006/jmbi.1993.1346;
Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H.,
Walbum E., Vandekerckhove J., Celis J.E.;
"Molecular cloning and expression of the transformation sensitive
epithelial marker stratifin. A member of a protein family that has
been involved in the protein kinase C signalling pathway.";
J. Mol. Biol. 231:982-998(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
PubMed=9659898; DOI=10.1016/S1097-2765(00)80002-7;
Hermeking H., Lengauer C., Polyak K., He T.-C., Zhang L.,
Thiagalingam S., Kinzler K.W., Vogelstein B.;
"14-3-3 sigma is a p53-regulated inhibitor of G2/M progression.";
Mol. Cell 1:3-11(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[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 MRNA] (ISOFORMS 1 AND 2).
TISSUE=Cervix, Lung, and Placenta;
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).
[7]
PROTEIN SEQUENCE OF 42-49 AND 118-122.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[8]
IDENTIFICATION IN A COMPLEX WITH XPO7; ARHGAP1; EIF4A1; VPS26A; VPS29
AND VPS35.
PubMed=15282546; DOI=10.1038/sj.emboj.7600338;
Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.;
"Exportin 7 defines a novel general nuclear export pathway.";
EMBO J. 23:3227-3236(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[10]
FUNCTION IN MDM2 UBIQUITINATION, AND UBIQUITINATION BY RFFL.
PubMed=18382127; DOI=10.4161/cc.7.5.5701;
Yang W., Dicker D.T., Chen J., El-Deiry W.S.;
"CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing
MDM2.";
Cell Cycle 7:670-682(2008).
[11]
INTERACTION WITH GAB2.
PubMed=19172738; DOI=10.1038/emboj.2008.159;
Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D.,
Guilhaus M., James D.E., Daly R.J.;
"Phosphorylation-dependent binding of 14-3-3 terminates signalling by
the Gab2 docking protein.";
EMBO J. 27:2305-2316(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
INTERACTION WITH SLITRK1.
PubMed=19640509; DOI=10.1016/j.biopsych.2009.05.033;
Kajiwara Y., Buxbaum J.D., Grice D.E.;
"SLITRK1 binds 14-3-3 and regulates neurite outgrowth in a
phosphorylation-dependent manner.";
Biol. Psychiatry 66:918-925(2009).
[15]
INTERACTION WITH SRPK2.
PubMed=19592491; DOI=10.1074/jbc.M109.026237;
Jang S.W., Liu X., Fu H., Rees H., Yepes M., Levey A., Ye K.;
"Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell
cycle and cell death in neurons.";
J. Biol. Chem. 284:24512-24525(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-248, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
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).
[18]
INTERACTION WITH COPS6 AND COP1.
PubMed=21625211; DOI=10.1038/onc.2011.192;
Choi H.H., Gully C., Su C.H., Velazquez-Torres G., Chou P.C.,
Tseng C., Zhao R., Phan L., Shaiken T., Chen J., Yeung S.C., Lee M.H.;
"COP9 signalosome subunit 6 stabilizes COP1, which functions as an E3
ubiquitin ligase for 14-3-3sigma.";
Oncogene 30:4791-4801(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
INTERACTION WITH PI4KB, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=23572552; DOI=10.1128/mBio.00098-13;
Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L.,
DeRisi J.L.;
"ACBD3 interaction with TBC1 domain 22 protein is differentially
affected by enteroviral and kobuviral 3A protein binding.";
MBio 4:E00098-E00098(2013).
[21]
INTERACTION WITH DAPK2.
PubMed=26047703; DOI=10.1016/j.bbrc.2015.05.105;
Yuasa K., Ota R., Matsuda S., Isshiki K., Inoue M., Tsuji A.;
"Suppression of death-associated protein kinase 2 by interaction with
14-3-3 proteins.";
Biochem. Biophys. Res. Commun. 464:70-75(2015).
[22]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH PHOSPHOSERINE
PEPTIDE.
PubMed=15731107; DOI=10.1074/jbc.M500982200;
Wilker E.W., Grant R.A., Artim S.C., Yaffe M.B.;
"A structural basis for 14-3-3sigma functional specificity.";
J. Biol. Chem. 280:18891-18898(2005).
[23]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-231 IN COMPLEX WITH PADI6
PHOSPHOPEPTIDES.
PubMed=22634725; DOI=10.1016/j.jsb.2012.05.010;
Rose R., Rose M., Ottmann C.;
"Identification and structural characterization of two 14-3-3 binding
sites in the human peptidylarginine deiminase type VI.";
J. Struct. Biol. 180:65-72(2012).
-!- FUNCTION: Adapter protein implicated in the regulation of a large
spectrum of both general and specialized signaling pathways. Binds
to a large number of partners, usually by recognition of a
phosphoserine or phosphothreonine motif. Binding generally results
in the modulation of the activity of the binding partner. When
bound to KRT17, regulates protein synthesis and epithelial cell
growth by stimulating Akt/mTOR pathway. May also regulate MDM2
autoubiquitination and degradation and thereby activate p53/TP53.
{ECO:0000269|PubMed:18382127}.
-!- FUNCTION: p53-regulated inhibitor of G2/M progression.
{ECO:0000269|PubMed:18382127}.
-!- SUBUNIT: Homodimer. Interacts with KRT17 and SAMSN1 (By
similarity). Found in a complex with XPO7, EIF4A1, ARHGAP1,
VPS26A, VPS29 and VPS35. Interacts with GAB2. Interacts with
SRPK2. Interacts with COPS6. Interacts with COP1; this interaction
leads to proteasomal degradation. Interacts with the 'Thr-369'
phosphorylated form of DAPK2 (PubMed:26047703). Interacts with
PI4KB (PubMed:23572552). Interacts with SLITRK1 (PubMed:19640509).
{ECO:0000250, ECO:0000250|UniProtKB:O70456,
ECO:0000269|PubMed:15282546, ECO:0000269|PubMed:15731107,
ECO:0000269|PubMed:19172738, ECO:0000269|PubMed:19592491,
ECO:0000269|PubMed:19640509, ECO:0000269|PubMed:21625211,
ECO:0000269|PubMed:22634725, ECO:0000269|PubMed:23572552,
ECO:0000269|PubMed:26047703}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-476295, EBI-476295;
P00519:ABL1; NbExp=2; IntAct=EBI-476295, EBI-375543;
Q96IF1:AJUBA; NbExp=2; IntAct=EBI-476295, EBI-949782;
P10398:ARAF; NbExp=2; IntAct=EBI-476295, EBI-365961;
Q92934:BAD; NbExp=4; IntAct=EBI-476295, EBI-700771;
Q68D86:CCDC102B; NbExp=3; IntAct=EBI-476295, EBI-10171570;
P51946:CCNH; NbExp=3; IntAct=EBI-476295, EBI-741406;
Q8NHY2:COP1; NbExp=6; IntAct=EBI-476295, EBI-1176214;
Q7L5N1:COPS6; NbExp=7; IntAct=EBI-476295, EBI-486838;
P00533:EGFR; NbExp=8; IntAct=EBI-476295, EBI-297353;
Q9UJM3:ERRFI1; NbExp=3; IntAct=EBI-476295, EBI-2941912;
Q9NYF3:FAM53C; NbExp=3; IntAct=EBI-476295, EBI-1644252;
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-476295, EBI-10175124;
P98177:FOXO4; NbExp=3; IntAct=EBI-476295, EBI-4481939;
O60269:GPRIN2; NbExp=2; IntAct=EBI-476295, EBI-740397;
P56524:HDAC4; NbExp=4; IntAct=EBI-476295, EBI-308629;
Q9UQL6:HDAC5; NbExp=3; IntAct=EBI-476295, EBI-715576;
Q8WUI4:HDAC7; NbExp=3; IntAct=EBI-476295, EBI-1048378;
Q14103-4:HNRNPD; NbExp=7; IntAct=EBI-476295, EBI-432545;
Q17RB8:LONRF1; NbExp=3; IntAct=EBI-476295, EBI-2341787;
P43355:MAGEA1; NbExp=3; IntAct=EBI-476295, EBI-740978;
Q9Y2U5:MAP3K2; NbExp=2; IntAct=EBI-476295, EBI-357393;
P27448:MARK3; NbExp=2; IntAct=EBI-476295, EBI-707595;
Q13064:MKRN3; NbExp=3; IntAct=EBI-476295, EBI-2340269;
O00444:PLK4; NbExp=2; IntAct=EBI-476295, EBI-746202;
Q96QF0:RAB3IP; NbExp=3; IntAct=EBI-476295, EBI-747844;
P04049:RAF1; NbExp=3; IntAct=EBI-476295, EBI-365996;
Q8NFH8-2:REPS2; NbExp=2; IntAct=EBI-476295, EBI-8029141;
Q13470:TNK1; NbExp=2; IntAct=EBI-476295, EBI-1383444;
P04637:TP53; NbExp=4; IntAct=EBI-476295, EBI-366083;
Q96HA8:WDYHV1; NbExp=3; IntAct=EBI-476295, EBI-741158;
P63104:YWHAZ; NbExp=2; IntAct=EBI-476295, EBI-347088;
Q53FD0:ZC2HC1C; NbExp=3; IntAct=EBI-476295, EBI-740767;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. Secreted.
Note=May be secreted by a non-classical secretory pathway.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P31947-1; Sequence=Displayed;
Name=2;
IsoId=P31947-2; Sequence=VSP_021768;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Present mainly in tissues enriched in
stratified squamous keratinizing epithelium.
-!- PTM: Ubiquitinated. Ubiquitination by RFFL induces proteasomal
degradation and indirectly regulates p53/TP53 activation.
{ECO:0000269|PubMed:18382127}.
-!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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EMBL; M93010; AAA59546.1; -; mRNA.
EMBL; X57348; CAA40623.1; -; mRNA.
EMBL; AF029081; AAC52029.1; -; Genomic_DNA.
EMBL; AF029082; AAC52030.1; -; mRNA.
EMBL; CR541905; CAG46703.1; -; mRNA.
EMBL; CR541926; CAG46724.1; -; mRNA.
EMBL; AL034380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000329; AAH00329.1; -; mRNA.
EMBL; BC000995; AAH00995.1; -; mRNA.
EMBL; BC001550; AAH01550.1; -; mRNA.
EMBL; BC002995; AAH02995.1; -; mRNA.
EMBL; BC023552; AAH23552.1; -; mRNA.
CCDS; CCDS288.1; -. [P31947-1]
PIR; S34753; S34753.
PIR; S38956; S38956.
RefSeq; NP_006133.1; NM_006142.3. [P31947-1]
UniGene; Hs.523718; -.
PDB; 1YWT; X-ray; 2.40 A; A/B=1-248.
PDB; 1YZ5; X-ray; 2.80 A; A/B=1-248.
PDB; 3IQJ; X-ray; 1.15 A; A=1-231.
PDB; 3IQU; X-ray; 1.05 A; A=1-231.
PDB; 3IQV; X-ray; 1.20 A; A=1-231.
PDB; 3LW1; X-ray; 1.28 A; A=1-248.
PDB; 3MHR; X-ray; 1.15 A; A=1-231.
PDB; 3O8I; X-ray; 2.00 A; A=1-231.
PDB; 3P1N; X-ray; 1.40 A; A=1-231.
PDB; 3P1O; X-ray; 1.90 A; A=1-231.
PDB; 3P1P; X-ray; 1.95 A; A=1-231.
PDB; 3P1Q; X-ray; 1.70 A; A=1-231.
PDB; 3P1R; X-ray; 1.70 A; A=1-231.
PDB; 3P1S; X-ray; 1.65 A; A=1-231.
PDB; 3SMK; X-ray; 2.10 A; A=1-231.
PDB; 3SML; X-ray; 1.90 A; A=1-231.
PDB; 3SMM; X-ray; 2.00 A; A=1-231.
PDB; 3SMN; X-ray; 2.00 A; A=1-231.
PDB; 3SMO; X-ray; 1.80 A; A=1-231.
PDB; 3SP5; X-ray; 1.80 A; A=1-231.
PDB; 3SPR; X-ray; 1.99 A; A=1-231.
PDB; 3T0L; X-ray; 1.60 A; A=1-231.
PDB; 3T0M; X-ray; 1.62 A; A=1-231.
PDB; 3U9X; X-ray; 1.80 A; A=1-231.
PDB; 3UX0; X-ray; 1.75 A; A=1-231.
PDB; 4DAT; X-ray; 1.40 A; A=1-231.
PDB; 4DAU; X-ray; 2.00 A; A=1-231.
PDB; 4DHM; X-ray; 1.70 A; A=1-231.
PDB; 4DHN; X-ray; 1.80 A; A=1-231.
PDB; 4DHO; X-ray; 1.70 A; A=1-231.
PDB; 4DHP; X-ray; 1.75 A; A=1-231.
PDB; 4DHQ; X-ray; 1.75 A; A=1-231.
PDB; 4DHR; X-ray; 1.40 A; A=1-231.
PDB; 4DHS; X-ray; 1.74 A; A=1-231.
PDB; 4DHT; X-ray; 1.80 A; A=1-231.
PDB; 4DHU; X-ray; 1.67 A; A=1-231.
PDB; 4FL5; X-ray; 1.90 A; A/B=1-231.
PDB; 4FR3; X-ray; 1.90 A; A=1-231.
PDB; 4IEA; X-ray; 1.70 A; A=1-231.
PDB; 4JC3; X-ray; 2.05 A; A=1-231.
PDB; 4JDD; X-ray; 2.10 A; A=1-231.
PDB; 4QLI; X-ray; 1.45 A; A=1-231.
PDB; 4Y32; X-ray; 1.70 A; A/B=1-231.
PDB; 4Y3B; X-ray; 1.80 A; A/B=1-231.
PDB; 4Y5I; X-ray; 1.40 A; A/B=1-231.
PDB; 5BTV; X-ray; 1.70 A; A=1-231.
PDB; 5HF3; X-ray; 1.80 A; A=1-231.
PDB; 5LTW; X-ray; 4.50 A; A/B/E/F/I/J=1-231.
PDB; 5LU1; X-ray; 2.40 A; A/B/E/F=1-231.
PDB; 5LU2; X-ray; 2.50 A; A/B=1-231.
PDB; 5MHC; X-ray; 1.20 A; A=1-231.
PDB; 5MOC; X-ray; 1.80 A; A=1-231.
PDB; 5MXO; X-ray; 1.20 A; A=1-231.
PDB; 5MY9; X-ray; 1.33 A; A=1-231.
PDB; 5MYC; X-ray; 1.46 A; A=1-231.
PDB; 5N5R; X-ray; 1.80 A; A=1-231.
PDB; 5N5T; X-ray; 1.80 A; A=1-231.
PDB; 5N5W; X-ray; 1.37 A; A=1-231.
PDB; 5N75; X-ray; 1.80 A; A=1-231.
PDB; 5OEG; X-ray; 3.15 A; A=1-231.
PDB; 5OEH; X-ray; 2.35 A; A=1-231.
PDB; 5OK9; X-ray; 2.35 A; A/B/E/F=1-231.
PDB; 5OKF; X-ray; 3.20 A; A/B/C/D=1-231.
PDB; 5OM0; X-ray; 3.20 A; A/B=1-231.
PDB; 5OMA; X-ray; 3.90 A; A/B/C/D=1-231.
PDB; 6FAU; X-ray; 1.25 A; A/C=1-231.
PDB; 6FAV; X-ray; 1.40 A; A/C=1-231.
PDB; 6FAW; X-ray; 1.40 A; A/C=1-231.
PDB; 6FBB; X-ray; 1.30 A; A=1-231.
PDB; 6FBW; X-ray; 1.45 A; A/C=1-231.
PDB; 6FBY; X-ray; 1.50 A; A/C=1-231.
PDB; 6FCP; X-ray; 1.45 A; A=1-231.
PDB; 6FI4; X-ray; 2.00 A; A=1-231.
PDB; 6FI5; X-ray; 1.70 A; A=1-231.
PDBsum; 1YWT; -.
PDBsum; 1YZ5; -.
PDBsum; 3IQJ; -.
PDBsum; 3IQU; -.
PDBsum; 3IQV; -.
PDBsum; 3LW1; -.
PDBsum; 3MHR; -.
PDBsum; 3O8I; -.
PDBsum; 3P1N; -.
PDBsum; 3P1O; -.
PDBsum; 3P1P; -.
PDBsum; 3P1Q; -.
PDBsum; 3P1R; -.
PDBsum; 3P1S; -.
PDBsum; 3SMK; -.
PDBsum; 3SML; -.
PDBsum; 3SMM; -.
PDBsum; 3SMN; -.
PDBsum; 3SMO; -.
PDBsum; 3SP5; -.
PDBsum; 3SPR; -.
PDBsum; 3T0L; -.
PDBsum; 3T0M; -.
PDBsum; 3U9X; -.
PDBsum; 3UX0; -.
PDBsum; 4DAT; -.
PDBsum; 4DAU; -.
PDBsum; 4DHM; -.
PDBsum; 4DHN; -.
PDBsum; 4DHO; -.
PDBsum; 4DHP; -.
PDBsum; 4DHQ; -.
PDBsum; 4DHR; -.
PDBsum; 4DHS; -.
PDBsum; 4DHT; -.
PDBsum; 4DHU; -.
PDBsum; 4FL5; -.
PDBsum; 4FR3; -.
PDBsum; 4IEA; -.
PDBsum; 4JC3; -.
PDBsum; 4JDD; -.
PDBsum; 4QLI; -.
PDBsum; 4Y32; -.
PDBsum; 4Y3B; -.
PDBsum; 4Y5I; -.
PDBsum; 5BTV; -.
PDBsum; 5HF3; -.
PDBsum; 5LTW; -.
PDBsum; 5LU1; -.
PDBsum; 5LU2; -.
PDBsum; 5MHC; -.
PDBsum; 5MOC; -.
PDBsum; 5MXO; -.
PDBsum; 5MY9; -.
PDBsum; 5MYC; -.
PDBsum; 5N5R; -.
PDBsum; 5N5T; -.
PDBsum; 5N5W; -.
PDBsum; 5N75; -.
PDBsum; 5OEG; -.
PDBsum; 5OEH; -.
PDBsum; 5OK9; -.
PDBsum; 5OKF; -.
PDBsum; 5OM0; -.
PDBsum; 5OMA; -.
PDBsum; 6FAU; -.
PDBsum; 6FAV; -.
PDBsum; 6FAW; -.
PDBsum; 6FBB; -.
PDBsum; 6FBW; -.
PDBsum; 6FBY; -.
PDBsum; 6FCP; -.
PDBsum; 6FI4; -.
PDBsum; 6FI5; -.
ProteinModelPortal; P31947; -.
SMR; P31947; -.
BioGrid; 109072; 261.
DIP; DIP-29861N; -.
ELM; P31947; -.
IntAct; P31947; 170.
MINT; P31947; -.
STRING; 9606.ENSP00000340989; -.
BindingDB; P31947; -.
ChEMBL; CHEMBL1909482; -.
iPTMnet; P31947; -.
PhosphoSitePlus; P31947; -.
SwissPalm; P31947; -.
BioMuta; SFN; -.
DMDM; 398953; -.
OGP; P31947; -.
SWISS-2DPAGE; P31947; -.
EPD; P31947; -.
MaxQB; P31947; -.
PaxDb; P31947; -.
PeptideAtlas; P31947; -.
PRIDE; P31947; -.
TopDownProteomics; P31947-1; -. [P31947-1]
TopDownProteomics; P31947-2; -. [P31947-2]
DNASU; 2810; -.
Ensembl; ENST00000339276; ENSP00000340989; ENSG00000175793. [P31947-1]
GeneID; 2810; -.
KEGG; hsa:2810; -.
UCSC; uc001bnc.2; human. [P31947-1]
CTD; 2810; -.
DisGeNET; 2810; -.
EuPathDB; HostDB:ENSG00000175793.11; -.
GeneCards; SFN; -.
HGNC; HGNC:10773; SFN.
HPA; CAB006268; -.
HPA; CAB040552; -.
HPA; HPA011105; -.
MIM; 601290; gene.
neXtProt; NX_P31947; -.
OpenTargets; ENSG00000175793; -.
PharmGKB; PA177; -.
eggNOG; KOG0841; Eukaryota.
eggNOG; COG5040; LUCA.
GeneTree; ENSGT00760000119116; -.
HOGENOM; HOG000240379; -.
HOVERGEN; HBG050423; -.
InParanoid; P31947; -.
KO; K06644; -.
OMA; SIEQKGN; -.
OrthoDB; EOG091G0VKY; -.
PhylomeDB; P31947; -.
TreeFam; TF102003; -.
Reactome; R-HSA-111447; Activation of BAD and translocation to mitochondria.
Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
Reactome; R-HSA-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
SignaLink; P31947; -.
SIGNOR; P31947; -.
ChiTaRS; SFN; human.
EvolutionaryTrace; P31947; -.
GeneWiki; Stratifin; -.
GenomeRNAi; 2810; -.
PRO; PR:P31947; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000175793; Expressed in 231 organ(s), highest expression level in amniotic fluid.
CleanEx; HS_SFN; -.
Genevisible; P31947; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IEA:InterPro.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0008426; F:protein kinase C inhibitor activity; TAS:ProtInc.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0061436; P:establishment of skin barrier; ISS:UniProtKB.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:HGNC.
GO; GO:0031424; P:keratinization; IEA:Ensembl.
GO; GO:0003334; P:keratinocyte development; IEA:Ensembl.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:HGNC.
GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IEA:Ensembl.
GO; GO:0006469; P:negative regulation of protein kinase activity; TAS:ProtInc.
GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
GO; GO:0045606; P:positive regulation of epidermal cell differentiation; ISS:UniProtKB.
GO; GO:0046827; P:positive regulation of protein export from nucleus; IEA:Ensembl.
GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
GO; GO:0010482; P:regulation of epidermal cell division; ISS:UniProtKB.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:HGNC.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd10019; 14-3-3_sigma; 1.
Gene3D; 1.20.190.20; -; 1.
InterPro; IPR000308; 14-3-3.
InterPro; IPR023409; 14-3-3_CS.
InterPro; IPR036815; 14-3-3_dom_sf.
InterPro; IPR023410; 14-3-3_domain.
InterPro; IPR037435; 14-3-3_sigma.
PANTHER; PTHR18860; PTHR18860; 1.
Pfam; PF00244; 14-3-3; 1.
PIRSF; PIRSF000868; 14-3-3; 1.
PRINTS; PR00305; 1433ZETA.
SMART; SM00101; 14_3_3; 1.
SUPFAM; SSF48445; SSF48445; 1.
PROSITE; PS00796; 1433_1; 1.
PROSITE; PS00797; 1433_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Secreted; Ubl conjugation.
CHAIN 1 248 14-3-3 protein sigma.
/FTId=PRO_0000058643.
SITE 56 56 Interaction with phosphoserine on
interacting protein.
SITE 129 129 Interaction with phosphoserine on
interacting protein.
MOD_RES 5 5 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 74 74 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 248 248 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231}.
VAR_SEQ 85 116 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_021768.
VARIANT 155 155 M -> I (in dbSNP:rs11542705).
/FTId=VAR_048095.
CONFLICT 77 77 K -> M (in Ref. 4; CAG46703).
{ECO:0000305}.
CONFLICT 120 120 Y -> H (in Ref. 2; AAA59546).
{ECO:0000305}.
CONFLICT 242 242 A -> V (in Ref. 2; AAA59546).
{ECO:0000305}.
HELIX 3 15 {ECO:0000244|PDB:3IQU}.
HELIX 19 31 {ECO:0000244|PDB:3IQU}.
HELIX 38 69 {ECO:0000244|PDB:3IQU}.
HELIX 80 104 {ECO:0000244|PDB:3IQU}.
HELIX 107 110 {ECO:0000244|PDB:3IQU}.
HELIX 114 134 {ECO:0000244|PDB:3IQU}.
STRAND 137 139 {ECO:0000244|PDB:3T0M}.
HELIX 140 161 {ECO:0000244|PDB:3IQU}.
HELIX 167 182 {ECO:0000244|PDB:3IQU}.
HELIX 187 204 {ECO:0000244|PDB:3IQU}.
HELIX 205 207 {ECO:0000244|PDB:3IQU}.
HELIX 210 230 {ECO:0000244|PDB:3IQU}.
SEQUENCE 248 AA; 27774 MW; 7F4B44E3AA59ECE6 CRC64;
MERASLIQKA KLAEQAERYE DMAAFMKGAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR
VLSSIEQKSN EEGSEEKGPE VREYREKVET ELQGVCDTVL GLLDSHLIKE AGDAESRVFY
LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH
YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADNAGEEGG
EAPQEPQS


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