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UniProtKB/Swiss-Prot entry P31947


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name 1433S_HUMAN
Primary accession number P31947
Secondary accession numbers Q6FH30 Q6FH51 Q96DH0
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on July 1, 1993 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 96)
Name and origin of the protein
Protein name 14-3-3 protein sigma
Synonyms Stratifin
Epithelial cell marker protein 1
Gene name
Name: SFN
Synonyms: HME1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Epithelium;
PubMed=1390337 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1006/jmbi.1993.1346; PubMed=8515476 [NCBI, ExPASy, EBI, Israel, Japan]
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).
DOI=10.1016/S1097-2765(00)80002-7; PubMed=9659898 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1002/elps.11501301199; PubMed=1286667 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1038/sj.emboj.7600338; PubMed=15282546 [NCBI, ExPASy, EBI, Israel, Japan]
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 MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[13]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH PHOSPHOSERINE PEPTIDE.
DOI=10.1074/jbc.M500982200; PubMed=15731107 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M93010; AAA59546.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X57348; CAA40623.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF029081; AAC52029.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF029082; AAC52030.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR541905; CAG46703.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR541926; CAG46724.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL034380; CAB92118.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000329; AAH00329.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000995; AAH00995.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001550; AAH01550.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002995; AAH02995.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC023552; AAH23552.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00013890; -.
IPI00411765; -.
PIR S34753; S34753.
S38956; S38956.
RefSeq NP_006133.1; -.
UniGene Hs.523718
3D structure databases
PDB
1YWT; X-ray; 2.40 A; A/B=1-248.[ExPASy / RCSB / EBI]
1YZ5; X-ray; 2.80 A; A/B=1-248.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1YWT; -.
1YZ5; -.
ModBase P31947.
Protein-protein interaction databases
IntAct P31947; 18.
PTM databases
PhosphoSite P31947; -.
Enzyme and pathway databases
Pathway_Interaction_DB a6b1_a6b4_integrin_pathway; a6b1 and a6b4 Integrin signaling.
pi3kciaktpathway; Class I PI3K signaling events mediated by Akt.
foxopathway; FoxO family signaling.
insulin_glucose_pathway; Insulin-mediated glucose transport.
p38_mk2pathway; p38 signaling mediated by MAPKAP kinases.
nfat_3pathway; Role of Calcineurin-dependent NFAT signaling in lymphocytes.
pi3kplctrkpathway; Trk receptor signaling mediated by PI3K and PLC-gamma.
2D gel databases
SWISS-2DPAGE P31947; -.
Aarhus/Ghent-2DPAGE 9109; IEF.
Cornea-2DPAGE P31947; -.
OGP P31947; -.
Organism-specific databases
GeneCards GC01P027062; -.
H-InvDB HIX0000327; -.
HGNC HGNC:10773; SFN.
GenAtlas SFN.
HPA CAB006268; -.
HPA011105; -.
MIM 601290; gene. [NCBI / EBI]
PharmGKB PA177; -.
Gene expression databases
ArrayExpress P31947; -.
Bgee P31947; -.
CleanEx HS_SFN; -.
GermOnline ENSG00000175793; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (traceable author statement from ProtInc).
GO:0005615; Cellular component: extracellular space (traceable author statement from ProtInc).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0019904; Molecular function: protein domain specific binding (inferred from electronic annotation from InterPro).
GO:0008426; Molecular function: protein kinase C inhibitor activity (traceable author statement from ProtInc).
GO:0008630; Biological process: DNA damage response, signal transduction resulting in induction of apoptosis (inferred from direct assay from HGNC).
GO:0043154; Biological process: negative regulation of caspase activity (inferred from direct assay from HGNC).
GO:0006469; Biological process: negative regulation of protein kinase activity (traceable author statement from ProtInc).
GO:0001836; Biological process: release of cytochrome c from mitochondria (inferred from direct assay from HGNC).
QuickGo view.
Family and domain databases
InterPro IPR000308; 14-3-3.
Graphical view of domain structure.
Gene3D G3DSA:1.20.190.20; 14-3-3; 1.
PANTHER PTHR18860; 14-3-3; 1.
Pfam PF00244; 14-3-3; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000868; 14-3-3; 1.
PRINTS PR00305; 1433ZETA.
ProDom PD000600; 14-3-3; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00101; 14_3_3; 1.
SMART graphical view of domain structure.
PROSITE PS00796; 1433_1; 1.
PS00797; 1433_2; 1.
Proteomic databases
PeptideAtlas P31947; -.
PRIDE P31947; -.
Genome annotation databases
Ensembl ENSG00000175793; Homo sapiens. [Contig view]
GeneID 2810; -.
KEGG hsa:2810; -.
Phylogenomic databases
HOGENOM P31947; -.
HOVERGEN P31947; -.
OMA P31947; FMKSAVE.
Other
NextBio 11071; -.
SOURCE SFN; Homo sapiens.
ProtoNet P31947.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism; Secreted.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   248  248     14-3-3 protein sigma. PRO_0000058643
SITE   56    56  1     Interaction with phosphoserine on interacting protein. 
SITE   129   129  1     Interaction with phosphoserine on interacting protein. 
MOD_RES   64    64        Phosphoserine (By similarity). 
MOD_RES   216   216        Phosphoserine (By similarity). 
MOD_RES   248   248        Phosphoserine. 
VAR_SEQ   85   116        Missing (in isoform 2). VSP_021768
VARIANT   155   155  1     M -> I (in dbSNP:rs11542705 [NCBI]). VAR_048095 [3D]
CONFLICT   77    77        K -> M (in Ref. 4; CAG46703). 
CONFLICT   120   120        Y -> H (in Ref. 2; AAA59546). 
CONFLICT   242   242        A -> V (in Ref. 2; AAA59546). 
HELIX   3    15  13      
HELIX   19    31  13      
HELIX   38    66  29      
HELIX   67    69  3      
HELIX   80   104  25      
TURN   105   107  3      
STRAND   108   110  3      
HELIX   114   133  20      
HELIX   137   161  25      
HELIX   167   182  16      
HELIX   187   202  16      
HELIX   205   207  3      
TURN   210   212  3      
HELIX   213   229  17      
Sequence information
Length: 248 AA [This is the length of the unprocessed precursor] Molecular weight: 27774 Da [This is the MW of the unprocessed precursor] CRC64: 7F4B44E3AA59ECE6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MERASLIQKA KLAEQAERYE DMAAFMKGAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR 

        70         80         90        100        110        120 
VLSSIEQKSN EEGSEEKGPE VREYREKVET ELQGVCDTVL GLLDSHLIKE AGDAESRVFY 

       130        140        150        160        170        180 
LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH 

       190        200        210        220        230        240 
YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADNAGEEGG 


EAPQEPQS 

P31947 in FASTA format

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