O70456 (1433S_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
14-3-3 protein sigma

Alternative name(s):
Stratifin

Gene names

Name:	Sfn
Synonyms:	Mkrn3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	248 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.7
Subunit structure	Homodimer. Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. Interacts with GAB2 By similarity. Interacts with KRT17. Interacts with SAMSN1. Interacts with SRPK2 By similarity. Interacts with COPS6 By similarity. Interacts with RFWD2; this interaction leads to proteasomal degradation By similarity. Ref.7 Ref.8
Subcellular location	Cytoplasm. Nucleus. Secreted By similarity. Note: May be secreted by a non-classical secretory pathway By similarity. Ref.7
Tissue specificity	Expressed in the basal layer of skin epithelium and in outer root sheath of hair follicle. Ref.7
Induction	Induced in damaged or stressed epidermis. Ref.7
Miscellaneous	14-3-3 proteins have been shown to be PKC activators, but this effect could be non-specific and only due to the acidic nature of the protein.
Sequence similarities	Belongs to the 14-3-3 family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Secreted
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	intrinsic apoptotic signaling pathway in response to DNA damage Inferred from electronic annotation. Source: Compara keratinocyte differentiation Inferred from mutant phenotype PubMed 16239341. Source: MGI keratinocyte proliferation Inferred from genetic interaction PubMed 17041603. Source: MGI negative regulation of cell proliferation Inferred from genetic interaction PubMed 17041603. Source: MGI negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of cell growth Inferred from direct assay Ref.7. Source: UniProtKB positive regulation of protein export from nucleus Inferred from direct assay PubMed 17938205. Source: UniProtKB regulation of cyclin-dependent protein serine/threonine kinase activity Inferred from direct assay PubMed 10767298. Source: MGI release of cytochrome c from mitochondria Inferred from electronic annotation. Source: Compara skin development Inferred from mutant phenotype PubMed 16239341. Source: MGI
Cellular_component	cytoplasm Inferred from direct assay Ref.7. Source: UniProtKB extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	protein kinase binding Inferred from direct assay PubMed 10767298. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Krt17	Q9QWL7	3	EBI-1544118,EBI-309015

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 248	248	14-3-3 protein sigma		PRO_0000058644
Sites
	Site	56	1	Interaction with phosphoserine on interacting protein By similarity
	Site	129	1	Interaction with phosphoserine on interacting protein By similarity
Amino acid modifications
	Modified residue	5	1	Phosphoserine By similarity
	Modified residue	64	1	Phosphoserine Ref.6
	Modified residue	216	1	Phosphoserine Ref.6
Experimental info
	Sequence conflict	244 – 248	5	EEPQS → DDPHI in AAC14344. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O70456 [UniParc]. Last modified June 28, 2011. Version 2. Checksum: C1C40905824B3F48	FASTA	248	27,706
	10 20 30 40 50 60 MERASLIQKA KLAEQAERYE DMAAFMKSAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR 70 80 90 100 110 120 VLSSIEQKSN EEGSEEKGPE VKEYREKVET ELRGVCDTVL GLLDSHLIKG AGDAESRVFY 130 140 150 160 170 180 LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH 190 200 210 220 230 240 YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADSAGEEGG EAPEEPQS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Karpitskiy V.V., Shaw A.S. Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: FVB/N.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Heart and Stomach.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Lubec G., Kang S.U., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-12; 42-49; 61-68 AND 215-224, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[6]	"Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol." Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., Burlingame A.L. Proteomics 5:388-398(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND SER-216, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[7]	"A keratin cytoskeletal protein regulates protein synthesis and epithelial cell growth." Kim S., Wong P., Coulombe P.A. Nature 441:362-365(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH KRT17, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
[8]	"SLy2 targets the nuclear SAP30/HDAC1 complex." Brandt S., Ellwanger K., Beuter-Gunia C., Schuster M., Hausser A., Schmitz I., Beer-Hammer S. Int. J. Biochem. Cell Biol. 42:1472-1481(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SAMSN1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF058798 mRNA. Translation: AAC14344.1. AK146490 mRNA. Translation: BAE27209.1. AK169358 mRNA. Translation: BAE41107.1. AL627228 Genomic DNA. Translation: CAM14836.1. CH466552 Genomic DNA. Translation: EDL30056.1.
IPI	IPI00118286.
RefSeq	NP_061224.2. NM_018754.2.
UniGene	Mm.44482.
3D structure databases
ProteinModelPortal	O70456.
SMR	O70456. Positions 1-231.
ModBase	Search...
Protein-protein interaction databases
IntAct	O70456. 2 interactions.
MINT	MINT-240814.
STRING	10090.ENSMUSP00000050374.
Proteomic databases
PaxDb	O70456.
PRIDE	O70456.
Protocols and materials databases
DNASU	55948.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000057311; ENSMUSP00000050374; ENSMUSG00000047281.
GeneID	55948.
KEGG	mmu:55948.
Organism-specific databases
CTD	2810.
MGI	MGI:1891831. Sfn.
Phylogenomic databases
eggNOG	COG5040.
GeneTree	ENSGT00690000101991.
HOGENOM	HOG000240379.
HOVERGEN	HBG050423.
InParanoid	Q3TEZ1.
KO	K06644.
OMA	AFMKSAV.
OrthoDB	EOG4XH00X.
Enzyme and pathway databases
Reactome	REACT_147847. Translocation of Glut4 to the Plasma Membrane.
Gene expression databases
Bgee	O70456.
CleanEx	MM_MKRN3. MM_SFN.
Genevestigator	O70456.
GermOnline	ENSMUSG00000047281. Mus musculus.
Family and domain databases
Gene3D	1.20.190.20. 1 hit.
InterPro	IPR000308. 14-3-3. IPR023409. 14-3-3_CS. IPR023410. 14-3-3_domain. [Graphical view]
PANTHER	PTHR18860. PTHR18860. 1 hit.
Pfam	PF00244. 14-3-3. 1 hit. [Graphical view]
PIRSF	PIRSF000868. 14-3-3. 1 hit.
PRINTS	PR00305. 1433ZETA.
SMART	SM00101. 14_3_3. 1 hit. [Graphical view]
SUPFAM	SSF48445. 14-3-3. 1 hit.
PROSITE	PS00796. 1433_1. 1 hit. PS00797. 1433_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL1909483.
NextBio	311642.
SOURCE	Search...

Entry information

Entry name

1433S_MOUSE

Accession

Primary (citable) accession number: O70456
Secondary accession number(s): Q3TEZ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	June 28, 2011
Last modified:	May 1, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program