14-3-3 protein epsilon - Mus musculus (Mouse)

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P62259 (1433E_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 93. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
14-3-3 protein epsilon
Short name=14-3-3E

Gene names

Name:

Ywhae

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	255 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.
Subunit structure	Homodimer. Heterodimerizes with YWHAZ By similarity. Interacts with NDEL1, ARHGEF28 and TIAM2. Interacts with ABL1 (phosphorylated form); the interaction retains it in the cytoplasm. Weakly interacts with CDKN1B. Interacts with GAB2 By similarity. Interacts with PKA-phosphorylated AANAT By similarity. Interacts with phosphorylated GRB10. Interacts with the phosphorylated (by AKT1) form of SRPK2 By similarity. Ref.6 Ref.7 Ref.8 Ref.9
Subcellular location	Cytoplasm By similarity. Melanosome By similarity.
Developmental stage	In the E8.5 embryo, expressed throughout the embryo. Within a day, expression was more marked in mesenchyme than elsewhere (e.g. epithelial tissue, where it was generally low), although levels in neural tissue rose again by about E12.5. This difference was maintained until E15.5 when expression levels started to drop in most tissues, with those of the nervous system, tooth, and kidney being exceptions. Strongly expressed in early mesenchyme. The expression decreased as the mesenchyme differentiated. Ref.1
Sequence similarities	Belongs to the 14-3-3 family.

Ontologies

Keywords
Cellular component	Cytoplasm
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cerebral cortex development Inferred from mutant phenotype Ref.7. Source: MGI hippocampus development Inferred from mutant phenotype Ref.7. Source: MGI negative regulation of protein dephosphorylation Inferred from direct assay Ref.7. Source: MGI neuron migration Inferred from mutant phenotype Ref.7. Source: MGI protein targeting Inferred from direct assay PubMed 12446771. Source: MGI
Cellular_component	axon part Inferred from electronic annotation. Source: Compara cytoplasmic vesicle membrane Traceable author statement. Source: Reactome cytosol Traceable author statement. Source: Reactome kinesin complex Inferred from electronic annotation. Source: Compara melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 14651853. Source: MGI
Molecular_function	protein domain specific binding Inferred from direct assay PubMed 12446771. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Fbxo4	Q8CHQ0	2	EBI-356480,EBI-3895153
Lrrk2	Q5S006	3	EBI-356480,EBI-2693710

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 255

255

14-3-3 protein epsilon

PRO_0000058619

Sites

Site

Interaction with phosphoserine on interacting protein By similarity

Site

130

Interaction with phosphoserine on interacting protein By similarity

Amino acid modifications

Modified residue

N-acetylmethionine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

118

N6-acetyllysine By similarity

Modified residue

123

N6-acetyllysine By similarity

Modified residue

210

Phosphoserine Ref.10

Sequences

Sequence

Length

Mass (Da)

Tools

P62259 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 07817CCBD1F75B26
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FASTA

255

29,174

        10         20         30         40         50         60 
MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW 

        70         80         90        100        110        120 
RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF 

       130        140        150        160        170        180 
YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF 

       190        200        210        220        230        240 
YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE 

       250 
EQNKEALQDV EDENQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The mouse 14-3-3 epsilon isoform, a kinase regulator whose expression pattern is modulated in mesenchyme and neuronal differentiation." McConnell J.E., Armstrong J.F., Bard J.B. Dev. Biol. 169:218-228(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE. Strain: Swiss. Tissue: Kidney.
[2]	Takihara Y., Irie K., Nomura M., Motaleb M., Matsumoto K., Shimada K. Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: 129/Sv.
[3]	"High-throughput sequence identification of gene coding variants within alcohol-related QTLs." Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M. Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ILS and ISS.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[5]	Lubec G., Klug S., Friebe K., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 131-141; 154-170 AND 197-215, MASS SPECTROMETRY. Tissue: Brain and Hippocampus.
[6]	"Identification of a novel interaction of 14-3-3 with p190RhoGEF." Zhai J., Lin H., Shamim M., Schlaepfer W.W., Canete-Soler R. J. Biol. Chem. 276:41318-41324(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARHGEF28.
[7]	"14-3-3epsilon is important for neuronal migration by binding to NUDEL: a molecular explanation for Miller-Dieker syndrome." Toyo-oka K., Shionoya A., Gambello M.J., Cardoso C., Leventer R., Ward H.L., Ayala R., Tsai L.-H., Dobyns W., Ledbetter D., Hirotsune S., Wynshaw-Boris A. Nat. Genet. 34:274-285(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NDEL1.
[8]	"Phosphorylation of grb10 regulates its interaction with 14-3-3." Urschel S., Bassermann F., Bai R.Y., Munch S., Peschel C., Duyster J. J. Biol. Chem. 280:16987-16993(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRB10.
[9]	"Rho-kinase modulates the function of STEF, a Rac GEF, through its phosphorylation." Takefuji M., Mori K., Morita Y., Arimura N., Nishimura T., Nakayama M., Hoshino M., Iwamatsu A., Murohara T., Kaibuchi K., Amano M. Biochem. Biophys. Res. Commun. 355:788-794(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TIAM2.
[10]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z19599 mRNA. Translation: CAA79659.1. D87663 mRNA. Translation: BAA13424.1. AF483478 mRNA. Translation: AAL90752.1. AF483479 mRNA. Translation: AAL90753.1. BC058686 mRNA. Translation: AAH58686.1.
IPI	IPI00118384.
PIR	S31975. I48337.
RefSeq	NP_033562.3. NM_009536.4.
UniGene	Mm.234700.
3D structure databases
ProteinModelPortal	P62259.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62259. 14 interactions.
MINT	MINT-209058.
PTM databases
PhosphoSite	P62259.
2D gel databases
REPRODUCTION-2DPAGE	P62259.
Proteomic databases
PaxDb	P62259.
PRIDE	P62259.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000067664; ENSMUSP00000070993; ENSMUSG00000020849.
GeneID	22627.
KEGG	mmu:22627.
UCSC	uc007ket.2. mouse.
Organism-specific databases
CTD	7531.
MGI	MGI:894689. Ywhae.
Phylogenomic databases
eggNOG	COG5040.
HOGENOM	HOG000240379.
HOVERGEN	HBG050423.
InParanoid	P62259.
KO	K06630.
OMA	KESALIM.
OrthoDB	EOG4HHP34.
Enzyme and pathway databases
Reactome	REACT_147847. Translocation of Glut4 to the Plasma Membrane.
Gene expression databases
ArrayExpress	P62259.
Bgee	P62259.
Genevestigator	P62259.
GermOnline	ENSMUSG00000020849. 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
ChiTaRS	YWHAE. mouse.
NextBio	302987.
SOURCE	Search...

Entry information

Entry name

1433E_MOUSE

Accession

Primary (citable) accession number: P62259
Secondary accession number(s): P29360, P42655, Q63631

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
Last sequence update:	July 5, 2004
Last modified:	May 29, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents