14-3-3 protein epsilon - Rattus norvegicus (Rat)

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P62260 (1433E_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. History...

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

Documents (1) |

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

Alternative name(s):
Mitochondrial import stimulation factor L subunit
Short name=MSF L

Gene names

Name:

Ywhae

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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 By similarity. 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. Interacts with phosphorylated GRB10 By similarity. Interacts with PKA-phosphorylated AANAT. Interacts with the phosphorylated (by AKT1) form of SRPK2 By similarity. Ref.7
Subcellular location	Cytoplasm By similarity. Melanosome By similarity.
Developmental stage	Present at high levels in the pineal gland early in development and decreased steadily thereafter. 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 electronic annotation. Source: Compara hippocampus development Inferred from electronic annotation. Source: Compara negative regulation of protein dephosphorylation Inferred from electronic annotation. Source: Compara neuron migration Inferred from electronic annotation. Source: Compara protein targeting Inferred from electronic annotation. Source: Compara signal transduction Traceable author statement Ref.3. Source: RGD
Cellular_component	axon part Inferred from direct assay PubMed 17202468. Source: RGD kinesin complex Inferred from direct assay PubMed 17202468. Source: RGD melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	protein kinase C inhibitor activity Traceable author statement Ref.3. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FBXO4	Q9UKT5	2	EBI-356462,EBI-960409	From a different organism.

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_0000058620

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 Ref.5

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 By similarity

Experimental info

Sequence conflict

K → T in AAC52676. Ref.3

Sequence conflict

120

F → S in AAC52676. Ref.3

Sequence conflict

123

K → Y in AAC52676. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P62260 [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]	"Cloning and characterization of the epsilon and zeta isoforms of the 14-3-3 proteins." Roseboom P.H., Weller J.L., Babila T., Aitken A., Sellers L.A., Moffet J.R., Namboodiri M.A., Klein D.C. DNA Cell Biol. 13:629-640(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE. Tissue: Pineal gland.
[2]	"cDNA cloning and characterization of mitochondrial import stimulation factor (MSF) purified from rat liver cytosol." Alam R., Hachiya N., Sakaguchi M., Shun-Ichiro K., Iwanaga S., Kitajima M., Mihara K., Omura T. J. Biochem. 116:416-425(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"Association of a 14-3-3 protein with CMP-NeuAc:GM1 alpha 2,3-sialyltransferase." Gao L., Gu X.B., Yu D.S., Yu R.K., Zeng G. Biochem. Biophys. Res. Commun. 224:103-107(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[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]. Tissue: Pituitary.
[5]	Bienvenut W.V., von Kriegsheim A., Kolch W. Submitted (JUN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-12; 30-42; 95-106; 143-153 AND 216-225, ACETYLATION AT MET-1, MASS SPECTROMETRY. Tissue: Fibroblast.
[6]	Lubec G., Diao W., Afjehi-Sadat L., Chen W.-Q., Kang S.U., Lubec S. Submitted (SEP-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 20-50; 62-73; 87-94; 107-123; 131-170 AND 197-225, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain, Hippocampus and Spinal cord.
[7]	"Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-binding switch in melatonin synthesis." Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H., Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T., Beauverger P., Ferry G., Boutin J.A., Klein D.C. Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 131-142 AND 154-170, INTERACTION WITH AANAT, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M84416 mRNA. Translation: AAC37659.1. D30739 mRNA. Translation: BAA06401.1. U53882 mRNA. Translation: AAC52676.1. BC063163 mRNA. Translation: AAH63163.1.
IPI	IPI00325135.
PIR	JX0341.
RefSeq	NP_113791.1. NM_031603.1.
UniGene	Rn.4225.
3D structure databases
ProteinModelPortal	P62260.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-37260N.
IntAct	P62260. 5 interactions.
MINT	MINT-1597410.
STRING	10116.ENSRNOP00000007100.
PTM databases
PhosphoSite	P62260.
2D gel databases
World-2DPAGE	0004:P62260.
Proteomic databases
PaxDb	P62260.
PRIDE	P62260.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000007100; ENSRNOP00000007100; ENSRNOG00000005290.
GeneID	29753.
KEGG	rno:29753.
Organism-specific databases
CTD	7531.
RGD	62000. Ywhae.
Phylogenomic databases
eggNOG	COG5040.
GeneTree	ENSGT00690000101991.
HOGENOM	HOG000240379.
HOVERGEN	HBG050423.
InParanoid	P62260.
KO	K06630.
OMA	KESALIM.
OrthoDB	EOG4HHP34.
Gene expression databases
Genevestigator	P62260.
GermOnline	ENSRNOG00000005290. Rattus norvegicus.
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
NextBio	610291.

Entry information

Entry name

1433E_RAT

Accession

Primary (citable) accession number: P62260
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 1, 2013
This is version 91 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

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

Experimental info

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

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents