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

Last modified June 11, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length255 AA.
Sequence statusComplete.
Protein existenceEvidence 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 componentCytoplasm
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcerebral cortex development

Inferred from electronic annotation. Source: Ensembl

hippocampus development

Inferred from electronic annotation. Source: Ensembl

negative regulation of peptidyl-serine dephosphorylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein serine/threonine kinase activity

Traceable author statement Ref.3. Source: GOC

neuron migration

Inferred from electronic annotation. Source: Ensembl

protein targeting

Inferred from electronic annotation. Source: Ensembl

regulation of membrane repolarization

Inferred from electronic annotation. Source: Ensembl

regulation of potassium ion transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.3. Source: RGD

   Cellular_componentaxon

Inferred from direct assay PubMed 17202468. Source: RGD

extracellular vesicular exosome

Inferred from electronic annotation. Source: Ensembl

kinesin complex

Inferred from direct assay PubMed 17202468. Source: RGD

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionenzyme binding

Inferred from physical interaction Ref.3. Source: RGD

potassium channel regulator activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 19860830PubMed 21242966. Source: IntAct

protein complex binding

Inferred from physical interaction PubMed 17202468. Source: RGD

protein kinase C inhibitor activity

Traceable author statement Ref.3. Source: RGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CSNK1A1P678282EBI-356462,EBI-7540603From a different organism.
FBXO4Q9UKT52EBI-356462,EBI-960409From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25525514-3-3 protein epsilon
PRO_0000058620

Sites

Site571Interaction with phosphoserine on interacting protein By similarity
Site1301Interaction with phosphoserine on interacting protein By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.5
Modified residue501N6-acetyllysine By similarity
Modified residue691N6-acetyllysine By similarity
Modified residue1181N6-acetyllysine By similarity
Modified residue1231N6-acetyllysine By similarity
Modified residue2101Phosphoserine By similarity

Experimental info

Sequence conflict731K → T in AAC52676. Ref.3
Sequence conflict1201F → S in AAC52676. Ref.3
Sequence conflict1231K → Y in AAC52676. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P62260 [UniParc].

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

FASTA25529,174
        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' 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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.
PIRJX0341.
RefSeqNP_113791.1. NM_031603.1.
UniGeneRn.4225.

3D structure databases

ProteinModelPortalP62260.
SMRP62260. Positions 3-232.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248364. 8 interactions.
DIPDIP-37260N.
IntActP62260. 9 interactions.
MINTMINT-1597410.
STRING10116.ENSRNOP00000007100.

PTM databases

PhosphoSiteP62260.

2D gel databases

World-2DPAGE0004:P62260.

Proteomic databases

PaxDbP62260.
PRIDEP62260.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000007100; ENSRNOP00000007100; ENSRNOG00000005290.
GeneID29753.
KEGGrno:29753.

Organism-specific databases

CTD7531.
RGD62000. Ywhae.

Phylogenomic databases

eggNOGCOG5040.
GeneTreeENSGT00730000110613.
HOGENOMHOG000240379.
HOVERGENHBG050423.
InParanoidP62260.
KOK06630.
OMAMQESDKP.
OrthoDBEOG7HHWT3.
PhylomeDBP62260.
TreeFamTF102003.

Gene expression databases

GenevestigatorP62260.

Family and domain databases

Gene3D1.20.190.20. 1 hit.
InterProIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERPTHR18860. PTHR18860. 1 hit.
PfamPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFPIRSF000868. 14-3-3. 1 hit.
PRINTSPR00305. 1433ZETA.
SMARTSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMSSF48445. SSF48445. 1 hit.
PROSITEPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio610291.
PROP62260.

Entry information

Entry name1433E_RAT
AccessionPrimary (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: June 11, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families