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Protein

14-3-3 protein epsilon

Gene

Ywhae

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei57 – 571Interaction with phosphoserine on interacting proteinBy similarity
Sitei130 – 1301Interaction with phosphoserine on interacting proteinBy similarity

GO - Molecular functioni

  1. enzyme binding Source: RGD
  2. poly(A) RNA binding Source: Ensembl
  3. potassium channel regulator activity Source: Ensembl
  4. protein complex binding Source: RGD
  5. protein kinase C inhibitor activity Source: RGD

GO - Biological processi

  1. cerebral cortex development Source: Ensembl
  2. hippocampus development Source: Ensembl
  3. negative regulation of peptidyl-serine dephosphorylation Source: Ensembl
  4. negative regulation of protein serine/threonine kinase activity Source: GOC
  5. neuron migration Source: Ensembl
  6. protein targeting Source: Ensembl
  7. regulation of membrane repolarization Source: Ensembl
  8. regulation of potassium ion transmembrane transporter activity Source: Ensembl
  9. signal transduction Source: RGD
  10. substantia nigra development Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_299983. Regulation of HSF1-mediated heat shock response.
REACT_309697. NADE modulates death signalling.
REACT_311560. HSF1 activation.
REACT_319206. Regulation of PLK1 Activity at G2/M Transition.
REACT_325897. Signaling by Hippo.
REACT_328763. Recruitment of mitotic centrosome proteins and complexes.
REACT_329529. Anchoring of the basal body to the plasma membrane.
REACT_330785. Activation of BAD and translocation to mitochondria.
REACT_333441. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_347820. Translocation of GLUT4 to the plasma membrane.
REACT_352967. Loss of Nlp from mitotic centrosomes.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Ywhae
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi62000. Ywhae.

Subcellular locationi

Cytoplasm By similarity. Melanosome By similarity

GO - Cellular componenti

  1. axon Source: RGD
  2. extracellular vesicular exosome Source: Ensembl
  3. focal adhesion Source: Ensembl
  4. kinesin complex Source: RGD
  5. melanosome Source: UniProtKB-SubCell
  6. membrane Source: Ensembl
  7. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25525514-3-3 protein epsilonPRO_0000058620Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei50 – 501N6-acetyllysineBy similarity
Modified residuei69 – 691N6-acetyllysineBy similarity
Modified residuei118 – 1181N6-acetyllysineBy similarity
Modified residuei123 – 1231N6-acetyllysineBy similarity
Modified residuei210 – 2101PhosphoserineBy similarity
Modified residuei232 – 2321PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP62260.
PRIDEiP62260.

2D gel databases

World-2DPAGE0004:P62260.

PTM databases

PhosphoSiteiP62260.

Expressioni

Developmental stagei

Present at high levels in the pineal gland early in development and decreased steadily thereafter.1 Publication

Gene expression databases

GenevestigatoriP62260.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CSNK1A1P678282EBI-356462,EBI-7540603From a different organism.
FBXO4Q9UKT52EBI-356462,EBI-960409From a different organism.

Protein-protein interaction databases

BioGridi248364. 8 interactions.
DIPiDIP-37260N.
IntActiP62260. 10 interactions.
MINTiMINT-1597410.
STRINGi10116.ENSRNOP00000007100.

Structurei

3D structure databases

ProteinModelPortaliP62260.
SMRiP62260. Positions 3-232.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 14-3-3 family.Curated

Phylogenomic databases

eggNOGiCOG5040.
GeneTreeiENSGT00760000119116.
HOGENOMiHOG000240379.
HOVERGENiHBG050423.
InParanoidiP62260.
KOiK06630.
OMAiMQESDKP.
OrthoDBiEOG7HHWT3.
PhylomeDBiP62260.
TreeFamiTF102003.

Family and domain databases

InterProiIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERiPTHR18860. PTHR18860. 1 hit.
PfamiPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFiPIRSF000868. 14-3-3. 1 hit.
PRINTSiPR00305. 1433ZETA.
SMARTiSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMiSSF48445. SSF48445. 1 hit.
PROSITEiPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P62260-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK
60 70 80 90 100
NVIGARRASW RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI
110 120 130 140 150
LDVLDKHLIP AANTGESKVF YYKMKGDYHR YLAEFATGND RKEAAENSLV
160 170 180 190 200
AYKAASDIAM TELPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD
210 220 230 240 250
DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE EQNKEALQDV

EDENQ
Length:255
Mass (Da):29,174
Last modified:July 5, 2004 - v1
Checksum:i07817CCBD1F75B26
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731K → T in AAC52676 (PubMed:8694795).Curated
Sequence conflicti120 – 1201F → S in AAC52676 (PubMed:8694795).Curated
Sequence conflicti123 – 1231K → Y in AAC52676 (PubMed:8694795).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84416 mRNA. Translation: AAC37659.1.
D30739 mRNA. Translation: BAA06401.1.
U53882 mRNA. Translation: AAC52676.1.
BC063163 mRNA. Translation: AAH63163.1.
PIRiJX0341.
RefSeqiNP_113791.1. NM_031603.1.
UniGeneiRn.4225.

Genome annotation databases

EnsembliENSRNOT00000007100; ENSRNOP00000007100; ENSRNOG00000005290.
GeneIDi29753.
KEGGirno:29753.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84416 mRNA. Translation: AAC37659.1.
D30739 mRNA. Translation: BAA06401.1.
U53882 mRNA. Translation: AAC52676.1.
BC063163 mRNA. Translation: AAH63163.1.
PIRiJX0341.
RefSeqiNP_113791.1. NM_031603.1.
UniGeneiRn.4225.

3D structure databases

ProteinModelPortaliP62260.
SMRiP62260. Positions 3-232.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248364. 8 interactions.
DIPiDIP-37260N.
IntActiP62260. 10 interactions.
MINTiMINT-1597410.
STRINGi10116.ENSRNOP00000007100.

PTM databases

PhosphoSiteiP62260.

2D gel databases

World-2DPAGE0004:P62260.

Proteomic databases

PaxDbiP62260.
PRIDEiP62260.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000007100; ENSRNOP00000007100; ENSRNOG00000005290.
GeneIDi29753.
KEGGirno:29753.

Organism-specific databases

CTDi7531.
RGDi62000. Ywhae.

Phylogenomic databases

eggNOGiCOG5040.
GeneTreeiENSGT00760000119116.
HOGENOMiHOG000240379.
HOVERGENiHBG050423.
InParanoidiP62260.
KOiK06630.
OMAiMQESDKP.
OrthoDBiEOG7HHWT3.
PhylomeDBiP62260.
TreeFamiTF102003.

Enzyme and pathway databases

ReactomeiREACT_299983. Regulation of HSF1-mediated heat shock response.
REACT_309697. NADE modulates death signalling.
REACT_311560. HSF1 activation.
REACT_319206. Regulation of PLK1 Activity at G2/M Transition.
REACT_325897. Signaling by Hippo.
REACT_328763. Recruitment of mitotic centrosome proteins and complexes.
REACT_329529. Anchoring of the basal body to the plasma membrane.
REACT_330785. Activation of BAD and translocation to mitochondria.
REACT_333441. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_347820. Translocation of GLUT4 to the plasma membrane.
REACT_352967. Loss of Nlp from mitotic centrosomes.

Miscellaneous databases

NextBioi610291.
PROiP62260.

Gene expression databases

GenevestigatoriP62260.

Family and domain databases

InterProiIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERiPTHR18860. PTHR18860. 1 hit.
PfamiPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFiPIRSF000868. 14-3-3. 1 hit.
PRINTSiPR00305. 1433ZETA.
SMARTiSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMiSSF48445. SSF48445. 1 hit.
PROSITEiPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1993) [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(1993) [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(1995) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary.
  5. Bienvenut W.V., von Kriegsheim A., Kolch W.
    Submitted (MAY-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 (AUG-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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 131-142 AND 154-170, INTERACTION WITH AANAT, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry namei1433E_RAT
AccessioniPrimary (citable) accession number: P62260
Secondary accession number(s): P29360, P42655, Q63631
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: April 1, 2015
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.