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Protein

14-3-3 protein gamma

Gene

Ywhag

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.

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • enzyme regulator activity Source: RGD
  • insulin-like growth factor receptor binding Source: UniProtKB
  • poly(A) RNA binding Source: Ensembl
  • protein kinase C binding Source: UniProtKB
  • receptor tyrosine kinase binding Source: RGD

GO - Biological processi

  • cellular response to insulin stimulus Source: RGD
  • protein targeting Source: Ensembl
  • regulation of catalytic activity Source: GOC
  • regulation of neuron differentiation Source: UniProtKB
  • regulation of synaptic plasticity Source: UniProtKB
  • signal transduction Source: RGD
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-RNO-111447. Activation of BAD and translocation to mitochondria.
R-RNO-1445148. Translocation of GLUT4 to the plasma membrane.
R-RNO-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-RNO-380259. Loss of Nlp from mitotic centrosomes.
R-RNO-380270. Recruitment of mitotic centrosome proteins and complexes.
R-RNO-5620912. Anchoring of the basal body to the plasma membrane.
R-RNO-5625740. RHO GTPases activate PKNs.
R-RNO-5628897. TP53 Regulates Metabolic Genes.
R-RNO-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.

Names & Taxonomyi

Protein namesi
Recommended name:
14-3-3 protein gamma
Cleaved into the following chain:
Gene namesi
Name:Ywhag
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi62002. Ywhag.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • extracellular exosome Source: Ensembl
  • focal adhesion Source: Ensembl
  • membrane Source: Ensembl
  • membrane-bounded vesicle Source: RGD
  • myelin sheath Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24724714-3-3 protein gammaPRO_0000367910Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 24724614-3-3 protein gamma, N-terminally processedPRO_0000058609Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylvaline; in 14-3-3 protein gamma, N-terminally processedBy similarity
Modified residuei71 – 711PhosphoserineBy similarity
Modified residuei133 – 1331PhosphotyrosineCombined sources
Modified residuei145 – 1451PhosphothreonineBy similarity
Modified residuei215 – 2151PhosphoserineCombined sources
Modified residuei234 – 2341PhosphothreonineBy similarity
Modified residuei235 – 2351PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by various PKC isozymes.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP61983.
PRIDEiP61983.

PTM databases

iPTMnetiP61983.
PhosphoSiteiP61983.

Expressioni

Tissue specificityi

Localized in neurons, and axonally transported to the nerve terminals. May be also present, at lower levels, in various other tissues.1 Publication

Gene expression databases

GenevisibleiP61983. RN.

Interactioni

Subunit structurei

Homodimer. Interacts with MDM4 (phosphorylated); negatively regulates MDM4 activity toward TP53. Interacts with RAF1, SSH1 and CRTC2/TORC2. Interacts with ABL1 (phosphorylated form); the interaction retains it in the cytoplasm. Interacts with GAB2, SAMSN1 and SIRT2 (By similarity). Interacts with PKA-phosphorylated AANAT. Interacts with the 'Thr-369' phosphorylated form of DAPK2 (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei57 – 571Interaction with phosphoserine on interacting proteinBy similarity
Sitei132 – 1321Interaction with phosphoserine on interacting proteinBy similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
LRRK2Q5S0076EBI-359821,EBI-5323863From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi248553. 4 interactions.
IntActiP61983. 4 interactions.
MINTiMINT-1205891.
STRINGi10116.ENSRNOP00000001954.

Chemistry

BindingDBiP61983.

Structurei

3D structure databases

ProteinModelPortaliP61983.
SMRiP61983. Positions 1-235.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 14-3-3 family.Curated

Phylogenomic databases

eggNOGiKOG0841. Eukaryota.
COG5040. LUCA.
GeneTreeiENSGT00760000119116.
HOGENOMiHOG000240379.
HOVERGENiHBG050423.
InParanoidiP61983.
KOiK16198.
OMAiIKNCGET.
OrthoDBiEOG7HHWT3.
PhylomeDBiP61983.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P61983-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK
60 70 80 90 100
NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV
110 120 130 140 150
LSLLDNYLIK NCSETQYESK VFYLKMKGDY YRYLAEVATG EKRATVVESS
160 170 180 190 200
EKAYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA
210 220 230 240
FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD DGGEGNN
Length:247
Mass (Da):28,303
Last modified:January 23, 2007 - v2
Checksum:iB0D16C6DE1F4455D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D17447 mRNA. Translation: BAA04261.1.
S55305 mRNA. Translation: AAA13844.1.
BC127496 mRNA. Translation: AAI27497.1.
PIRiB49023.
RefSeqiNP_062249.1. NM_019376.2.
UniGeneiRn.29936.

Genome annotation databases

EnsembliENSRNOT00000001954; ENSRNOP00000001954; ENSRNOG00000001436.
ENSRNOT00000084730; ENSRNOP00000069671; ENSRNOG00000001436.
GeneIDi56010.
KEGGirno:56010.
UCSCiRGD:62002. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D17447 mRNA. Translation: BAA04261.1.
S55305 mRNA. Translation: AAA13844.1.
BC127496 mRNA. Translation: AAI27497.1.
PIRiB49023.
RefSeqiNP_062249.1. NM_019376.2.
UniGeneiRn.29936.

3D structure databases

ProteinModelPortaliP61983.
SMRiP61983. Positions 1-235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248553. 4 interactions.
IntActiP61983. 4 interactions.
MINTiMINT-1205891.
STRINGi10116.ENSRNOP00000001954.

Chemistry

BindingDBiP61983.

PTM databases

iPTMnetiP61983.
PhosphoSiteiP61983.

Proteomic databases

PaxDbiP61983.
PRIDEiP61983.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000001954; ENSRNOP00000001954; ENSRNOG00000001436.
ENSRNOT00000084730; ENSRNOP00000069671; ENSRNOG00000001436.
GeneIDi56010.
KEGGirno:56010.
UCSCiRGD:62002. rat.

Organism-specific databases

CTDi7532.
RGDi62002. Ywhag.

Phylogenomic databases

eggNOGiKOG0841. Eukaryota.
COG5040. LUCA.
GeneTreeiENSGT00760000119116.
HOGENOMiHOG000240379.
HOVERGENiHBG050423.
InParanoidiP61983.
KOiK16198.
OMAiIKNCGET.
OrthoDBiEOG7HHWT3.
PhylomeDBiP61983.
TreeFamiTF102003.

Enzyme and pathway databases

ReactomeiR-RNO-111447. Activation of BAD and translocation to mitochondria.
R-RNO-1445148. Translocation of GLUT4 to the plasma membrane.
R-RNO-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-RNO-380259. Loss of Nlp from mitotic centrosomes.
R-RNO-380270. Recruitment of mitotic centrosome proteins and complexes.
R-RNO-5620912. Anchoring of the basal body to the plasma membrane.
R-RNO-5625740. RHO GTPases activate PKNs.
R-RNO-5628897. TP53 Regulates Metabolic Genes.
R-RNO-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.

Miscellaneous databases

NextBioi611075.
PROiP61983.

Gene expression databases

GenevisibleiP61983. RN.

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. "Molecular cloning of rat cDNAs for beta and gamma subtypes of 14-3-3 protein and developmental changes in expression of their mRNAs in the nervous system."
    Watanabe M., Isobe T., Ichimura T., Kuwano R., Takahashi Y., Kondo H.
    Brain Res. Mol. Brain Res. 17:135-146(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: Brown Norway and Wistar.
    Tissue: Brain.
  2. "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: Liver.
  3. Lubec G., Chen W.-Q., Kang S.U.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 5-10; 13-56; 62-69; 78-83; 89-120; 133-142 AND 126-247, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Hippocampus.
  4. "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 144-162, INTERACTION WITH AANAT, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-133 AND SER-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry namei1433G_RAT
AccessioniPrimary (citable) accession number: P61983
Secondary accession number(s): A0JPM0
, O70457, P35214, Q9UDP2, Q9UN99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 114 of the entry and version 2 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

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 one 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.