P68510 (1433F_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
14-3-3 protein eta

Gene names

Name:

Ywhah

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	246 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. Negatively regulates the kinase activity of PDPK1 By similarity.
Subunit structure	Homodimer By similarity. Interacts with many nuclear hormone receptors and cofactors including AR, ESR1, ESR2, MC2R, NR3C1, NRIP1, PPARBP and THRA. Interacts with ABL1 (phosphorylated form); the interaction retains it in the cytoplasm. Weakly interacts with CDKN1B By similarity. Interacts with ARHGEF28 and CDK16. Interacts with KCNK18 in a phosphorylation-dependent manner. Interacts with SAMSN1. Interacts with the 'Ser-241' phosphorylated form of PDPK1 By similarity. Ref.1 Ref.9 Ref.10 Ref.12
Subcellular location	Cytoplasm.
Post-translational modification	Phosphorylated on Ser-59 by protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion. Ref.8
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	cytoskeleton organization Non-traceable author statement PubMed 12176032. Source: ProtInc glucocorticoid catabolic process Inferred from sequence or structural similarity. Source: UniProtKB glucocorticoid receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB intracellular protein transport Inferred from direct assay PubMed 12446771. Source: MGI negative regulation of apoptotic process Non-traceable author statement PubMed 12176032. Source: ProtInc negative regulation of dendrite morphogenesis Inferred from direct assay Ref.3. Source: MGI positive regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB regulation of mitosis Non-traceable author statement PubMed 12176032. Source: ProtInc regulation of sodium ion transmembrane transporter activity Inferred from direct assay PubMed 16728661. Source: BHF-UCL
Cellular_component	cytoplasm Inferred from direct assay Ref.3. Source: MGI intercalated disc Inferred by curator PubMed 16728661. Source: BHF-UCL
Molecular_function	actin binding Inferred from direct assay PubMed 12176032. Source: ProtInc glucocorticoid receptor binding Inferred from sequence or structural similarity. Source: UniProtKB protein domain specific binding Inferred from direct assay PubMed 12446771. Source: MGI sodium channel regulator activity Inferred from direct assay PubMed 16728661. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Lrrk2	Q5S006	4	EBI-444641,EBI-2693710
TNFAIP3	P21580	3	EBI-444641,EBI-527670	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 246	245	14-3-3 protein eta		PRO_0000058624
Sites
	Site	57	1	Interaction with phosphoserine on interacting protein By similarity
	Site	132	1	Interaction with phosphoserine on interacting protein By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylglycine By similarity
	Modified residue	25	1	Phosphoserine By similarity
	Modified residue	59	1	Phosphoserine Ref.8
	Modified residue	117	1	Phosphotyrosine Ref.11
Experimental info
	Sequence conflict	15 – 16	2	EQ → DE in BAA13422. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P68510 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: C12F62B4ABA76DA3	FASTA	246	28,212
	10 20 30 40 50 60 MGDREQLLQR ARLAEQAERY DDMASAMKAV TELNEPLSNE DRNLLSVAYK NVVGARRSSW 70 80 90 100 110 120 RVISSIEQKT MADGNEKKLE KVKAYREKIE KELETVCNDV LALLDKFLIK NCNDFQYESK 130 140 150 160 170 180 VFYLKMKGDY YRYLAEVASG EKKNSVVEAS EAAYKEAFEI SKEHMQPTHP IRLGLALNFS 190 200 210 220 230 240 VFYYEIQNAP EQACLLAKQA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDE EAGEGN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Cdk-like protein PCTAIRE-1 from mouse brain associates with p11 and 14-3-3 proteins." Sladeczek F., Camonis J.H., Burnol A.-F., Le Bouffant F. Mol. Gen. Genet. 254:571-577(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CDK16. Tissue: Brain.
[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]	"Association of the TLX-2 homeodomain and 14-3-3eta signaling proteins." Tang S.J., Seun T.-C., McInnes R.R., Buchwald M. J. Biol. Chem. 273:25356-25363(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Isolation and structure of the mouse 14-3-3 eta chain gene and the distribution of 14-3-3 eta mRNA in the mouse brain." Toyooka K., Muratake T., Watanabe H., Hayashi S., Ichikawa T., Usui H., Washiyama K., Kumanishi T., Takahashi Y. Brain Res. Mol. Brain Res. 100:13-20(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Heart, Kidney and Sympathetic ganglion.
[6]	"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: FVB/N. Tissue: Mammary tumor.
[7]	Lubec G., Kang S.U., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 13-56; 62-69; 92-106; 111-120; 133-172 AND 199-227, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[8]	"A novel sphingosine-dependent protein kinase (SDK1) specifically phosphorylates certain isoforms of 14-3-3 protein." Megidish T., Cooper J., Zhang L., Fu H., Hakomori S. J. Biol. Chem. 273:21834-21845(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-59.
[9]	"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.
[10]	"Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation." Czirjak G., Vuity D., Enyedi P. J. Biol. Chem. 283:15672-15680(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KCNK18.
[11]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-117, MASS SPECTROMETRY. Tissue: Brain.
[12]	"SLy2 targets the nuclear SAP30/HDAC1 complex." Brandt S., Ellwanger K., Beuter-Gunia C., Schuster M., Hausser A., Schmitz I., Beer-Hammer S. Int. J. Biochem. Cell Biol. 42:1472-1481(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SAMSN1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U57311 mRNA. Translation: AAC53256.1. D87661 mRNA. Translation: BAA13422.1. AF077002 mRNA. Translation: AAC36290.1. AB063572 Genomic DNA. Translation: BAB79599.1. AK077596 mRNA. Translation: BAC36887.1. AK149224 mRNA. Translation: BAE28768.1. AK168520 mRNA. Translation: BAE40399.1. AK169035 mRNA. Translation: BAE40826.1. AK169189 mRNA. Translation: BAE40965.1. BC008187 mRNA. Translation: AAH08187.1. BC061497 mRNA. Translation: AAH61497.1.
IPI	IPI00227392.
RefSeq	NP_035868.1. NM_011738.2.
UniGene	Mm.332314. Mm.409488.
3D structure databases
ProteinModelPortal	P68510.
SMR	P68510. Positions 2-236.
ModBase	Search...
Protein-protein interaction databases
IntAct	P68510. 8 interactions.
MINT	MINT-198030.
PTM databases
PhosphoSite	P68510.
2D gel databases
UCD-2DPAGE	P68510.
Proteomic databases
PaxDb	P68510.
PRIDE	P68510.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000019109; ENSMUSP00000019109; ENSMUSG00000018965.
GeneID	22629.
KEGG	mmu:22629.
UCSC	uc008xag.2. mouse.
Organism-specific databases
CTD	7533.
MGI	MGI:109194. Ywhah.
Phylogenomic databases
eggNOG	COG5040.
GeneTree	ENSGT00690000101832.
HOGENOM	HOG000240379.
HOVERGEN	HBG050423.
InParanoid	P68510.
KO	K16198.
OMA	ESSEAAY.
OrthoDB	EOG48PMM0.
Enzyme and pathway databases
Reactome	REACT_147847. Translocation of Glut4 to the Plasma Membrane.
Gene expression databases
Bgee	P68510.
Genevestigator	P68510.
GermOnline	ENSMUSG00000018965. 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
NextBio	302995.
SOURCE	Search...

Entry information

Entry name

1433F_MOUSE

Accession

Primary (citable) accession number: P68510
Secondary accession number(s): P11576, P70198, Q3TGZ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 23, 2004
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program