14-3-3 protein zeta/delta - Rattus norvegicus (Rat)

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P63102 (1433Z_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 90. History...

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

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
14-3-3 protein zeta/delta

Alternative name(s):
Mitochondrial import stimulation factor S1 subunit
Protein kinase C inhibitor protein 1
Short name=KCIP-1

Gene names

Name:	Ywhaz
Synonyms:	Msfs1

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	245 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. Heterodimerizes with YWHAE By similarity. Homo- and hetero-dimerization is inhibited by phosphorylation on Ser-58 By similarity. Interacts with FOXO4, NOXA1, SSH1 and ARHGEF2. Interacts with CDK16 and with WEE1 (C-terminal). Interacts with MLF1 (phosphorylated form); the interaction retains it in the cytoplasm. Interacts with Thr-phosphorylated ITGB2. Interacts with Pseudomonas aeruginosa exoS (unphosphorylated form). Interacts with BAX; the interaction occurs in the cytoplasm. Under stress conditions, MAPK8-mediated phosphorylation releases BAX to mitochondria. Interacts with phosphorylated RAF1; the interaction is inhibited when YWHAZ is phosphorylated on Thr-232. Interacts with TP53; the interaction enhances p53 transcriptional activity. The Ser-58 phosphorylated form inhibits this interaction and p53 transcriptional activity. Interacts with ABL1 (phosphorylated form); the interaction retains ABL1 in the cytoplasm. Interacts with PKA-phosphorylated AANAT; the interaction modulates AANAT enzymatic activity by increasing affinity for arylalkylamines and acetyl-CoA and protecting the enzyme from dephosphorylation and proteasomal degradation. It may also prevent thiol-dependent inactivation. Interacts with AKT1; the interaction phosphorylates YWHAZ and modulates dimerization By similarity. Interacts with GAB2 and SAMSN1. Binds to TLK2 By similarity. Interacts with BSPRY. Interacts with BCL2L11. Ref.7 Ref.9 Ref.10
Subcellular location	Cytoplasm. Melanosome. Note: Located to stage I to stage IV melanosomes By similarity.
Tissue specificity	Highly expressed in brain (at protein level). Ref.9
Post-translational modification	The delta, brain-specific form differs from the zeta form in being phosphorylated By similarity. Phosphorylation on Ser-184 by MAPK8; promotes dissociation of BAX and translocation of BAX to mitochondria. Phosphorylation on Thr-232; inhibits binding of RAF1 By similarity. Phosphorylated on Ser-58 by PKA and protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion. Phosphorylation on Ser-58 by PKA; disrupts homodimerization and heterodimerization with YHAE and TP53 By similarity.
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	histamine secretion by mast cell Inferred from mutant phenotype PubMed 12499633. Source: RGD protein targeting to mitochondrion Inferred from direct assay Ref.3. Source: RGD regulation of cell death Inferred from electronic annotation. Source: Compara
Cellular_component	cell leading edge Inferred from direct assay Ref.9. Source: RGD melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 16981892. Source: RGD nucleus Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from direct assay Ref.9. Source: RGD postsynaptic density Inferred from direct assay PubMed 11178869. Source: RGD protein complex Inferred from direct assay PubMed 11563969. Source: RGD
Molecular_function	protein domain specific binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 245

245

14-3-3 protein zeta/delta

PRO_0000058630

Sites

Site

Interaction with phosphoserine on interacting protein By similarity

Site

127

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

Phosphoserine; by PKA By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

184

Phosphoserine By similarity

Modified residue

207

Phosphoserine By similarity

Modified residue

232

Phosphothreonine; by CK1 By similarity

Experimental info

Sequence conflict

T → M in AAA80544. Ref.2

Sequence conflict

109

A → R in AAC37660. Ref.8

Sequences

Sequence

Length

Mass (Da)

Tools

P63102 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 2164DF3793B45B7A
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FASTA

245

27,771

        10         20         30         40         50         60 
MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR 

        70         80         90        100        110        120 
VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNAS QPESKVFYLK 

       130        140        150        160        170        180 
MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE 

       190        200        210        220        230        240 
ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG 


EGGEN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of rat cDNAs for the zeta and theta subtypes of 14-3-3 protein and differential distributions of their mRNAs in the brain." Watanabe M., Isobe T., Ichimura T., Kuwano R., Takahashi Y., Kondo H., Inoue Y. Brain Res. Mol. Brain Res. 25:113-121(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Wistar. Tissue: Brain.
[2]	"A gene variation of 14-3-3 zeta isoform in rat hippocampus." Murakami K., Situ S.Y., Eshete F. Gene 179:245-249(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Hippocampus.
[3]	"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.
[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: Brain and Lung.
[5]	Bienvenut W.V., von Kriegsheim A., Kolch W. Submitted (JUN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-9; 12-49; 61-68; 92-115; 128-157 AND 213-222, ACETYLATION AT MET-1, MASS SPECTROMETRY. Tissue: Fibroblast and Pheochromocytoma.
[6]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U., Lubec S. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 12-55; 57-68; 84-115; 121-167; 159-187 AND 194-245, 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 28-41; 61-68 AND 128-139, INTERACTION WITH AANAT, MASS SPECTROMETRY.
[8]	"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] OF 58-245. Strain: Sprague-Dawley. Tissue: Pineal gland.
[9]	"Characterization of zetin 1/rBSPRY, a novel binding partner of 14-3-3 proteins." Birkenfeld J., Kartmann B., Anliker B., Ono K., Schloetcke B., Betz H., Roth D. Biochem. Biophys. Res. Commun. 302:526-533(2003) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INTERACTION WITH BSPRY.
[10]	"Identification of a novel Bcl-2-interacting mediator of cell death (Bim) E3 ligase, tripartite motif-containing protein 2 (TRIM2), and its role in rapid ischemic tolerance-induced neuroprotection." Thompson S., Pearson A.N., Ashley M.D., Jessick V., Murphy B.M., Gafken P., Henshall D.C., Morris K.T., Simon R.P., Meller R. J. Biol. Chem. 286:19331-19339(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BCL2L11.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D17615 mRNA. Translation: BAA04534.1. U37252 mRNA. Translation: AAA80544.1. D30740 mRNA. Translation: BAA06402.1. BC070941 mRNA. Translation: AAH70941.2. BC094305 mRNA. Translation: AAH94305.1. L07913 mRNA. Translation: AAC37660.1.
IPI	IPI00324893.
PIR	JC2502. JC5232. S59915.
RefSeq	NP_037143.2. NM_013011.3.
UniGene	Rn.1292.
3D structure databases
ProteinModelPortal	P63102.
SMR	P63102. Positions 1-230.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-36916N. DIP-488N.
IntAct	P63102. 1 interaction.
MINT	MINT-197638.
PTM databases
PhosphoSite	P63102.
Proteomic databases
PaxDb	P63102.
PRIDE	P63102.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000035628; ENSRNOP00000030885; ENSRNOG00000008195.
GeneID	25578.
KEGG	rno:25578.
UCSC	RGD:3980. rat.
Organism-specific databases
CTD	7534.
RGD	3980. Ywhaz.
Phylogenomic databases
eggNOG	COG5040.
GeneTree	ENSGT00690000101832.
HOGENOM	HOG000240379.
HOVERGEN	HBG050423.
InParanoid	P63102.
KO	K16197.
OMA	VMDKNEL.
OrthoDB	EOG4N30PR.
Gene expression databases
Genevestigator	P63102.
GermOnline	ENSRNOG00000008195. 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	303003.

Entry information

Entry name

1433Z_RAT

Accession

Primary (citable) accession number: P63102
Secondary accession number(s): P35215

Q6IRF4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	September 13, 2004
Last modified:	May 1, 2013
This is version 90 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

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

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