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P63101 (1433Z_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 zeta/delta
Alternative name(s):
Protein kinase C inhibitor protein 1
Short name=KCIP-1
SEZ-2
Gene names
Name:Ywhaz
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length245 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. 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 BSPRY. Interacts with Thr-phosphorylated ITGB2 By similarity. 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 By similarity. It may also prevent thiol-dependent inactivation By similarity. Interacts with AKT1; the interaction phosphorylates YWHAZ and modulates dimerization By similarity. Interacts with GAB2 By similarity. Interacts with SAMSN1. Interacts with BCL2L11 and TLK2. Ref.3 Ref.4 Ref.9 Ref.10 Ref.12 Ref.13

Subcellular location

Cytoplasm. Melanosome. Note: Located to stage I to stage IV melanosomes By similarity.

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. Ref.8

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_processhistamine secretion by mast cell

Inferred from electronic annotation. Source: Ensembl

protein targeting

Inferred from direct assay PubMed 12446771. Source: MGI

protein targeting to mitochondrion

Inferred from electronic annotation. Source: Ensembl

regulation of cell death

Inferred from genetic interaction PubMed 19451227. Source: MGI

response to drug

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell leading edge

Inferred from electronic annotation. Source: Ensembl

cytoplasmic vesicle membrane

Traceable author statement. Source: Reactome

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from electronic annotation. Source: Ensembl

mast cell granule

Inferred from electronic annotation. Source: GOC

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 14651853. Source: MGI

nucleus

Inferred from direct assay PubMed 15615787. Source: MGI

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprotein binding

Inferred from physical interaction Ref.10. Source: UniProtKB

protein domain specific binding

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Hist1h3iP6843317EBI-354751,EBI-1179609From a different organism.
Lrrk2Q5S0064EBI-354751,EBI-2693710
Mlf1Q9QWV43EBI-354751,EBI-354765

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24524514-3-3 protein zeta/delta
PRO_0000058628

Sites

Site561Interaction with phosphoserine on interacting protein By similarity
Site1271Interaction with phosphoserine on interacting protein By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue31N6-acetyllysine By similarity
Modified residue581Phosphoserine; by PKA Ref.8
Modified residue681N6-acetyllysine By similarity
Modified residue1841Phosphoserine By similarity
Modified residue2071Phosphoserine By similarity
Modified residue2321Phosphothreonine; by CK1 By similarity

Experimental info

Sequence conflict781M → V in BAA11751. Ref.4
Sequence conflict1391K → R in BAE36724. Ref.5
Sequence conflict218 – 2192MQ → IE in BAA13421. Ref.2
Sequence conflict2361E → D in BAA11751. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P63101 [UniParc].

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

FASTA24527,771
        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' references
[1]"Molecular characterization of seizure-related genes isolated by differential screening."
Kajiwara K., Nagawawa H., Shimizu-Nishikawa K., Ookura T., Kimura M., Sugaya E.
Biochem. Biophys. Res. Commun. 219:795-799(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Brain.
[2]"14-3-3 family members play an important role in tumorigenic transformation of NIH 3T3 cells and retinoic acid-mediated F9 cell differentiation."
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]"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.
[4]"14-3-3 zeta protein binds to the carboxyl half of mouse wee1 kinase."
Honda R., Ohba Y., Yasuda H.
Biochem. Biophys. Res. Commun. 230:262-265(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH WEE1.
[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. expand/collapse author list , 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: Blastocyst, Bone marrow macrophage, Egg, Embryonic kidney and Thymus.
[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: C57BL/6.
Tissue: Brain.
[7]Lubec G., Kang S.U., Klug S., Friebe K., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 12-55; 61-68; 84-115; 128-167 AND 194-245, IDENTIFICATION BY 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-58.
[9]"Nuclear localization of protein kinase U-alpha is regulated by 14-3-3."
Zhang S., Xing H., Muslin A.J.
J. Biol. Chem. 274:24865-24872(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TLK2.
[10]"MADM, a novel adaptor protein that mediates phosphorylation of the 14-3-3 binding site of myeloid leukemia factor 1."
Lim R., Winteringham L.N., Williams J.H., McCulloch R.K., Ingley E., Tiao J.Y.-H., Lalonde J.-P., Tsai S., Tilbrook P.A., Sun Y., Wu X., Morris S.W., Klinken S.P.
J. Biol. Chem. 277:40997-41008(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MLF1.
[11]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic 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.
[13]"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
D78647 mRNA. Translation: BAA11464.1.
D87660 mRNA. Translation: BAA13421.1.
U79231 mRNA. Translation: AAC53254.1.
D83037 mRNA. Translation: BAA11751.1.
AK083368 mRNA. Translation: BAC38887.1.
AK145657 mRNA. Translation: BAE26570.1.
AK146800 mRNA. Translation: BAE27442.1.
AK150381 mRNA. Translation: BAE29512.1.
AK151900 mRNA. Translation: BAE30783.1.
AK162099 mRNA. Translation: BAE36724.1.
AK167128 mRNA. Translation: BAE39275.1.
BC050891 mRNA. Translation: AAH50891.1.
BC089334 mRNA. Translation: AAH89334.1.
CCDSCCDS27432.1.
PIRJC5384.
RefSeqNP_001240734.1. NM_001253805.1.
NP_001240735.1. NM_001253806.1.
NP_035870.1. NM_011740.3.
UniGeneMm.3360.

3D structure databases

ProteinModelPortalP63101.
SMRP63101. Positions 1-230.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204623. 159 interactions.
DIPDIP-31894N.
IntActP63101. 686 interactions.
MINTMINT-101845.

PTM databases

PhosphoSiteP63101.

2D gel databases

REPRODUCTION-2DPAGEP63101.
UCD-2DPAGEP63101.

Proteomic databases

MaxQBP63101.
PaxDbP63101.
PRIDEP63101.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022894; ENSMUSP00000022894; ENSMUSG00000022285.
ENSMUST00000110361; ENSMUSP00000105990; ENSMUSG00000022285.
ENSMUST00000110362; ENSMUSP00000105991; ENSMUSG00000022285.
GeneID22631.
KEGGmmu:22631.
UCSCuc007vmz.2. mouse.

Organism-specific databases

CTD7534.
MGIMGI:109484. Ywhaz.

Phylogenomic databases

eggNOGCOG5040.
GeneTreeENSGT00730000110424.
HOGENOMHOG000240379.
HOVERGENHBG050423.
InParanoidP63101.
KOK16197.
OMARYDDMAG.
OrthoDBEOG7HHWT3.
PhylomeDBP63101.
TreeFamTF102003.

Enzyme and pathway databases

ReactomeREACT_147847. Translocation of Glut4 to the Plasma Membrane.

Gene expression databases

ArrayExpressP63101.
BgeeP63101.
GenevestigatorP63101.

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

ChiTaRSYWHAZ. mouse.
NextBio303003.
PROP63101.
SOURCESearch...

Entry information

Entry name1433Z_MOUSE
AccessionPrimary (citable) accession number: P63101
Secondary accession number(s): P35215 expand/collapse secondary AC list , P70197, P97286, Q3TSF1, Q5EBQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: July 9, 2014
This is version 110 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot