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Protein

14-3-3 protein zeta/delta

Gene

Ywhaz

Organism
Mus musculus (Mouse)
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
Sitei56 – 561Interaction with phosphoserine on interacting proteinBy similarity
Sitei127 – 1271Interaction with phosphoserine on interacting proteinBy similarity

GO - Molecular functioni

GO - Biological processi

  • establishment of Golgi localization Source: MGI
  • Golgi reassembly Source: MGI
  • protein targeting Source: MGI
  • regulation of cell death Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_291378. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
REACT_294984. Interleukin-3, 5 and GM-CSF signaling.
REACT_300665. KSRP destabilizes mRNA.
REACT_302653. Translocation of GLUT4 to the plasma membrane.
REACT_304203. GP1b-IX-V activation signalling.
REACT_307305. Rap1 signalling.
REACT_318722. Activation of BAD and translocation to mitochondria.
REACT_351655. deactivation of the beta-catenin transactivating complex.
REACT_358414. RHO GTPases activate PKNs.
REACT_360191. TP53 Regulates Metabolic Genes.

Names & Taxonomyi

Protein namesi
Recommended name:
14-3-3 protein zeta/delta
Alternative name(s):
Protein kinase C inhibitor protein 1
Short name:
KCIP-1
SEZ-2
Gene namesi
Name:Ywhaz
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:109484. Ywhaz.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: MGI
  • cytoplasmic vesicle membrane Source: Reactome
  • cytosol Source: Reactome
  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
  • focal adhesion Source: MGI
  • melanosome Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24524514-3-3 protein zeta/deltaPRO_0000058628Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei3 – 31N6-acetyllysineBy similarity
Modified residuei58 – 581Phosphoserine; by PKA1 Publication
Modified residuei68 – 681N6-acetyllysineBy similarity
Modified residuei184 – 1841PhosphoserineBy similarity
Modified residuei207 – 2071PhosphoserineBy similarity
Modified residuei232 – 2321Phosphothreonine; by CK1By similarity

Post-translational modificationi

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 similarity1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP63101.
PaxDbiP63101.
PRIDEiP63101.

2D gel databases

REPRODUCTION-2DPAGEP63101.
UCD-2DPAGEP63101.

PTM databases

PhosphoSiteiP63101.

Expressioni

Gene expression databases

BgeeiP63101.
ExpressionAtlasiP63101. baseline and differential.
GenevisibleiP63101. MM.

Interactioni

Subunit structurei

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.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Hist1h3iP6843317EBI-354751,EBI-1179609From a different organism.
Lrrk2Q5S0064EBI-354751,EBI-2693710
Mlf1Q9QWV43EBI-354751,EBI-354765

Protein-protein interaction databases

BioGridi204623. 163 interactions.
DIPiDIP-31894N.
IntActiP63101. 688 interactions.
MINTiMINT-101845.
STRINGi10090.ENSMUSP00000022894.

Structurei

3D structure databases

ProteinModelPortaliP63101.
SMRiP63101. Positions 1-230.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 14-3-3 family.Curated

Phylogenomic databases

eggNOGiCOG5040.
GeneTreeiENSGT00760000119116.
HOGENOMiHOG000240379.
HOVERGENiHBG050423.
InParanoidiP63101.
KOiK16197.
OMAiRYDDMAG.
OrthoDBiEOG7HHWT3.
PhylomeDBiP63101.
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.

P63101-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN
60 70 80 90 100
VVGARRSSWR VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL
110 120 130 140 150
LEKFLIPNAS QPESKVFYLK MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ
160 170 180 190 200
EAFEISKKEM QPTHPIRLGL ALNFSVFYYE ILNSPEKACS LAKTAFDEAI
210 220 230 240
AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG EGGEN
Length:245
Mass (Da):27,771
Last modified:September 13, 2004 - v1
Checksum:i2164DF3793B45B7A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 781M → V in BAA11751 (PubMed:9016762).Curated
Sequence conflicti139 – 1391K → R in BAE36724 (PubMed:16141072).Curated
Sequence conflicti218 – 2192MQ → IE in BAA13421 (Ref. 2) Curated
Sequence conflicti236 – 2361E → D in BAA11751 (PubMed:9016762).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS27432.1.
PIRiJC5384.
RefSeqiNP_001240734.1. NM_001253805.1.
NP_001240735.1. NM_001253806.1.
NP_035870.1. NM_011740.3.
XP_011243654.1. XM_011245352.1.
UniGeneiMm.3360.

Genome annotation databases

EnsembliENSMUST00000022894; ENSMUSP00000022894; ENSMUSG00000022285.
ENSMUST00000110361; ENSMUSP00000105990; ENSMUSG00000022285.
ENSMUST00000110362; ENSMUSP00000105991; ENSMUSG00000022285.
GeneIDi22631.
KEGGimmu:22631.
UCSCiuc007vmz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS27432.1.
PIRiJC5384.
RefSeqiNP_001240734.1. NM_001253805.1.
NP_001240735.1. NM_001253806.1.
NP_035870.1. NM_011740.3.
XP_011243654.1. XM_011245352.1.
UniGeneiMm.3360.

3D structure databases

ProteinModelPortaliP63101.
SMRiP63101. Positions 1-230.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204623. 163 interactions.
DIPiDIP-31894N.
IntActiP63101. 688 interactions.
MINTiMINT-101845.
STRINGi10090.ENSMUSP00000022894.

PTM databases

PhosphoSiteiP63101.

2D gel databases

REPRODUCTION-2DPAGEP63101.
UCD-2DPAGEP63101.

Proteomic databases

MaxQBiP63101.
PaxDbiP63101.
PRIDEiP63101.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022894; ENSMUSP00000022894; ENSMUSG00000022285.
ENSMUST00000110361; ENSMUSP00000105990; ENSMUSG00000022285.
ENSMUST00000110362; ENSMUSP00000105991; ENSMUSG00000022285.
GeneIDi22631.
KEGGimmu:22631.
UCSCiuc007vmz.2. mouse.

Organism-specific databases

CTDi7534.
MGIiMGI:109484. Ywhaz.

Phylogenomic databases

eggNOGiCOG5040.
GeneTreeiENSGT00760000119116.
HOGENOMiHOG000240379.
HOVERGENiHBG050423.
InParanoidiP63101.
KOiK16197.
OMAiRYDDMAG.
OrthoDBiEOG7HHWT3.
PhylomeDBiP63101.
TreeFamiTF102003.

Enzyme and pathway databases

ReactomeiREACT_291378. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
REACT_294984. Interleukin-3, 5 and GM-CSF signaling.
REACT_300665. KSRP destabilizes mRNA.
REACT_302653. Translocation of GLUT4 to the plasma membrane.
REACT_304203. GP1b-IX-V activation signalling.
REACT_307305. Rap1 signalling.
REACT_318722. Activation of BAD and translocation to mitochondria.
REACT_351655. deactivation of the beta-catenin transactivating complex.
REACT_358414. RHO GTPases activate PKNs.
REACT_360191. TP53 Regulates Metabolic Genes.

Miscellaneous databases

ChiTaRSiYwhaz. mouse.
NextBioi303003.
PROiP63101.
SOURCEiSearch...

Gene expression databases

BgeeiP63101.
ExpressionAtlasiP63101. baseline and differential.
GenevisibleiP63101. MM.

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 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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  12. 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.

Entry informationi

Entry namei1433Z_MOUSE
AccessioniPrimary (citable) accession number: P63101
Secondary accession number(s): P35215
, P70197, P97286, Q3TSF1, Q5EBQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: July 22, 2015
This is version 121 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.