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Protein

14-3-3 protein beta/alpha

Gene

Ywhab

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. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2. Negative regulator of signaling cascades that mediate activatation of MAP kinases via AKAP13.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-111447. Activation of BAD and translocation to mitochondria.
R-MMU-1445148. Translocation of GLUT4 to the plasma membrane.
R-MMU-165159. mTOR signalling.
R-MMU-166208. mTORC1-mediated signalling.
R-MMU-2028269. Signaling by Hippo.
R-MMU-392517. Rap1 signalling.
R-MMU-450385. Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
R-MMU-5625740. RHO GTPases activate PKNs.
R-MMU-5628897. TP53 Regulates Metabolic Genes.
R-MMU-5673000. RAF activation.
R-MMU-5674135. MAP2K and MAPK activation.
R-MMU-5675221. Negative regulation of MAPK pathway.
R-MMU-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.

Names & Taxonomyi

Protein namesi
Recommended name:
14-3-3 protein beta/alpha
Alternative name(s):
Protein kinase C inhibitor protein 1
Short name:
KCIP-1
Cleaved into the following chain:
Gene namesi
Name:Ywhab
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1891917. Ywhab.

Subcellular locationi

  • Cytoplasm By similarity
  • Melanosome By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24624614-3-3 protein beta/alphaPRO_0000367902Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 24624514-3-3 protein beta/alpha, N-terminally processedPRO_0000000005Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylthreonine; in 14-3-3 protein beta/alpha, N-terminally processedBy similarity
Modified residuei5 – 51N6-acetyllysineBy similarity
Modified residuei51 – 511N6-acetyllysineBy similarity
Modified residuei60 – 601Phosphoserine1 Publication
Modified residuei70 – 701N6-acetyllysineBy similarity
Modified residuei84 – 841Nitrated tyrosineCombined sources
Modified residuei106 – 1061Nitrated tyrosineCombined sources
Modified residuei117 – 1171N6-acetyllysineBy similarity
Modified residuei186 – 1861PhosphoserineBy similarity
Modified residuei232 – 2321PhosphoserineBy similarity
Isoform Short (identifier: Q9CQV8-2)
Modified residuei1 – 11N-acetylmethionine By similarityBy similarity

Post-translational modificationi

Isoform alpha differs from isoform beta in being phosphorylated (By similarity). Phosphorylated on Ser-60 by protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion.By similarity1 Publication
Isoform Short contains a N-acetylmethionine at position 1.By similarity

Keywords - PTMi

Acetylation, Nitration, Phosphoprotein

Proteomic databases

EPDiQ9CQV8.
MaxQBiQ9CQV8.
PaxDbiQ9CQV8.
PRIDEiQ9CQV8.
TopDownProteomicsiQ9CQV8-1. [Q9CQV8-1]

2D gel databases

UCD-2DPAGEQ9CQV8.

PTM databases

iPTMnetiQ9CQV8.
PhosphoSiteiQ9CQV8.
SwissPalmiQ9CQV8.

Expressioni

Gene expression databases

BgeeiQ9CQV8.
ExpressionAtlasiQ9CQV8. baseline and differential.
GenevisibleiQ9CQV8. MM.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with SAMSN1 and PRKCE (PubMed:18604201, PubMed:20478393). Interacts with AKAP13. Interacts with SSH1 and TORC2/CRTC2. Interacts with ABL1; the interaction results in cytoplasmic location of ABL1 and inhibition of cABL-mediated apoptosis. Interacts with ROR2 (dimer); the interaction results in phosphorylation of YWHAB on tyrosine residues. Interacts with GAB2. Interacts with YAP1 (phosphorylated form). Interacts with the phosphorylated (by AKT1) form of SRPK2. Interacts with PKA-phosphorylated AANAT. Interacts with MYO1C. Interacts with SIRT2 (By similarity). Interacts with the 'Thr-369' phosphorylated form of DAPK2 (PubMed:26047703).By similarity3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei58 – 581Interaction with phosphoserine on interacting proteinBy similarity
Sitei129 – 1291Interaction with phosphoserine on interacting proteinBy similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Lrrk2Q5S0063EBI-771608,EBI-2693710
PrkceP160546EBI-771608,EBI-298451
Synpo2Q91YE83EBI-771608,EBI-7623057

GO - Molecular functioni

Protein-protein interaction databases

BioGridi207648. 23 interactions.
IntActiQ9CQV8. 626 interactions.
MINTiMINT-1869492.
STRINGi10090.ENSMUSP00000018470.

Structurei

Secondary structure

1
246
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1713Combined sources
Helixi21 – 3313Combined sources
Helixi40 – 6829Combined sources
Helixi75 – 10531Combined sources
Helixi107 – 1104Combined sources
Helixi114 – 13421Combined sources
Helixi137 – 16125Combined sources
Helixi167 – 18216Combined sources
Helixi187 – 20317Combined sources
Helixi205 – 2073Combined sources
Turni210 – 2123Combined sources
Helixi213 – 23018Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GNTX-ray2.41A1-239[»]
5F74X-ray2.35A1-246[»]
ProteinModelPortaliQ9CQV8.
SMRiQ9CQV8. Positions 2-232.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 14-3-3 family.Curated

Phylogenomic databases

eggNOGiKOG0841. Eukaryota.
COG5040. LUCA.
GeneTreeiENSGT00760000119116.
HOGENOMiHOG000240379.
HOVERGENiHBG050423.
InParanoidiQ9CQV8.
KOiK16197.
OMAiMGREYRE.
OrthoDBiEOG7HHWT3.
PhylomeDBiQ9CQV8.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform Long (identifier: Q9CQV8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY
60 70 80 90 100
KNVVGARRSS WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL
110 120 130 140 150
ELLDKYLILN ATQAESKVFY LKMKGDYFRY LSEVASGENK QTTVSNSQQA
160 170 180 190 200
YQEAFEISKK EMQPTHPIRL GLALNFSVFY YEILNSPEKA CSLAKTAFDE
210 220 230 240
AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD AGEGEN
Length:246
Mass (Da):28,086
Last modified:January 23, 2007 - v3
Checksum:i51C366ED85B38EED
GO
Isoform Short (identifier: Q9CQV8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: Missing.

Note: No experimental confirmation available.By similarity
Show »
Length:244
Mass (Da):27,854
Checksum:iF42896ED9EC6F0D5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101Q → H in AAC14343 (Ref. 1) Curated
Sequence conflicti74 – 741N → D in AAC14343 (Ref. 1) Curated
Sequence conflicti126 – 1261D → Y in BAE29538 (PubMed:16141072).Curated
Sequence conflicti126 – 1261D → Y in BAE30278 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 22Missing in isoform Short. CuratedVSP_018634

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF058797 mRNA. Translation: AAC14343.1.
AK002632 mRNA. Translation: BAB22246.1.
AK004872 mRNA. Translation: BAB23631.1.
AK011389 mRNA. Translation: BAB27587.1.
AK083367 mRNA. Translation: BAC38886.1.
AK144061 mRNA. Translation: BAE25678.1.
AK150414 mRNA. Translation: BAE29538.1.
AK151294 mRNA. Translation: BAE30278.1.
AK158932 mRNA. Translation: BAE34730.1.
CCDSiCCDS17019.1. [Q9CQV8-1]
RefSeqiNP_061223.2. NM_018753.6. [Q9CQV8-1]
XP_006499972.1. XM_006499909.1. [Q9CQV8-1]
UniGeneiMm.34319.
Mm.491117.

Genome annotation databases

EnsembliENSMUST00000018470; ENSMUSP00000018470; ENSMUSG00000018326. [Q9CQV8-1]
GeneIDi54401.
KEGGimmu:54401.
UCSCiuc008ntp.1. mouse. [Q9CQV8-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF058797 mRNA. Translation: AAC14343.1.
AK002632 mRNA. Translation: BAB22246.1.
AK004872 mRNA. Translation: BAB23631.1.
AK011389 mRNA. Translation: BAB27587.1.
AK083367 mRNA. Translation: BAC38886.1.
AK144061 mRNA. Translation: BAE25678.1.
AK150414 mRNA. Translation: BAE29538.1.
AK151294 mRNA. Translation: BAE30278.1.
AK158932 mRNA. Translation: BAE34730.1.
CCDSiCCDS17019.1. [Q9CQV8-1]
RefSeqiNP_061223.2. NM_018753.6. [Q9CQV8-1]
XP_006499972.1. XM_006499909.1. [Q9CQV8-1]
UniGeneiMm.34319.
Mm.491117.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GNTX-ray2.41A1-239[»]
5F74X-ray2.35A1-246[»]
ProteinModelPortaliQ9CQV8.
SMRiQ9CQV8. Positions 2-232.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207648. 23 interactions.
IntActiQ9CQV8. 626 interactions.
MINTiMINT-1869492.
STRINGi10090.ENSMUSP00000018470.

PTM databases

iPTMnetiQ9CQV8.
PhosphoSiteiQ9CQV8.
SwissPalmiQ9CQV8.

2D gel databases

UCD-2DPAGEQ9CQV8.

Proteomic databases

EPDiQ9CQV8.
MaxQBiQ9CQV8.
PaxDbiQ9CQV8.
PRIDEiQ9CQV8.
TopDownProteomicsiQ9CQV8-1. [Q9CQV8-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000018470; ENSMUSP00000018470; ENSMUSG00000018326. [Q9CQV8-1]
GeneIDi54401.
KEGGimmu:54401.
UCSCiuc008ntp.1. mouse. [Q9CQV8-1]

Organism-specific databases

CTDi7529.
MGIiMGI:1891917. Ywhab.

Phylogenomic databases

eggNOGiKOG0841. Eukaryota.
COG5040. LUCA.
GeneTreeiENSGT00760000119116.
HOGENOMiHOG000240379.
HOVERGENiHBG050423.
InParanoidiQ9CQV8.
KOiK16197.
OMAiMGREYRE.
OrthoDBiEOG7HHWT3.
PhylomeDBiQ9CQV8.
TreeFamiTF102003.

Enzyme and pathway databases

ReactomeiR-MMU-111447. Activation of BAD and translocation to mitochondria.
R-MMU-1445148. Translocation of GLUT4 to the plasma membrane.
R-MMU-165159. mTOR signalling.
R-MMU-166208. mTORC1-mediated signalling.
R-MMU-2028269. Signaling by Hippo.
R-MMU-392517. Rap1 signalling.
R-MMU-450385. Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
R-MMU-5625740. RHO GTPases activate PKNs.
R-MMU-5628897. TP53 Regulates Metabolic Genes.
R-MMU-5673000. RAF activation.
R-MMU-5674135. MAP2K and MAPK activation.
R-MMU-5675221. Negative regulation of MAPK pathway.
R-MMU-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.

Miscellaneous databases

ChiTaRSiYwhab. mouse.
NextBioi311260.
PROiQ9CQV8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQV8.
ExpressionAtlasiQ9CQV8. baseline and differential.
GenevisibleiQ9CQV8. 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. Karpitskiy V.V., Shaw A.S.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  2. "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: Bone marrow, Embryo, Kidney, Liver, Thymus and Visual cortex.
  3. Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-12; 14-57; 61-70; 84-117; 128-169; 196-246 AND 215-224, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J and OF1.
    Tissue: Brain and Hippocampus.
  4. "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-60.
  5. Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-84 AND TYR-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  6. "The regulated assembly of a PKCepsilon complex controls the completion of cytokinesis."
    Saurin A.T., Durgan J., Cameron A.J., Faisal A., Marber M.S., Parker P.J.
    Nat. Cell Biol. 10:891-901(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRKCE.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. Cited for: INTERACTION WITH SAMSN1.
  9. "Suppression of death-associated protein kinase 2 by interaction with 14-3-3 proteins."
    Yuasa K., Ota R., Matsuda S., Isshiki K., Inoue M., Tsuji A.
    Biochem. Biophys. Res. Commun. 464:70-75(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAPK2.

Entry informationi

Entry namei1433B_MOUSE
AccessioniPrimary (citable) accession number: Q9CQV8
Secondary accession number(s): O70455, Q3TY33, Q3UAN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.