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Protein

14-3-3 protein beta/alpha

Gene

YWHAB

Organism
Ovis aries (Sheep)
Status
Reviewed-Annotation score: Annotation score: 3 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

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
OrganismiOvis aries (Sheep)
Taxonomic identifieri9940 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
Proteomesi
  • UP000002356 Componenti: Unplaced

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 – 19319314-3-3 protein beta/alphaPRO_0000367905Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 19319214-3-3 protein beta/alpha, N-terminally processedPRO_0000000009Add
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 processed1 Publication
Modified residuei5 – 51N6-acetyllysineBy similarity
Modified residuei51 – 511N6-acetyllysineBy similarity
Modified residuei60 – 601PhosphoserineBy similarity
Modified residuei70 – 701N6-acetyllysineBy similarity
Modified residuei84 – 841Nitrated tyrosineBy similarity
Modified residuei149 – 1491Phosphoserine1 Publication
Modified residuei183 – 1831PhosphoserineBy similarity
Isoform Short (identifier: P68251-2)
Modified residuei1 – 11N-acetylmethionine

Post-translational modificationi

Form alpha differs from form beta in being phosphorylated. Phosphorylated on Ser-60 by protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion (By similarity).By similarity

Keywords - PTMi

Acetylation, Nitration, Phosphoprotein

PTM databases

iPTMnetiP68251.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with SAMSN1 and PRKCE (By similarity). 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 (By similarity). Interacts with PKA-phosphorylated AANAT (PubMed:11427721). Interacts with MYO1C. Interacts with SIRT2 (By similarity). Interacts with the 'Thr-369' phosphorylated form of DAPK2 (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei58 – 581Interaction with phosphoserine on interacting proteinBy similarity
Sitei92 – 921Interaction with phosphoserine on interacting proteinBy similarity

Structurei

3D structure databases

ProteinModelPortaliP68251.
SMRiP68251. Positions 3-184.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 14-3-3 family.Curated

Phylogenomic databases

HOVERGENiHBG050423.

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. 2 hits.
[Graphical view]
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: Fragments.

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

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

Note: It is uncertain whether isoform Short is produced by alternative initiation or another biological event.

Isoform Long (identifier: P68251-1) [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 GKEYKMKGDY FRYLSEVASG
110 120 130 140 150
DNKQTTVSNS QQAYQEAFEI SKKEMQPTHP IRLGLALNFS VFYYEILNSP
160 170 180 190
EAIAELDTLN EESYKDSTLI MQLLRDNLTL WTSENQGDEG DAG
Length:193
Mass (Da):22,054
Last modified:January 23, 2007 - v2
Checksum:i923914FE5226E608
GO
Isoform Short (identifier: P68251-2) [UniParc]FASTAAdd to basket

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

Show »
Length:191
Mass (Da):21,821
Checksum:iF767595DE749678B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-adjacent residuesi84 – 852Curated
Non-adjacent residuesi150 – 1512Curated
Non-terminal residuei193 – 1931

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 22Missing in isoform Short. CuratedVSP_018636

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

3D structure databases

ProteinModelPortaliP68251.
SMRiP68251. Positions 3-184.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiP68251.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG050423.

Miscellaneous databases

NextBioi20806512.

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. 2 hits.
[Graphical view]
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

  1. "Multiple isoforms of a protein kinase C inhibitor (KCIP-1/14-3-3) from sheep brain. Amino acid sequence of phosphorylated forms."
    Toker A., Sellers L.A., Amess B., Patel Y., Harris A., Aitken A.
    Eur. J. Biochem. 206:453-461(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 3-193.
    Tissue: Brain.
  2. "Protein kinase C inhibitor proteins. Purification from sheep brain and sequence similarity to lipocortins and 14-3-3 protein."
    Toker A., Ellis C.A., Sellers L.A., Aitken A.
    Eur. J. Biochem. 191:421-429(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 3-24 (ISOFORM LONG).
    Tissue: Brain.
  3. "14-3-3 alpha and delta are the phosphorylated forms of raf-activating 14-3-3 beta and zeta. In vivo stoichiometric phosphorylation in brain at a Ser-Pro-Glu-Lys motif."
    Aitken A., Howell S., Jones D., Madrazo J., Patel Y.
    J. Biol. Chem. 270:5706-5709(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-149, IDENTIFICATION BY MASS SPECTROMETRY.
  4. "Electrospray mass spectroscopy analysis with online trapping of posttranslationally modified mammalian and avian brain 14-3-3 isoforms."
    Aitken A., Patel Y., Martin H., Jones D., Robinson K., Madrazo J., Howell S.
    J. Protein Chem. 13:463-465(1994)
    Cited for: ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "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: INTERACTION WITH AANAT.

Entry informationi

Entry namei1433B_SHEEP
AccessioniPrimary (citable) accession number: P68251
Secondary accession number(s): P29358
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 76 of the entry and version 2 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. 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.