P31946 · 1433B_HUMAN
- Protein14-3-3 protein beta/alpha
- GeneYWHAB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids246 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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. 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 activation of MAP kinases via AKAP13.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 58 | Interaction with phosphoserine on interacting protein | ||||
Sequence: R | ||||||
Site | 129 | Interaction with phosphoserine on interacting protein | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | focal adhesion | |
Cellular Component | melanosome | |
Cellular Component | membrane | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | vacuolar membrane | |
Molecular Function | cadherin binding | |
Molecular Function | enzyme binding | |
Molecular Function | histone deacetylase binding | |
Molecular Function | identical protein binding | |
Molecular Function | phosphoprotein binding | |
Molecular Function | phosphoserine residue binding | |
Molecular Function | protein domain specific binding | |
Molecular Function | protein kinase inhibitor activity | |
Biological Process | cytoplasmic sequestering of protein | |
Biological Process | negative regulation of G protein-coupled receptor signaling pathway | |
Biological Process | negative regulation of protein dephosphorylation | |
Biological Process | positive regulation of catalytic activity | |
Biological Process | protein localization | |
Biological Process | protein targeting | |
Biological Process | signal transduction |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name14-3-3 protein beta/alpha
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP31946
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Note: (Microbial infection) Upon infection with Chlamydia trachomatis, this protein is associated with the pathogen-containing vacuole membrane where it colocalizes with IncG.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_064762 | 99 | found in a renal cell carcinoma sample; somatic mutation | |||
Sequence: V → I |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 191 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed; alternate | ||||
Sequence: M | |||||||
Modified residue | 1 | UniProt | N-acetylmethionine; in 14-3-3 protein beta/alpha; alternate | ||||
Sequence: M | |||||||
Modified residue | 1 | UniProt | In isoform P31946-2; N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000367900 | 1-246 | UniProt | 14-3-3 protein beta/alpha | |||
Sequence: MTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLELLDKYLIPNATQPESKVFYLKMKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGDEGDAGEGEN | |||||||
Modified residue | 2 | UniProt | N-acetylthreonine; in 14-3-3 protein beta/alpha, N-terminally processed | ||||
Sequence: T | |||||||
Modified residue | 2 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Chain | PRO_0000000003 | 2-246 | UniProt | 14-3-3 protein beta/alpha, N-terminally processed | |||
Sequence: TMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLELLDKYLIPNATQPESKVFYLKMKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGDEGDAGEGEN | |||||||
Modified residue | 5 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 6 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 32 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 39 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 47 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 50 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 51 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 51 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 60 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 70 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 84 | UniProt | 3'-nitrotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 106 | UniProt | 3'-nitrotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 117 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 130 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 132 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 136 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 186 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 212 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 213 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 216 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 217 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 232 | UniProt | Phosphoserine | ||||
Sequence: S |
Post-translational modification
The alpha, brain-specific form differs from the beta form in being phosphorylated. Phosphorylated on Ser-60 by protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Interaction
Subunit
Homodimer (PubMed:17717073).
Interacts with SAMSN1 and PRKCE (By similarity).
Interacts with AKAP13 (PubMed:21224381).
Interacts with SSH1 and TORC2/CRTC2 (PubMed:15159416, PubMed:15454081).
Interacts with ABL1; the interaction results in cytoplasmic location of ABL1 and inhibition of cABL-mediated apoptosis (PubMed:15696159).
Interacts with ROR2 (dimer); the interaction results in phosphorylation of YWHAB on tyrosine residues (PubMed:17717073).
Interacts with GAB2 (PubMed:19172738).
Interacts with YAP1 (phosphorylated form) (PubMed:17974916).
Interacts with the phosphorylated (by AKT1) form of SRPK2 (PubMed:19592491).
Interacts with PKA-phosphorylated AANAT (PubMed:11427721).
Interacts with MYO1C (PubMed:24636949).
Interacts with SIRT2 (PubMed:18249187).
Interacts with the 'Thr-369' phosphorylated form of DAPK2 (PubMed:26047703).
Interacts with PI4KB, TBC1D22A and TBC1D22B (PubMed:23572552).
Interacts with the 'Ser-1134' and 'Ser-1161' phosphorylated form of SOS1 (PubMed:22827337).
Interacts (via phosphorylated form) with YWHAB; this interaction occurs in a protein kinase AKT1-dependent manner (PubMed:15538381).
Interacts with SLITRK1 (PubMed:19640509).
Interacts with SYNPO2 (phosphorylated form); YWHAB competes with ACTN2 for interaction with SYNPO2 (By similarity).
Interacts with RIPOR2 (via phosphorylated form) isoform 2; this interaction occurs in a chemokine-dependent manner and does not compete for binding of RIPOR2 with RHOA nor blocks inhibition of RIPOR2-mediated RHOA activity (PubMed:25588844).
Interacts with MARK2 and MARK3 (PubMed:16959763).
Interacts with TESK1; the interaction is dependent on the phosphorylation of TESK1 'Ser-437' and inhibits TESK1 kinase activity (PubMed:11555644).
Interacts with MEFV (PubMed:27030597).
Interacts with HDAC4 (PubMed:33537682).
Interacts with ADAM22 (via C-terminus) (PubMed:15882968).
Interacts with SAMSN1 and PRKCE (By similarity).
Interacts with AKAP13 (PubMed:21224381).
Interacts with SSH1 and TORC2/CRTC2 (PubMed:15159416, PubMed:15454081).
Interacts with ABL1; the interaction results in cytoplasmic location of ABL1 and inhibition of cABL-mediated apoptosis (PubMed:15696159).
Interacts with ROR2 (dimer); the interaction results in phosphorylation of YWHAB on tyrosine residues (PubMed:17717073).
Interacts with GAB2 (PubMed:19172738).
Interacts with YAP1 (phosphorylated form) (PubMed:17974916).
Interacts with the phosphorylated (by AKT1) form of SRPK2 (PubMed:19592491).
Interacts with PKA-phosphorylated AANAT (PubMed:11427721).
Interacts with MYO1C (PubMed:24636949).
Interacts with SIRT2 (PubMed:18249187).
Interacts with the 'Thr-369' phosphorylated form of DAPK2 (PubMed:26047703).
Interacts with PI4KB, TBC1D22A and TBC1D22B (PubMed:23572552).
Interacts with the 'Ser-1134' and 'Ser-1161' phosphorylated form of SOS1 (PubMed:22827337).
Interacts (via phosphorylated form) with YWHAB; this interaction occurs in a protein kinase AKT1-dependent manner (PubMed:15538381).
Interacts with SLITRK1 (PubMed:19640509).
Interacts with SYNPO2 (phosphorylated form); YWHAB competes with ACTN2 for interaction with SYNPO2 (By similarity).
Interacts with RIPOR2 (via phosphorylated form) isoform 2; this interaction occurs in a chemokine-dependent manner and does not compete for binding of RIPOR2 with RHOA nor blocks inhibition of RIPOR2-mediated RHOA activity (PubMed:25588844).
Interacts with MARK2 and MARK3 (PubMed:16959763).
Interacts with TESK1; the interaction is dependent on the phosphorylation of TESK1 'Ser-437' and inhibits TESK1 kinase activity (PubMed:11555644).
Interacts with MEFV (PubMed:27030597).
Interacts with HDAC4 (PubMed:33537682).
Interacts with ADAM22 (via C-terminus) (PubMed:15882968).
(Microbial infection) Interacts with herpes simplex virus 1 protein UL46.
(Microbial infection) Probably interacts with Chlamydia trachomatis protein IncG.
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative initiation.
P31946-1
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.
- NameLong
- Length246
- Mass (Da)28,082
- Last updated2007-01-23 v3
- Checksum6BE1A9BF97468017
P31946-2
- NameShort
- Differences from canonical
- 1-2: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0J9YWE8 | A0A0J9YWE8_HUMAN | YWHAB | 149 | ||
A0A0J9YWZ2 | A0A0J9YWZ2_HUMAN | YWHAB | 81 | ||
Q4VY19 | Q4VY19_HUMAN | YWHAB | 100 | ||
Q4VY20 | Q4VY20_HUMAN | YWHAB | 74 |
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_018632 | 1-2 | in isoform Short | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X57346 EMBL· GenBank· DDBJ | CAA40621.1 EMBL· GenBank· DDBJ | mRNA | ||
AK292717 EMBL· GenBank· DDBJ | BAF85406.1 EMBL· GenBank· DDBJ | mRNA | ||
AL008725 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471077 EMBL· GenBank· DDBJ | EAW75893.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471077 EMBL· GenBank· DDBJ | EAW75894.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471077 EMBL· GenBank· DDBJ | EAW75896.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC001359 EMBL· GenBank· DDBJ | AAH01359.1 EMBL· GenBank· DDBJ | mRNA |