P31947 · 1433S_HUMAN
- Protein14-3-3 protein sigma
- GeneSFN
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids248 (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 (PubMed:15731107, PubMed:22634725, PubMed:28202711, PubMed:37797010).
Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif (PubMed:15731107, PubMed:22634725, PubMed:28202711, PubMed:37797010).
Binding generally results in the modulation of the activity of the binding partner (PubMed:15731107, PubMed:22634725, PubMed:28202711, PubMed:37797010).
Promotes cytosolic retention of GBP1 GTPase by binding to phosphorylated GBP1, thereby inhibiting the innate immune response (PubMed:37797010).
Also acts as a TP53/p53-regulated inhibitor of G2/M progression (PubMed:9659898).
When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway (By similarity).
Acts to maintain desmosome cell junction adhesion in epithelial cells via interacting with and sequestering PKP3 to the cytoplasm, thereby restricting its translocation to existing desmosome structures and therefore maintaining desmosome protein homeostasis (PubMed:24124604).
May also regulate MDM2 autoubiquitination and degradation and thereby activate p53/TP53 (PubMed:18382127).
Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif (PubMed:15731107, PubMed:22634725, PubMed:28202711, PubMed:37797010).
Binding generally results in the modulation of the activity of the binding partner (PubMed:15731107, PubMed:22634725, PubMed:28202711, PubMed:37797010).
Promotes cytosolic retention of GBP1 GTPase by binding to phosphorylated GBP1, thereby inhibiting the innate immune response (PubMed:37797010).
Also acts as a TP53/p53-regulated inhibitor of G2/M progression (PubMed:9659898).
When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway (By similarity).
Acts to maintain desmosome cell junction adhesion in epithelial cells via interacting with and sequestering PKP3 to the cytoplasm, thereby restricting its translocation to existing desmosome structures and therefore maintaining desmosome protein homeostasis (PubMed:24124604).
May also regulate MDM2 autoubiquitination and degradation and thereby activate p53/TP53 (PubMed:18382127).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 56 | Interaction with phosphoserine on interacting protein | ||||
Sequence: R | ||||||
Site | 129 | Interaction with phosphoserine on interacting protein | ||||
Sequence: R |
GO annotations
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name14-3-3 protein sigma
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP31947
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_048095 | 155 | in dbSNP:rs11542705 | |||
Sequence: M → I |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 263 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 chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000058643 | 1-248 | UniProt | 14-3-3 protein sigma | |||
Sequence: MERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSEEKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWTADNAGEEGGEAPQEPQS | |||||||
Modified residue | 5 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 37 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 45 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 48 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 74 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 74 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 130 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 207 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 209 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 216 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 217 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 248 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 248 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Ubiquitinated. Ubiquitination by RFFL induces proteasomal degradation and indirectly regulates p53/TP53 activation.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Interaction
Subunit
Homodimer (PubMed:28202711).
Interacts with KRT17 and SAMSN1 (By similarity).
Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29 and VPS35 (PubMed:15282546).
Interacts with GAB2 (PubMed:19172738).
Interacts with SRPK2 (PubMed:19592491).
Interacts with COPS6 (PubMed:21625211).
Interacts with COP1; this interaction leads to proteasomal degradation (PubMed:21625211).
Interacts with the 'Thr-369' phosphorylated form of DAPK2 (PubMed:26047703).
Interacts with PI4KB (PubMed:23572552).
Interacts with SLITRK1 (PubMed:19640509).
Interacts with LRRK2; this interaction is dependent on LRRK2 phosphorylation (PubMed:28202711).
Interacts with PKP3 (via N-terminus); the interaction maintains the cytoplasmic pool of PKP3 and restricts PKP3 localization to existing desmosome cell junctions (PubMed:24124604).
Interacts with LCP2 (PubMed:33159816).
Interacts with KRT17 and SAMSN1 (By similarity).
Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29 and VPS35 (PubMed:15282546).
Interacts with GAB2 (PubMed:19172738).
Interacts with SRPK2 (PubMed:19592491).
Interacts with COPS6 (PubMed:21625211).
Interacts with COP1; this interaction leads to proteasomal degradation (PubMed:21625211).
Interacts with the 'Thr-369' phosphorylated form of DAPK2 (PubMed:26047703).
Interacts with PI4KB (PubMed:23572552).
Interacts with SLITRK1 (PubMed:19640509).
Interacts with LRRK2; this interaction is dependent on LRRK2 phosphorylation (PubMed:28202711).
Interacts with PKP3 (via N-terminus); the interaction maintains the cytoplasmic pool of PKP3 and restricts PKP3 localization to existing desmosome cell junctions (PubMed:24124604).
Interacts with LCP2 (PubMed:33159816).
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P31947-1
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.
- Name1
- Length248
- Mass (Da)27,774
- Last updated1993-07-01 v1
- Checksum7F4B44E3AA59ECE6
P31947-2
- Name2
- Differences from canonical
- 85-116: Missing
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 77 | in Ref. 4; CAG46703 | ||||
Sequence: K → M | ||||||
Alternative sequence | VSP_021768 | 85-116 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 120 | in Ref. 2; AAA59546 | ||||
Sequence: Y → H | ||||||
Sequence conflict | 242 | in Ref. 2; AAA59546 | ||||
Sequence: A → V |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M93010 EMBL· GenBank· DDBJ | AAA59546.1 EMBL· GenBank· DDBJ | mRNA | ||
X57348 EMBL· GenBank· DDBJ | CAA40623.1 EMBL· GenBank· DDBJ | mRNA | ||
AF029081 EMBL· GenBank· DDBJ | AAC52029.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF029082 EMBL· GenBank· DDBJ | AAC52030.1 EMBL· GenBank· DDBJ | mRNA | ||
CR541905 EMBL· GenBank· DDBJ | CAG46703.1 EMBL· GenBank· DDBJ | mRNA | ||
CR541926 EMBL· GenBank· DDBJ | CAG46724.1 EMBL· GenBank· DDBJ | mRNA | ||
AL034380 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC000329 EMBL· GenBank· DDBJ | AAH00329.1 EMBL· GenBank· DDBJ | mRNA | ||
BC000995 EMBL· GenBank· DDBJ | AAH00995.1 EMBL· GenBank· DDBJ | mRNA | ||
BC001550 EMBL· GenBank· DDBJ | AAH01550.1 EMBL· GenBank· DDBJ | mRNA | ||
BC002995 EMBL· GenBank· DDBJ | AAH02995.1 EMBL· GenBank· DDBJ | mRNA | ||
BC023552 EMBL· GenBank· DDBJ | AAH23552.1 EMBL· GenBank· DDBJ | mRNA |