P07737 · PROF1_HUMAN
- ProteinProfilin-1
- GenePFN1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids140 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProfilin-1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP07737
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Amyotrophic lateral sclerosis 18 (ALS18)
- Note
- DescriptionA neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.
- See alsoMIM:614808
Natural variants in ALS18
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_068925 | 71 | C>G | in ALS18; the mutant protein is detected in the insoluble fraction of cells; dbSNP:rs387907264 | |
VAR_068926 | 114 | M>T | in ALS18; the mutant protein is detected in the insoluble fraction of cells; dbSNP:rs387907265 | |
VAR_068927 | 117 | E>G | in ALS18; uncertain significance; like the wild-type the mutant protein is detected in the soluble fraction of cells; dbSNP:rs140547520 | |
VAR_068928 | 118 | G>V | in ALS18; the mutant protein is detected in the insoluble fraction of cells; dbSNP:rs387907266 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_068925 | 71 | in ALS18; the mutant protein is detected in the insoluble fraction of cells; dbSNP:rs387907264 | |||
Sequence: C → G | ||||||
Natural variant | VAR_068926 | 114 | in ALS18; the mutant protein is detected in the insoluble fraction of cells; dbSNP:rs387907265 | |||
Sequence: M → T | ||||||
Natural variant | VAR_068927 | 117 | in ALS18; uncertain significance; like the wild-type the mutant protein is detected in the soluble fraction of cells; dbSNP:rs140547520 | |||
Sequence: E → G | ||||||
Natural variant | VAR_068928 | 118 | in ALS18; the mutant protein is detected in the insoluble fraction of cells; dbSNP:rs387907266 | |||
Sequence: G → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 115 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
Protein family/group 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 | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000199571 | 2-140 | UniProt | Profilin-1 | |||
Sequence: AGWNAYIDNLMADGTCQDAAIVGYKDSPSVWAAVPGKTFVNITPAEVGVLVGKDRSSFYVNGLTLGGQKCSVIRDSLLQDGEFSMDLRTKSTGGAPTFNVTVTKTDKTLVLLMGKEGVHGGLINKKCYEMASHLRRSQY | |||||||
Modified residue | 28 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 39 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 54 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Cross-link | 54 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||
Sequence: K | |||||||
Modified residue | 57 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 57 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 58 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 60 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 65 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 77 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 85 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 90 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 92 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 93 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 102 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 104 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 105 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 106 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 108 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 129 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 138 | UniProt | Phosphoserine; by ROCK1 | ||||
Sequence: S |
Post-translational modification
Phosphorylation at Ser-138 reduces its affinity for G-actin and blocks its interaction with HTT, reducing its ability to inhibit androgen receptor (AR) and HTT aggregation.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Expressed in epididymis (at protein level).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Found in a complex with XPO6, Ran, ACTB and PFN1 (PubMed:14592989).
Interacts with ACTB (PubMed:10411937).
Interacts with VASP (PubMed:17914456, PubMed:18689676).
Interacts with HTT (PubMed:18573880).
Interacts with SH3BGRL (PubMed:34331014).
Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio (PubMed:17914456, PubMed:18689676).
Interacts with ACTMAP (PubMed:36173861).
Interacts with ACTB (PubMed:10411937).
Interacts with VASP (PubMed:17914456, PubMed:18689676).
Interacts with HTT (PubMed:18573880).
Interacts with SH3BGRL (PubMed:34331014).
Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio (PubMed:17914456, PubMed:18689676).
Interacts with ACTMAP (PubMed:36173861).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P07737 | act21 P07830 | 3 | EBI-713780, EBI-7195234 | |
XENO | P07737 | ACTA1 P68135 | 2 | EBI-713780, EBI-367540 | |
BINARY | P07737 | ACTB P60709 | 3 | EBI-713780, EBI-353944 | |
BINARY | P07737 | VASP P50552 | 2 | EBI-713780, EBI-748201 | |
BINARY | P07737 | WASF1 Q92558 | 3 | EBI-713780, EBI-1548747 | |
XENO | P07737 | Wasl O08816 | 4 | EBI-713780, EBI-6142604 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length140
- Mass (Da)15,054
- Last updated2007-01-23 v2
- ChecksumF725119E55A289EB
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J03191 EMBL· GenBank· DDBJ | AAA36486.1 EMBL· GenBank· DDBJ | mRNA | ||
GU727630 EMBL· GenBank· DDBJ | ADU87632.1 EMBL· GenBank· DDBJ | mRNA | ||
BT007001 EMBL· GenBank· DDBJ | AAP35647.1 EMBL· GenBank· DDBJ | mRNA | ||
AK312168 EMBL· GenBank· DDBJ | BAG35102.1 EMBL· GenBank· DDBJ | mRNA | ||
CR407670 EMBL· GenBank· DDBJ | CAG28598.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471108 EMBL· GenBank· DDBJ | EAW90381.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471108 EMBL· GenBank· DDBJ | EAW90383.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471108 EMBL· GenBank· DDBJ | EAW90384.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC002475 EMBL· GenBank· DDBJ | AAH02475.1 EMBL· GenBank· DDBJ | mRNA | ||
BC006768 EMBL· GenBank· DDBJ | AAH06768.1 EMBL· GenBank· DDBJ | mRNA | ||
BC013439 EMBL· GenBank· DDBJ | AAH13439.1 EMBL· GenBank· DDBJ | mRNA | ||
BC015164 EMBL· GenBank· DDBJ | AAH15164.1 EMBL· GenBank· DDBJ | mRNA | ||
BC057828 EMBL· GenBank· DDBJ | AAH57828.1 EMBL· GenBank· DDBJ | mRNA |