Q6IBS0 · TWF2_HUMAN
- ProteinTwinfilin-2
- GeneTWF2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids349 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles. May play a role in regulating the mature length of the middle and short rows of stereocilia (By similarity).
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
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTwinfilin-2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ6IBS0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Perinuclear and G-actin-rich cortical actin structure sublocalization.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_042407 | 72 | in dbSNP:rs35114109 | |||
Sequence: R → C | ||||||
Natural variant | VAR_042408 | 76 | in dbSNP:rs35711542 | |||
Sequence: Q → R | ||||||
Natural variant | VAR_042409 | 103 | in a lung neuroendocrine carcinoma sample; somatic mutation; dbSNP:rs867679383 | |||
Sequence: A → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 353 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000233136 | 2-349 | UniProt | Twinfilin-2 | |||
Sequence: AHQTGIHATEELKEFFAKARAGSVRLIKVVIEDEQLVLGASQEPVGRWDQDYDRAVLPLLDAQQPCYLLYRLDSQNAQGFEWLFLAWSPDNSPVRLKMLYAATRATVKKEFGGGHIKDELFGTVKDDLSFAGYQKHLSSCAAPAPLTSAERELQQIRINEVKTEISVESKHQTLQGLAFPLQPEAQRALQQLKQKMVNYIQMKLDLERETIELVHTEPTDVAQLPSRVPRDAARYHFFLYKHTHEGDPLESVVFIYSMPGYKCSIKERMLYSSCKSRLLDSVEQDFHLEIAKKIEIGDGAELTAEFLYDEVHPKQHAFKQAFAKPKGPGGKRGHKRLIRGPGENGDDS | |||||||
Modified residue | 14 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 149 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 167 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 309 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 309 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 349 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 349 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
In vitro, phosphorylated by PRKCZ, CK2 and SRC.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Ubiquitously expressed (at protein level).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with G-actin; ADP-actin form and capping protein (CP). May also be able to interact with TWF1 and phosphoinositides, PI(4,5)P2. When bound to PI(4,5)P2, it is down-regulated. Interacts with MYO7A (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q6IBS0 | TERF2IP Q9NYB0 | 2 | EBI-722204, EBI-750109 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-139 | ADF-H 1 | ||||
Sequence: QTGIHATEELKEFFAKARAGSVRLIKVVIEDEQLVLGASQEPVGRWDQDYDRAVLPLLDAQQPCYLLYRLDSQNAQGFEWLFLAWSPDNSPVRLKMLYAATRATVKKEFGGGHIKDELFGTVKDDLSFAGYQKHLS | ||||||
Domain | 177-313 | ADF-H 2 | ||||
Sequence: GLAFPLQPEAQRALQQLKQKMVNYIQMKLDLERETIELVHTEPTDVAQLPSRVPRDAARYHFFLYKHTHEGDPLESVVFIYSMPGYKCSIKERMLYSSCKSRLLDSVEQDFHLEIAKKIEIGDGAELTAEFLYDEVH | ||||||
Region | 322-349 | Disordered | ||||
Sequence: AFAKPKGPGGKRGHKRLIRGPGENGDDS |
Sequence similarities
Belongs to the actin-binding proteins ADF family. Twinfilin subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length349
- Mass (Da)39,548
- Last updated2006-05-02 v2
- Checksum635EF8C04EFCE92B
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
D6RG15 | D6RG15_HUMAN | TWF2 | 254 | ||
A0A7I2YQM6 | A0A7I2YQM6_HUMAN | TWF2 | 44 | ||
A0A7I2V2U8 | A0A7I2V2U8_HUMAN | TWF2 | 296 | ||
A0A7I2V3T5 | A0A7I2V3T5_HUMAN | TWF2 | 51 | ||
A0A7I2V5B1 | A0A7I2V5B1_HUMAN | TWF2 | 251 | ||
A0A7I2V5D3 | A0A7I2V5D3_HUMAN | TWF2 | 318 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 110 | in Ref. 4; CAG33013 | ||||
Sequence: K → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y17169 EMBL· GenBank· DDBJ | CAB38055.1 EMBL· GenBank· DDBJ | mRNA | ||
AL136773 EMBL· GenBank· DDBJ | CAB66707.1 EMBL· GenBank· DDBJ | mRNA | ||
AF109365 EMBL· GenBank· DDBJ | AAQ13513.1 EMBL· GenBank· DDBJ | mRNA | ||
CR456732 EMBL· GenBank· DDBJ | CAG33013.1 EMBL· GenBank· DDBJ | mRNA | ||
CR533520 EMBL· GenBank· DDBJ | CAG38551.1 EMBL· GenBank· DDBJ | mRNA | ||
BC000327 EMBL· GenBank· DDBJ | AAH00327.1 EMBL· GenBank· DDBJ | mRNA | ||
BC003161 EMBL· GenBank· DDBJ | AAH03161.1 EMBL· GenBank· DDBJ | mRNA | ||
BC016452 EMBL· GenBank· DDBJ | AAH16452.1 EMBL· GenBank· DDBJ | mRNA |