Q9JL04 · FMN2_MOUSE
- ProteinFormin-2
- GeneFmn2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1578 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Actin-binding protein that is involved in actin cytoskeleton assembly and reorganization (PubMed:18848445, PubMed:21620703).
Acts as an actin nucleation factor and promotes assembly of actin filaments together with SPIRE1 and SPIRE2 (PubMed:18848445, PubMed:21620703).
Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport (PubMed:21983562).
Required for asymmetric spindle positioning, asymmetric oocyte division and polar body extrusion during female germ cell meiosis (PubMed:12447394, PubMed:18848445, PubMed:19062278, PubMed:21620703).
Plays a role in responses to DNA damage, cellular stress and hypoxia by protecting CDKN1A against degradation, and thereby plays a role in stress-induced cell cycle arrest (By similarity).
Also acts in the nucleus: together with SPIRE1 and SPIRE2, promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage (By similarity).
Protects cells against apoptosis by protecting CDKN1A against degradation (By similarity).
Acts as an actin nucleation factor and promotes assembly of actin filaments together with SPIRE1 and SPIRE2 (PubMed:18848445, PubMed:21620703).
Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport (PubMed:21983562).
Required for asymmetric spindle positioning, asymmetric oocyte division and polar body extrusion during female germ cell meiosis (PubMed:12447394, PubMed:18848445, PubMed:19062278, PubMed:21620703).
Plays a role in responses to DNA damage, cellular stress and hypoxia by protecting CDKN1A against degradation, and thereby plays a role in stress-induced cell cycle arrest (By similarity).
Also acts in the nucleus: together with SPIRE1 and SPIRE2, promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage (By similarity).
Protects cells against apoptosis by protecting CDKN1A against degradation (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
Names & Taxonomy
Protein names
- Recommended nameFormin-2
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9JL04
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Cytoplasmic vesicle membrane ; Peripheral membrane protein
Note: Colocalizes with the actin cytoskeleton (PubMed:21705804).
Recruited to the membranes via its interaction with SPIRE1 (PubMed:21705804).
Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion (PubMed:21620703).
Accumulates in the nucleus following DNA damage (By similarity).
Recruited to the membranes via its interaction with SPIRE1 (PubMed:21705804).
Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion (PubMed:21620703).
Accumulates in the nucleus following DNA damage (By similarity).
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
No visible phenotype in male mice, but female mice show reduced fertility and produce at most one to three pups per litter (PubMed:12447394).
Female mice display defects in asymmetric spindle positioning, asymmetric cell division and polar body extrusion during oocyte meiosis (PubMed:12447394).
During early pregnancy, females present normal numbers of implantation sites, but only very few normal-looking embryos (PubMed:12447394).
Most of the embryos show developmental delays and gross morphological defects, leading to embryonic death (PubMed:12447394).
Female mice display defects in asymmetric spindle positioning, asymmetric cell division and polar body extrusion during oocyte meiosis (PubMed:12447394).
During early pregnancy, females present normal numbers of implantation sites, but only very few normal-looking embryos (PubMed:12447394).
Most of the embryos show developmental delays and gross morphological defects, leading to embryonic death (PubMed:12447394).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 1571 | Strongly reduced interaction with SPIRE1. | ||||
Sequence: K → A or E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 89 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000194889 | 1-1578 | Formin-2 | |||
Sequence: MGNQDGKLKRSAGDASHEGGGAEDAAGPRDAEITKKASGSKKALGKHGKGGGGSGETSKKKSKSDSRASVFSNLRIRKNLTKGKGACDSREDVLDSQALPIGELDSAHSIVTKTPDLSLSAEETGLSDTECADPFEVIHPGASRPAEAGVGIQATAEDLETAAGAQDGQRTSSGSDTDIYSFHSATEQEDLLSDIQQAIRLQQQQQQKLLLQDSEEPAAPPTAISPQPGAFLGLDQFLLGPRSEAEKDTVQALPVRPDLPETTKSLVPEHPPSSGSHLTSETPGYATAPSAVTDSLSSPAFTFPEAGPGEGAAGVPVAGTGDTDEECEEDAFEDAPRGSPGEEWVPEVEEASQRLEKEPEEGMRESITSAVVSLPGSPAPSPRCFKPYPLITPCYIKTTTRQLSSPNHSPSQSPNQSPRIKKRPDPSVSRSSRTALASAAAPAKKHRLEGGLTGGLSRSADWTEELGVRTPGAGGSVHLLGRGATADDSGGGSPVLAAKAPGAPATADGFQNVFTGRTLLEKLFSQQENGPPEEAEKFCSRIIAMGLLLPFSDCFREPCNQNAGSSSAPFDQDQLYTWAAVSQPTHSMDYSEGQFPRREPSMWPSSKLPEEEPSPKDVDTEPKSSILESPKKCSNGVQQEVFDVKSEGQATVIQQLEQTIEDLRTKIAELEKQYPALDLEGPRGLSGLENGLTASADVSLDALVLHGKVAQPPRTLEAKSIQTSPTEEGRILTLPPPKAPPEGLLGSPAAASGESALLTSPSGPQTKFCSEISLIVSPRRISVQLDAQQIQSASQLPPPPPLLGSDSQGQPSQPSLHTESETSHEHSVSSSFGNNCNVPPAPPLPCTESSSFMPGLGMAIPPPPCLSDITVPALPSPTAPALQFSNLQGPEMLPAPPQPPPLPGLGVPPPPPAPPLPGMGIPPPPPLPGMGIPPPPPLPGMGISPLPPLPGMGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGSGIPPPPALPGVAIPPPPPLPGMGVPPPAPPPPGAGIPPPPLLPGSGPPHSSQVGSSTLPAAPQGCGFLFPPLPTGLFGLGMNQDRVARKQLIEPCRPMKPLYWTRIQLHSKRDSSPSLIWEKIEEPSIDCHEFEELFSKTAVKERKKPISDTISKTKAKQVVKLLSNKRSQAVGILMSSLHLDMKDIQHAVVNLDNSVVDLETLQALYENRAQSDELEKIEKHSRSSKDKENAKSLDKPEQFLYELSLIPNFSERVFCILFQSTFSESICSIRRKLELLQKLCETLKNGPGVMQVLGLVLAFGNYMNAGNKTRGQADGFGLDILPKLKDVKSSDNSRSLLSYIVSYYLRNFDEDAGKEQCVFPLAEPQELFQASQMKFEDFQKDLRKLKKDLKACEAEAGKVYQVSSAEHMQPFKENMEQFISQAKIDQESQEAALTETHKCFLETTAYYFMKPKLGEKEVSPNVFFSVWHEFSSDFKDAWKKENKLILQERVKEAEEVCRQKKGKSLYKVKPRHDSGIKAKISMKT | ||||||
Modified residue | 89 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 459 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 489 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 493 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in brain and in oocytes (at protein level) (PubMed:12447394, PubMed:19062278).
Expressed almost exclusively in the developing and mature central nervous system (PubMed:10781961).
Detected in oocytes (PubMed:12447394, PubMed:19062278).
Expressed almost exclusively in the developing and mature central nervous system (PubMed:10781961).
Detected in oocytes (PubMed:12447394, PubMed:19062278).
Developmental stage
Expression begins at embryonic day 9.5 in the developing spinal cord and brain structures and continues in neonatal and adult brain structures including the olfactory bulb, cortex, thalamus, hypothalamus, hippocampus and cerebellum.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, coiled coil, domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-73 | Disordered | ||||
Sequence: MGNQDGKLKRSAGDASHEGGGAEDAAGPRDAEITKKASGSKKALGKHGKGGGGSGETSKKKSKSDSRASVFSN | ||||||
Compositional bias | 10-39 | Basic and acidic residues | ||||
Sequence: RSAGDASHEGGGAEDAAGPRDAEITKKASG | ||||||
Region | 208-230 | Disordered | ||||
Sequence: KLLLQDSEEPAAPPTAISPQPGA | ||||||
Region | 244-383 | Disordered | ||||
Sequence: EAEKDTVQALPVRPDLPETTKSLVPEHPPSSGSHLTSETPGYATAPSAVTDSLSSPAFTFPEAGPGEGAAGVPVAGTGDTDEECEEDAFEDAPRGSPGEEWVPEVEEASQRLEKEPEEGMRESITSAVVSLPGSPAPSPR | ||||||
Compositional bias | 267-300 | Polar residues | ||||
Sequence: VPEHPPSSGSHLTSETPGYATAPSAVTDSLSSPA | ||||||
Compositional bias | 343-364 | Basic and acidic residues | ||||
Sequence: EWVPEVEEASQRLEKEPEEGMR | ||||||
Compositional bias | 401-422 | Polar residues | ||||
Sequence: RQLSSPNHSPSQSPNQSPRIKK | ||||||
Region | 401-458 | Disordered | ||||
Sequence: RQLSSPNHSPSQSPNQSPRIKKRPDPSVSRSSRTALASAAAPAKKHRLEGGLTGGLSR | ||||||
Region | 587-634 | Disordered | ||||
Sequence: SMDYSEGQFPRREPSMWPSSKLPEEEPSPKDVDTEPKSSILESPKKCS | ||||||
Compositional bias | 610-626 | Basic and acidic residues | ||||
Sequence: EEEPSPKDVDTEPKSSI | ||||||
Coiled coil | 643-683 | |||||
Sequence: DVKSEGQATVIQQLEQTIEDLRTKIAELEKQYPALDLEGPR | ||||||
Region | 714-765 | Disordered | ||||
Sequence: RTLEAKSIQTSPTEEGRILTLPPPKAPPEGLLGSPAAASGESALLTSPSGPQ | ||||||
Domain | 735-1124 | FH1 | ||||
Sequence: PPPKAPPEGLLGSPAAASGESALLTSPSGPQTKFCSEISLIVSPRRISVQLDAQQIQSASQLPPPPPLLGSDSQGQPSQPSLHTESETSHEHSVSSSFGNNCNVPPAPPLPCTESSSFMPGLGMAIPPPPCLSDITVPALPSPTAPALQFSNLQGPEMLPAPPQPPPLPGLGVPPPPPAPPLPGMGIPPPPPLPGMGIPPPPPLPGMGISPLPPLPGMGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGSGIPPPPALPGVAIPPPPPLPGMGVPPPAPPPPGAGIPPPPLLPGSGPPHSSQVGSSTLPAAPQGCGFLFPPLP | ||||||
Region | 786-836 | Disordered | ||||
Sequence: DAQQIQSASQLPPPPPLLGSDSQGQPSQPSLHTESETSHEHSVSSSFGNNC | ||||||
Region | 880-944 | Disordered | ||||
Sequence: PALQFSNLQGPEMLPAPPQPPPLPGLGVPPPPPAPPLPGMGIPPPPPLPGMGIPPPPPLPGMGIS | ||||||
Compositional bias | 892-944 | Pro residues | ||||
Sequence: MLPAPPQPPPLPGLGVPPPPPAPPLPGMGIPPPPPLPGMGIPPPPPLPGMGIS | ||||||
Repeat | 919-929 | 1 | ||||
Sequence: MGIPPPPPLPG | ||||||
Region | 919-1039 | 12 X 11 AA tandem repeats of [MV]-G-I-P-P-P-P-P-L-P-G | ||||
Sequence: MGIPPPPPLPGMGIPPPPPLPGMGISPLPPLPGMGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPG | ||||||
Repeat | 930-940 | 2 | ||||
Sequence: MGIPPPPPLPG | ||||||
Repeat | 941-951 | 3 | ||||
Sequence: MGISPLPPLPG | ||||||
Repeat | 952-962 | 4 | ||||
Sequence: MGIPPPPPLPG | ||||||
Repeat | 963-973 | 5 | ||||
Sequence: VGIPPPPPLPG | ||||||
Repeat | 974-984 | 6 | ||||
Sequence: VGIPPPPPLPG | ||||||
Repeat | 985-995 | 7 | ||||
Sequence: VGIPPPPPLPG | ||||||
Repeat | 996-1006 | 8 | ||||
Sequence: VGIPPPPPLPG | ||||||
Repeat | 1007-1017 | 9 | ||||
Sequence: VGIPPPPPLPG | ||||||
Repeat | 1018-1028 | 10 | ||||
Sequence: VGIPPPPPLPG | ||||||
Repeat | 1029-1039 | 11 | ||||
Sequence: VGIPPPPPLPG | ||||||
Compositional bias | 1037-1097 | Pro residues | ||||
Sequence: LPGVGIPPPPPLPGSGIPPPPALPGVAIPPPPPLPGMGVPPPAPPPPGAGIPPPPLLPGSG | ||||||
Region | 1037-1108 | Disordered | ||||
Sequence: LPGVGIPPPPPLPGSGIPPPPALPGVAIPPPPPLPGMGVPPPAPPPPGAGIPPPPLLPGSGPPHSSQVGSST | ||||||
Repeat | 1040-1050 | 12 | ||||
Sequence: VGIPPPPPLPG | ||||||
Domain | 1139-1554 | FH2 | ||||
Sequence: RKQLIEPCRPMKPLYWTRIQLHSKRDSSPSLIWEKIEEPSIDCHEFEELFSKTAVKERKKPISDTISKTKAKQVVKLLSNKRSQAVGILMSSLHLDMKDIQHAVVNLDNSVVDLETLQALYENRAQSDELEKIEKHSRSSKDKENAKSLDKPEQFLYELSLIPNFSERVFCILFQSTFSESICSIRRKLELLQKLCETLKNGPGVMQVLGLVLAFGNYMNAGNKTRGQADGFGLDILPKLKDVKSSDNSRSLLSYIVSYYLRNFDEDAGKEQCVFPLAEPQELFQASQMKFEDFQKDLRKLKKDLKACEAEAGKVYQVSSAEHMQPFKENMEQFISQAKIDQESQEAALTETHKCFLETTAYYFMKPKLGEKEVSPNVFFSVWHEFSSDFKDAWKKENKLILQERVKEAEEVCRQK | ||||||
Coiled coil | 1419-1455 | |||||
Sequence: QELFQASQMKFEDFQKDLRKLKKDLKACEAEAGKVYQ | ||||||
Region | 1571-1578 | Important for interaction with SPIRE1 | ||||
Sequence: KAKISMKT |
Sequence similarities
Belongs to the formin homology family. Cappuccino subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,578
- Mass (Da)167,387
- Last updated2008-01-15 v2
- ChecksumDD0FDC8FC25C47DB
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0A6YY57 | A0A0A6YY57_MOUSE | Fmn2 | 145 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 10-39 | Basic and acidic residues | ||||
Sequence: RSAGDASHEGGGAEDAAGPRDAEITKKASG | ||||||
Sequence conflict | 33 | in Ref. 2; AAH94606 | ||||
Sequence: I → T | ||||||
Compositional bias | 267-300 | Polar residues | ||||
Sequence: VPEHPPSSGSHLTSETPGYATAPSAVTDSLSSPA | ||||||
Compositional bias | 343-364 | Basic and acidic residues | ||||
Sequence: EWVPEVEEASQRLEKEPEEGMR | ||||||
Sequence conflict | 348 | in Ref. 2; AAH94606 | ||||
Sequence: V → M | ||||||
Sequence conflict | 372 | in Ref. 2; AAH94606 | ||||
Sequence: V → A | ||||||
Compositional bias | 401-422 | Polar residues | ||||
Sequence: RQLSSPNHSPSQSPNQSPRIKK | ||||||
Sequence conflict | 430-432 | in Ref. 2; AAH94606 | ||||
Sequence: RSS → PSP | ||||||
Compositional bias | 610-626 | Basic and acidic residues | ||||
Sequence: EEEPSPKDVDTEPKSSI | ||||||
Sequence conflict | 745 | in Ref. 2; AAH94606 | ||||
Sequence: L → P | ||||||
Compositional bias | 892-944 | Pro residues | ||||
Sequence: MLPAPPQPPPLPGLGVPPPPPAPPLPGMGIPPPPPLPGMGIPPPPPLPGMGIS | ||||||
Sequence conflict | 936-946 | in Ref. 2; AAH94606 | ||||
Sequence: Missing | ||||||
Compositional bias | 1037-1097 | Pro residues | ||||
Sequence: LPGVGIPPPPPLPGSGIPPPPALPGVAIPPPPPLPGMGVPPPAPPPPGAGIPPPPLLPGSG | ||||||
Sequence conflict | 1040 | in Ref. 2; AAH94606 | ||||
Sequence: V → M | ||||||
Sequence conflict | 1142 | in Ref. 2; AAH94606 | ||||
Sequence: L → P |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF218940 EMBL· GenBank· DDBJ | AAF72883.1 EMBL· GenBank· DDBJ | mRNA | ||
BC094606 EMBL· GenBank· DDBJ | AAH94606.1 EMBL· GenBank· DDBJ | mRNA |