Q96PY5
Gene name |
FMNL2 (FHOD2, KIAA1902) |
Protein name |
Formin-like protein 2 |
Names |
Formin homology 2 domain-containing protein 2 |
Species |
Homo sapiens (Human) |
KEGG Pathway |
hsa:114793 |
EC number |
|
Protein Class |
|
Descriptions
(Annotation from UniProt)
The DAD domain may regulate activation via by an autoinhibitory interaction with the N-terminus. This autoinhibition may be released upon competitive binding of an activated GTPase. The release of DAD may allow the FH2 domain to nucleate and elongate nonbranched actin filaments.
Autoinhibitory domains (AIDs)
Target domain |
23-469 (GBD/FH3 domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
2 structures for Q96PY5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 4YC7 | X-ray | 250 A | B | 1-379 | PDB |
| AF-Q96PY5-F1 | Predicted | AlphaFoldDB |
No variants for Q96PY5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q96PY5 | |||||
No associated diseases with Q96PY5
5 regional properties for Q96PY5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Formin, FH3 domain | 278 - 482 | IPR010472 |
| domain | Formin, GTPase-binding domain | 23 - 275 | IPR010473 |
| domain | Diaphanous autoregulatory (DAD) domain | 1039 - 1076 | IPR014767 |
| domain | Rho GTPase-binding/formin homology 3 (GBD/FH3) domain | 23 - 469 | IPR014768 |
| domain | Formin, FH2 domain | 616 - 1053 | IPR015425 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| actin filament binding | Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits. |
| cadherin binding | Binding to cadherin, a type I membrane protein involved in cell adhesion. |
| small GTPase binding | Binding to a small monomeric GTPase. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| cell migration | The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. Cell migration is a central process in the development and maintenance of multicellular organisms. |
| cortical actin cytoskeleton organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of actin-based cytoskeletal structures in the cell cortex, i.e. just beneath the plasma membrane. |
| cytoskeleton organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures. |
| regulation of cell morphogenesis | Any process that modulates the frequency, rate or extent of cell morphogenesis. Cell morphogenesis is the developmental process in which the shape of a cell is generated and organized. |
| regulation of cell shape | Any process that modulates the surface configuration of a cell. |
6 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9VUC6 | Frl | Formin-like protein | Drosophila melanogaster (Fruit fly) | EV |
| Q8IVF7 | FMNL3 | Formin-like protein 3 | Homo sapiens (Human) | SS |
| O95466 | FMNL1 | Formin-like protein 1 | Homo sapiens (Human) | SS |
| Q6ZPF4 | Fmnl3 | Formin-like protein 3 | Mus musculus (Mouse) | SS |
| Q9JL26 | Fmnl1 | Formin-like protein 1 | Mus musculus (Mouse) | SS |
| A2APV2 | Fmnl2 | Formin-like protein 2 | Mus musculus (Mouse) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGNAGSMDSQ | QTDFRAHNVP | LKLPMPEPGE | LEERFAIVLN | AMNLPPDKAR | LLRQYDNEKK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| WELICDQERF | QVKNPPHTYI | QKLKGYLDPA | VTRKKFRRRV | QESTQVLREL | EISLRTNHIG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| WVREFLNEEN | KGLDVLVEYL | SFAQYAVTFD | FESVESTVES | SVDKSKPWSR | SIEDLHRGSN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LPSPVGNSVS | RSGRHSALRY | NTLPSRRTLK | NSRLVSKKDD | VHVCIMCLRA | IMNYQYGFNM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VMSHPHAVNE | IALSLNNKNP | RTKALVLELL | AAVCLVRGGH | EIILSAFDNF | KEVCGEKQRF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EKLMEHFRNE | DNNIDFMVAS | MQFINIVVHS | VEDMNFRVHL | QYEFTKLGLD | EYLDKLKHTE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SDKLQVQIQA | YLDNVFDVGA | LLEDAETKNA | ALERVEELEE | NISHLSEKLQ | DTENEAMSKI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VELEKQLMQR | NKELDVVREI | YKDANTQVHT | LRKMVKEKEE | AIQRQSTLEK | KIHELEKQGT |
| 490 | 500 | 510 | 520 | 530 | 540 |
| IKIQKKGDGD | IAILPVVASG | TLSMGSEVVA | GNSVGPTMGA | ASSGPLPPPP | PPLPPSSDTP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ETVQNGPVTP | PMPPPPPPPP | PPPPPPPPPP | PPPLPGPAAE | TVPAPPLAPP | LPSAPPLPGT |
| 610 | 620 | 630 | 640 | 650 | 660 |
| SSPTVVFNSG | LAAVKIKKPI | KTKFRMPVFN | WVALKPNQIN | GTVFNEIDDE | RILEDLNVDE |
| 670 | 680 | 690 | 700 | 710 | 720 |
| FEEIFKTKAQ | GPAIDLSSSK | QKIPQKGSNK | VTLLEANRAK | NLAITLRKAG | KTADEICKAI |
| 730 | 740 | 750 | 760 | 770 | 780 |
| HVFDLKTLPV | DFVECLMRFL | PTENEVKVLR | LYERERKPLE | NLSDEDRFMM | QFSKIERLMQ |
| 790 | 800 | 810 | 820 | 830 | 840 |
| KMTIMAFIGN | FAESIQMLTP | QLHAIIAASV | SIKSSQKLKK | ILEIILALGN | YMNSSKRGAV |
| 850 | 860 | 870 | 880 | 890 | 900 |
| YGFKLQSLDL | LLDTKSTDRK | QTLLHYISNV | VKEKYHQVSL | FYNELHYVEK | AAAVSLENVL |
| 910 | 920 | 930 | 940 | 950 | 960 |
| LDVKELQRGM | DLTKREYTMH | DHNTLLKEFI | LNNEGKLKKL | QDDAKIAQDA | FDDVVKYFGE |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| NPKTTPPSVF | FPVFVRFVKA | YKQAEEENEL | RKKQEQALME | KLLEQEALME | QQDPKSPSHK |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| SKRQQQELIA | ELRRRQVKDN | RHVYEGKDGA | IEDIITVLKT | VPFTARTAKR | GSRFFCEPVL |
| TEEYHY |