Protein detail
NF1
Neurofibromin (Neurofibromatosis-related protein NF-1) [Cleaved into: Neurofibromin truncated]
Entry name NF1 | UniProt ID | EVMP score 0.50 |
Frequency 2 | Transmembrane count | Protein classification Cancer-related genesDisease related genesHuman disease related genesPlasma proteinsPredicted intracellular proteinsPredicted membrane proteinsRAS pathway related proteins |
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
Neurofibromin (Neurofibromatosis-related protein NF-1) [Cleaved into: Neurofibromin truncated]
Protein Class
Cancer-related genesDisease related genesHuman disease related genesPlasma proteinsPredicted intracellular proteinsPredicted membrane proteinsRAS pathway related proteins
Protein Function
- Cancer-related genes:Mutational cancer driver genes
- Predicted intracellular proteins
- Cancer-related genes:Mutated cancer genes
- Human disease related genes:Cancers:Cancers of endocrine organs
- RAS pathway related proteins
- Human disease related genes:Cancers:Cancers of haematopoietic and lymphoid tissues
- Disease related genes
- Human disease related genes:Congenital malformations:Other congenital malformations
Ensembl
Entrez Gene Symbol
Gene Description
Neurofibromin 1
Chromosome
17
Position
31094927-31382116
Frequency
2
EVMP Score
0.50
Fluorescence & Localization
Function & Pathway
Protein Function
- Cancer-related genes:Mutational cancer driver genes
- Predicted intracellular proteins
- Cancer-related genes:Mutated cancer genes
- Human disease related genes:Cancers:Cancers of endocrine organs
- RAS pathway related proteins
- Human disease related genes:Cancers:Cancers of haematopoietic and lymphoid tissues
- Disease related genes
- Human disease related genes:Congenital malformations:Other congenital malformations
Cellular Component
Molecular Function
Biological Process
KEGG
Reactome
- R-hsa-5663202 diseases of signal transduction by growth factor receptors and second messengers
- R-hsa-5684996 mapk1 mapk3 signaling
- R-hsa-5683057 mapk family signaling cascades
- R-hsa-6802957 oncogenic mapk signaling
- R-hsa-6802953 ras signaling downstream of nf1 loss of function variants
- R-hsa-5658442 regulation of ras by gaps
Mediation Categories
Adhesion and uptake mediationClinical-translation mediationFusion and delivery mediationImmune mediationReceptor-signaling mediation
Relations & Evidence
Enzyme-Mediated Modification
6 records.
| Substrate Gene Symbol | Enzyme Gene Symbol | Enzyme UniProt ID | Residue Type | Residue Offset | Modification | Database | References |
|---|---|---|---|---|---|---|---|
| NF1 | PRKCA | P17252 | S | 2,808 | phosphorylation | PhosphoSite | |
| NF1 | PRKCA | P17252 | S | 2,829 | phosphorylation | KEA | KEA:17570479 |
| NF1 | MAPK8 | P45983 | S | 2,515 | phosphorylation | KEA | KEA:17570479 |
| NF1 | CDK1 | P06493 | S | 2,515 | phosphorylation | KEA | KEA:17570479 |
| NF1 | CDK1 | P06493 | S | 864 | phosphorylation | KEA | KEA:17570479 |
| NF1 | MAPK8 | P45983 | S | 864 | phosphorylation | KEA | KEA:17570479 |
Ligand-Receptor Signaling
8 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| intracellular | intracellular | ComPPI | No | No | No | No | No |
| intracellular | intracellular | GO_Intercell | No | No | No | No | No |
| intracellular | intracellular | UniProt_location | No | No | No | No | No |
| intracellular | intracellular | OmniPath | No | No | No | No | No |
| transmembrane | transmembrane | Ramilowski_location | No | No | No | No | No |
| transmembrane | transmembrane | OmniPath | No | No | No | No | No |
| plasma_membrane | plasma_membrane | UniProt_location | No | No | No | No | No |
| plasma_membrane | plasma_membrane | OmniPath | No | No | No | No | No |
Regulatory Interaction Network
5 records.
| Source Protein Symbol | Source UniProt ID | Target Protein Symbol | Target UniProt ID | Is Directed | Is Stimulation | Is Inhibition | Database | References |
|---|---|---|---|---|---|---|---|---|
| NF1 | P21359 | RASH | P01112 | Yes | Yes | Yes | WangSIGNORHPRDHINTIntActInnateDBSPIKE_LCSPIKE | InnateDB:8628317HPRD:8628317SIGNOR:24431436HINT:8628317HINT:26635368HINT:30655611IntAct:26635368SIGNOR:19777070SPIKE_LC:19718661SPIKE:19718661 |
| SPRE1 | Q7Z699 | NF1 | P21359 | Yes | Yes | No | HINTSIGNOR | HINT:26635368HINT:32697994HINT:27313208SIGNOR:32697994 |
| NF1 | P21359 | RASK | P01116 | Yes | No | Yes | WangHINTSIGNOR | SIGNOR:32697994HINT:32697994HINT:31611389 |
| RBX2 | Q9UBF6 | NF1 | P21359 | Yes | No | Yes | SIGNOR | SIGNOR:23136067 |
| KPCA | P17252 | NF1 | P21359 | Yes | No | No | PhosphoSiteKEANetworKIN_KEAiPTMnet | KEA:17570479PhosphoSite:26490262 |
Protein Complex Composition
320 records.
| Component Name | Component Gene Symbols | Component UniProt ID | Stoichiometry | Database | Database IDs | References |
|---|---|---|---|---|---|---|
| Ub:RING_E3 | RNF182UBA52 | P62987Q8N6D2 | 0:0 | SIGNOR | SIGNOR:SIGNOR-C519 | |
| Ub:RING_E3 | RNF148UBA52 | P62987Q8N7C7 | 0:0 | SIGNOR | SIGNOR:SIGNOR-C519 | |
| Ub:RING_E3 | RNF152UBA52 | P62987Q8N8N0 | 0:0 | SIGNOR | SIGNOR:SIGNOR-C519 | |
| Ub:RING_E3 | RNF169UBA52 | P62987Q8NCN4 | 0:0 | SIGNOR | SIGNOR:SIGNOR-C519 | |
| Ub:RING_E3 | RNF128UBA52 | P62987Q8TEB7 | 0:0 | SIGNOR | SIGNOR:SIGNOR-C519 | |
| Ub:RING_E3 | RNF139UBA52 | P62987Q8WU17 | 0:0 | SIGNOR | SIGNOR:SIGNOR-C519 | |
| Ub:RING_E3 | RNF138UBA52 | P62987Q8WVD3 | 0:0 | SIGNOR | SIGNOR:SIGNOR-C519 | |
| Ub:RING_E3 | RNF141UBA52 | P62987Q8WVD5 | 0:0 | SIGNOR | SIGNOR:SIGNOR-C519 | |
| Ub:RING_E3 | RNF133UBA52 | P62987Q8WVZ7 | 0:0 | SIGNOR | SIGNOR:SIGNOR-C519 | |
| Ub:RING_E3 | RNF166UBA52 | P62987Q96A37 | 0:0 | SIGNOR | SIGNOR:SIGNOR-C519 |
Isolation & Detection Technology
1 record.
| EV Isolation Method | Detection Method | Number of References | References |
|---|---|---|---|
| Protein Organic Solvent Precipitation | Mass spectrometry | 1 | 32384937 |
Sequence, Structure & Domains
Sequences
Length
2,839
Mass
319,372
Sequence
MAAHRPVEWVQAVVSRFDEQLPIKTGQQNTHTKVSTEHNKECLINISKYKFSLVISGLTTILKNVNNMRIFGEAAEKNLYLSQLIILDTLEKCLAGQPKDTMRLDETMLVKQLLPEICHFLHTCREGNQHAAELRNSASGVLFSLSCNNFNAVFSRISTRLQELTVCSEDNVDVHDIELLQYINVDCAKLKRLLKETAFKFKALKKVAQLAVINSLEKAFWNWVENYPDEFTKLYQIPQTDMAECAEKLFDLVDGFAESTKRKAAVWPLQIILLILCPEIIQDISKDVVDENNMNKKLFLDSLRKALAGHGGSRQLTESAAIACVKLCKASTYINWEDNSVIFLLVQSMVVDLKNLLFNPSKPFSRGSQPADVDLMIDCLVSCFRISPHNNQHFKICLAQNSPSTFHYVLVNSLHRIITNSALDWWPKIDAVYCHSVELRNMFGETLHKAVQGCGAHPAIRMAPSLTFKEKVTSLKFKEKPTDLETRSYKYLLLSMVKLIHADPKLLLCNPRKQGPETQGSTAELITGLVQLVPQSHMPEIAQEAMEALLVLHQLDSIDLWNPDAPVETFWEISSQMLFYICKKLTSHQMLSSTEILKWLREILICRNKFLLKNKQADRSSCHFLLFYGVGCDIPSSGNTSQMSMDHEELLRTPGASLRKGKGNSSMDSAAGCSGTPPICRQAQTKLEVALYMFLWNPDTEAVLVAMSCFRHLCEEADIRCGVDEVSVHNLLPNYNTFMEFASVSNMMSTGRAALQKRVMALLRRIEHPTAGNTEAWEDTHAKWEQATKLILNYPKAKMEDGQAAESLHKTIVKRRMSHVSGGGSIDLSDTDSLQEWINMTGFLCALGGVCLQQRSNSGLATYSPPMGPVSERKGSMISVMSSEGNADTPVSKFMDRLLSLMVCNHEKVGLQIRTNVKDLVGLELSPALYPMLFNKLKNTISKFFDSQGQVLLTDTNTQFVEQTIAIMKNLLDNHTEGSSEHLGQASIETMMLNLVRYVRVLGNMVHAIQIKTKLCQLVEVMMARRDDLSFCQEMKFRNKMVEYLTDWVMGTSNQAADDDVKCLTRDLDQASMEAVVSLLAGLPLQPEEGDGVELMEAKSQLFLKYFTLFMNLLNDCSEVEDESAQTGGRKRGMSRRLASLRHCTVLAMSNLLNANVDSGLMHSIGLGYHKDLQTRATFMEVLTKILQQGTEFDTLAETVLADRFERLVELVTMMGDQGELPIAMALANVVPCSQWDELARVLVTLFDSRHLLYQLLWNMFSKEVELADSMQTLFRGNSLASKIMTFCFKVYGATYLQKLLDPLLRIVITSSDWQHVSFEVDPTRLEPSESLEENQRNLLQMTEKFFHAIISSSSEFPPQLRSVCHCLYQATCHSLLNKATVKEKKENKKSVVSQRFPQNSIGAVGSAMFLRFINPAIVSPYEAGILDKKPPPRIERGLKLMSKILQSIANHVLFTKEEHMRPFNDFVKSNFDAARRFFLDIASDCPTSDAVNHSLSFISDGNVLALHRLLWNNQEKIGQYLSSNRDHKAVGRRPFDKMATLLAYLGPPEHKPVADTHWSSLNLTSSKFEEFMTRHQVHEKEEFKALKTLSIFYQAGTSKAGNPIFYYVARRFKTGQINGDLLIYHVLLTLKPYYAKPYEIVVDLTHTGPSNRFKTDFLSKWFVVFPGFAYDNVSAVYIYNCNSWVREYTKYHERLLTGLKGSKRLVFIDCPGKLAEHIEHEQQKLPAATLALEEDLKVFHNALKLAHKDTKVSIKVGSTAVQVTSAERTKVLGQSVFLNDIYYASEIEEICLVDENQFTLTIANQGTPLTFMHQECEAIVQSIIHIRTRWELSQPDSIPQHTKIRPKDVPGTLLNIALLNLGSSDPSLRSAAYNLLCALTCTFNLKIEGQLLETSGLCIPANNTLFIVSISKTLAANEPHLTLEFLEECISGFSKSSIELKHLCLEYMTPWLSNLVRFCKHNDDAKRQRVTAILDKLITMTINEKQMYPSIQAKIWGSLGQITDLLDVVLDSFIKTSATGGLGSIKAEVMADTAVALASGNVKLVSSKVIGRMCKIIDKTCLSPTPTLEQHLMWDDIAILARYMLMLSFNNSLDVAAHLPYLFHVVTFLVATGPLSLRASTHGLVINIIHSLCTCSQLHFSEETKQVLRLSLTEFSLPKFYLLFGISKVKSAAVIAFRSSYRDRSFSPGSYERETFALTSLETVTEALLEIMEACMRDIPTCKWLDQWTELAQRFAFQYNPSLQPRALVVFGCISKRVSHGQIKQIIRILSKALESCLKGPDTYNSQVLIEATVIALTKLQPLLNKDSPLHKALFWVAVAVLQLDEVNLYSAGTALLEQNLHTLDSLRIFNDKSPEEVFMAIRNPLEWHCKQMDHFVGLNFNSNFNFALVGHLLKGYRHPSPAIVARTVRILHTLLTLVNKHRNCDKFEVNTQSVAYLAALLTVSEEVRSRCSLKHRKSLLLTDISMENVPMDTYPIHHGDPSYRTLKETQPWSSPKGSEGYLAATYPTVGQTSPRARKSMSLDMGQPSQANTKKLLGTRKSFDHLISDTKAPKRQEMESGITTPPKMRRVAETDYEMETQRISSSQQHPHLRKVSVSESNVLLDEEVLTDPKIQALLLTVLATLVKYTTDEFDQRILYEYLAEASVVFPKVFPVVHNLLDSKINTLLSLCQDPNLLNPIHGIVQSVVYHEESPPQYQTSYLQSFGFNGLWRFAGPFSKQTQIPDYAELIVKFLDALIDTYLPGIDEETSEESLLTPTSPYPPALQSQLSITANLNLSNSMTSLATSQHSPGIDKENVELSPTTGHCNSGRTRHGSASQVQKQRSAGSFKRNSIKKIV
Alternative Products
Event=Alternative splicing; Named isoforms=6; Comment=Experimental confirmation may be lacking for some isoforms.; Name=II; IsoId=P21359-1; Sequence=Displayed; Name=I; IsoId=P21359-2; Sequence=VSP_001628; Name=3; IsoId=P21359-3; Sequence=VSP_001629, VSP_001630; Name=4; IsoId=P21359-4; Sequence=VSP_001631, VSP_001632; Name=5; IsoId=P21359-5; Sequence=VSP_043467, VSP_043468; Name=6; IsoId=P21359-6; Sequence=VSP_001628, VSP_053587
Alternative Sequence
548..551; ALLV -> VRGK (in isoform 3); 552..2839; Missing (in isoform 3); 574..593; SSQMLFYICKKLTSHQMLSS -> RYMYFYFLNSTFKFYFVFLS (in isoform 5); 594..2839; Missing (in isoform 5); 1371..1391; Missing (in isoform I and isoform 6); 1591..1598; SIFYQAGT -> TPPPEPET (in isoform 4); 1599..2839; Missing (in isoform 4); 2792; P -> PASLPCSNSAVFMQLFPHQ (in isoform 6)
3D Structural Models
Turn
31..33; 47..49; 531..534; 566..568; 693..696; 728..730; 900..903; 907..909; 947..949; 1026..1028; 1049..1052; 1201..1204; 1217..1219; 1310..1312; 1421..1425; 1582..1586; 1615..1617; 1632..1636; 1662..1664; 1698..1702; 2109..2112; 2180..2184; 2242..2244; 2285..2287; 2382..2384; 2393..2395; 2427..2429; 2443..2445; 2607..2609; 2651..2653; 2709..2715
Helix
5..18; 34..46; 51..66; 73..96; 106..111; 114..121; 130..146; 150..166; 174..181; 187..201; 206..226; 228..236; 240..256; 260..276; 278..285; 294..307; 314..331; 341..357; 373..386; 394..398; 404..419; 429..435; 436..454; 483..502; 505..508; 522..530; 539..551; 555..558; 559..561; 569..587; 593..617; 678..691; 700..708; 711..720; 724..727; 735..745; 752..762; 763..765; 771..793; 832..846; 849..851; 890..899; 910..923; 927..929; 930..942; 955..973; 979..983; 989..1000; 1006..1021; 1034..1046; 1053..1056; 1060..1063; 1064..1080; 1095..1116; 1135..1155; 1157..1160; 1162..1167; 1173..1190; 1197..1200; 1208..1216; 1220..1228; 1233..1235; 1236..1249; 1253..1267; 1271..1273; 1280..1309; 1315..1317; 1323..1325; 1332..1351; 1354..1356; 1359..1370; 1392..1394; 1398..1400; 1401..1411; 1414..1419; 1433..1451; 1459..1464; 1465..1483; 1510..1514; 1517..1520; 1531..1533; 1535..1544; 1569..1578; 1587..1590; 1610..1612; 1620..1631; 1650..1652; 1656..1661; 1668..1672; 1684..1692; 1694..1697; 1714..1717; 1721..1723; 1728..1732; 1785..1787; 1817..1833; 1847..1849; 1851..1861; 1867..1884; 1906..1918; 1920..1922; 1923..1936; 1939..1949; 1950..1952; 1957..1960; 1968..1984; 1989..2000; 2004..2006; 2007..2021; 2026..2041; 2043..2057; 2058..2060; 2061..2063; 2069..2071; 2075..2089; 2090..2092; 2096..2108; 2116..2134; 2143..2155; 2159..2165; 2173..2177; 2199..2219; 2225..2237; 2245..2250; 2252..2255; 2261..2280; 2289..2301; 2302..2304; 2311..2314; 2317..2323; 2328..2347; 2356..2363; 2365..2367; 2368..2378; 2386..2392; 2396..2399; 2403..2424; 2434..2436; 2437..2441; 2447..2452; 2613..2629; 2633..2649; 2654..2657; 2658..2671; 2675..2690; 2700..2702; 2704..2706; 2728..2742
Beta Strand
336..338; 360..362; 367..371; 387..389; 399..402; 424..426; 516..518; 1091..1093; 1277..1279; 1328..1330; 1426..1429; 1490..1492; 1592..1598; 1604..1609; 1639..1644; 1674..1681; 1706..1711; 1738..1749; 1751..1757; 1759..1767; 1770..1772; 1775..1777; 1780..1784; 1788..1795; 1798..1803; 1810..1813; 1961..1963; 1965..1967; 2137..2139; 2351..2354
3D Structure
Electron microscopy (16); X-ray crystallography (10)
Domain & Motif Annotations
Compositional Bias
2801..2827; Polar residues
Motif
2555..2571; Bipartite nuclear localization signal
Domain (CC)
Binds phospholipids via its C-terminal CRAL-TRIO domain. Binds primarily glycerophospholipids with monounsaturated C18:1 and/or C16:1 fatty acid moieties and a phosphatidylethanolamine or phosphatidylcholine headgroup. Has lesser affinity for lipids containing phosphatidylserine and phosphatidylinositol.
Domain (FT)
1251..1482; Ras-GAP; 1580..1738; CRAL-TRIO
Region
1580..1837; Lipid binding; 2787..2839; Disordered
Clinical Relevance
Disease Involvement
Cancer-related genesDisease variantTumor suppressor
Drugs
Interaction Protein
ENSG00000166068ENSG00000166913ENSG00000174775
Interaction Count
3
Interaction Dataset
intact_biogridbiogrid_opencell