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P97526 (NF1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neurofibromin
Alternative name(s):
Neurofibromatosis-related protein NF-1
Gene names
Name:Nf1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length2820 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Stimulates the GTPase activity of Ras. NF1 shows greater affinity for Ras GAP, but lower specific activity. May be a regulator of Ras activity By similarity.

Subcellular location

Nucleus By similarity. Nucleusnucleolus By similarity.

Domain

Binds phospholipids via a region that includes the 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 By similarity.

Sequence similarities

Contains 1 CRAL-TRIO domain.

Contains 1 Ras-GAP domain.

Ontologies

Keywords
   Cellular componentNucleus
   LigandLipid-binding
   Molecular functionGTPase activation
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from sequence or structural similarity. Source: HGNC

Ras protein signal transduction

Inferred from sequence or structural similarity. Source: HGNC

Schwann cell development

Inferred from sequence or structural similarity. Source: HGNC

actin cytoskeleton organization

Inferred from sequence or structural similarity. Source: HGNC

adrenal gland development

Inferred from sequence or structural similarity. Source: HGNC

artery morphogenesis

Inferred from sequence or structural similarity. Source: HGNC

brain development

Inferred from sequence or structural similarity. Source: HGNC

camera-type eye morphogenesis

Inferred from sequence or structural similarity. Source: HGNC

cell communication

Inferred from sequence or structural similarity. Source: HGNC

cerebral cortex development

Inferred from sequence or structural similarity. Source: HGNC

collagen fibril organization

Inferred from sequence or structural similarity. Source: HGNC

extracellular matrix organization

Inferred from sequence or structural similarity. Source: HGNC

forebrain astrocyte development

Inferred from sequence or structural similarity. Source: HGNC

forebrain morphogenesis

Inferred from sequence or structural similarity. Source: HGNC

heart development

Inferred from sequence or structural similarity. Source: HGNC

liver development

Inferred from sequence or structural similarity. Source: HGNC

metanephros development

Inferred from sequence or structural similarity. Source: HGNC

myelination in peripheral nervous system

Inferred from sequence or structural similarity. Source: HGNC

negative regulation of MAP kinase activity

Inferred from sequence or structural similarity. Source: HGNC

negative regulation of MAPK cascade

Inferred from sequence or structural similarity. Source: HGNC

negative regulation of Ras protein signal transduction

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of fibroblast proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuroblast proliferation

Inferred from sequence or structural similarity. Source: HGNC

negative regulation of oligodendrocyte differentiation

Inferred from sequence or structural similarity. Source: HGNC

negative regulation of protein kinase activity

Inferred from sequence or structural similarity. Source: HGNC

negative regulation of transcription factor import into nucleus

Inferred from sequence or structural similarity. Source: HGNC

osteoblast differentiation

Inferred from sequence or structural similarity. Source: HGNC

peripheral nervous system development

Inferred from sequence or structural similarity. Source: HGNC

phosphatidylinositol 3-kinase signaling

Inferred from sequence or structural similarity. Source: HGNC

pigmentation

Inferred from sequence or structural similarity. Source: HGNC

positive regulation of Ras GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of adenylate cyclase activity

Inferred from sequence or structural similarity. Source: HGNC

positive regulation of apoptotic process

Inferred from sequence or structural similarity. Source: HGNC

positive regulation of neuron apoptotic process

Inferred from sequence or structural similarity. Source: HGNC

regulation of Ras GTPase activity

Inferred from mutant phenotype PubMed 1570015. Source: HGNC

regulation of angiogenesis

Inferred from sequence or structural similarity. Source: HGNC

regulation of bone resorption

Inferred from sequence or structural similarity. Source: HGNC

regulation of cell-matrix adhesion

Inferred from sequence or structural similarity. Source: HGNC

regulation of glial cell differentiation

Inferred from sequence or structural similarity. Source: HGNC

regulation of neuron differentiation

Inferred from mutant phenotype PubMed 18218617. Source: RGD

response to hypoxia

Inferred from sequence or structural similarity. Source: HGNC

smooth muscle tissue development

Inferred from sequence or structural similarity. Source: HGNC

spinal cord development

Inferred from sequence or structural similarity. Source: HGNC

sympathetic nervous system development

Inferred from sequence or structural similarity. Source: HGNC

visual learning

Inferred from sequence or structural similarity. Source: HGNC

wound healing

Inferred from sequence or structural similarity. Source: HGNC

   Cellular_componentaxon

Inferred from direct assay PubMed 1550670. Source: HGNC

cytoplasm

Inferred from direct assay PubMed 1550670. Source: HGNC

dendrite

Inferred from direct assay PubMed 1550670. Source: HGNC

intrinsic component of the cytoplasmic side of the plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

membrane

Inferred from direct assay PubMed 11356864. Source: RGD

neuron projection

Inferred from direct assay PubMed 11356864. Source: RGD

nucleus

Inferred from direct assay PubMed 1550670. Source: HGNC

postsynaptic density

Inferred from direct assay PubMed 11356864. Source: RGD

protein complex

Inferred from direct assay PubMed 11356864. Source: RGD

   Molecular_functionRas GTPase activator activity

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule binding

Inferred from direct assay PubMed 7568895. Source: MGI

phosphatidylcholine binding

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylethanolamine binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11356864PubMed 18313395. Source: RGD

syndecan binding

Inferred from physical interaction PubMed 11356864. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 28202819Neurofibromin
PRO_0000056667

Regions

Domain1237 – 1432196Ras-GAP
Domain1561 – 1719159CRAL-TRIO
Region1561 – 1818258Lipid binding By similarity
Motif2536 – 255217Bipartite nuclear localization signal By similarity
Compositional bias1354 – 13574Poly-Ser

Amino acid modifications

Modified residue21N-acetylalanine Ref.3
Modified residue8661Phosphoserine By similarity
Modified residue8781Phosphoserine By similarity
Modified residue21691Phosphoserine By similarity
Modified residue24961Phosphoserine By similarity
Modified residue25021Phosphoserine By similarity
Modified residue25241Phosphoserine By similarity
Modified residue27981Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P97526 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: FC108487E86DA89F

FASTA2,820317,083
        10         20         30         40         50         60 
MAAHRPVEWV QAVVSRFDEQ LPIKTGQQNT HTKVSTEHNK ECLINISKYK FSLVISGLTT 

        70         80         90        100        110        120 
ILKNVNNMRI FGEAAEKNLY LSQLIILDTL EKCLAGQPKD TMRLDETMLV KQLLPEICHF 

       130        140        150        160        170        180 
LHTCREGNQH AAELRNSASG VLFSLSCNNF NAVFSRISTR LQELTVCSED NVDVHDIELL 

       190        200        210        220        230        240 
QYINVDCAKL KRLLKETAFK FKALKKVAQL AVINSLEKAF WNWVENYPDE FTKLYQIPQT 

       250        260        270        280        290        300 
DMAECAGKLF DLVDGFAEST KRKAAVWPLQ IILLILCPEI IQDISRDVVD ENNTNKKLFL 

       310        320        330        340        350        360 
DSLRKALAGH GGSRQLTESA AIACVKLCKA STYINWEDNS VIFLLVQSMV VDLKNLLFNP 

       370        380        390        400        410        420 
SKPFSRGSQP ADVDLMIDCL VSCFRISPHN NQHFKICLAQ NSPSTFHYVL VNSLHRIITN 

       430        440        450        460        470        480 
SAWDWWPKID AVYCHSVELR NMFGETLHKA VQGCGAHPAL RMAPSLTFKE KVTSLKFKEK 

       490        500        510        520        530        540 
PTDLEARSYK YLLLSMVKLI HADPKLLLCN PRKQGPETQG STAELITGLV QLVPQSHMPE 

       550        560        570        580        590        600 
VAQEAMEALL VLHQLDSIDL WNPDAPVETF WEISSQMLFY ICKKLTSHQM LSSTEILKWL 

       610        620        630        640        650        660 
REILICRNKF LLKNKQADRS SCHSLYLYGV GCDLPASGNV TQMSVDHEES LRTCAPGASL 

       670        680        690        700        710        720 
RKGRGNSSMD STAGCSGTPP ICRQAQTKLE VALYMFLWSP DTEVVLVAMS CFRHLCEEAD 

       730        740        750        760        770        780 
IRCGVDEVSV HNFLPNYNTF MEFASVSNML STGRAALQKR VMALLRRIEH PTAGNTEAWE 

       790        800        810        820        830        840 
DTHAKWEQAT KLILNYPKAK MEDGQAAESL HKTIVKRRMS HVSGGGSIDL SDTDSLQEWI 

       850        860        870        880        890        900 
NMTGFLCALG GVCLQQRSSS GLATYSPPMG PVSERKGSMI SVMSSEGNVD SPVSRFMDRL 

       910        920        930        940        950        960 
LSLMVCNHEK VGLQIRTNVK DLVGLELSPA LYPMLFNKLK SAISKFFDSQ GQVLLTDSNT 

       970        980        990       1000       1010       1020 
QFVEQTIAIM KNLLDNHTEG SSEHLGQASI ETMMLNLVRY VRVLGNMVHA IQIKTKLCQL 

      1030       1040       1050       1060       1070       1080 
VEVMMARRDD LSFCQEMKFR NKMVEYLTDW VMGTSNQAAD DDVKCLTRDL DQASMEAVVS 

      1090       1100       1110       1120       1130       1140 
LLAGLPLQPE EGDGVELMEA KSQLFLKYFT LFMNLLNDCS EVEDENAQTG GRKRGMSRRL 

      1150       1160       1170       1180       1190       1200 
ASLRHCTVLA MSNLLNANVD SGLMHSIGLG YHKDLQTRAT FMEVLTKILQ QGTEFDTLAE 

      1210       1220       1230       1240       1250       1260 
TVLADRFERL VELVTMMGDQ GELPIAMALA NVVPCSQWDE LARVLVTLFD SRHLLYQLLW 

      1270       1280       1290       1300       1310       1320 
NMFSKEVELA DSMQTLFRGN SLASKIMTFC FKVYGATYLQ KLLDPLLRII ITSSDWQHVS 

      1330       1340       1350       1360       1370       1380 
FEVDPTRLEP SESLEENQRN LLQMTEKFFH AIISSSSEFP SQLRSVCHCL YQVVSQRFPQ 

      1390       1400       1410       1420       1430       1440 
NSIGAVGSAM FLRFINPAIV SPYEAGILDK KPPPRIERGL KLMSKVLQSI ANHVLFTKEE 

      1450       1460       1470       1480       1490       1500 
HMRPFNDFVK SNFDLARRFF LDIASDCPTS DAVNHSLSFI SDGNVLALHR LLWNNQEKIG 

      1510       1520       1530       1540       1550       1560 
QYLSSNRDHK AVGRRPFDKM ATLLAYLGPP EHKPVADTHW SSLNLTSSKF EEFMTRHQVH 

      1570       1580       1590       1600       1610       1620 
EKEEFKALKT LSIFYQAGTS KAGNPIFYYV ARRFKTGQIN GDLLIYHVLL TLKPYYAKPY 

      1630       1640       1650       1660       1670       1680 
EIVVDLTHTG PSNRFKTDFL SKWFVVFPGF AYDNVSAVYI YNCNSWVREY TKYHERLLTG 

      1690       1700       1710       1720       1730       1740 
LKGSKRLIFI DCPGKLAEHI EHEQQKLPAA TLALEEDLKV FHNALKLAHK DTKVSIKVGS 

      1750       1760       1770       1780       1790       1800 
TAVQVTSAER TKVLGQSVFL NDIYYASEIE EICLVDENQF TLTIANQGTP LTFMHQECEA 

      1810       1820       1830       1840       1850       1860 
IVQSIIHIRT RWELSQPDSI PQHTKIRPKD VPGTLLNIAL LNLGSSDPSL RSAAYNLLCA 

      1870       1880       1890       1900       1910       1920 
LTCTFNLKIE GQLLETSGLC IPANNTLFIV SISKTLAANE PHLTLEFLEE CISGFSKSSI 

      1930       1940       1950       1960       1970       1980 
ELKHLCLEYM TPWLSNLVRF CKHNDDAKRQ RVTAILDKLI TMTINEKQMY PSIQAKIWGS 

      1990       2000       2010       2020       2030       2040 
LGQITDLLDV VLDSFIKTSA TGGLGSIKAE VMADTAVALA SGNVKLVSSK VIGRMCKIID 

      2050       2060       2070       2080       2090       2100 
KTCLSPTPTL EQHLMWDDIA ILARYMLMLS FNNSLDVAAH LPYLFHVVTF LVATGPLSLR 

      2110       2120       2130       2140       2150       2160 
ASTHGLVINI IHSLCTCSQL HFSEETKQVL RLSLTEFSLP KFYLLFGISK VKSAAVIAFR 

      2170       2180       2190       2200       2210       2220 
SSYRDRSFSP GSYERETFAL TSLETVTEAL LEIMEACMRD IPTCKWLDQW TELAQRFAFQ 

      2230       2240       2250       2260       2270       2280 
YNPSLQPRAL VVFGCISKRV SHGQIKQIIR ILSKALESCL KGPDTYNSQV LIEATVIALT 

      2290       2300       2310       2320       2330       2340 
KLQPLLNKDS PLHKALFWVA VAVLQLDEVN LYSAGTALLE QNLHTLDSLR IFNDKSPEEV 

      2350       2360       2370       2380       2390       2400 
FMAIRNPLEW HCKQMDHFVG LNFNSNFNFA LVGHLLKGYR HPSPAIVART VRILHTLLTL 

      2410       2420       2430       2440       2450       2460 
VNKHRNCDKF EVNTQSVAYL AALLTVSEEV RSRCSLKHRK SLLLTDISME NVPMDTYPIH 

      2470       2480       2490       2500       2510       2520 
HGDPSSRTLK ETQPWSSPRG SEGYLAATYP AVGQTSPRAR KSMSLDMGQP SQANTKKLLG 

      2530       2540       2550       2560       2570       2580 
TRKSFDHLIS DTKAPKRQEM ESGITTPPKM RRVAETDYEM ETQRISSSQQ HPHLRKVSVS 

      2590       2600       2610       2620       2630       2640 
ESNVLLDEEV LTDPKIQALL LTVLATLVKY TTDEFDQRIL YEYLAEASVV FPKVFPLVHN 

      2650       2660       2670       2680       2690       2700 
LLDSKINTLL SLCQDPNLLN PIHGIVQSVV YHEESPPQYQ TSYLQSFGFN GLWRFAGPFS 

      2710       2720       2730       2740       2750       2760 
KQTQIPDYAE LIVKFLDALI DTYLPGIDEE TSEESLLTPT SPYPPALQSQ LSITANLNLS 

      2770       2780       2790       2800       2810       2820 
NSMTSLATSQ HSPGIDKENV ELSPTTGHCN SGRTRHGSAS QVQKQRSAGS FKRNSIKKIV 

« Hide

References

[1]"Differential splicing of the neurofibromatosis type 1 (NF1) gene in rats: homologous splice variants in human are expressed in rat cells."
Kyritsis A.P., Lee P.S., Mochizuki H., Nishi T., Levin V.A., Saya H.
Int. J. Oncol. 1:149-152(1992)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Brain.
[2]"Differential tissue-specific expression of neurofibromin isoform mRNAs in rat."
Suzuki H., Takahashi K., Yasumoto K., Fuse N., Shibahara S.
J. Biochem. 120:1048-1054(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Brain.
[3]Bienvenut W.V., von Kriegsheim A.F., Kolch W.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-24; 51-63; 78-92; 104-111; 207-218; 249-262; 298-305; 355-366; 462-469; 491-498; 767-785; 792-798; 972-999; 1003-1014; 1179-1209; 1244-1252; 1266-1278; 1293-1327; 1340-1364; 1394-1410; 1426-1438; 1451-1457; 1491-1507; 1550-1556; 1570-1592; 1619-1634; 1707-1726; 1738-1750; 1810-1825; 1830-1851; 1952-1976; 1998-2025; 2132-2150; 2153-2160; 2167-2175; 2206-2228; 2262-2281; 2331-2345; 2468-2498; 2502-2516; 2596-2618 AND 2702-2714, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Pheochromocytoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D45201 mRNA. Translation: BAA08141.1.
PIRJC5196.
RefSeqNP_036741.1. NM_012609.1.
UniGeneRn.10686.

3D structure databases

ProteinModelPortalP97526.
SMRP97526. Positions 1208-1531, 1562-1818.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246735. 2 interactions.
IntActP97526. 4 interactions.
MINTMINT-198504.
STRING10116.ENSRNOP00000049106.

PTM databases

PhosphoSiteP97526.

Proteomic databases

PaxDbP97526.
PRIDEP97526.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24592.
KEGGrno:24592.

Organism-specific databases

CTD4763.
RGD3168. Nf1.

Phylogenomic databases

eggNOGCOG5261.
HOGENOMHOG000047020.
HOVERGENHBG006486.
KOK08052.
PhylomeDBP97526.

Gene expression databases

GenevestigatorP97526.

Family and domain databases

Gene3D1.10.506.10. 1 hit.
1.25.10.10. 7 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR001251. CRAL-TRIO_dom.
IPR028553. Neurofibromin.
IPR001936. RasGAP.
IPR023152. RasGAP_CS.
IPR008936. Rho_GTPase_activation_prot.
[Graphical view]
PANTHERPTHR10194:SF60. PTHR10194:SF60. 1 hit.
PfamPF13716. CRAL_TRIO_2. 1 hit.
PF00616. RasGAP. 1 hit.
[Graphical view]
SMARTSM00323. RasGAP. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]
SUPFAMSSF48350. SSF48350. 1 hit.
SSF48371. SSF48371. 8 hits.
PROSITEPS50191. CRAL_TRIO. 1 hit.
PS00509. RAS_GTPASE_ACTIV_1. 1 hit.
PS50018. RAS_GTPASE_ACTIV_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio603784.
PROP97526.

Entry information

Entry nameNF1_RAT
AccessionPrimary (citable) accession number: P97526
Entry history
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families