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P97526

- NF1_RAT

UniProt

P97526 - NF1_RAT

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Protein

Neurofibromin

Gene
Nf1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. microtubule binding Source: MGI
  2. phosphatidylcholine binding Source: UniProtKB
  3. phosphatidylethanolamine binding Source: UniProtKB
  4. protein binding Source: RGD
  5. Ras GTPase activator activity Source: UniProtKB
  6. syndecan binding Source: RGD

GO - Biological processi

  1. actin cytoskeleton organization Source: HGNC
  2. adrenal gland development Source: HGNC
  3. artery morphogenesis Source: HGNC
  4. brain development Source: HGNC
  5. camera-type eye morphogenesis Source: HGNC
  6. cell communication Source: HGNC
  7. cerebral cortex development Source: HGNC
  8. collagen fibril organization Source: HGNC
  9. extracellular matrix organization Source: HGNC
  10. forebrain astrocyte development Source: HGNC
  11. forebrain morphogenesis Source: HGNC
  12. heart development Source: HGNC
  13. liver development Source: HGNC
  14. MAPK cascade Source: HGNC
  15. metanephros development Source: HGNC
  16. myelination in peripheral nervous system Source: HGNC
  17. negative regulation of fibroblast proliferation Source: UniProtKB
  18. negative regulation of MAPK cascade Source: HGNC
  19. negative regulation of MAP kinase activity Source: HGNC
  20. negative regulation of neuroblast proliferation Source: HGNC
  21. negative regulation of oligodendrocyte differentiation Source: HGNC
  22. negative regulation of protein kinase activity Source: HGNC
  23. negative regulation of Ras protein signal transduction Source: RefGenome
  24. negative regulation of transcription factor import into nucleus Source: HGNC
  25. osteoblast differentiation Source: HGNC
  26. peripheral nervous system development Source: HGNC
  27. phosphatidylinositol 3-kinase signaling Source: HGNC
  28. pigmentation Source: HGNC
  29. positive regulation of adenylate cyclase activity Source: HGNC
  30. positive regulation of apoptotic process Source: HGNC
  31. positive regulation of neuron apoptotic process Source: HGNC
  32. positive regulation of Ras GTPase activity Source: UniProtKB
  33. Ras protein signal transduction Source: HGNC
  34. regulation of angiogenesis Source: HGNC
  35. regulation of bone resorption Source: HGNC
  36. regulation of cell-matrix adhesion Source: HGNC
  37. regulation of glial cell differentiation Source: HGNC
  38. regulation of neuron differentiation Source: RGD
  39. regulation of Ras GTPase activity Source: HGNC
  40. response to hypoxia Source: HGNC
  41. Schwann cell development Source: HGNC
  42. smooth muscle tissue development Source: HGNC
  43. spinal cord development Source: HGNC
  44. sympathetic nervous system development Source: HGNC
  45. visual learning Source: HGNC
  46. wound healing Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Neurofibromin
Alternative name(s):
Neurofibromatosis-related protein NF-1
Gene namesi
Name:Nf1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi3168. Nf1.

Subcellular locationi

Nucleus By similarity. Nucleusnucleolus By similarity

GO - Cellular componenti

  1. axon Source: HGNC
  2. cytoplasm Source: HGNC
  3. dendrite Source: HGNC
  4. intrinsic component of the cytoplasmic side of the plasma membrane Source: RefGenome
  5. membrane Source: RGD
  6. neuron projection Source: RGD
  7. nucleus Source: HGNC
  8. postsynaptic density Source: RGD
  9. protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 28202819NeurofibrominPRO_0000056667Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei866 – 8661Phosphoserine By similarity
Modified residuei878 – 8781Phosphoserine By similarity
Modified residuei2169 – 21691Phosphoserine By similarity
Modified residuei2496 – 24961Phosphoserine By similarity
Modified residuei2502 – 25021Phosphoserine By similarity
Modified residuei2524 – 25241Phosphoserine By similarity
Modified residuei2798 – 27981Phosphoserine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP97526.
PRIDEiP97526.

PTM databases

PhosphoSiteiP97526.

Expressioni

Gene expression databases

GenevestigatoriP97526.

Interactioni

Protein-protein interaction databases

BioGridi246735. 2 interactions.
IntActiP97526. 4 interactions.
MINTiMINT-198504.
STRINGi10116.ENSRNOP00000049106.

Structurei

3D structure databases

ProteinModelPortaliP97526.
SMRiP97526. Positions 1208-1531, 1562-1818.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1237 – 1432196Ras-GAPAdd
BLAST
Domaini1561 – 1719159CRAL-TRIOAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1561 – 1818258Lipid binding By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2536 – 255217Bipartite nuclear localization signal By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1354 – 13574Poly-Ser

Domaini

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 similaritiesi

Contains 1 CRAL-TRIO domain.
Contains 1 Ras-GAP domain.

Phylogenomic databases

eggNOGiCOG5261.
HOGENOMiHOG000047020.
HOVERGENiHBG006486.
KOiK08052.
PhylomeDBiP97526.

Family and domain databases

Gene3Di1.10.506.10. 1 hit.
1.25.10.10. 7 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR001251. CRAL-TRIO_dom.
IPR028553. Neurofibromin.
IPR001936. RasGAP.
IPR023152. RasGAP_CS.
IPR008936. Rho_GTPase_activation_prot.
[Graphical view]
PANTHERiPTHR10194:SF60. PTHR10194:SF60. 1 hit.
PfamiPF13716. CRAL_TRIO_2. 1 hit.
PF00616. RasGAP. 1 hit.
[Graphical view]
SMARTiSM00323. RasGAP. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF48371. SSF48371. 8 hits.
PROSITEiPS50191. CRAL_TRIO. 1 hit.
PS00509. RAS_GTPASE_ACTIV_1. 1 hit.
PS50018. RAS_GTPASE_ACTIV_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P97526-1 [UniParc]FASTAAdd to Basket

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MAAHRPVEWV QAVVSRFDEQ LPIKTGQQNT HTKVSTEHNK ECLINISKYK     50
FSLVISGLTT ILKNVNNMRI FGEAAEKNLY LSQLIILDTL EKCLAGQPKD 100
TMRLDETMLV KQLLPEICHF LHTCREGNQH AAELRNSASG VLFSLSCNNF 150
NAVFSRISTR LQELTVCSED NVDVHDIELL QYINVDCAKL KRLLKETAFK 200
FKALKKVAQL AVINSLEKAF WNWVENYPDE FTKLYQIPQT DMAECAGKLF 250
DLVDGFAEST KRKAAVWPLQ IILLILCPEI IQDISRDVVD ENNTNKKLFL 300
DSLRKALAGH GGSRQLTESA AIACVKLCKA STYINWEDNS VIFLLVQSMV 350
VDLKNLLFNP SKPFSRGSQP ADVDLMIDCL VSCFRISPHN NQHFKICLAQ 400
NSPSTFHYVL VNSLHRIITN SAWDWWPKID AVYCHSVELR NMFGETLHKA 450
VQGCGAHPAL RMAPSLTFKE KVTSLKFKEK PTDLEARSYK YLLLSMVKLI 500
HADPKLLLCN PRKQGPETQG STAELITGLV QLVPQSHMPE VAQEAMEALL 550
VLHQLDSIDL WNPDAPVETF WEISSQMLFY ICKKLTSHQM LSSTEILKWL 600
REILICRNKF LLKNKQADRS SCHSLYLYGV GCDLPASGNV TQMSVDHEES 650
LRTCAPGASL RKGRGNSSMD STAGCSGTPP ICRQAQTKLE VALYMFLWSP 700
DTEVVLVAMS CFRHLCEEAD IRCGVDEVSV HNFLPNYNTF MEFASVSNML 750
STGRAALQKR VMALLRRIEH PTAGNTEAWE DTHAKWEQAT KLILNYPKAK 800
MEDGQAAESL HKTIVKRRMS HVSGGGSIDL SDTDSLQEWI NMTGFLCALG 850
GVCLQQRSSS GLATYSPPMG PVSERKGSMI SVMSSEGNVD SPVSRFMDRL 900
LSLMVCNHEK VGLQIRTNVK DLVGLELSPA LYPMLFNKLK SAISKFFDSQ 950
GQVLLTDSNT QFVEQTIAIM KNLLDNHTEG SSEHLGQASI ETMMLNLVRY 1000
VRVLGNMVHA IQIKTKLCQL VEVMMARRDD LSFCQEMKFR NKMVEYLTDW 1050
VMGTSNQAAD DDVKCLTRDL DQASMEAVVS LLAGLPLQPE EGDGVELMEA 1100
KSQLFLKYFT LFMNLLNDCS EVEDENAQTG GRKRGMSRRL ASLRHCTVLA 1150
MSNLLNANVD SGLMHSIGLG YHKDLQTRAT FMEVLTKILQ QGTEFDTLAE 1200
TVLADRFERL VELVTMMGDQ GELPIAMALA NVVPCSQWDE LARVLVTLFD 1250
SRHLLYQLLW NMFSKEVELA DSMQTLFRGN SLASKIMTFC FKVYGATYLQ 1300
KLLDPLLRII ITSSDWQHVS FEVDPTRLEP SESLEENQRN LLQMTEKFFH 1350
AIISSSSEFP SQLRSVCHCL YQVVSQRFPQ NSIGAVGSAM FLRFINPAIV 1400
SPYEAGILDK KPPPRIERGL KLMSKVLQSI ANHVLFTKEE HMRPFNDFVK 1450
SNFDLARRFF LDIASDCPTS DAVNHSLSFI SDGNVLALHR LLWNNQEKIG 1500
QYLSSNRDHK AVGRRPFDKM ATLLAYLGPP EHKPVADTHW SSLNLTSSKF 1550
EEFMTRHQVH EKEEFKALKT LSIFYQAGTS KAGNPIFYYV ARRFKTGQIN 1600
GDLLIYHVLL TLKPYYAKPY EIVVDLTHTG PSNRFKTDFL SKWFVVFPGF 1650
AYDNVSAVYI YNCNSWVREY TKYHERLLTG LKGSKRLIFI DCPGKLAEHI 1700
EHEQQKLPAA TLALEEDLKV FHNALKLAHK DTKVSIKVGS TAVQVTSAER 1750
TKVLGQSVFL NDIYYASEIE EICLVDENQF TLTIANQGTP LTFMHQECEA 1800
IVQSIIHIRT RWELSQPDSI PQHTKIRPKD VPGTLLNIAL LNLGSSDPSL 1850
RSAAYNLLCA LTCTFNLKIE GQLLETSGLC IPANNTLFIV SISKTLAANE 1900
PHLTLEFLEE CISGFSKSSI ELKHLCLEYM TPWLSNLVRF CKHNDDAKRQ 1950
RVTAILDKLI TMTINEKQMY PSIQAKIWGS LGQITDLLDV VLDSFIKTSA 2000
TGGLGSIKAE VMADTAVALA SGNVKLVSSK VIGRMCKIID KTCLSPTPTL 2050
EQHLMWDDIA ILARYMLMLS FNNSLDVAAH LPYLFHVVTF LVATGPLSLR 2100
ASTHGLVINI IHSLCTCSQL HFSEETKQVL RLSLTEFSLP KFYLLFGISK 2150
VKSAAVIAFR SSYRDRSFSP GSYERETFAL TSLETVTEAL LEIMEACMRD 2200
IPTCKWLDQW TELAQRFAFQ YNPSLQPRAL VVFGCISKRV SHGQIKQIIR 2250
ILSKALESCL KGPDTYNSQV LIEATVIALT KLQPLLNKDS PLHKALFWVA 2300
VAVLQLDEVN LYSAGTALLE QNLHTLDSLR IFNDKSPEEV FMAIRNPLEW 2350
HCKQMDHFVG LNFNSNFNFA LVGHLLKGYR HPSPAIVART VRILHTLLTL 2400
VNKHRNCDKF EVNTQSVAYL AALLTVSEEV RSRCSLKHRK SLLLTDISME 2450
NVPMDTYPIH HGDPSSRTLK ETQPWSSPRG SEGYLAATYP AVGQTSPRAR 2500
KSMSLDMGQP SQANTKKLLG TRKSFDHLIS DTKAPKRQEM ESGITTPPKM 2550
RRVAETDYEM ETQRISSSQQ HPHLRKVSVS ESNVLLDEEV LTDPKIQALL 2600
LTVLATLVKY TTDEFDQRIL YEYLAEASVV FPKVFPLVHN LLDSKINTLL 2650
SLCQDPNLLN PIHGIVQSVV YHEESPPQYQ TSYLQSFGFN GLWRFAGPFS 2700
KQTQIPDYAE LIVKFLDALI DTYLPGIDEE TSEESLLTPT SPYPPALQSQ 2750
LSITANLNLS NSMTSLATSQ HSPGIDKENV ELSPTTGHCN SGRTRHGSAS 2800
QVQKQRSAGS FKRNSIKKIV 2820
Length:2,820
Mass (Da):317,083
Last modified:May 1, 1997 - v1
Checksum:iFC108487E86DA89F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D45201 mRNA. Translation: BAA08141.1.
PIRiJC5196.
RefSeqiNP_036741.1. NM_012609.1.
UniGeneiRn.10686.

Genome annotation databases

GeneIDi24592.
KEGGirno:24592.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D45201 mRNA. Translation: BAA08141.1 .
PIRi JC5196.
RefSeqi NP_036741.1. NM_012609.1.
UniGenei Rn.10686.

3D structure databases

ProteinModelPortali P97526.
SMRi P97526. Positions 1208-1531, 1562-1818.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 246735. 2 interactions.
IntActi P97526. 4 interactions.
MINTi MINT-198504.
STRINGi 10116.ENSRNOP00000049106.

PTM databases

PhosphoSitei P97526.

Proteomic databases

PaxDbi P97526.
PRIDEi P97526.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 24592.
KEGGi rno:24592.

Organism-specific databases

CTDi 4763.
RGDi 3168. Nf1.

Phylogenomic databases

eggNOGi COG5261.
HOGENOMi HOG000047020.
HOVERGENi HBG006486.
KOi K08052.
PhylomeDBi P97526.

Miscellaneous databases

NextBioi 603784.
PROi P97526.

Gene expression databases

Genevestigatori P97526.

Family and domain databases

Gene3Di 1.10.506.10. 1 hit.
1.25.10.10. 7 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR001251. CRAL-TRIO_dom.
IPR028553. Neurofibromin.
IPR001936. RasGAP.
IPR023152. RasGAP_CS.
IPR008936. Rho_GTPase_activation_prot.
[Graphical view ]
PANTHERi PTHR10194:SF60. PTHR10194:SF60. 1 hit.
Pfami PF13716. CRAL_TRIO_2. 1 hit.
PF00616. RasGAP. 1 hit.
[Graphical view ]
SMARTi SM00323. RasGAP. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view ]
SUPFAMi SSF48350. SSF48350. 1 hit.
SSF48371. SSF48371. 8 hits.
PROSITEi PS50191. CRAL_TRIO. 1 hit.
PS00509. RAS_GTPASE_ACTIV_1. 1 hit.
PS50018. RAS_GTPASE_ACTIV_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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
    Tissue: Pheochromocytoma.

Entry informationi

Entry nameiNF1_RAT
AccessioniPrimary (citable) accession number: P97526
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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