| Tag | Content |
|---|
| EKPD ID | EKS-HOS-00051 |
| Classification | | Group/Family | Score | E-Value | Start | End | Domain Length |
|---|
| TKL/RAF | 414.3 | 1.3E-123 | 134 | 391 | 258 |
|
| Status | Reviewed |
| Ensembl Protein | ENSP00000441186 |
| UniProt Accession | P04049; B0LPH8; B2R5N3; Q15278; Q9UC20; |
| Protein Name | RAF proto-oncogene serine/threonine-protein kinase |
| Protein Synonyms/Alias | Proto-oncogene c-RAF; cRaf; Raf-1; |
| Gene Name | RAF1 |
| Gene Synonyms/Alias | RAF1; RAF; |
| Ensembl Information | |
| Organism | Homo sapiens |
| Functional Description | Serine/threonine-protein kinase that acts as aregulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2- antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation. |
| Protein Length | 433 |
Protein Sequence
(FASTA) | | MCVDWSNIRQ LFSQHRYSTP HAFTFNTSSP SSEGSLSQRQ RSTSTPNVHM VSTTLPVDSR 60 | | MIEDAIRSHS ESASPSALSS SPNNLSPTGW SQPKTPVPAQ RERAPVSGTQ EKNKIRPRGQ 120 | | RDSSYYWEIE ASEVMLSTRI GSGSFGTVYK GKWHGDVAVK ILKVVDPTPE QFQAFRNEVA 180 | | VLRKTRHVNI LLFMGYMTKD NLAIVTQWCE GSSLYKHLHV QETKFQMFQL IDIARQTAQG 240 | | MDYLHAKNII HRDMKSNNIF LHEGLTVKIG DFGLATVKSR WSGSQQVEQP TGSVLWMAPE 300 | | VIRMQDNNPF SFQSDVYSYG IVLYELMTGE LPYSHINNRD QIIFMVGRGY ASPDLSKLYK 360 | | NCPKAMKRLV ADCVKKVKEE RPLFPQILSS IELLQHSLPK INRSASEPSL HRAAHTEDIN 420 | | ACTLTTSPRL PVF 433 |
|
Nucleotide Sequence
(FASTA) | | ATGTGTGTGG ACTGGAGTAA CATCAGACAA CTCTTTTCTC AGCACAGATA TTCTACACCT 60 | | CACGCCTTCA CCTTTAACAC CTCCAGTCCC TCATCTGAAG GTTCCCTCTC CCAGAGGCAG 120 | | AGGTCGACAT CCACACCTAA TGTCCACATG GTCAGCACCA CCCTGCCTGT GGACAGCAGG 180 | | ATGATTGAGG ATGCAATTCG AAGTCACAGC GAATCAGCCT CACCTTCAGC CCTGTCCAGT 240 | | AGCCCCAACA ATCTGAGCCC AACAGGCTGG TCACAGCCGA AAACCCCCGT GCCAGCACAA 300 | | AGAGAGCGGG CACCAGTATC TGGGACCCAG GAGAAAAACA AAATTAGGCC TCGTGGACAG 360 | | AGAGATTCAA GCTATTATTG GGAAATAGAA GCCAGTGAAG TGATGCTGTC CACTCGGATT 420 | | GGGTCAGGCT CTTTTGGAAC TGTTTATAAG GGTAAATGGC ACGGAGATGT TGCAGTAAAG 480 | | ATCCTAAAGG TTGTCGACCC AACCCCAGAG CAATTCCAGG CCTTCAGGAA TGAGGTGGCT 540 | | GTTCTGCGCA AAACACGGCA TGTGAACATT CTGCTTTTCA TGGGGTACAT GACAAAGGAC 600 | | AACCTGGCAA TTGTGACCCA GTGGTGCGAG GGCAGCAGCC TCTACAAACA CCTGCATGTC 660 | | CAGGAGACCA AGTTTCAGAT GTTCCAGCTA ATTGACATTG CCCGGCAGAC GGCTCAGGGA 720 | | ATGGACTATT TGCATGCAAA GAACATCATC CATAGAGACA TGAAATCCAA CAATATATTT 780 | | CTCCATGAAG GCTTAACAGT GAAAATTGGA GATTTTGGTT TGGCAACAGT AAAGTCACGC 840 | | TGGAGTGGTT CTCAGCAGGT TGAACAACCT ACTGGCTCTG TCCTCTGGAT GGCCCCAGAG 900 | | GTGATCCGAA TGCAGGATAA CAACCCATTC AGTTTCCAGT CGGATGTCTA CTCCTATGGC 960 | | ATCGTATTGT ATGAACTGAT GACGGGGGAG CTTCCTTATT CTCACATCAA CAACCGAGAT 1020 | | CAGATCATCT TCATGGTGGG CCGAGGATAT GCCTCCCCAG ATCTTAGTAA GCTATATAAG 1080 | | AACTGCCCCA AAGCAATGAA GAGGCTGGTA GCTGACTGTG TGAAGAAAGT AAAGGAAGAG 1140 | | AGGCCTCTTT TTCCCCAGAT CCTGTCTTCC ATTGAGCTGC TCCAACACTC TCTACCGAAG 1200 | | ATCAACCGGA GCGCTTCCGA GCCATCCTTG CATCGGGCAG CCCACACTGA GGATATCAAT 1260 | | GCTTGCACGC TGACCACGTC CCCGAGGCTG CCTGTCTTCT AG 1302 |
|
| Domain Profile | S: 1 velaekiGsGrfGtvyrgkwhGdvavkllnveelseeqleaFkkevaaykktRhenivLF 60 | v+l+++iGsG+fGtvy+gkwhGdvavk+l+v ++++eq++aF++eva+++ktRh+ni+LF | Q: 134 VMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLF 193 | 57899******************************************************* |
| S: 61 mGyvskpelaivtslckgssLykllheqetkldlaklidiarqiaqgmdYLhakkilhkD 120 | mGy++k++laivt++c+gssLyk+lh+qetk+++ +lidiarq+aqgmdYLhak+i+h+D | Q: 194 MGYMTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRD 253 | ************************************************************ |
| S: 121 lksknilleeglkvvitDFgllsvkrllsgrrekqleipkgwilylapeviralsidleq 180 | +ks+ni+l+egl+v+i+DFgl++vk+++sg ++q+e+p+g++l++apevir+ q | Q: 254 MKSNNIFLHEGLTVKIGDFGLATVKSRWSG--SQQVEQPTGSVLWMAPEVIRM------Q 305 | ******************************..*********************......* |
| S: 181 delpfskesDvyafGivlyellarelpyke.esadqilfavgrG.lkpdlskvksklpke 238 | d++pfs++sDvy++Givlyel+++elpy++ +++dqi+f+vgrG ++pdlsk+++++pk+ | Q: 306 DNNPFSFQSDVYSYGIVLYELMTGELPYSHiNNRDQIIFMVGRGyASPDLSKLYKNCPKA 365 | ************************************************************ |
| S: 239 lkellleClkfekeeRPlftqilkkl 264 | +k+l+++C+k+ keeRPlf+qil+++ | Q: 366 MKRLVADCVKKVKEERPLFPQILSSI 391 | **********************9875 |
|
Domain Sequence
(FASTA) | | VMLSTRIGSG SFGTVYKGKW HGDVAVKILK VVDPTPEQFQ AFRNEVAVLR KTRHVNILLF 60 | | MGYMTKDNLA IVTQWCEGSS LYKHLHVQET KFQMFQLIDI ARQTAQGMDY LHAKNIIHRD 120 | | MKSNNIFLHE GLTVKIGDFG LATVKSRWSG SQQVEQPTGS VLWMAPEVIR MQDNNPFSFQ 180 | | SDVYSYGIVL YELMTGELPY SHINNRDQII FMVGRGYASP DLSKLYKNCP KAMKRLVADC 240 | | VKKVKEERPL FPQILSSI 258 |
|
| Keyword | 3D-structure; Alternative splicing; ATP-binding; Cell membrane; Complete proteome; Cytoplasm; Deafness; Direct protein sequencing; Disease mutation; Kinase; Membrane; Metal-binding; Methylation; Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; Reference proteome; Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger. |
| Sequence Source | Ensembl |
| Orthology | |
| Gene Ontology | |
| KEGG | |
| InterPros | |
| Pfam | |
| SMARTs | |
| Prosites | |
| Prints | |
| Created Date | 20-Feb-2013 |