HUMAN:BRAF

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	BRAF (synonyms: BRAF1, RAFB1)
Protein Name(s)	Serine/threonine-protein kinase B-raf Proto-oncogene B-Raf p94 v-Raf murine sarcoma viral oncogene homolog B1
External Links
UniProt	P15056
EMBL	M95712 AC006344 EU600171 AC006347 CH236950 BC101757 BC112079 X65187 M21001 AM989472 AM989473 AM989474 AM989475 AM989476 AM989477
CCDS	CCDS5863.1
PIR	A57977
RefSeq	NP_004324.2
UniGene	Hs.550061 Hs.600998 Hs.605380 Hs.659507
PDB	1UWH 1UWJ 2FB8 2L05 3C4C 3D4Q 3IDP 3II5 3NY5 3OG7 3PPJ 3PPK 3PRF 3PRI 3PSB 3PSD 3Q4C 3Q96 3SKC 3TV4 3TV6 4DBN 4E26 4E4X 4EHE 4EHG 4FC0 4FK3 4G9C 4G9R 4H58 4JVG 4KSP 4KSQ 4MBJ 4MNE 4MNF 4PP7
PDBsum	1UWH 1UWJ 2FB8 2L05 3C4C 3D4Q 3IDP 3II5 3NY5 3OG7 3PPJ 3PPK 3PRF 3PRI 3PSB 3PSD 3Q4C 3Q96 3SKC 3TV4 3TV6 4DBN 4E26 4E4X 4EHE 4EHG 4FC0 4FK3 4G9C 4G9R 4H58 4JVG 4KSP 4KSQ 4MBJ 4MNE 4MNF 4PP7
ProteinModelPortal	P15056
SMR	P15056
BioGrid	107141
DIP	DIP-1045N
IntAct	P15056
MINT	MINT-1574728
STRING	9606.ENSP00000288602
BindingDB	P15056
ChEMBL	CHEMBL5145
DrugBank	DB08912 DB08896 DB00398 DB08881
GuidetoPHARMACOLOGY	1943
PhosphoSite	P15056
DMDM	50403720
MaxQB	P15056
PaxDb	P15056
PRIDE	P15056
DNASU	673
Ensembl	ENST00000288602
GeneID	673
KEGG	hsa:673
UCSC	uc003vwc.4
CTD	673
GeneCards	GC07M140424
GeneReviews	BRAF
H-InvDB	HIX0167822
HGNC	HGNC:1097
HPA	CAB004552 HPA001328
MIM	114500 115150 164757 211980 605027 613706 613707
neXtProt	NX_P15056
Orphanet	1340 54595 58017 99872 500 648 251612
PharmGKB	PA25408
eggNOG	COG0515
GeneTree	ENSGT00760000118807
HOVERGEN	HBG001886
InParanoid	P15056
KO	K04365
OMA	HRTRTSS
OrthoDB	EOG7F5128
PhylomeDB	P15056
TreeFam	TF317006
BRENDA	2.7.10.2
Reactome	REACT_111080 REACT_12002 REACT_12076 REACT_12077 REACT_20568
SignaLink	P15056
ChiTaRS	BRAF
EvolutionaryTrace	P15056
GeneWiki	BRAF_(gene)
GenomeRNAi	673
NextBio	2776
PMAP-CutDB	P15056
PRO	PR:P15056
Proteomes	UP000005640
Bgee	P15056
CleanEx	HS_BRAF
ExpressionAtlas	P15056
Genevestigator	P15056
GO	GO:0044297 GO:0005829 GO:0005739 GO:0043005 GO:0005634 GO:0005886 GO:0005524 GO:0005509 GO:0042802 GO:0004709 GO:0004672 GO:0004674 GO:0000186 GO:0043367 GO:0071277 GO:0035690 GO:0008543 GO:0060291 GO:0002318 GO:0043066 GO:2000352 GO:0010764 GO:0043524 GO:2000301 GO:0048011 GO:0009887 GO:0070374 GO:0010628 GO:0033138 GO:0051496 GO:1900026 GO:0043368 GO:0051291 GO:0006468 GO:0042127 GO:0051591 GO:0070849 GO:0043434 GO:0007264 GO:0035019 GO:0007268 GO:0008542
InterPro	IPR020454 IPR011009 IPR002219 IPR000719 IPR017441 IPR003116 IPR001245 IPR008271 IPR029071
Pfam	PF00130 PF07714 PF02196
PRINTS	PR00008
SMART	SM00109 SM00455
SUPFAM	SSF54236 SSF56112
PROSITE	PS00107 PS50011 PS00108 PS50898 PS00479 PS50081

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0010828	positive regulation of glucose transmembrane transport	PMID:23010278^[1]	ECO:0000314			P		Figure 2.	complete CACAO 5181
	GO:0090150	establishment of protein localization to membrane	PMID:23010278^[1]	ECO:0000314			P		Figure 3: Coexpression of B-RAF enhanced SGLT1 protein abundance at the cell surface.	complete CACAO 5327
involved_in	GO:0070413	trehalose metabolism in response to stress	PMID:9837904^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0090150	establishment of protein localization to membrane	PMID:23010278^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010828	positive regulation of glucose transmembrane transport	PMID:23010278^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
NOT\|enables	GO:0031267	small GTPase binding	PMID:12194967^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O95057	F		Seeded From UniProt	complete
involved_in	GO:0071277	cellular response to calcium ion	PMID:18567582^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070374	positive regulation of ERK1 and ERK2 cascade	PMID:22065586^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	PMID:22065586^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:17563371^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	PMID:18567582^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:17563371^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:19667065^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0033138	positive regulation of peptidyl-serine phosphorylation	PMID:19667065^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:19667065^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:88190 PANTHER:PTN000584635 RGD:619908	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000584576 RGD:2148 UniProtKB:P04049 UniProtKB:P15056	C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:88065 MGI:MGI:88190 PANTHER:PTN000584576	C		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0003079 MGI:MGI:1346881 MGI:MGI:2443258 PANTHER:PTN001908122 RGD:1359261 RGD:619908 RGD:620063 TAIR:locus:2144613 UniProtKB:O43283 UniProtKB:P04049 UniProtKB:P10398 UniProtKB:P15056 UniProtKB:P80192 UniProtKB:Q02779 UniProtKB:Q13418 UniProtKB:Q13546 UniProtKB:Q16584	F		Seeded From UniProt	complete
involved_in	GO:0000165	MAPK cascade	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001907370 RGD:3531 WB:WBGene00003030	P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:25437913^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P15056	F	occurs_in:(GO:0005829)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:25155755^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P15056	F	occurs_in:(GO:0005829)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22510884^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P15056	F	occurs_in:(GO:0005829)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22169110^[12]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P15056	F	occurs_in:(GO:0005829)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19727074^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P15056	F	occurs_in:(GO:0005829)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16858395^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P15056	F	occurs_in:(GO:0005829)	Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR001245 InterPro:IPR008271	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR017441	F		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR001245 InterPro:IPR008271	P		Seeded From UniProt	complete
involved_in	GO:0007165	signal transduction	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003116	P		Seeded From UniProt	complete
involved_in	GO:0035556	intracellular signal transduction	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002219	P		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:9207797^[15]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0009887	animal organ morphogenesis	PMID:9207797^[15]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:2284096^[16]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:2284096^[16]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	Reactome:R-HSA-6803240 Reactome:R-HSA-6803233 Reactome:R-HSA-6803230 Reactome:R-HSA-6802926 Reactome:R-HSA-6802925 Reactome:R-HSA-6802924 Reactome:R-HSA-6802922 Reactome:R-HSA-6802921 Reactome:R-HSA-6802919 Reactome:R-HSA-6802916 Reactome:R-HSA-6802914 Reactome:R-HSA-6802908 Reactome:R-HSA-5675198	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-8936731 Reactome:R-HSA-8936676 Reactome:R-HSA-6803240 Reactome:R-HSA-6803234 Reactome:R-HSA-6803230 Reactome:R-HSA-6803227 Reactome:R-HSA-6802943 Reactome:R-HSA-6802942 Reactome:R-HSA-6802941 Reactome:R-HSA-6802938 Reactome:R-HSA-6802937 Reactome:R-HSA-6802930 Reactome:R-HSA-6802924 Reactome:R-HSA-6802921 Reactome:R-HSA-6802919 Reactome:R-HSA-6802918 Reactome:R-HSA-6802916 Reactome:R-HSA-6802915 Reactome:R-HSA-6802914 Reactome:R-HSA-6802912 Reactome:R-HSA-6802911 Reactome:R-HSA-6802910 Reactome:R-HSA-5675433 Reactome:R-HSA-5675431 Reactome:R-HSA-5675417 Reactome:R-HSA-5674140 Reactome:R-HSA-5674132 Reactome:R-HSA-5674130 Reactome:R-HSA-5672980 Reactome:R-HSA-5672978 Reactome:R-HSA-5672973 Reactome:R-HSA-5672972 Reactome:R-HSA-5672969 Reactome:R-HSA-5672966 Reactome:R-HSA-5672961 Reactome:R-HSA-5672960 Reactome:R-HSA-5672951 Reactome:R-HSA-5672950 Reactome:R-HSA-1295634 Reactome:R-HSA-1295604	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0000165	MAPK cascade	Reactome:R-HSA-5673001	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
involved_in	GO:0016310	phosphorylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	F		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0723	F		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 Pakladok, T et al. (2012) Stimulation of the Na(+)-coupled glucose transporter SGLT1 by B-RAF. Biochem. Biophys. Res. Commun. 427 689-93 PubMed GONUTS page
↑ Bell, W et al. (1998) Composition and functional analysis of the Saccharomyces cerevisiae trehalose synthase complex. J. Biol. Chem. 273 33311-9 PubMed GONUTS page
↑ Kontani, K et al. (2002) Di-Ras, a distinct subgroup of ras family GTPases with unique biochemical properties. J. Biol. Chem. 277 41070-8 PubMed GONUTS page
↑ ^4.0 ^4.1 Ren, JG et al. (2008) IQGAP1 integrates Ca2+/calmodulin and B-Raf signaling. J. Biol. Chem. 283 22972-82 PubMed GONUTS page
↑ ^5.0 ^5.1 Oh, YT et al. (2012) Oncogenic Ras and B-Raf proteins positively regulate death receptor 5 expression through co-activation of ERK and JNK signaling. J. Biol. Chem. 287 257-67 PubMed GONUTS page
↑ ^6.0 ^6.1 Ren, JG et al. (2007) IQGAP1 modulates activation of B-Raf. Proc. Natl. Acad. Sci. U.S.A. 104 10465-9 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Polzien, L et al. (2009) Identification of novel in vivo phosphorylation sites of the human proapoptotic protein BAD: pore-forming activity of BAD is regulated by phosphorylation. J. Biol. Chem. 284 28004-20 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 ^8.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Thevakumaran, N et al. (2015) Crystal structure of a BRAF kinase domain monomer explains basis for allosteric regulation. Nat. Struct. Mol. Biol. 22 37-43 PubMed GONUTS page
↑ Haling, JR et al. (2014) Structure of the BRAF-MEK complex reveals a kinase activity independent role for BRAF in MAPK signaling. Cancer Cell 26 402-13 PubMed GONUTS page
↑ Röring, M et al. (2012) Distinct requirement for an intact dimer interface in wild-type, V600E and kinase-dead B-Raf signalling. EMBO J. 31 2629-47 PubMed GONUTS page
↑ Packer, LM et al. (2011) Nilotinib and MEK inhibitors induce synthetic lethality through paradoxical activation of RAF in drug-resistant chronic myeloid leukemia. Cancer Cell 20 715-27 PubMed GONUTS page
↑ Rajakulendran, T et al. (2009) A dimerization-dependent mechanism drives RAF catalytic activation. Nature 461 542-5 PubMed GONUTS page
↑ Terai, K & Matsuda, M (2006) The amino-terminal B-Raf-specific region mediates calcium-dependent homo- and hetero-dimerization of Raf. EMBO J. 25 3556-64 PubMed GONUTS page
↑ ^15.0 ^15.1 Wojnowski, L et al. (1997) Endothelial apoptosis in Braf-deficient mice. Nat. Genet. 16 293-7 PubMed GONUTS page
↑ ^16.0 ^16.1 Sithanandam, G et al. (1990) Complete coding sequence of a human B-raf cDNA and detection of B-raf protein kinase with isozyme specific antibodies. Oncogene 5 1775-80 PubMed GONUTS page

[PMID:23010278-1] 1.0 ^1.1 ^1.2 ^1.3 Pakladok, T et al. (2012) Stimulation of the Na(+)-coupled glucose transporter SGLT1 by B-RAF. Biochem. Biophys. Res. Commun. 427 689-93 PubMed GONUTS page

[PMID:9837904-2] Bell, W et al. (1998) Composition and functional analysis of the Saccharomyces cerevisiae trehalose synthase complex. J. Biol. Chem. 273 33311-9 PubMed GONUTS page

[PMID:12194967-3] Kontani, K et al. (2002) Di-Ras, a distinct subgroup of ras family GTPases with unique biochemical properties. J. Biol. Chem. 277 41070-8 PubMed GONUTS page

[PMID:18567582-4] 4.0 ^4.1 Ren, JG et al. (2008) IQGAP1 integrates Ca2+/calmodulin and B-Raf signaling. J. Biol. Chem. 283 22972-82 PubMed GONUTS page

[PMID:22065586-5] 5.0 ^5.1 Oh, YT et al. (2012) Oncogenic Ras and B-Raf proteins positively regulate death receptor 5 expression through co-activation of ERK and JNK signaling. J. Biol. Chem. 287 257-67 PubMed GONUTS page

[PMID:17563371-6] 6.0 ^6.1 Ren, JG et al. (2007) IQGAP1 modulates activation of B-Raf. Proc. Natl. Acad. Sci. U.S.A. 104 10465-9 PubMed GONUTS page

[PMID:19667065-7] 7.0 ^7.1 ^7.2 Polzien, L et al. (2009) Identification of novel in vivo phosphorylation sites of the human proapoptotic protein BAD: pore-forming activity of BAD is regulated by phosphorylation. J. Biol. Chem. 284 28004-20 PubMed GONUTS page

[PMID:21873635-8] 8.0 ^8.1 ^8.2 ^8.3 ^8.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:25437913-9] Thevakumaran, N et al. (2015) Crystal structure of a BRAF kinase domain monomer explains basis for allosteric regulation. Nat. Struct. Mol. Biol. 22 37-43 PubMed GONUTS page

[PMID:25155755-10] Haling, JR et al. (2014) Structure of the BRAF-MEK complex reveals a kinase activity independent role for BRAF in MAPK signaling. Cancer Cell 26 402-13 PubMed GONUTS page

[PMID:22510884-11] Röring, M et al. (2012) Distinct requirement for an intact dimer interface in wild-type, V600E and kinase-dead B-Raf signalling. EMBO J. 31 2629-47 PubMed GONUTS page

[PMID:22169110-12] Packer, LM et al. (2011) Nilotinib and MEK inhibitors induce synthetic lethality through paradoxical activation of RAF in drug-resistant chronic myeloid leukemia. Cancer Cell 20 715-27 PubMed GONUTS page

[PMID:19727074-13] Rajakulendran, T et al. (2009) A dimerization-dependent mechanism drives RAF catalytic activation. Nature 461 542-5 PubMed GONUTS page

[PMID:16858395-14] Terai, K & Matsuda, M (2006) The amino-terminal B-Raf-specific region mediates calcium-dependent homo- and hetero-dimerization of Raf. EMBO J. 25 3556-64 PubMed GONUTS page

[PMID:9207797-15] 15.0 ^15.1 Wojnowski, L et al. (1997) Endothelial apoptosis in Braf-deficient mice. Nat. Genet. 16 293-7 PubMed GONUTS page

[PMID:2284096-16] 16.0 ^16.1 Sithanandam, G et al. (1990) Complete coding sequence of a human B-raf cDNA and detection of B-raf protein kinase with isozyme specific antibodies. Oncogene 5 1775-80 PubMed GONUTS page

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HUMAN:BRAF

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