LOCUS 125651 648 aa 15-DEC-1998 DEFINITION RAF PROTO-ONCOGENE SERINE/THREONINE-PROTEIN KINASE (RAF-1) (C-RAF). ACCESSION 125651 PID g125651 DBSOURCE SWISS-PROT: locus KRAF_HUMAN, accession P04049 class: standard. created: Nov 1, 1986. sequence updated: Nov 1, 1986. annotation updated: Dec 15, 1998. xrefs: gi: 35841, gi: 35842, gi: 66762 xrefs (non-sequence databases): MIM 164760, PROSITE PS00107, PROSITE PS00108, PROSITE PS00479, PROSITE PS50011, PFAM PF00069, PFAM PF00130 KEYWORDS TRANSFERASE; SERINE/THREONINE-PROTEIN KINASE; PROTO-ONCOGENE; ZINC; ATP-BINDING; PHORBOL-ESTER BINDING; 3D-STRUCTURE. SOURCE human. ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Vertebrata; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 648) AUTHORS Bonner,T.I., Oppermann,H., Seeburg,P., Kerby,S.B., Gunnell,M.A., Young,A.C. and Rapp,U.R. TITLE The complete coding sequence of the human raf oncogene and the corresponding structure of the c-raf-1 gene JOURNAL Nucleic Acids Res. 14 (2), 1009-1015 (1986) MEDLINE 86120351 REMARK SEQUENCE FROM N.A. REFERENCE 2 (residues 1 to 648) AUTHORS Nassar,N., Horn,G., Herrmann,C., Scherer,A., McCormick,F. and Wittinghofer,A. TITLE The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue JOURNAL Nature 375 (6532), 554-560 (1995) MEDLINE 95312074 REMARK X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 51-131. REFERENCE 3 (residues 1 to 648) AUTHORS Nassar,N., Horn,G., Herrmann,C., Block,C., Janknecht,R. and Wittinghofer,A. TITLE Ras/Rap effector specificity determined by charge reversal JOURNAL Nat. Struct. Biol. 3 (8), 723-729 (1996) MEDLINE 96313130 REMARK X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 56-131. REFERENCE 4 (residues 1 to 648) AUTHORS Emerson,S.D., Madison,V.S., Palermo,R.E., Waugh,D.S., Scheffler,J.E., Tsao,K.L., Kiefer,S.E., Liu,S.P. and Fry,D.C. TITLE Solution structure of the Ras-binding domain of c-Raf-1 and identification of its Ras interaction surface JOURNAL Biochemistry 34 (21), 6911-6918 (1995) MEDLINE 95284022 REMARK STRUCTURE BY NMR OF 55-132. REFERENCE 5 (residues 1 to 648) AUTHORS Mott,H.R., Carpenter,J.W., Zhong,S., Ghosh,S., Bell,R.M. and Campbell,S.L. TITLE The solution structure of the Raf-1 cysteine-rich domain: a novel ras and phospholipid binding site JOURNAL Proc. Natl. Acad. Sci. U.S.A. 93 (16), 8312-8317 (1996) MEDLINE 96323218 REMARK STRUCTURE BY NMR OF 136-187. COMMENT ------------------------------------------------------------------- This SWISS-PROT entry is copyright. It is produced through a collaboration between the Swiss Institute of Bioinformatics and the EMBL outstation - the European Bioinformatics Institute. The original entry is available from http://www.expasy.ch/sprot and http://www.ebi.ac.uk/sprot ------------------------------------------------------------------. [FUNCTION] INVOLVED IN THE TRANSDUCTION OF MITOGENIC SIGNALS FROM THE CELL MEMBRANE TO THE NUCLEUS. PART OF THE RAS-DEPENDENT SIGNALLING PATHWAY FROM RECEPTORS TO THE NUCLEUS. [SIMILARITY] WITH THE CONSERVED CATALYTIC DOMAINS OF SER/THR-PROTEIN KINASES. BELONGS TO THE MIL/RAF SUBFAMILY. [SIMILARITY] CONTAINS A COPY OF THE ZINC-DEPENDENT PHORBOL-ESTER AND DAG BINDING DOMAIN. FEATURES Location/Qualifiers source 1..648 /organism="Homo sapiens" /db_xref="taxon:9606" 1..648 Protein 1..648 /product="RAF PROTO-ONCOGENE SERINE/THREONINE-PROTEIN KINASE" /EC_number="2.7.1.-" Region 139..184 /note="PHORBOL-ESTER AND DAG BINDING." /region_name="Domain" Region 349..609 /note="PROTEIN KINASE." /region_name="Domain" Site 355..363 /note="ATP." /site_type="np-binding" Site 375 /note="ATP." /site_type="binding" Site 468 /site_type="active" ORIGIN 1 mehiqgawkt isngfgfkda vfdgsscisp tivqqfgyqr rasddgkltd psktsntirv 61 flpnkqrtvv nvrngmslhd clmkalkvrg lqpeccavfr llhehkgkka rldwntdaas 121 ligeelqvdf ldhvpltthn farktflkla fcdicqkfll ngfrcqtcgy kfhehcstkv 181 ptmcvdwsni rqlllfpnst igdsgvpalp sltmrrmres vsrmpvssqh rystphaftf 241 ntsspssegs lsqrqrstst pnvhmvsttl pvdsrmieda irshsesasp salssspnnl 301 sptgwsqpkt pvpaqrerap vsgtqeknki rprgqrdssy yweieasevm lstrigsgsf 361 gtvykgkwhg dvavkilkvv dptpeqfqaf rnevavlrkt rhvnillfmg ymtkdnlaiv 421 tqwcegssly khlhvqetkf qmfqlidiar qtaqgmdylh akniihrdmk snniflhegl 481 tvkigdfgla tvksrwsgsq qveqptgsvl wmapevirmq dnnpfsfqsd vysygivlye 541 lmtgelpysh innrdqiifm vgrgyaspdl sklykncpka mkrlvadcvk kvkeerplfp 601 qilssiellq hslpkinrsa sepslhraah tedinactlt tsprlpvf //
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