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Immunogen sequence: MASPSSFTY YCPPSSSPVW SEPLYSLRPE HARERLQDDS VETVTSIEQA KVEEKIQEVF SSYKFNHLVP RLVLQREKHF HYLKRGLRQL TDAYECLDAS RPWLCYWILH SLELLDEPIP QIVATDVCQF LELCQSPEGG FGGGPGQYPH LAPTYAAVNA LCIIGTEEAY DIINREKLLQ YLYSLKQPDG SFLMHVGGEV DVRSAYCAAS VASLTNIITP DLFEGTAEWI ARCQNWEGGI GGVPGMEAHG GYTFCGLAAL VILKRERSLN LKSLLQWVTS RQMRFEGGFQ GRCNKLVDGC YSFWQAGLLP LLHRALHAQG DPALSMSHWM FHQQALQEYI LMCCQCPAGG LLDKPGK (1-356 aa encoded by BC020232)
Eukaryotic cells contain 3 different types of prenyltransferases that attach either a farnesyl group (15 carbons) or a geranylgeranyl group (20 carbons) in thioether linkage to C-terminal cysteine residues in a variety of proteins. These posttranslational modifications provide a mechanism for membrane localization of proteins that lack a transmembrane domain. CAAX farnesyltransferase (FTase) attaches a farnesyl group from farnesyl pyrophosphate to cysteine residues at the fourth position from the C terminus of proteins that end in the CAAX box, where C is cysteine, A is usually but not always an aliphatic amino acid, and X is typically methionine or serine. This enzyme has the ability to farnesylate peptides as short as 4 residues in length that conform to the CAAX consensus sequence. The gene for the beta subunit of CAAX farnesyltransferase (FNTB) has been pinpointed to 14q23-q24 by Southern blot hybridization and PCR analyses of panels of human/Chinese hamster somatic cell hybrid lines and by fluorescence chromosomal in situ hybridization.
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Protein Aliases: CAAX farnesyltransferase subunit beta; EC 2.5.1.58; ft beta; FTase beta; FTase-beta; Protein farnesyltransferase subunit beta; Ras proteins prenyltransferase subunit beta
Gene Aliases: 2010013E13Rik; AA409500; FNTB; FPTB
UniProt ID: (Human) P49356, (Mouse) Q8K2I1
Entrez Gene ID: (Human) 2342, (Mouse) 110606
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