ID FNTB_HUMAN Reviewed; 437 AA. AC P49356; B2RDX6; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 19-FEB-2014, entry version 139. DE RecName: Full=Protein farnesyltransferase subunit beta; DE Short=FTase-beta; DE EC=2.5.1.58; DE AltName: Full=CAAX farnesyltransferase subunit beta; DE AltName: Full=Ras proteins prenyltransferase subunit beta; GN Name=FNTB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF ASP-200; GLY-249 AND RP GLY-349, CATALYTIC ACTIVITY, FUNCTION, AND SUBUNIT. RC TISSUE=Placenta; RX PubMed=8494894; DOI=10.1021/bi00070a028; RA Omer C.A., Kral A.M., Diehl R.E., Prendergast G.C., Powers S., RA Allen C.M., Gibbs J.B., Kohl N.E.; RT "Characterization of recombinant human farnesyl-protein transferase: RT cloning, expression, farnesyl diphosphate binding, and functional RT homology with yeast prenyl-protein transferases."; RL Biochemistry 32:5167-5176(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 51-437. RC TISSUE=Retina; RX PubMed=8276393; DOI=10.1006/geno.1993.1432; RA Andres D.A., Milatovich A., Ozcelik T., Wenzlau J.M., Brown M.S., RA Goldstein J.L., Francke U.; RT "cDNA cloning of the two subunits of human CAAX farnesyltransferase RT and chromosomal mapping of FNTA and FNTB loci and related sequences."; RL Genomics 18:105-112(1993). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA; RP FARNESYL DIPHOSPHATE AND INHIBITOR L-739,750, SUBUNIT, AND COFACTOR. RX PubMed=11687658; DOI=10.1073/pnas.241407898; RA Long S.B., Hancock P.J., Kral A.M., Hellinga H.W., Beese L.S.; RT "The crystal structure of human protein farnesyltransferase reveals RT the basis for inhibition by CaaX tetrapeptides and their mimetics."; RL Proc. Natl. Acad. Sci. U.S.A. 98:12948-12953(2001). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA; RP FARNESYL DIPHOSPHATE AND INHIBITORS, SUBUNIT, COFACTOR, CATALYTIC RP ACTIVITY, AND FUNCTION. RX PubMed=12036349; DOI=10.1021/jm010531d; RA Bell I.M., Gallicchio S.N., Abrams M., Beese L.S., Beshore D.C., RA Bhimnathwala H., Bogusky M.J., Buser C.A., Culberson J.C., Davide J., RA Ellis-Hutchings M., Fernandes C., Gibbs J.B., Graham S.L., RA Hamilton K.A., Hartman G.D., Heimbrook D.C., Homnick C.F., Huber H.E., RA Huff J.R., Kassahun K., Koblan K.S., Kohl N.E., Lobell R.B., RA Lynch J.J. Jr., Robinson R., Rodrigues A.D., Taylor J.S., Walsh E.S., RA Williams T.M., Zartman C.B.; RT "3-aminopyrrolidinone farnesyltransferase inhibitors: design of RT macrocyclic compounds with improved pharmacokinetics and excellent RT cell potency."; RL J. Med. Chem. 45:2388-2409(2002). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA; RP FARNESYL DIPHOSPHATE AND INHIBITOR, SUBUNIT, COFACTOR, CATALYTIC RP ACTIVITY, AND FUNCTION. RX PubMed=12825937; DOI=10.1021/jm020587n; RA deSolms S.J., Ciccarone T.M., MacTough S.C., Shaw A.W., Buser C.A., RA Ellis-Hutchings M., Fernandes C., Hamilton K.A., Huber H.E., RA Kohl N.E., Lobell R.B., Robinson R.G., Tsou N.N., Walsh E.S., RA Graham S.L., Beese L.S., Taylor J.S.; RT "Dual protein farnesyltransferase-geranylgeranyltransferase-I RT inhibitors as potential cancer chemotherapeutic agents."; RL J. Med. Chem. 46:2973-2984(2003). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA RP AND FARNESYL DIPHOSPHATE ANALOG, COFACTOR, AND SUBUNIT. RX PubMed=15451670; DOI=10.1016/j.jmb.2004.08.056; RA Reid T.S., Terry K.L., Casey P.J., Beese L.S.; RT "Crystallographic analysis of CaaX prenyltransferases complexed with RT substrates defines rules of protein substrate selectivity."; RL J. Mol. Biol. 343:417-433(2004). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA RP AND FARNESYL DIPHOSPHATE ANALOG, CATALYTIC ACTIVITY, COFACTOR, RP SUBUNIT, FUNCTION, AND MUTAGENESIS OF TRP-102. RX PubMed=16893176; DOI=10.1021/bi060295e; RA Terry K.L., Casey P.J., Beese L.S.; RT "Conversion of protein farnesyltransferase to a RT geranylgeranyltransferase."; RL Biochemistry 45:9746-9755(2006). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND RP FNTA, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, AND SUBUNIT. RX PubMed=19246009; DOI=10.1016/j.chembiol.2009.01.014; RA Hast M.A., Fletcher S., Cummings C.G., Pusateri E.E., Blaskovich M.A., RA Rivas K., Gelb M.H., Van Voorhis W.C., Sebti S.M., Hamilton A.D., RA Beese L.S.; RT "Structural basis for binding and selectivity of antimalarial and RT anticancer ethylenediamine inhibitors to protein RT farnesyltransferase."; RL Chem. Biol. 16:181-192(2009). CC -!- FUNCTION: Essential subunit of the farnesyltransferase complex. CC Catalyzes the transfer of a farnesyl moiety from farnesyl CC diphosphate to a cysteine at the fourth position from the C- CC terminus of several proteins having the C-terminal sequence Cys- CC aliphatic-aliphatic-X. CC -!- CATALYTIC ACTIVITY: Farnesyl diphosphate + protein-cysteine = S- CC farnesyl protein + diphosphate. CC -!- COFACTOR: Binds 1 zinc ion per subunit. CC -!- SUBUNIT: Heterodimer of FNTA and FNTB. CC -!- INTERACTION: CC P49354:FNTA; NbExp=7; IntAct=EBI-602349, EBI-602336; CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta CC family. CC -!- SIMILARITY: Contains 5 PFTB repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L00635; AAA35854.1; -; mRNA. DR EMBL; AK315714; BAG38073.1; -; mRNA. DR EMBL; CH471061; EAW80897.1; -; Genomic_DNA. DR EMBL; BC020232; AAH20232.1; -; mRNA. DR EMBL; L10414; AAA86286.1; -; mRNA. DR PIR; B49274; B49274. DR RefSeq; NP_002019.1; NM_002028.3. DR UniGene; Hs.325531; -. DR PDB; 1JCQ; X-ray; 2.30 A; B=1-437. DR PDB; 1LD7; X-ray; 2.00 A; B=1-437. DR PDB; 1LD8; X-ray; 1.80 A; B=1-437. DR PDB; 1MZC; X-ray; 2.00 A; B=1-437. DR PDB; 1S63; X-ray; 1.90 A; B=1-437. DR PDB; 1SA4; X-ray; 2.10 A; B=1-437. DR PDB; 1TN6; X-ray; 1.80 A; B=1-437. DR PDB; 2F0Y; X-ray; 2.70 A; B=1-437. DR PDB; 2H6F; X-ray; 1.50 A; B=1-437. DR PDB; 2H6G; X-ray; 1.85 A; B=1-437. DR PDB; 2H6H; X-ray; 1.80 A; B=1-437. DR PDB; 2H6I; X-ray; 3.00 A; B=1-437. DR PDB; 2IEJ; X-ray; 1.80 A; B=1-437. DR PDB; 3E37; X-ray; 1.80 A; B=1-437. DR PDBsum; 1JCQ; -. DR PDBsum; 1LD7; -. DR PDBsum; 1LD8; -. DR PDBsum; 1MZC; -. DR PDBsum; 1S63; -. DR PDBsum; 1SA4; -. DR PDBsum; 1TN6; -. DR PDBsum; 2F0Y; -. DR PDBsum; 2H6F; -. DR PDBsum; 2H6G; -. DR PDBsum; 2H6H; -. DR PDBsum; 2H6I; -. DR PDBsum; 2IEJ; -. DR PDBsum; 3E37; -. DR ProteinModelPortal; P49356; -. DR SMR; P49356; 15-424. DR BioGrid; 108627; 4. DR IntAct; P49356; 2. DR MINT; MINT-238879; -. DR STRING; 9606.ENSP00000246166; -. DR BindingDB; P49356; -. DR ChEMBL; CHEMBL2096991; -. DR PhosphoSite; P49356; -. DR DMDM; 1346696; -. DR PeptideAtlas; P49356; -. DR PRIDE; P49356; -. DR DNASU; 2342; -. DR Ensembl; ENST00000246166; ENSP00000246166; ENSG00000257365. DR GeneID; 2342; -. DR KEGG; hsa:2342; -. DR UCSC; uc001xia.3; human. DR CTD; 2342; -. DR GeneCards; GC14P065454; -. DR HGNC; HGNC:3785; FNTB. DR MIM; 134636; gene. DR neXtProt; NX_P49356; -. DR PharmGKB; PA28202; -. DR HOVERGEN; HBG008173; -. DR InParanoid; P49356; -. DR KO; K05954; -. DR OMA; RGAYCAI; -. DR OrthoDB; EOG7P02HV; -. DR PhylomeDB; P49356; -. DR TreeFam; TF353162; -. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_116125; Disease. DR EvolutionaryTrace; P49356; -. DR GeneWiki; FNTB; -. DR GenomeRNAi; 2342; -. DR NextBio; 9505; -. DR PRO; PR:P49356; -. DR ArrayExpress; P49356; -. DR Bgee; P49356; -. DR CleanEx; HS_FNTB; -. DR Genevestigator; P49356; -. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005875; C:microtubule associated complex; IDA:BHF-UCL. DR GO; GO:0005965; C:protein farnesyltransferase complex; IDA:UniProtKB. DR GO; GO:0004311; F:farnesyltranstransferase activity; IEA:Ensembl. DR GO; GO:0004660; F:protein farnesyltransferase activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl. DR GO; GO:0045787; P:positive regulation of cell cycle; IEA:Ensembl. DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl. DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IEA:Ensembl. DR GO; GO:0018343; P:protein farnesylation; IDA:UniProtKB. DR GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; TAS:Reactome. DR GO; GO:0034097; P:response to cytokine; IEA:Ensembl. DR GO; GO:0010035; P:response to inorganic substance; IEA:Ensembl. DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl. DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; TAS:Reactome. DR GO; GO:0042060; P:wound healing; IEA:Ensembl. DR InterPro; IPR026872; FTB. DR InterPro; IPR001330; Prenyltrans. DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase. DR PANTHER; PTHR11774:SF6; PTHR11774:SF6; 1. DR Pfam; PF00432; Prenyltrans; 2. DR SUPFAM; SSF48239; SSF48239; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Metal-binding; Prenyltransferase; KW Reference proteome; Repeat; Transferase; Zinc. FT CHAIN 1 437 Protein farnesyltransferase subunit beta. FT /FTId=PRO_0000119761. FT REPEAT 123 164 PFTB 1. FT REPEAT 174 215 PFTB 2. FT REPEAT 222 263 PFTB 3. FT REPEAT 270 312 PFTB 4. FT REPEAT 332 374 PFTB 5. FT REGION 248 251 Farnesyl diphosphate binding. FT REGION 291 294 Farnesyl diphosphate binding. FT REGION 300 303 Farnesyl diphosphate binding. FT METAL 297 297 Zinc; catalytic. FT METAL 299 299 Zinc; catalytic. FT METAL 362 362 Zinc; via tele nitrogen; catalytic. FT SITE 102 102 Important for selectivity against FT geranylgeranyl diphosphate. FT MUTAGEN 102 102 W->T: Removes the steric hindrance that FT normally precludes geranylgeranyl FT diphosphate binding. Reduces FT farnesyltransferase activity and confers FT geranylgeranyltransferase activity. FT MUTAGEN 200 200 D->N: Reduced catalytic efficiency. FT MUTAGEN 249 249 G->V: Reduced catalytic efficiency. FT MUTAGEN 349 349 G->S: Reduced catalytic efficiency. FT CONFLICT 283 283 R -> L (in Ref. 5; AAA86286). FT HELIX 24 26 FT HELIX 28 33 FT HELIX 43 60 FT HELIX 75 85 FT STRAND 87 89 FT HELIX 91 96 FT HELIX 100 113 FT HELIX 120 133 FT STRAND 138 143 FT HELIX 150 163 FT HELIX 166 169 FT HELIX 174 182 FT STRAND 191 194 FT HELIX 201 213 FT TURN 219 224 FT HELIX 225 232 FT STRAND 237 239 FT HELIX 249 262 FT HELIX 265 267 FT HELIX 270 279 FT TURN 283 285 FT STRAND 287 291 FT HELIX 300 303 FT TURN 304 306 FT HELIX 307 317 FT STRAND 325 327 FT HELIX 332 342 FT HELIX 360 374 FT STRAND 375 378 FT STRAND 381 384 FT HELIX 390 392 FT TURN 399 401 FT HELIX 405 416 SQ SEQUENCE 437 AA; 48774 MW; 8E8E571846146709 CRC64; MASPSSFTYY CPPSSSPVWS EPLYSLRPEH ARERLQDDSV ETVTSIEQAK VEEKIQEVFS SYKFNHLVPR LVLQREKHFH YLKRGLRQLT DAYECLDASR PWLCYWILHS LELLDEPIPQ IVATDVCQFL ELCQSPEGGF GGGPGQYPHL APTYAAVNAL CIIGTEEAYD IINREKLLQY LYSLKQPDGS FLMHVGGEVD VRSAYCAASV ASLTNIITPD LFEGTAEWIA RCQNWEGGIG GVPGMEAHGG YTFCGLAALV ILKRERSLNL KSLLQWVTSR QMRFEGGFQG RCNKLVDGCY SFWQAGLLPL LHRALHAQGD PALSMSHWMF HQQALQEYIL MCCQCPAGGL LDKPGKSRDF YHTCYCLSGL SIAQHFGSGA MLHDVVLGVP ENALQPTHPV YNIGPDKVIQ ATTYFLQKPV PGFEELKDET SAEPATD //