FNTB_HUMAN
ID FNTB_HUMAN Reviewed; 437 AA.
AC P49356; B2RDX6; B4E1A0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 205.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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., Allen C.M.,
RA Gibbs J.B., Kohl N.E.;
RT "Characterization of recombinant human farnesyl-protein transferase:
RT cloning, expression, farnesyl diphosphate binding, and functional homology
RT with yeast prenyl-protein transferases.";
RL Biochemistry 32:5167-5176(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 51-437 (ISOFORM 1/2).
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 and
RT chromosomal mapping of FNTA and FNTB loci and related sequences.";
RL Genomics 18:105-112(1993).
RN [7]
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
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., Buerckstuemmer T.,
RA 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 [9]
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 the
RT basis for inhibition by CaaX tetrapeptides and their mimetics.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12948-12953(2001).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA;
RP FARNESYL DIPHOSPHATE AND INHIBITORS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY,
RP 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., Hamilton K.A.,
RA Hartman G.D., Heimbrook D.C., Homnick C.F., Huber H.E., Huff J.R.,
RA Kassahun K., Koblan K.S., Kohl N.E., Lobell R.B., Lynch J.J. Jr.,
RA Robinson R., Rodrigues A.D., Taylor J.S., Walsh E.S., Williams T.M.,
RA Zartman C.B.;
RT "3-aminopyrrolidinone farnesyltransferase inhibitors: design of macrocyclic
RT compounds with improved pharmacokinetics and excellent cell potency.";
RL J. Med. Chem. 45:2388-2409(2002).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA;
RP FARNESYL DIPHOSPHATE AND INHIBITOR, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY,
RP 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., Kohl N.E.,
RA Lobell R.B., Robinson R.G., Tsou N.N., Walsh E.S., Graham S.L., Beese L.S.,
RA Taylor J.S.;
RT "Dual protein farnesyltransferase-geranylgeranyltransferase-I inhibitors as
RT potential cancer chemotherapeutic agents.";
RL J. Med. Chem. 46:2973-2984(2003).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA AND
RP 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 [13]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA AND
RP FARNESYL DIPHOSPHATE ANALOG, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT,
RP 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 [14]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND FNTA,
RP 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 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 diphosphate
CC to a cysteine at the fourth position from the C-terminus of several
CC proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X.
CC {ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937,
CC ECO:0000269|PubMed:16893176, ECO:0000269|PubMed:19246009,
CC ECO:0000269|PubMed:8494894}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] =
CC diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:13345, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11535,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:86019,
CC ChEBI:CHEBI:175763; EC=2.5.1.58;
CC Evidence={ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937,
CC ECO:0000269|PubMed:16893176, ECO:0000269|PubMed:19246009,
CC ECO:0000269|PubMed:8494894};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:11687658, ECO:0000269|PubMed:12036349,
CC ECO:0000269|PubMed:12825937, ECO:0000269|PubMed:15451670,
CC ECO:0000269|PubMed:16893176, ECO:0000269|PubMed:19246009};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:11687658,
CC ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937,
CC ECO:0000269|PubMed:15451670, ECO:0000269|PubMed:16893176,
CC ECO:0000269|PubMed:19246009};
CC -!- SUBUNIT: Heterodimer of FNTA and FNTB. {ECO:0000269|PubMed:11687658,
CC ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937,
CC ECO:0000269|PubMed:15451670, ECO:0000269|PubMed:16893176,
CC ECO:0000269|PubMed:19246009, ECO:0000269|PubMed:8494894}.
CC -!- INTERACTION:
CC P49356; P21549: AGXT; NbExp=3; IntAct=EBI-602349, EBI-727098;
CC P49356; Q9BWW8: APOL6; NbExp=3; IntAct=EBI-602349, EBI-11574440;
CC P49356; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-602349, EBI-1166928;
CC P49356; Q8N4L8: CCDC24; NbExp=3; IntAct=EBI-602349, EBI-1104933;
CC P49356; G5E9A7: DMWD; NbExp=3; IntAct=EBI-602349, EBI-10976677;
CC P49356; P49354: FNTA; NbExp=13; IntAct=EBI-602349, EBI-602336;
CC P49356; P31273: HOXC8; NbExp=3; IntAct=EBI-602349, EBI-1752118;
CC P49356; A5PL33-2: KRBA1; NbExp=3; IntAct=EBI-602349, EBI-14148872;
CC P49356; Q9H0W8: SMG9; NbExp=3; IntAct=EBI-602349, EBI-2872322;
CC P49356; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-602349, EBI-5235340;
CC P49356; O43711: TLX3; NbExp=3; IntAct=EBI-602349, EBI-3939165;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P49356-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49356-2; Sequence=VSP_054657;
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC family. {ECO:0000305}.
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DR EMBL; L00635; AAA35854.1; -; mRNA.
DR EMBL; AK303739; BAG64712.1; -; mRNA.
DR EMBL; AK315714; BAG38073.1; -; mRNA.
DR EMBL; AL135745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW80897.1; -; Genomic_DNA.
DR EMBL; BC020232; AAH20232.1; -; mRNA.
DR EMBL; L10414; AAA86286.1; -; mRNA.
DR CCDS; CCDS9769.1; -. [P49356-1]
DR PIR; B49274; B49274.
DR RefSeq; NP_001189487.1; NM_001202558.1. [P49356-2]
DR RefSeq; NP_002019.1; NM_002028.3. [P49356-1]
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 AlphaFoldDB; P49356; -.
DR SMR; P49356; -.
DR BioGRID; 108627; 92.
DR BioGRID; 1529403; 2.
DR ComplexPortal; CPX-2165; Protein farnesyltransferase complex.
DR CORUM; P49356; -.
DR IntAct; P49356; 55.
DR MINT; P49356; -.
DR STRING; 9606.ENSP00000246166; -.
DR BindingDB; P49356; -.
DR ChEMBL; CHEMBL272; -.
DR DrugBank; DB07216; (11S)-8-CHLORO-11-[1-(METHYLSULFONYL)PIPERIDIN-4-YL]-6-PIPERAZIN-1-YL-11H-BENZO[5,6]CYCLOHEPTA[1,2-B]PYRIDINE.
DR DrugBank; DB08674; (20S)-19,20,21,22-TETRAHYDRO-19-OXO-5H-18,20-ETHANO-12,14-ETHENO-6,10-METHENO-18H-BENZ[D]IMIDAZO[4,3-K][1,6,9,12]OXATRIAZA-CYCLOOCTADECOSINE-9-CARBONITRILE.
DR DrugBank; DB08676; (20S)-19,20,22,23-TETRAHYDRO-19-OXO-5H,21H-18,20-ETHANO-12,14-ETHENO-6,10-METHENOBENZ[D]IMIDAZO[4,3-L][1,6,9,13]OXATRIAZACYCLONOADECOSINE-9-CARBONITRILE.
DR DrugBank; DB06953; 2-CHLORO-5-(3-CHLORO-PHENYL)-6-[(4-CYANO-PHENYL)-(3-METHYL-3H-IMIDAZOL-4-YL)- METHOXYMETHYL]-NICOTINONITRILE.
DR DrugBank; DB07771; [(3,7,11-TRIMETHYL-DODECA-2,6,10-TRIENYLOXYCARBAMOYL)-METHYL]-PHOSPHONIC ACID.
DR DrugBank; DB07895; ALPHA-HYDROXYFARNESYLPHOSPHONIC ACID.
DR DrugBank; DB04893; AZD3409.
DR DrugBank; DB07780; Farnesyl diphosphate.
DR DrugBank; DB07841; Geranylgeranyl diphosphate.
DR DrugBank; DB07227; L-778123.
DR DrugBank; DB06448; Lonafarnib.
DR DrugBank; DB04960; Tipifarnib.
DR DrugCentral; P49356; -.
DR GuidetoPHARMACOLOGY; 2826; -.
DR iPTMnet; P49356; -.
DR PhosphoSitePlus; P49356; -.
DR BioMuta; FNTB; -.
DR DMDM; 1346696; -.
DR EPD; P49356; -.
DR jPOST; P49356; -.
DR MassIVE; P49356; -.
DR MaxQB; P49356; -.
DR PaxDb; P49356; -.
DR PeptideAtlas; P49356; -.
DR PRIDE; P49356; -.
DR ProteomicsDB; 55995; -. [P49356-1]
DR ProteomicsDB; 5739; -.
DR Antibodypedia; 54004; 280 antibodies from 33 providers.
DR DNASU; 2342; -.
DR Ensembl; ENST00000246166.3; ENSP00000246166.2; ENSG00000257365.8. [P49356-1]
DR GeneID; 100529261; -.
DR GeneID; 2342; -.
DR KEGG; hsa:100529261; -.
DR KEGG; hsa:2342; -.
DR MANE-Select; ENST00000246166.3; ENSP00000246166.2; NM_002028.4; NP_002019.1.
DR UCSC; uc001xia.4; human. [P49356-1]
DR CTD; 100529261; -.
DR CTD; 2342; -.
DR DisGeNET; 100529261; -.
DR DisGeNET; 2342; -.
DR GeneCards; FNTB; -.
DR HGNC; HGNC:3785; FNTB.
DR HPA; ENSG00000257365; Tissue enhanced (brain).
DR MIM; 134636; gene.
DR neXtProt; NX_P49356; -.
DR OpenTargets; ENSG00000257365; -.
DR PharmGKB; PA28202; -.
DR VEuPathDB; HostDB:ENSG00000257365; -.
DR eggNOG; KOG0365; Eukaryota.
DR GeneTree; ENSGT00950000183128; -.
DR HOGENOM; CLU_028946_0_1_1; -.
DR InParanoid; P49356; -.
DR OMA; GADYYHT; -.
DR OrthoDB; 1042804at2759; -.
DR PhylomeDB; P49356; -.
DR TreeFam; TF353162; -.
DR BRENDA; 2.5.1.58; 2681.
DR BRENDA; 2.5.1.59; 2681.
DR PathwayCommons; P49356; -.
DR Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-HSA-9648002; RAS processing.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR SignaLink; P49356; -.
DR SIGNOR; P49356; -.
DR BioGRID-ORCS; 100529261; 13 hits in 136 CRISPR screens.
DR BioGRID-ORCS; 2342; 621 hits in 1068 CRISPR screens.
DR EvolutionaryTrace; P49356; -.
DR GeneWiki; FNTB; -.
DR Pharos; P49356; Tclin.
DR PRO; PR:P49356; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P49356; protein.
DR Bgee; ENSG00000257365; Expressed in C1 segment of cervical spinal cord and 96 other tissues.
DR ExpressionAtlas; P49356; baseline and differential.
DR Genevisible; P49356; HS.
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:0004660; F:protein farnesyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0018343; P:protein farnesylation; IDA:UniProtKB.
DR GO; GO:0018342; P:protein prenylation; IBA:GO_Central.
DR CDD; cd02893; FTase; 1.
DR InterPro; IPR026872; FTB.
DR InterPro; IPR001330; PFTB_repeat.
DR InterPro; IPR045089; PGGT1B-like.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11774; PTHR11774; 1.
DR PANTHER; PTHR11774:SF6; PTHR11774:SF6; 1.
DR Pfam; PF00432; Prenyltrans; 5.
DR SUPFAM; SSF48239; SSF48239; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Lipid metabolism; Metal-binding;
KW Phosphoprotein; Prenyltransferase; Reference proteome; Repeat; Transferase;
KW Zinc.
FT CHAIN 1..437
FT /note="Protein farnesyltransferase subunit beta"
FT /id="PRO_0000119761"
FT REPEAT 123..164
FT /note="PFTB 1"
FT REPEAT 174..215
FT /note="PFTB 2"
FT REPEAT 222..263
FT /note="PFTB 3"
FT REPEAT 270..312
FT /note="PFTB 4"
FT REPEAT 332..374
FT /note="PFTB 5"
FT BINDING 248..251
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000269|PubMed:11687658,
FT ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937,
FT ECO:0000269|PubMed:15451670, ECO:0000269|PubMed:16893176"
FT BINDING 291..294
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000269|PubMed:11687658,
FT ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937,
FT ECO:0000269|PubMed:15451670, ECO:0000269|PubMed:16893176"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11687658,
FT ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937,
FT ECO:0000269|PubMed:15451670, ECO:0000269|PubMed:16893176,
FT ECO:0000269|PubMed:19246009"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11687658,
FT ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937,
FT ECO:0000269|PubMed:15451670, ECO:0000269|PubMed:16893176,
FT ECO:0000269|PubMed:19246009"
FT BINDING 300..303
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000269|PubMed:11687658,
FT ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937,
FT ECO:0000269|PubMed:15451670, ECO:0000269|PubMed:16893176"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11687658,
FT ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937,
FT ECO:0000269|PubMed:15451670, ECO:0000269|PubMed:16893176,
FT ECO:0000269|PubMed:19246009"
FT SITE 102
FT /note="Important for selectivity against geranylgeranyl
FT diphosphate"
FT /evidence="ECO:0000269|PubMed:16893176"
FT MOD_RES 436
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2I1"
FT VAR_SEQ 1..48
FT /note="MASPSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQ ->
FT MI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054657"
FT MUTAGEN 102
FT /note="W->T: Removes the steric hindrance that normally
FT precludes geranylgeranyl diphosphate binding. Reduces
FT farnesyltransferase activity and confers
FT geranylgeranyltransferase activity."
FT /evidence="ECO:0000269|PubMed:16893176"
FT MUTAGEN 200
FT /note="D->N: Reduced catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:8494894"
FT MUTAGEN 249
FT /note="G->V: Reduced catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:8494894"
FT MUTAGEN 349
FT /note="G->S: Reduced catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:8494894"
FT CONFLICT 283
FT /note="R -> L (in Ref. 6; AAA86286)"
FT /evidence="ECO:0000305"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:2H6F"
FT HELIX 28..33
FT /evidence="ECO:0007829|PDB:2H6F"
FT HELIX 43..60
FT /evidence="ECO:0007829|PDB:2H6F"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:2H6F"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2IEJ"
FT HELIX 91..96
FT /evidence="ECO:0007829|PDB:2H6F"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:2H6F"
FT HELIX 120..133
FT /evidence="ECO:0007829|PDB:2H6F"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:2H6F"
FT HELIX 150..163
FT /evidence="ECO:0007829|PDB:2H6F"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:2H6F"
FT HELIX 174..182
FT /evidence="ECO:0007829|PDB:2H6F"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:2H6F"
FT HELIX 201..213
FT /evidence="ECO:0007829|PDB:2H6F"
FT TURN 219..224
FT /evidence="ECO:0007829|PDB:2H6F"
FT HELIX 225..232
FT /evidence="ECO:0007829|PDB:2H6F"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:2H6F"
FT HELIX 249..262
FT /evidence="ECO:0007829|PDB:2H6F"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:2H6F"
FT HELIX 270..279
FT /evidence="ECO:0007829|PDB:2H6F"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:2H6F"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:2H6F"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:2H6F"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:2H6F"
FT HELIX 307..317
FT /evidence="ECO:0007829|PDB:2H6F"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:2F0Y"
FT HELIX 332..342
FT /evidence="ECO:0007829|PDB:2H6F"
FT HELIX 360..374
FT /evidence="ECO:0007829|PDB:2H6F"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:2H6F"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:2H6F"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:2H6F"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:2H6F"
FT HELIX 405..416
FT /evidence="ECO:0007829|PDB:2H6F"
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
