ID FNTA_HUMAN Reviewed; 379 AA. AC P49354; A6NJW0; Q53XJ9; Q9UDC1; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 27-MAR-2024, entry version 218. DE RecName: Full=Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha; DE EC=2.5.1.58 {ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937, ECO:0000269|PubMed:16893176, ECO:0000269|PubMed:19246009, ECO:0000269|PubMed:8419339, ECO:0000269|PubMed:8494894}; DE EC=2.5.1.59 {ECO:0000269|PubMed:16893176}; DE AltName: Full=CAAX farnesyltransferase subunit alpha; DE AltName: Full=FTase-alpha; DE AltName: Full=Ras proteins prenyltransferase subunit alpha; DE AltName: Full=Type I protein geranyl-geranyltransferase subunit alpha; DE Short=GGTase-I-alpha; GN Name=FNTA; 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). 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF LYS-164, FUNCTION, RP CATALYTIC ACTIVITY, AND SUBUNIT. RX PubMed=8419339; DOI=10.1016/s0021-9258(18)54087-4; RA Andres D.A., Goldstein J.L., Ho Y.K., Brown M.S.; RT "Mutational analysis of alpha-subunit of protein farnesyltransferase. RT Evidence for a catalytic role."; RL J. Biol. Chem. 268:1383-1390(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF ASN-199, CATALYTIC RP ACTIVITY, AND FUNCTION. 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Synovium; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon, and Lung; 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-261 (ISOFORM 2). RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] 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 [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH FNTB, AND SUBUNIT. 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 [16] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FNTB, SUBUNIT, RP FUNCTION, AND CATALYTIC ACTIVITY. 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 [17] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FNTB, SUBUNIT, RP FUNCTION, AND CATALYTIC ACTIVITY. 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 [18] RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FNTB, AND SUBUNIT. RX PubMed=15170324; DOI=10.1021/bi049723b; RA Reid T.S., Beese L.S.; RT "Crystal structures of the anticancer clinical candidates R115777 RT (Tipifarnib) and BMS-214662 complexed with protein farnesyltransferase RT suggest a mechanism of FTI selectivity."; RL Biochemistry 43:6877-6884(2004). RN [19] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH FNTB, 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 [20] RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH FNTB, FUNCTION, RP SUBUNIT, AND CATALYTIC ACTIVITY. 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 [21] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-379 IN COMPLEX WITH FNTB, RP SUBUNIT, FUNCTION, AND CATALYTIC ACTIVITY. 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 both the farnesyltransferase and the CC geranylgeranyltransferase complex. Contributes to the transfer of a CC farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl CC diphosphate to a cysteine at the fourth position from the C-terminus of CC several proteins having the C-terminal sequence Cys-aliphatic- CC aliphatic-X. May positively regulate neuromuscular junction development CC downstream of MUSK via its function in RAC1 prenylation and activation. CC {ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937, CC ECO:0000269|PubMed:16893176, ECO:0000269|PubMed:19246009, CC ECO:0000269|PubMed:8419339, 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:8419339, ECO:0000269|PubMed:8494894}; CC -!- CATALYTIC ACTIVITY: CC Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] = CC diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]; CC Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537, CC ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533, CC ChEBI:CHEBI:86021; EC=2.5.1.59; CC Evidence={ECO:0000269|PubMed:16893176}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P29703}; CC -!- ACTIVITY REGULATION: Activated by the AGRIN-induced phosphorylation CC which is mediated by MUSK. {ECO:0000250|UniProtKB:Q61239}. CC -!- SUBUNIT: Heterodimer of FNTA and FNTB (farnesyltransferase) CC (PubMed:8419339, PubMed:11687658, PubMed:12036349, PubMed:12825937, CC PubMed:15170324, PubMed:15451670, PubMed:16893176, PubMed:19246009). CC Heterodimer of FNTA and PGGT1B (geranylgeranyltransferase) (By CC similarity). {ECO:0000250|UniProtKB:Q04631, CC ECO:0000269|PubMed:11687658, ECO:0000269|PubMed:12036349, CC ECO:0000269|PubMed:12825937, ECO:0000269|PubMed:15170324, CC ECO:0000269|PubMed:15451670, ECO:0000269|PubMed:16893176, CC ECO:0000269|PubMed:19246009, ECO:0000269|PubMed:8419339}. CC -!- INTERACTION: CC P49354; O00189: AP4M1; NbExp=3; IntAct=EBI-602336, EBI-3914106; CC P49354; P49356: FNTB; NbExp=13; IntAct=EBI-602336, EBI-602349; CC P49354; P53609: PGGT1B; NbExp=8; IntAct=EBI-602336, EBI-8456634; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P49354-1; Sequence=Displayed; CC Name=2; CC IsoId=P49354-2; Sequence=VSP_036468; CC -!- PTM: Phosphorylated. Phosphorylation is mediated by MUSK upon AGRIN CC stimulation and results in the activation of FNTA (By similarity). CC {ECO:0000250|UniProtKB:Q61239}. CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L10413; AAA86285.1; -; mRNA. DR EMBL; L00634; AAA35853.1; -; mRNA. DR EMBL; AC110275; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BT009854; AAP88856.1; -; mRNA. DR EMBL; AK292121; BAF84810.1; -; mRNA. DR EMBL; AC113191; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC017029; AAH17029.2; -; mRNA. DR EMBL; BC084566; AAH84566.1; -; mRNA. DR EMBL; AL698961; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS6140.1; -. [P49354-1] DR PIR; A47659; A47659. DR RefSeq; NP_002018.1; NM_002027.2. [P49354-1] DR PDB; 1JCQ; X-ray; 2.30 A; A=1-379. DR PDB; 1LD7; X-ray; 2.00 A; A=1-379. DR PDB; 1LD8; X-ray; 1.80 A; A=1-379. DR PDB; 1MZC; X-ray; 2.00 A; A=1-379. DR PDB; 1S63; X-ray; 1.90 A; A=1-379. DR PDB; 1SA4; X-ray; 2.10 A; A=1-379. DR PDB; 1TN6; X-ray; 1.80 A; A=1-379. DR PDB; 2F0Y; X-ray; 2.70 A; A=1-379. DR PDB; 2H6F; X-ray; 1.50 A; A=1-379. DR PDB; 2H6G; X-ray; 1.85 A; A=1-379. DR PDB; 2H6H; X-ray; 1.80 A; A=1-379. DR PDB; 2H6I; X-ray; 3.00 A; A=1-379. DR PDB; 2IEJ; X-ray; 1.80 A; A=1-379. DR PDB; 3E37; X-ray; 1.80 A; A=1-379. 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; P49354; -. DR SMR; P49354; -. DR BioGRID; 108625; 100. DR ComplexPortal; CPX-2157; Protein geranylgeranyl transferase type I complex. DR ComplexPortal; CPX-2165; Protein farnesyltransferase complex. DR CORUM; P49354; -. DR IntAct; P49354; 40. DR MINT; P49354; -. DR STRING; 9606.ENSP00000303423; -. DR BindingDB; P49354; -. DR ChEMBL; CHEMBL271; -. 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; DB08180; 2-[METHYL-(5-GERANYL-4-METHYL-PENT-3-ENYL)-AMINO]-ETHYL-DIPHOSPHATE. 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 DrugCentral; P49354; -. DR iPTMnet; P49354; -. DR MetOSite; P49354; -. DR PhosphoSitePlus; P49354; -. DR SwissPalm; P49354; -. DR BioMuta; FNTA; -. DR DMDM; 1346694; -. DR EPD; P49354; -. DR jPOST; P49354; -. DR MassIVE; P49354; -. DR MaxQB; P49354; -. DR PaxDb; 9606-ENSP00000303423; -. DR PeptideAtlas; P49354; -. DR ProteomicsDB; 55993; -. [P49354-1] DR ProteomicsDB; 55994; -. [P49354-2] DR Pumba; P49354; -. DR Antibodypedia; 1067; 336 antibodies from 33 providers. DR DNASU; 2339; -. DR Ensembl; ENST00000302279.8; ENSP00000303423.3; ENSG00000168522.13. [P49354-1] DR GeneID; 2339; -. DR KEGG; hsa:2339; -. DR MANE-Select; ENST00000302279.8; ENSP00000303423.3; NM_002027.3; NP_002018.1. DR UCSC; uc003xps.5; human. [P49354-1] DR AGR; HGNC:3782; -. DR CTD; 2339; -. DR DisGeNET; 2339; -. DR GeneCards; FNTA; -. DR HGNC; HGNC:3782; FNTA. DR HPA; ENSG00000168522; Low tissue specificity. DR MIM; 134635; gene. DR neXtProt; NX_P49354; -. DR OpenTargets; ENSG00000168522; -. DR PharmGKB; PA28199; -. DR VEuPathDB; HostDB:ENSG00000168522; -. DR eggNOG; KOG0530; Eukaryota. DR GeneTree; ENSGT00550000074935; -. DR HOGENOM; CLU_026582_1_1_1; -. DR InParanoid; P49354; -. DR OMA; DRLICED; -. DR OrthoDB; 20949at2759; -. DR PhylomeDB; P49354; -. DR TreeFam; TF313038; -. DR BRENDA; 2.5.1.58; 2681. DR BRENDA; 2.5.1.59; 2681. DR PathwayCommons; P49354; -. DR Reactome; R-HSA-111465; Apoptotic cleavage of cellular proteins. 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; P49354; -. DR SIGNOR; P49354; -. DR BioGRID-ORCS; 2339; 612 hits in 1155 CRISPR screens. DR ChiTaRS; FNTA; human. DR EvolutionaryTrace; P49354; -. DR GeneWiki; FNTA; -. DR GenomeRNAi; 2339; -. DR Pharos; P49354; Tclin. DR PRO; PR:P49354; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; P49354; Protein. DR Bgee; ENSG00000168522; Expressed in esophagus squamous epithelium and 215 other cell types or tissues. DR ExpressionAtlas; P49354; baseline and differential. DR GO; GO:0005953; C:CAAX-protein geranylgeranyltransferase complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005875; C:microtubule associated complex; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IEA:GOC. DR GO; GO:0005965; C:protein farnesyltransferase complex; IDA:UniProtKB. DR GO; GO:0043014; F:alpha-tubulin binding; IDA:BHF-UCL. DR GO; GO:0004662; F:CAAX-protein geranylgeranyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008017; F:microtubule binding; IDA:BHF-UCL. DR GO; GO:0060090; F:molecular adaptor activity; EXP:DisProt. DR GO; GO:0004660; F:protein farnesyltransferase activity; IDA:UniProtKB. DR GO; GO:0004661; F:protein geranylgeranyltransferase activity; IDA:UniProtKB. DR GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IEA:Ensembl. DR GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl. DR GO; GO:0090045; P:positive regulation of deacetylase activity; IDA:BHF-UCL. DR GO; GO:0035022; P:positive regulation of Rac protein signal transduction; IEA:Ensembl. DR GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; IEA:Ensembl. DR GO; GO:0090044; P:positive regulation of tubulin deacetylation; IDA:BHF-UCL. DR GO; GO:0018343; P:protein farnesylation; IDA:UniProtKB. DR GO; GO:0018344; P:protein geranylgeranylation; IDA:UniProtKB. DR GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; IEA:Ensembl. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:ProtInc. DR DisProt; DP00558; -. DR Gene3D; 1.25.40.120; Protein prenylyltransferase; 1. DR InterPro; IPR002088; Prenyl_trans_a. DR PANTHER; PTHR11129; PROTEIN FARNESYLTRANSFERASE ALPHA SUBUNIT/RAB GERANYLGERANYL TRANSFERASE ALPHA SUBUNIT; 1. DR PANTHER; PTHR11129:SF1; PROTEIN FARNESYLTRANSFERASE_GERANYLGERANYLTRANSFERASE TYPE-1 SUBUNIT ALPHA; 1. DR Pfam; PF01239; PPTA; 5. DR SUPFAM; SSF48439; Protein prenylyltransferase; 1. DR PROSITE; PS51147; PFTA; 5. DR Genevisible; P49354; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Magnesium; Phosphoprotein; KW Prenyltransferase; Reference proteome; Repeat; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..379 FT /note="Protein FT farnesyltransferase/geranylgeranyltransferase type-1 FT subunit alpha" FT /id="PRO_0000119746" FT REPEAT 112..146 FT /note="PFTA 1" FT REPEAT 147..180 FT /note="PFTA 2" FT REPEAT 181..215 FT /note="PFTA 3" FT REPEAT 216..249 FT /note="PFTA 4" FT REPEAT 255..289 FT /note="PFTA 5" FT REGION 1..54 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 17..33 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 373 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT VAR_SEQ 68..134 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_036468" FT MUTAGEN 164 FT /note="K->N: Reduced activity." FT /evidence="ECO:0000269|PubMed:8419339" FT MUTAGEN 199 FT /note="N->K: Reduced catalytic efficiency." FT /evidence="ECO:0000269|PubMed:8494894" FT CONFLICT 241 FT /note="Y -> H (in Ref. 2)" FT /evidence="ECO:0000305" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:2H6F" FT HELIX 70..72 FT /evidence="ECO:0007829|PDB:2H6F" FT STRAND 87..90 FT /evidence="ECO:0007829|PDB:2H6F" FT HELIX 94..109 FT /evidence="ECO:0007829|PDB:2H6F" FT HELIX 114..126 FT /evidence="ECO:0007829|PDB:2H6F" FT HELIX 131..143 FT /evidence="ECO:0007829|PDB:2H6F" FT HELIX 148..161 FT /evidence="ECO:0007829|PDB:2H6F" FT HELIX 166..179 FT /evidence="ECO:0007829|PDB:2H6F" FT HELIX 185..195 FT /evidence="ECO:0007829|PDB:2H6F" FT HELIX 200..213 FT /evidence="ECO:0007829|PDB:2H6F" FT HELIX 216..218 FT /evidence="ECO:0007829|PDB:2F0Y" FT HELIX 219..229 FT /evidence="ECO:0007829|PDB:2H6F" FT HELIX 234..246 FT /evidence="ECO:0007829|PDB:2H6F" FT HELIX 253..269 FT /evidence="ECO:0007829|PDB:2H6F" FT HELIX 274..284 FT /evidence="ECO:0007829|PDB:2H6F" FT TURN 285..287 FT /evidence="ECO:0007829|PDB:2H6F" FT HELIX 289..291 FT /evidence="ECO:0007829|PDB:2H6F" FT HELIX 293..302 FT /evidence="ECO:0007829|PDB:2H6F" FT TURN 303..305 FT /evidence="ECO:0007829|PDB:2H6F" FT HELIX 309..324 FT /evidence="ECO:0007829|PDB:2H6F" FT HELIX 330..346 FT /evidence="ECO:0007829|PDB:2H6F" FT HELIX 350..352 FT /evidence="ECO:0007829|PDB:2H6F" FT HELIX 353..367 FT /evidence="ECO:0007829|PDB:2H6F" SQ SEQUENCE 379 AA; 44409 MW; E933CBA874AB92B9 CRC64; MAATEGVGEA AQGGEPGQPA QPPPQPHPPP PQQQHKEEMA AEAGEAVASP MDDGFVSLDS PSYVLYRDRA EWADIDPVPQ NDGPNPVVQI IYSDKFRDVY DYFRAVLQRD ERSERAFKLT RDAIELNAAN YTVWHFRRVL LKSLQKDLHE EMNYITAIIE EQPKNYQVWH HRRVLVEWLR DPSQELEFIA DILNQDAKNY HAWQHRQWVI QEFKLWDNEL QYVDQLLKED VRNNSVWNQR YFVISNTTGY NDRAVLEREV QYTLEMIKLV PHNESAWNYL KGILQDRGLS KYPNLLNQLL DLQPSHSSPY LIAFLVDIYE DMLENQCDNK EDILNKALEL CEILAKEKDT IRKEYWRYIG RSLQSKHSTE NDSPTNVQQ //