FNTA_HUMAN
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 03-AUG-2022, entry version 209.
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}.
CC -!- SUBUNIT: Interacts with MUSK; the interaction is direct and mediates
CC AGRIN-induced phosphorylation of FNTA (By similarity). Heterodimer of
CC FNTA and FNTB (farnesyltransferase). Heterodimer of FNTA and PGGT1B
CC (geranylgeranyltransferase). {ECO:0000250, ECO:0000269|PubMed:11687658,
CC ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937,
CC ECO:0000269|PubMed:15170324, ECO:0000269|PubMed:15451670,
CC ECO:0000269|PubMed:16893176, ECO:0000269|PubMed:19246009,
CC 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}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC family. {ECO:0000305}.
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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; 85.
DR ComplexPortal; CPX-2157; Protein geranylgeranyl transferase type I complex.
DR ComplexPortal; CPX-2165; Protein farnesyltransferase complex.
DR CORUM; P49354; -.
DR IntAct; P49354; 39.
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; P49354; -.
DR PeptideAtlas; P49354; -.
DR PRIDE; P49354; -.
DR ProteomicsDB; 55993; -. [P49354-1]
DR ProteomicsDB; 55994; -. [P49354-2]
DR Antibodypedia; 1067; 311 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 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; RRKYWQY; -.
DR OrthoDB; 1527547at2759; -.
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; 593 hits in 1079 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 213 other tissues.
DR ExpressionAtlas; P49354; baseline and differential.
DR Genevisible; P49354; HS.
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:0030548; F:acetylcholine receptor regulator activity; IEA:Ensembl.
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: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:0045213; P:neurotransmitter receptor metabolic process; IEA:Ensembl.
DR GO; GO:0090045; P:positive regulation of deacetylase activity; IDA:BHF-UCL.
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 InterPro; IPR002088; Prenyl_trans_a.
DR Pfam; PF01239; PPTA; 5.
DR PROSITE; PS51147; PFTA; 5.
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
