Full text data of FNTB
FNTB
[Confidence: low (only semi-automatic identification from reviews)]
Protein farnesyltransferase subunit beta; FTase-beta; 2.5.1.58 (CAAX farnesyltransferase subunit beta; Ras proteins prenyltransferase subunit beta)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Protein farnesyltransferase subunit beta; FTase-beta; 2.5.1.58 (CAAX farnesyltransferase subunit beta; Ras proteins prenyltransferase subunit beta)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P49356
ID FNTB_HUMAN Reviewed; 437 AA.
AC P49356; B2RDX6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1996, sequence version 1.
DT 22-JAN-2014, entry version 138.
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], AND MUTAGENESIS OF ASP-200; GLY-249 AND
RP GLY-349.
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 ALPHA SUBUNIT;
RP FARNESYL DIPHOSPHATE AND INHIBITOR L-739,750.
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 ALPHA SUBUNIT;
RP FARNESYL DIPHOSPHATE AND INHIBITORS.
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 ALPHA SUBUNIT;
RP FARNESYL DIPHOSPHATE AND INHIBITOR.
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).
CC -!- FUNCTION: Catalyzes the transfer of a farnesyl moiety from
CC farnesyl pyrophosphate to a cysteine at the fourth position from
CC the C-terminus of several proteins. The beta subunit is
CC responsible for peptide-binding.
CC -!- CATALYTIC ACTIVITY: Farnesyl diphosphate + protein-cysteine = S-
CC farnesyl protein + diphosphate.
CC -!- COFACTOR: Binds 1 zinc ion per subunit.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
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.
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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 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 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; IEA:InterPro.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004660; F:protein farnesyltransferase activity; IEA:UniProtKB-EC.
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:BHF-UCL.
DR GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; TAS:Reactome.
DR GO; GO:0034097; P:response to cytokine stimulus; 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 METAL 297 297 Zinc.
FT METAL 299 299 Zinc.
FT METAL 362 362 Zinc.
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
//
ID FNTB_HUMAN Reviewed; 437 AA.
AC P49356; B2RDX6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1996, sequence version 1.
DT 22-JAN-2014, entry version 138.
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], AND MUTAGENESIS OF ASP-200; GLY-249 AND
RP GLY-349.
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 ALPHA SUBUNIT;
RP FARNESYL DIPHOSPHATE AND INHIBITOR L-739,750.
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 ALPHA SUBUNIT;
RP FARNESYL DIPHOSPHATE AND INHIBITORS.
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 ALPHA SUBUNIT;
RP FARNESYL DIPHOSPHATE AND INHIBITOR.
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).
CC -!- FUNCTION: Catalyzes the transfer of a farnesyl moiety from
CC farnesyl pyrophosphate to a cysteine at the fourth position from
CC the C-terminus of several proteins. The beta subunit is
CC responsible for peptide-binding.
CC -!- CATALYTIC ACTIVITY: Farnesyl diphosphate + protein-cysteine = S-
CC farnesyl protein + diphosphate.
CC -!- COFACTOR: Binds 1 zinc ion per subunit.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
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.
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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 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 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; IEA:InterPro.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004660; F:protein farnesyltransferase activity; IEA:UniProtKB-EC.
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:BHF-UCL.
DR GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; TAS:Reactome.
DR GO; GO:0034097; P:response to cytokine stimulus; 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 METAL 297 297 Zinc.
FT METAL 299 299 Zinc.
FT METAL 362 362 Zinc.
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
//
MIM
134636
*RECORD*
*FIELD* NO
134636
*FIELD* TI
*134636 FARNESYLTRANSFERASE, CAAX BOX, BETA; FNTB
*FIELD* TX
DESCRIPTION
The CAAX farnesyltransferase (FTase) is an alpha/beta heterodimeric
read moreenzyme that attaches a farnesyl group to a single cysteine in several
cellular proteins, all of which end with a 'CAAX box,' where C is
cysteine, A is an aliphatic amino acid, and X is methionine or serine.
This posttranslational modification provides a mechanism for membrane
localization of proteins that lack a transmembrane domain (summary by
Andres et al., 1993).
CLONING
Using rat FNTA (132635) and FNTB cDNA, Andres et al. (1993) cloned the
corresponding human cDNAs. FNTB encodes a predicted 487-amino acid
protein that shares 96% sequence identity with the rat homolog.
MAPPING
Andres et al. (1993) localized the FNTB gene 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. They found a related farnesyltransferase gene, FNTBL1, on
chromosome 9.
BIOCHEMICAL FEATURES
Long et al. (2002) presented a complete series of structures
representing the major steps along the reaction coordinate of the enzyme
protein farnesyltransferase. From these observations, Long et al. (2002)
deduced the determinants of substrate specificity and an unusual
mechanism in which product release requires binding of substrate,
analogous to classically processive enzymes. A structural model for the
transition state consistent with previous mechanistic studies was also
constructed.
ANIMAL MODEL
Lee et al. (2010) used conditional knockout alleles for Fntb, Pggt1b
(602031), which encodes the beta subunit of GGTase-I, and a keratin-14
(KRT14; 148066)-Cre transgene to create mice lacking FTase or GGTase-I
in skin keratinocytes. Keratinocyte-specific Fntb knockout mice were
viable but developed severe alopecia. The interfollicular epidermis of
Fntb-deficient mice appeared normal; however, keratinocytes from these
mice could not proliferate in culture. As expected, nonfarnesylated
prelamin A (LMNA; 150330) and nonfarnesylated DNAJA1 (602837)
accumulated in Fntb-deficient keratinocytes. Keratinocyte-specific
Pggt1b knockout mice survived development but died shortly after birth.
Like Fntb-deficient keratinocytes, Pggt1b-deficient keratinocytes did
not proliferate in culture. Lee et al. (2010) concluded that both FTase
and GGTase-I are required for the homeostasis of skin keratinocytes.
*FIELD* RF
1. Andres, D. A.; Milatovich, A.; Ozcelik, T.; Wenzlau, J. M.; Brown,
M. S.; Goldstein, J. L.; Francke, U.: cDNA cloning of the two subunits
of human CAAX farnesyltransferase and chromosomal mapping of FNTA
and FNTB loci and related sequences. Genomics 18: 105-112, 1993.
2. Lee, R.; Chang, S. Y.; Trinh, H.; Tu, Y.; White, A. C.; Davies,
B. S. J.; Bergo, M. O.; Fong, L. G.; Lowry, W. E.; Young, S. G.:
Genetic studies on the functional relevance of the protein prenyltransferases
in skin keratinocytes. Hum. Molec. Genet. 19: 1603-1617, 2010.
3. Long, S. B.; Casey, P. J.; Beese, L. S.: Reaction path of protein
farnesyltransferase at atomic resolution. Nature 419: 645-650, 2002.
*FIELD* CN
George E. Tiller - updated: 11/21/2011
Ada Hamosh - updated: 10/18/2002
*FIELD* CD
Victor A. McKusick: 10/14/1993
*FIELD* ED
carol: 11/21/2011
terry: 11/21/2011
alopez: 10/21/2002
terry: 10/18/2002
carol: 10/14/1993
*RECORD*
*FIELD* NO
134636
*FIELD* TI
*134636 FARNESYLTRANSFERASE, CAAX BOX, BETA; FNTB
*FIELD* TX
DESCRIPTION
The CAAX farnesyltransferase (FTase) is an alpha/beta heterodimeric
read moreenzyme that attaches a farnesyl group to a single cysteine in several
cellular proteins, all of which end with a 'CAAX box,' where C is
cysteine, A is an aliphatic amino acid, and X is methionine or serine.
This posttranslational modification provides a mechanism for membrane
localization of proteins that lack a transmembrane domain (summary by
Andres et al., 1993).
CLONING
Using rat FNTA (132635) and FNTB cDNA, Andres et al. (1993) cloned the
corresponding human cDNAs. FNTB encodes a predicted 487-amino acid
protein that shares 96% sequence identity with the rat homolog.
MAPPING
Andres et al. (1993) localized the FNTB gene 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. They found a related farnesyltransferase gene, FNTBL1, on
chromosome 9.
BIOCHEMICAL FEATURES
Long et al. (2002) presented a complete series of structures
representing the major steps along the reaction coordinate of the enzyme
protein farnesyltransferase. From these observations, Long et al. (2002)
deduced the determinants of substrate specificity and an unusual
mechanism in which product release requires binding of substrate,
analogous to classically processive enzymes. A structural model for the
transition state consistent with previous mechanistic studies was also
constructed.
ANIMAL MODEL
Lee et al. (2010) used conditional knockout alleles for Fntb, Pggt1b
(602031), which encodes the beta subunit of GGTase-I, and a keratin-14
(KRT14; 148066)-Cre transgene to create mice lacking FTase or GGTase-I
in skin keratinocytes. Keratinocyte-specific Fntb knockout mice were
viable but developed severe alopecia. The interfollicular epidermis of
Fntb-deficient mice appeared normal; however, keratinocytes from these
mice could not proliferate in culture. As expected, nonfarnesylated
prelamin A (LMNA; 150330) and nonfarnesylated DNAJA1 (602837)
accumulated in Fntb-deficient keratinocytes. Keratinocyte-specific
Pggt1b knockout mice survived development but died shortly after birth.
Like Fntb-deficient keratinocytes, Pggt1b-deficient keratinocytes did
not proliferate in culture. Lee et al. (2010) concluded that both FTase
and GGTase-I are required for the homeostasis of skin keratinocytes.
*FIELD* RF
1. Andres, D. A.; Milatovich, A.; Ozcelik, T.; Wenzlau, J. M.; Brown,
M. S.; Goldstein, J. L.; Francke, U.: cDNA cloning of the two subunits
of human CAAX farnesyltransferase and chromosomal mapping of FNTA
and FNTB loci and related sequences. Genomics 18: 105-112, 1993.
2. Lee, R.; Chang, S. Y.; Trinh, H.; Tu, Y.; White, A. C.; Davies,
B. S. J.; Bergo, M. O.; Fong, L. G.; Lowry, W. E.; Young, S. G.:
Genetic studies on the functional relevance of the protein prenyltransferases
in skin keratinocytes. Hum. Molec. Genet. 19: 1603-1617, 2010.
3. Long, S. B.; Casey, P. J.; Beese, L. S.: Reaction path of protein
farnesyltransferase at atomic resolution. Nature 419: 645-650, 2002.
*FIELD* CN
George E. Tiller - updated: 11/21/2011
Ada Hamosh - updated: 10/18/2002
*FIELD* CD
Victor A. McKusick: 10/14/1993
*FIELD* ED
carol: 11/21/2011
terry: 11/21/2011
alopez: 10/21/2002
terry: 10/18/2002
carol: 10/14/1993