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P49356

- FNTB_HUMAN

UniProt

P49356 - FNTB_HUMAN

Protein

Protein farnesyltransferase subunit beta

Gene

FNTB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X.5 Publications

    Catalytic activityi

    Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate.5 Publications

    Cofactori

    Binds 1 zinc ion per subunit.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei102 – 1021Important for selectivity against geranylgeranyl diphosphate
    Metal bindingi297 – 2971Zinc; catalytic
    Metal bindingi299 – 2991Zinc; catalytic
    Metal bindingi362 – 3621Zinc; via tele nitrogen; catalytic

    GO - Molecular functioni

    1. farnesyltranstransferase activity Source: Ensembl
    2. protein binding Source: IntAct
    3. protein farnesyltransferase activity Source: UniProtKB
    4. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. negative regulation of cell proliferation Source: Ensembl
    2. phototransduction, visible light Source: Reactome
    3. positive regulation of cell cycle Source: Ensembl
    4. positive regulation of fibroblast proliferation Source: Ensembl
    5. positive regulation of nitric-oxide synthase biosynthetic process Source: Ensembl
    6. protein farnesylation Source: UniProtKB
    7. regulation of rhodopsin mediated signaling pathway Source: Reactome
    8. response to cytokine Source: Ensembl
    9. response to inorganic substance Source: Ensembl
    10. response to organic cyclic compound Source: Ensembl
    11. rhodopsin mediated signaling pathway Source: Reactome
    12. wound healing Source: Ensembl

    Keywords - Molecular functioni

    Prenyltransferase, Transferase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein farnesyltransferase subunit beta (EC:2.5.1.58)
    Short name:
    FTase-beta
    Alternative name(s):
    CAAX farnesyltransferase subunit beta
    Ras proteins prenyltransferase subunit beta
    Gene namesi
    Name:FNTB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:3785. FNTB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. microtubule associated complex Source: BHF-UCL
    3. protein farnesyltransferase complex Source: UniProtKB

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi102 – 1021W → T: Removes the steric hindrance that normally precludes geranylgeranyl diphosphate binding. Reduces farnesyltransferase activity and confers geranylgeranyltransferase activity. 1 Publication
    Mutagenesisi200 – 2001D → N: Reduced catalytic efficiency. 1 Publication
    Mutagenesisi249 – 2491G → V: Reduced catalytic efficiency. 1 Publication
    Mutagenesisi349 – 3491G → S: Reduced catalytic efficiency. 1 Publication

    Organism-specific databases

    PharmGKBiPA28202.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 437437Protein farnesyltransferase subunit betaPRO_0000119761Add
    BLAST

    Proteomic databases

    MaxQBiP49356.
    PeptideAtlasiP49356.
    PRIDEiP49356.

    PTM databases

    PhosphoSiteiP49356.

    Expressioni

    Gene expression databases

    BgeeiP49356.
    CleanExiHS_FNTB.
    GenevestigatoriP49356.

    Interactioni

    Subunit structurei

    Heterodimer of FNTA and FNTB.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FNTAP493547EBI-602349,EBI-602336

    Protein-protein interaction databases

    BioGridi108627. 7 interactions.
    IntActiP49356. 2 interactions.
    MINTiMINT-238879.
    STRINGi9606.ENSP00000246166.

    Structurei

    Secondary structure

    1
    437
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi24 – 263
    Helixi28 – 336
    Helixi43 – 6018
    Helixi75 – 8511
    Beta strandi87 – 893
    Helixi91 – 966
    Helixi100 – 11314
    Helixi120 – 13314
    Beta strandi138 – 1436
    Helixi150 – 16314
    Helixi166 – 1694
    Helixi174 – 1829
    Beta strandi191 – 1944
    Helixi201 – 21313
    Turni219 – 2246
    Helixi225 – 2328
    Beta strandi237 – 2393
    Helixi249 – 26214
    Helixi265 – 2673
    Helixi270 – 27910
    Turni283 – 2853
    Beta strandi287 – 2915
    Helixi300 – 3034
    Turni304 – 3063
    Helixi307 – 31711
    Beta strandi325 – 3273
    Helixi332 – 34211
    Helixi360 – 37415
    Beta strandi375 – 3784
    Beta strandi381 – 3844
    Helixi390 – 3923
    Turni399 – 4013
    Helixi405 – 41612

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JCQX-ray2.30B1-437[»]
    1LD7X-ray2.00B1-437[»]
    1LD8X-ray1.80B1-437[»]
    1MZCX-ray2.00B1-437[»]
    1S63X-ray1.90B1-437[»]
    1SA4X-ray2.10B1-437[»]
    1TN6X-ray1.80B1-437[»]
    2F0YX-ray2.70B1-437[»]
    2H6FX-ray1.50B1-437[»]
    2H6GX-ray1.85B1-437[»]
    2H6HX-ray1.80B1-437[»]
    2H6IX-ray3.00B1-437[»]
    2IEJX-ray1.80B1-437[»]
    3E37X-ray1.80B1-437[»]
    ProteinModelPortaliP49356.
    SMRiP49356. Positions 15-424.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49356.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati123 – 16442PFTB 1Add
    BLAST
    Repeati174 – 21542PFTB 2Add
    BLAST
    Repeati222 – 26342PFTB 3Add
    BLAST
    Repeati270 – 31243PFTB 4Add
    BLAST
    Repeati332 – 37443PFTB 5Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni248 – 2514Farnesyl diphosphate binding
    Regioni291 – 2944Farnesyl diphosphate binding
    Regioni300 – 3034Farnesyl diphosphate binding

    Sequence similaritiesi

    Contains 5 PFTB repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    HOVERGENiHBG008173.
    InParanoidiP49356.
    KOiK05954.
    OMAiKLLDFLW.
    OrthoDBiEOG7P02HV.
    PhylomeDBiP49356.
    TreeFamiTF353162.

    Family and domain databases

    Gene3Di1.50.10.20. 1 hit.
    InterProiIPR026872. FTB.
    IPR001330. Prenyltrans.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [Graphical view]
    PANTHERiPTHR11774:SF6. PTHR11774:SF6. 1 hit.
    PfamiPF00432. Prenyltrans. 2 hits.
    [Graphical view]
    SUPFAMiSSF48239. SSF48239. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P49356-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MASPSSFTYY CPPSSSPVWS EPLYSLRPEH ARERLQDDSV ETVTSIEQAK    50
    VEEKIQEVFS SYKFNHLVPR LVLQREKHFH YLKRGLRQLT DAYECLDASR 100
    PWLCYWILHS LELLDEPIPQ IVATDVCQFL ELCQSPEGGF GGGPGQYPHL 150
    APTYAAVNAL CIIGTEEAYD IINREKLLQY LYSLKQPDGS FLMHVGGEVD 200
    VRSAYCAASV ASLTNIITPD LFEGTAEWIA RCQNWEGGIG GVPGMEAHGG 250
    YTFCGLAALV ILKRERSLNL KSLLQWVTSR QMRFEGGFQG RCNKLVDGCY 300
    SFWQAGLLPL LHRALHAQGD PALSMSHWMF HQQALQEYIL MCCQCPAGGL 350
    LDKPGKSRDF YHTCYCLSGL SIAQHFGSGA MLHDVVLGVP ENALQPTHPV 400
    YNIGPDKVIQ ATTYFLQKPV PGFEELKDET SAEPATD 437
    Length:437
    Mass (Da):48,774
    Last modified:February 1, 1996 - v1
    Checksum:i8E8E571846146709
    GO
    Isoform 2 (identifier: P49356-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-48: MASPSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQ → MI

    Note: No experimental confirmation available.

    Show »
    Length:391
    Mass (Da):43,574
    Checksum:i00AC66972207B800
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti283 – 2831R → L in AAA86286. (PubMed:8276393)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4848MASPS…TSIEQ → MI in isoform 2. 1 PublicationVSP_054657Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L00635 mRNA. Translation: AAA35854.1.
    AK303739 mRNA. Translation: BAG64712.1.
    AK315714 mRNA. Translation: BAG38073.1.
    AL135745 Genomic DNA. No translation available.
    AL139022 Genomic DNA. No translation available.
    CH471061 Genomic DNA. Translation: EAW80897.1.
    BC020232 mRNA. Translation: AAH20232.1.
    L10414 mRNA. Translation: AAA86286.1.
    CCDSiCCDS9769.1. [P49356-1]
    PIRiB49274.
    RefSeqiNP_001189487.1. NM_001202558.1. [P49356-2]
    NP_002019.1. NM_002028.3. [P49356-1]
    UniGeneiHs.325531.

    Genome annotation databases

    EnsembliENST00000246166; ENSP00000246166; ENSG00000257365. [P49356-1]
    GeneIDi100529261.
    2342.
    KEGGihsa:2342.
    UCSCiuc001xia.3. human. [P49356-1]

    Polymorphism databases

    DMDMi1346696.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L00635 mRNA. Translation: AAA35854.1 .
    AK303739 mRNA. Translation: BAG64712.1 .
    AK315714 mRNA. Translation: BAG38073.1 .
    AL135745 Genomic DNA. No translation available.
    AL139022 Genomic DNA. No translation available.
    CH471061 Genomic DNA. Translation: EAW80897.1 .
    BC020232 mRNA. Translation: AAH20232.1 .
    L10414 mRNA. Translation: AAA86286.1 .
    CCDSi CCDS9769.1. [P49356-1 ]
    PIRi B49274.
    RefSeqi NP_001189487.1. NM_001202558.1. [P49356-2 ]
    NP_002019.1. NM_002028.3. [P49356-1 ]
    UniGenei Hs.325531.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JCQ X-ray 2.30 B 1-437 [» ]
    1LD7 X-ray 2.00 B 1-437 [» ]
    1LD8 X-ray 1.80 B 1-437 [» ]
    1MZC X-ray 2.00 B 1-437 [» ]
    1S63 X-ray 1.90 B 1-437 [» ]
    1SA4 X-ray 2.10 B 1-437 [» ]
    1TN6 X-ray 1.80 B 1-437 [» ]
    2F0Y X-ray 2.70 B 1-437 [» ]
    2H6F X-ray 1.50 B 1-437 [» ]
    2H6G X-ray 1.85 B 1-437 [» ]
    2H6H X-ray 1.80 B 1-437 [» ]
    2H6I X-ray 3.00 B 1-437 [» ]
    2IEJ X-ray 1.80 B 1-437 [» ]
    3E37 X-ray 1.80 B 1-437 [» ]
    ProteinModelPortali P49356.
    SMRi P49356. Positions 15-424.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108627. 7 interactions.
    IntActi P49356. 2 interactions.
    MINTi MINT-238879.
    STRINGi 9606.ENSP00000246166.

    Chemistry

    BindingDBi P49356.
    ChEMBLi CHEMBL2094108.

    PTM databases

    PhosphoSitei P49356.

    Polymorphism databases

    DMDMi 1346696.

    Proteomic databases

    MaxQBi P49356.
    PeptideAtlasi P49356.
    PRIDEi P49356.

    Protocols and materials databases

    DNASUi 2342.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000246166 ; ENSP00000246166 ; ENSG00000257365 . [P49356-1 ]
    GeneIDi 100529261.
    2342.
    KEGGi hsa:2342.
    UCSCi uc001xia.3. human. [P49356-1 ]

    Organism-specific databases

    CTDi 100529261.
    2342.
    GeneCardsi GC14P065454.
    HGNCi HGNC:3785. FNTB.
    MIMi 134636. gene.
    neXtProti NX_P49356.
    PharmGKBi PA28202.
    GenAtlasi Search...

    Phylogenomic databases

    HOVERGENi HBG008173.
    InParanoidi P49356.
    KOi K05954.
    OMAi KLLDFLW.
    OrthoDBi EOG7P02HV.
    PhylomeDBi P49356.
    TreeFami TF353162.

    Enzyme and pathway databases

    Reactomei REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.

    Miscellaneous databases

    EvolutionaryTracei P49356.
    GeneWikii FNTB.
    GenomeRNAii 2342.
    NextBioi 34055020.
    PROi P49356.
    SOURCEi Search...

    Gene expression databases

    Bgeei P49356.
    CleanExi HS_FNTB.
    Genevestigatori P49356.

    Family and domain databases

    Gene3Di 1.50.10.20. 1 hit.
    InterProi IPR026872. FTB.
    IPR001330. Prenyltrans.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [Graphical view ]
    PANTHERi PTHR11774:SF6. PTHR11774:SF6. 1 hit.
    Pfami PF00432. Prenyltrans. 2 hits.
    [Graphical view ]
    SUPFAMi SSF48239. SSF48239. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases."
      Omer C.A., Kral A.M., Diehl R.E., Prendergast G.C., Powers S., Allen C.M., Gibbs J.B., Kohl N.E.
      Biochemistry 32:5167-5176(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF ASP-200; GLY-249 AND GLY-349, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT.
      Tissue: Placenta.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Kidney and Testis.
    3. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Placenta.
    6. "cDNA cloning of the two subunits of human CAAX farnesyltransferase and chromosomal mapping of FNTA and FNTB loci and related sequences."
      Andres D.A., Milatovich A., Ozcelik T., Wenzlau J.M., Brown M.S., Goldstein J.L., Francke U.
      Genomics 18:105-112(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 51-437 (ISOFORM 1/2).
      Tissue: Retina.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics."
      Long S.B., Hancock P.J., Kral A.M., Hellinga H.W., Beese L.S.
      Proc. Natl. Acad. Sci. U.S.A. 98:12948-12953(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA; FARNESYL DIPHOSPHATE AND INHIBITOR L-739,750, SUBUNIT, COFACTOR.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA; FARNESYL DIPHOSPHATE AND INHIBITORS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, FUNCTION.
    11. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA; FARNESYL DIPHOSPHATE AND INHIBITOR, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, FUNCTION.
    12. "Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity."
      Reid T.S., Terry K.L., Casey P.J., Beese L.S.
      J. Mol. Biol. 343:417-433(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA AND FARNESYL DIPHOSPHATE ANALOG, COFACTOR, SUBUNIT.
    13. "Conversion of protein farnesyltransferase to a geranylgeranyltransferase."
      Terry K.L., Casey P.J., Beese L.S.
      Biochemistry 45:9746-9755(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA AND FARNESYL DIPHOSPHATE ANALOG, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, FUNCTION, MUTAGENESIS OF TRP-102.
    14. "Structural basis for binding and selectivity of antimalarial and anticancer ethylenediamine inhibitors to protein farnesyltransferase."
      Hast M.A., Fletcher S., Cummings C.G., Pusateri E.E., Blaskovich M.A., Rivas K., Gelb M.H., Van Voorhis W.C., Sebti S.M., Hamilton A.D., Beese L.S.
      Chem. Biol. 16:181-192(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND FNTA, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, SUBUNIT.

    Entry informationi

    Entry nameiFNTB_HUMAN
    AccessioniPrimary (citable) accession number: P49356
    Secondary accession number(s): B2RDX6, B4E1A0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 146 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3