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Q02293

- FNTB_RAT

UniProt

Q02293 - FNTB_RAT

Protein

Protein farnesyltransferase subunit beta

Gene

Fntb

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      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.4 Publications

    Catalytic activityi

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

    Cofactori

    Binds 1 zinc ion per subunit.12 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei102 – 1021Important for selectivity against geranylgeranyl diphosphateBy similarity
    Metal bindingi297 – 2971Zinc; catalytic3 Publications
    Metal bindingi299 – 2991Zinc; catalytic3 Publications
    Metal bindingi362 – 3621Zinc; via tele nitrogen; catalytic3 Publications

    GO - Molecular functioni

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

    GO - Biological processi

    1. negative regulation of cell proliferation Source: Ensembl
    2. positive regulation of cell cycle Source: RGD
    3. positive regulation of cell proliferation Source: RGD
    4. positive regulation of fibroblast proliferation Source: Ensembl
    5. positive regulation of nitric-oxide synthase biosynthetic process Source: RGD
    6. protein farnesylation Source: UniProtKB
    7. response to cytokine Source: RGD
    8. response to inorganic substance Source: RGD
    9. response to organic cyclic compound Source: RGD
    10. wound healing Source: Ensembl

    Keywords - Molecular functioni

    Prenyltransferase, Transferase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_227662. Inactivation, recovery and regulation of the phototransduction cascade.
    SABIO-RKQ02293.

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 6

    Organism-specific databases

    RGDi620119. Fntb.

    Subcellular locationi

    GO - Cellular componenti

    1. microtubule associated complex Source: Ensembl
    2. protein complex Source: RGD
    3. protein farnesyltransferase complex Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 437437Protein farnesyltransferase subunit betaPRO_0000119763Add
    BLAST

    Proteomic databases

    PaxDbiQ02293.
    PRIDEiQ02293.

    PTM databases

    PhosphoSiteiQ02293.

    Expressioni

    Gene expression databases

    GenevestigatoriQ02293.

    Interactioni

    Subunit structurei

    Heterodimer of FNTA and FNTB.14 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FntaQ0463114EBI-602454,EBI-602447

    Protein-protein interaction databases

    DIPiDIP-6132N.
    IntActiQ02293. 1 interaction.
    MINTiMINT-121917.
    STRINGi10116.ENSRNOP00000010588.

    Structurei

    Secondary structure

    1
    437
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi24 – 263
    Helixi28 – 336
    Helixi43 – 6523
    Helixi75 – 8511
    Helixi91 – 966
    Helixi100 – 11314
    Helixi120 – 13314
    Beta strandi138 – 1436
    Helixi150 – 16314
    Helixi166 – 1716
    Helixi174 – 18411
    Beta strandi191 – 1944
    Helixi201 – 21313
    Turni219 – 2246
    Helixi225 – 2328
    Beta strandi237 – 2393
    Helixi249 – 26113
    Helixi265 – 2673
    Helixi270 – 2789
    Turni283 – 2853
    Beta strandi287 – 2915
    Helixi300 – 3034
    Turni304 – 3063
    Helixi307 – 31711
    Beta strandi321 – 3233
    Beta strandi325 – 3273
    Helixi332 – 34211
    Beta strandi348 – 3503
    Beta strandi352 – 3554
    Helixi360 – 37415
    Beta strandi375 – 3784
    Beta strandi381 – 3844
    Helixi390 – 3923
    Turni399 – 4013
    Helixi405 – 41511
    Helixi424 – 4263
    Helixi434 – 4363

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D8DX-ray2.00B1-437[»]
    1D8EX-ray3.00B1-437[»]
    1FPPX-ray2.75B1-437[»]
    1FT1X-ray2.25B1-437[»]
    1FT2X-ray3.40B22-422[»]
    1FTImodel-B22-422[»]
    1HZ7model-B41-406[»]
    1JCRX-ray2.00B1-437[»]
    1JCSX-ray2.20B1-437[»]
    1KZOX-ray2.20B1-437[»]
    1KZPX-ray2.10B1-437[»]
    1KZRmodel-B17-423[»]
    1N94X-ray3.50B22-418[»]
    1N95X-ray2.30B22-423[»]
    1N9AX-ray3.20B22-423[»]
    1NI1X-ray2.30B22-423[»]
    1NL4X-ray2.70B23-423[»]
    1O1RX-ray2.30B1-427[»]
    1O1SX-ray2.30B1-427[»]
    1O1TX-ray2.10B1-427[»]
    1O5MX-ray2.30B1-437[»]
    1QBQX-ray2.40B1-437[»]
    1QE2model-B41-406[»]
    1SA5X-ray2.60B1-437[»]
    1TN7X-ray2.30B1-437[»]
    1TN8X-ray2.25B1-437[»]
    1X81X-ray3.50B22-418[»]
    2BEDX-ray2.70B23-423[»]
    2FTImodel-B22-422[»]
    2R2LX-ray2.23B23-423[»]
    2ZIRX-ray2.40B1-437[»]
    2ZISX-ray2.60B1-437[»]
    3DPYX-ray2.70B1-437[»]
    3E30X-ray2.45B1-437[»]
    3E32X-ray2.45B1-437[»]
    3E33X-ray1.90B1-437[»]
    3E34X-ray2.05B1-437[»]
    3EU5X-ray2.80B1-427[»]
    3EUVX-ray2.75B1-427[»]
    3FTImodel-B22-422[»]
    3KSLX-ray2.05B1-437[»]
    3KSQX-ray2.10B1-437[»]
    4GTMX-ray2.20B1-427[»]
    4GTOX-ray2.15B1-427[»]
    4GTPX-ray2.75B1-427[»]
    4GTQX-ray2.60B1-427[»]
    4GTRX-ray2.20B1-427[»]
    ProteinModelPortaliQ02293.
    SMRiQ02293. Positions 22-437.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ02293.

    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

    eggNOGiCOG5029.
    GeneTreeiENSGT00550000075042.
    HOGENOMiHOG000190594.
    HOVERGENiHBG008173.
    InParanoidiQ02293.
    KOiK05954.
    OMAiKLLDFLW.
    OrthoDBiEOG7P02HV.
    PhylomeDBiQ02293.
    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.

    Sequencei

    Sequence statusi: Complete.

    Q02293-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASSSSFTYY CPPSSSPVWS EPLYSLRPEH ARERLQDDSV ETVTSIEQAK    50
    VEEKIQEVFS SYKFNHLVPR LVLQREKHFH YLKRGLRQLT DAYECLDASR 100
    PWLCYWILHS LELLDEPIPQ IVATDVCQFL ELCQSPDGGF GGGPGQYPHL 150
    APTYAAVNAL CIIGTEEAYN VINREKLLQY LYSLKQPDGS FLMHVGGEVD 200
    VRSAYCAASV ASLTNIITPD LFEGTAEWIA RCQNWEGGIG GVPGMEAHGG 250
    YTFCGLAALV ILKKERSLNL KSLLQWVTSR QMRFEGGFQG RCNKLVDGCY 300
    SFWQAGLLPL LHRALHAQGD PALSMSHWMF HQQALQEYIL MCCQCPAGGL 350
    LDKPGKSRDF YHTCYCLSGL SIAQHFGSGA MLHDVVMGVP ENVLQPTHPV 400
    YNIGPDKVIQ ATTHFLQKPV PGFEECEDAV TSDPATD 437
    Length:437
    Mass (Da):48,673
    Last modified:April 1, 1993 - v1
    Checksum:i41A9D6D79CD319A8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M69056 mRNA. Translation: AAA41176.1.
    BC087675 mRNA. Translation: AAH87675.1.
    PIRiA40037.
    RefSeqiNP_742031.1. NM_172034.2.
    UniGeneiRn.8873.

    Genome annotation databases

    EnsembliENSRNOT00000010588; ENSRNOP00000010588; ENSRNOG00000007660.
    GeneIDi64511.
    KEGGirno:64511.
    UCSCiRGD:620119. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M69056 mRNA. Translation: AAA41176.1 .
    BC087675 mRNA. Translation: AAH87675.1 .
    PIRi A40037.
    RefSeqi NP_742031.1. NM_172034.2.
    UniGenei Rn.8873.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D8D X-ray 2.00 B 1-437 [» ]
    1D8E X-ray 3.00 B 1-437 [» ]
    1FPP X-ray 2.75 B 1-437 [» ]
    1FT1 X-ray 2.25 B 1-437 [» ]
    1FT2 X-ray 3.40 B 22-422 [» ]
    1FTI model - B 22-422 [» ]
    1HZ7 model - B 41-406 [» ]
    1JCR X-ray 2.00 B 1-437 [» ]
    1JCS X-ray 2.20 B 1-437 [» ]
    1KZO X-ray 2.20 B 1-437 [» ]
    1KZP X-ray 2.10 B 1-437 [» ]
    1KZR model - B 17-423 [» ]
    1N94 X-ray 3.50 B 22-418 [» ]
    1N95 X-ray 2.30 B 22-423 [» ]
    1N9A X-ray 3.20 B 22-423 [» ]
    1NI1 X-ray 2.30 B 22-423 [» ]
    1NL4 X-ray 2.70 B 23-423 [» ]
    1O1R X-ray 2.30 B 1-427 [» ]
    1O1S X-ray 2.30 B 1-427 [» ]
    1O1T X-ray 2.10 B 1-427 [» ]
    1O5M X-ray 2.30 B 1-437 [» ]
    1QBQ X-ray 2.40 B 1-437 [» ]
    1QE2 model - B 41-406 [» ]
    1SA5 X-ray 2.60 B 1-437 [» ]
    1TN7 X-ray 2.30 B 1-437 [» ]
    1TN8 X-ray 2.25 B 1-437 [» ]
    1X81 X-ray 3.50 B 22-418 [» ]
    2BED X-ray 2.70 B 23-423 [» ]
    2FTI model - B 22-422 [» ]
    2R2L X-ray 2.23 B 23-423 [» ]
    2ZIR X-ray 2.40 B 1-437 [» ]
    2ZIS X-ray 2.60 B 1-437 [» ]
    3DPY X-ray 2.70 B 1-437 [» ]
    3E30 X-ray 2.45 B 1-437 [» ]
    3E32 X-ray 2.45 B 1-437 [» ]
    3E33 X-ray 1.90 B 1-437 [» ]
    3E34 X-ray 2.05 B 1-437 [» ]
    3EU5 X-ray 2.80 B 1-427 [» ]
    3EUV X-ray 2.75 B 1-427 [» ]
    3FTI model - B 22-422 [» ]
    3KSL X-ray 2.05 B 1-437 [» ]
    3KSQ X-ray 2.10 B 1-437 [» ]
    4GTM X-ray 2.20 B 1-427 [» ]
    4GTO X-ray 2.15 B 1-427 [» ]
    4GTP X-ray 2.75 B 1-427 [» ]
    4GTQ X-ray 2.60 B 1-427 [» ]
    4GTR X-ray 2.20 B 1-427 [» ]
    ProteinModelPortali Q02293.
    SMRi Q02293. Positions 22-437.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6132N.
    IntActi Q02293. 1 interaction.
    MINTi MINT-121917.
    STRINGi 10116.ENSRNOP00000010588.

    Chemistry

    BindingDBi Q02293.
    ChEMBLi CHEMBL2095197.

    PTM databases

    PhosphoSitei Q02293.

    Proteomic databases

    PaxDbi Q02293.
    PRIDEi Q02293.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000010588 ; ENSRNOP00000010588 ; ENSRNOG00000007660 .
    GeneIDi 64511.
    KEGGi rno:64511.
    UCSCi RGD:620119. rat.

    Organism-specific databases

    CTDi 2342.
    RGDi 620119. Fntb.

    Phylogenomic databases

    eggNOGi COG5029.
    GeneTreei ENSGT00550000075042.
    HOGENOMi HOG000190594.
    HOVERGENi HBG008173.
    InParanoidi Q02293.
    KOi K05954.
    OMAi KLLDFLW.
    OrthoDBi EOG7P02HV.
    PhylomeDBi Q02293.
    TreeFami TF353162.

    Enzyme and pathway databases

    Reactomei REACT_227662. Inactivation, recovery and regulation of the phototransduction cascade.
    SABIO-RK Q02293.

    Miscellaneous databases

    EvolutionaryTracei Q02293.
    NextBioi 613294.
    PROi Q02293.

    Gene expression databases

    Genevestigatori Q02293.

    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. "cDNA cloning and expression of the peptide-binding beta subunit of rat p21ras farnesyltransferase, the counterpart of yeast DPR1/RAM1."
      Chen W.-J., Andres D.A., Goldstein J.L., Russell D.W., Brown M.S.
      Cell 66:327-334(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Brain.
    2. "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].
      Tissue: Brain.
    3. "Crystal structure of protein farnesyltransferase at 2.25-A resolution."
      Park H.-W., Boduluri S.R., Mooomaw J.F., Casey P.J., Beese L.S.
      Science 275:1800-1804(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH ZINC.
    4. Erratum
      Park H.-W., Boduluri S.R., Mooomaw J.F., Casey P.J., Beese L.S.
      Science 276:21-21(1997)
    5. "Protein farnesyltransferase: structure and implications for substrate binding."
      Dunten P., Kammlott U., Crowther R., Weber D., Palermo R., Birktoft J.
      Biochemistry 37:7907-7912(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC IONS, SUBUNIT, COFACTOR.
    6. "Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate."
      Long S.B., Casey P.J., Beese L.S.
      Biochemistry 37:9612-9618(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC IONS, COFACTOR, SUBUNIT.
    7. "Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue."
      Strickland C.L., Windsor W.T., Syto R., Wang L., Bond R., Wu Z., Schwartz J., Le H.V., Beese L.S., Weber P.C.
      Biochemistry 37:16601-16611(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS AND FARNESYL DIPHOSPHATE ANALOG, COFACTOR, SUBUNIT.
    8. "The basis for K-Ras4B binding specificity to protein farnesyltransferase revealed by 2 A resolution ternary complex structures."
      Long S.B., Casey P.J., Beese L.S.
      Structure 8:209-222(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FNTA AND KRAS, INTERACTION WITH KRAS, CATALYTIC ACTIVITY, COFACTOR, FUNCTION, SUBUNIT.
    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 FNTA AND GERANYLGERANYL DIPHOSPHATE, SUBUNIT.
    10. "Reaction path of protein farnesyltransferase at atomic resolution."
      Long S.B., Casey P.J., Beese L.S.
      Nature 419:645-650(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC IONS, SUBUNIT, COFACTOR.
    11. "Biochemical and structural studies with prenyl diphosphate analogues provide insights into isoprenoid recognition by protein farnesyl transferase."
      Turek-Etienne T.C., Strickland C.L., Distefano M.D.
      Biochemistry 42:3716-3724(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-427 IN COMPLEX WITH FNTA; GERANYLGERANYL DIPHOSPHATE AND ZINC IONS, COFACTOR, SUBUNIT.
    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 (2.25 ANGSTROMS) IN COMPLEX WITH FNTA AND ZINC IONS, COFACTOR, SUBUNIT.
    13. "Caged protein prenyltransferase substrates: tools for understanding protein prenylation."
      DeGraw A.J., Hast M.A., Xu J., Mullen D., Beese L.S., Barany G., Distefano M.D.
      Chem. Biol. Drug Des. 72:171-181(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC, COFACTOR, CATALYTIC ACTIVITY, SUBUNIT.
    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 (1.90 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, SUBUNIT.
    15. Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-427 IN COMPLEX WITH FNTA AND ZINC IONS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, FUNCTION.
    16. Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC, SUBUNIT, COFACTOR.
    17. Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-427 IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC IONS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, FUNCTION.

    Entry informationi

    Entry nameiFNTB_RAT
    AccessioniPrimary (citable) accession number: Q02293
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 133 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3