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P49354

- FNTA_HUMAN

UniProt

P49354 - FNTA_HUMAN

Protein

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha

Gene

FNTA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Essential subunit of both the farnesyltransferase and the geranylgeranyltransferase complex. Contributes to the transfer of a farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. May positively regulate neuromuscular junction development downstream of MUSK via its function in RAC1 prenylation and activation.6 Publications

    Catalytic activityi

    Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate.
    Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.

    Enzyme regulationi

    Activated by the AGRIN-induced phosphorylation which is mediated by MUSK.By similarity

    GO - Molecular functioni

    1. alpha-tubulin binding Source: BHF-UCL
    2. CAAX-protein geranylgeranyltransferase activity Source: UniProtKB-EC
    3. microtubule binding Source: BHF-UCL
    4. protein binding Source: IntAct
    5. protein farnesyltransferase activity Source: UniProtKB
    6. protein geranylgeranyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: Reactome
    2. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
    3. phototransduction, visible light Source: Reactome
    4. positive regulation of deacetylase activity Source: BHF-UCL
    5. positive regulation of tubulin deacetylation Source: BHF-UCL
    6. protein farnesylation Source: UniProtKB
    7. protein geranylgeranylation Source: UniProtKB
    8. regulation of rhodopsin mediated signaling pathway Source: Reactome
    9. rhodopsin mediated signaling pathway Source: Reactome
    10. transforming growth factor beta receptor signaling pathway Source: ProtInc

    Keywords - Molecular functioni

    Prenyltransferase, Transferase

    Enzyme and pathway databases

    ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
    REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (EC:2.5.1.58, EC:2.5.1.59)
    Alternative name(s):
    CAAX farnesyltransferase subunit alpha
    FTase-alpha
    Ras proteins prenyltransferase subunit alpha
    Type I protein geranyl-geranyltransferase subunit alpha
    Short name:
    GGTase-I-alpha
    Gene namesi
    Name:FNTA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:3782. FNTA.

    Subcellular locationi

    GO - Cellular componenti

    1. CAAX-protein geranylgeranyltransferase complex Source: UniProtKB
    2. cytoplasm Source: ProtInc
    3. cytosol Source: Reactome
    4. microtubule associated complex Source: BHF-UCL
    5. protein farnesyltransferase complex Source: UniProtKB

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi164 – 1641K → N: Reduced activity. 1 Publication
    Mutagenesisi199 – 1991N → K: Reduced catalytic efficiency. 1 Publication

    Organism-specific databases

    PharmGKBiPA28199.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 379378Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alphaPRO_0000119746Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei373 – 3731Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated. Phosphorylation is mediated by MUSK upon AGRIN stimulation and results in the activation of FNTA By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP49354.
    PaxDbiP49354.
    PRIDEiP49354.

    PTM databases

    PhosphoSiteiP49354.

    Miscellaneous databases

    PMAP-CutDBP49354.

    Expressioni

    Gene expression databases

    ArrayExpressiP49354.
    BgeeiP49354.
    CleanExiHS_FNTA.
    GenevestigatoriP49354.

    Organism-specific databases

    HPAiCAB010149.
    HPA018830.

    Interactioni

    Subunit structurei

    Interacts with MUSK; the interaction is direct and mediates AGRIN-induced phosphorylation of FNTA By similarity. Heterodimer of FNTA and FNTB (farnesyltransferase). Heterodimer of FNTA and PGGT1B (geranylgeranyltransferase).By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FNTBP493567EBI-602336,EBI-602349

    Protein-protein interaction databases

    BioGridi108625. 14 interactions.
    IntActiP49354. 12 interactions.
    MINTiMINT-238861.
    STRINGi9606.ENSP00000303423.

    Structurei

    Secondary structure

    1
    379
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi66 – 683
    Helixi70 – 723
    Beta strandi87 – 904
    Helixi94 – 10916
    Helixi114 – 12613
    Helixi131 – 14313
    Helixi148 – 16114
    Helixi166 – 17914
    Helixi185 – 19511
    Helixi200 – 21314
    Helixi216 – 2183
    Helixi219 – 22911
    Helixi234 – 24613
    Helixi253 – 26917
    Helixi274 – 28411
    Turni285 – 2873
    Helixi289 – 2913
    Helixi293 – 30210
    Turni303 – 3053
    Helixi309 – 32416
    Helixi330 – 34617
    Helixi350 – 3523
    Helixi353 – 36715

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JCQX-ray2.30A1-379[»]
    1LD7X-ray2.00A1-379[»]
    1LD8X-ray1.80A1-379[»]
    1MZCX-ray2.00A1-379[»]
    1S63X-ray1.90A1-379[»]
    1SA4X-ray2.10A1-379[»]
    1TN6X-ray1.80A1-379[»]
    2F0YX-ray2.70A1-379[»]
    2H6FX-ray1.50A1-379[»]
    2H6GX-ray1.85A1-379[»]
    2H6HX-ray1.80A1-379[»]
    2H6IX-ray3.00A1-379[»]
    2IEJX-ray1.80A1-379[»]
    3E37X-ray1.80A1-379[»]
    DisProtiDP00558.
    ProteinModelPortaliP49354.
    SMRiP49354. Positions 55-369.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49354.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati112 – 14635PFTA 1Add
    BLAST
    Repeati147 – 18034PFTA 2Add
    BLAST
    Repeati181 – 21535PFTA 3Add
    BLAST
    Repeati216 – 24934PFTA 4Add
    BLAST
    Repeati255 – 28935PFTA 5Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi22 – 3110Pro-rich

    Sequence similaritiesi

    Contains 5 PFTA repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5536.
    HOGENOMiHOG000188957.
    HOVERGENiHBG004498.
    InParanoidiP49354.
    KOiK05955.
    OMAiDATDYFR.
    PhylomeDBiP49354.
    TreeFamiTF313038.

    Family and domain databases

    InterProiIPR002088. Prenyl_trans_a.
    [Graphical view]
    PfamiPF01239. PPTA. 5 hits.
    [Graphical view]
    PROSITEiPS51147. PFTA. 5 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P49354-1) [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

    MAATEGVGEA AQGGEPGQPA QPPPQPHPPP PQQQHKEEMA AEAGEAVASP    50
    MDDGFVSLDS PSYVLYRDRA EWADIDPVPQ NDGPNPVVQI IYSDKFRDVY 100
    DYFRAVLQRD ERSERAFKLT RDAIELNAAN YTVWHFRRVL LKSLQKDLHE 150
    EMNYITAIIE EQPKNYQVWH HRRVLVEWLR DPSQELEFIA DILNQDAKNY 200
    HAWQHRQWVI QEFKLWDNEL QYVDQLLKED VRNNSVWNQR YFVISNTTGY 250
    NDRAVLEREV QYTLEMIKLV PHNESAWNYL KGILQDRGLS KYPNLLNQLL 300
    DLQPSHSSPY LIAFLVDIYE DMLENQCDNK EDILNKALEL CEILAKEKDT 350
    IRKEYWRYIG RSLQSKHSTE NDSPTNVQQ 379
    Length:379
    Mass (Da):44,409
    Last modified:February 1, 1996 - v1
    Checksum:iE933CBA874AB92B9
    GO
    Isoform 2 (identifier: P49354-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         68-134: Missing.

    Show »
    Length:312
    Mass (Da):36,493
    Checksum:i789D43774B90D5DA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti241 – 2411Y → H(PubMed:8419339)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei68 – 13467Missing in isoform 2. 1 PublicationVSP_036468Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L10413 mRNA. Translation: AAA86285.1.
    L00634 mRNA. Translation: AAA35853.1.
    AC110275 Genomic DNA. No translation available.
    BT009854 mRNA. Translation: AAP88856.1.
    AK292121 mRNA. Translation: BAF84810.1.
    AC113191 Genomic DNA. No translation available.
    BC017029 mRNA. Translation: AAH17029.2.
    BC084566 mRNA. Translation: AAH84566.1.
    AL698961 mRNA. No translation available.
    CCDSiCCDS6140.1. [P49354-1]
    PIRiA47659.
    RefSeqiNP_002018.1. NM_002027.2. [P49354-1]
    UniGeneiHs.370312.

    Genome annotation databases

    EnsembliENST00000302279; ENSP00000303423; ENSG00000168522. [P49354-1]
    GeneIDi2339.
    KEGGihsa:2339.
    UCSCiuc003xps.3. human. [P49354-1]

    Polymorphism databases

    DMDMi1346694.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L10413 mRNA. Translation: AAA86285.1 .
    L00634 mRNA. Translation: AAA35853.1 .
    AC110275 Genomic DNA. No translation available.
    BT009854 mRNA. Translation: AAP88856.1 .
    AK292121 mRNA. Translation: BAF84810.1 .
    AC113191 Genomic DNA. No translation available.
    BC017029 mRNA. Translation: AAH17029.2 .
    BC084566 mRNA. Translation: AAH84566.1 .
    AL698961 mRNA. No translation available.
    CCDSi CCDS6140.1. [P49354-1 ]
    PIRi A47659.
    RefSeqi NP_002018.1. NM_002027.2. [P49354-1 ]
    UniGenei Hs.370312.

    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 A 1-379 [» ]
    1LD7 X-ray 2.00 A 1-379 [» ]
    1LD8 X-ray 1.80 A 1-379 [» ]
    1MZC X-ray 2.00 A 1-379 [» ]
    1S63 X-ray 1.90 A 1-379 [» ]
    1SA4 X-ray 2.10 A 1-379 [» ]
    1TN6 X-ray 1.80 A 1-379 [» ]
    2F0Y X-ray 2.70 A 1-379 [» ]
    2H6F X-ray 1.50 A 1-379 [» ]
    2H6G X-ray 1.85 A 1-379 [» ]
    2H6H X-ray 1.80 A 1-379 [» ]
    2H6I X-ray 3.00 A 1-379 [» ]
    2IEJ X-ray 1.80 A 1-379 [» ]
    3E37 X-ray 1.80 A 1-379 [» ]
    DisProti DP00558.
    ProteinModelPortali P49354.
    SMRi P49354. Positions 55-369.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108625. 14 interactions.
    IntActi P49354. 12 interactions.
    MINTi MINT-238861.
    STRINGi 9606.ENSP00000303423.

    Chemistry

    BindingDBi P49354.
    ChEMBLi CHEMBL2094108.

    PTM databases

    PhosphoSitei P49354.

    Polymorphism databases

    DMDMi 1346694.

    Proteomic databases

    MaxQBi P49354.
    PaxDbi P49354.
    PRIDEi P49354.

    Protocols and materials databases

    DNASUi 2339.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302279 ; ENSP00000303423 ; ENSG00000168522 . [P49354-1 ]
    GeneIDi 2339.
    KEGGi hsa:2339.
    UCSCi uc003xps.3. human. [P49354-1 ]

    Organism-specific databases

    CTDi 2339.
    GeneCardsi GC08P042928.
    HGNCi HGNC:3782. FNTA.
    HPAi CAB010149.
    HPA018830.
    MIMi 134635. gene.
    neXtProti NX_P49354.
    PharmGKBi PA28199.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5536.
    HOGENOMi HOG000188957.
    HOVERGENi HBG004498.
    InParanoidi P49354.
    KOi K05955.
    OMAi DATDYFR.
    PhylomeDBi P49354.
    TreeFami TF313038.

    Enzyme and pathway databases

    Reactomei REACT_107. Apoptotic cleavage of cellular proteins.
    REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.

    Miscellaneous databases

    EvolutionaryTracei P49354.
    GeneWikii FNTA.
    GenomeRNAii 2339.
    NextBioi 9495.
    PMAP-CutDB P49354.
    PROi P49354.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49354.
    Bgeei P49354.
    CleanExi HS_FNTA.
    Genevestigatori P49354.

    Family and domain databases

    InterProi IPR002088. Prenyl_trans_a.
    [Graphical view ]
    Pfami PF01239. PPTA. 5 hits.
    [Graphical view ]
    PROSITEi PS51147. PFTA. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORM 1).
      Tissue: Retina.
    2. "Mutational analysis of alpha-subunit of protein farnesyltransferase. Evidence for a catalytic role."
      Andres D.A., Goldstein J.L., Ho Y.K., Brown M.S.
      J. Biol. Chem. 268:1383-1390(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF LYS-164, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
    3. "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 ASN-199, CATALYTIC ACTIVITY, FUNCTION.
      Tissue: Placenta.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "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] (ISOFORM 1).
      Tissue: Synovium.
    6. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Colon and Lung.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-261 (ISOFORM 2).
    9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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 FNTB, SUBUNIT.
    16. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FNTB, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY.
    17. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FNTB, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY.
    18. "Crystal structures of the anticancer clinical candidates R115777 (Tipifarnib) and BMS-214662 complexed with protein farnesyltransferase suggest a mechanism of FTI selectivity."
      Reid T.S., Beese L.S.
      Biochemistry 43:6877-6884(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FNTB, SUBUNIT.
    19. "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 FNTB, SUBUNIT.
    20. "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 FNTB, FUNCTION, SUBUNIT, CATALYTIC ACTIVITY.
    21. "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) OF 1-379 IN COMPLEX WITH FNTB, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiFNTA_HUMAN
    AccessioniPrimary (citable) accession number: P49354
    Secondary accession number(s): A6NJW0, Q53XJ9, Q9UDC1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 150 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 8
      Human chromosome 8: 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