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Q04631

- FNTA_RAT

UniProt

Q04631 - FNTA_RAT

Protein

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha

Gene

Fnta

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      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.4 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. CAAX-protein geranylgeranyltransferase activity Source: UniProtKB-EC
    2. protein binding Source: IntAct
    3. protein farnesyltransferase activity Source: RGD
    4. protein geranylgeranyltransferase activity Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Prenyltransferase, Transferase

    Enzyme and pathway databases

    SABIO-RKQ04631.

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

    Organism-specific databases

    RGDi2625. Fnta.

    Subcellular locationi

    GO - Cellular componenti

    1. CAAX-protein geranylgeranyltransferase complex Source: RGD
    2. cytoplasm Source: RGD
    3. protein farnesyltransferase complex Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 377376Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alphaPRO_0000119748Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    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

    Proteomic databases

    PaxDbiQ04631.
    PRIDEiQ04631.

    PTM databases

    PhosphoSiteiQ04631.

    Expressioni

    Gene expression databases

    GenevestigatoriQ04631.

    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 similarity16 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FntbQ0229314EBI-602447,EBI-602454
    KRASP01116-22EBI-602447,EBI-367427From a different organism.
    Pggt1bP536105EBI-602447,EBI-602610

    Protein-protein interaction databases

    DIPiDIP-6131N.
    IntActiQ04631. 8 interactions.
    MINTiMINT-121907.
    STRINGi10116.ENSRNOP00000019594.

    Structurei

    Secondary structure

    1
    377
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi58 – 603
    Helixi66 – 683
    Helixi70 – 723
    Beta strandi73 – 753
    Beta strandi87 – 904
    Helixi94 – 10916
    Helixi114 – 12613
    Helixi131 – 14313
    Helixi148 – 16114
    Helixi166 – 17914
    Turni182 – 1843
    Helixi185 – 19511
    Helixi200 – 21314
    Helixi216 – 2183
    Helixi219 – 22911
    Turni230 – 2323
    Helixi234 – 24613
    Beta strandi250 – 2523
    Helixi253 – 26917
    Beta strandi270 – 2723
    Helixi274 – 28411
    Turni285 – 2873
    Helixi289 – 2913
    Helixi293 – 3008
    Helixi303 – 3064
    Helixi309 – 32416
    Helixi330 – 34617
    Turni347 – 3493
    Helixi350 – 3523
    Helixi353 – 36715
    Turni369 – 3724

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D8DX-ray2.00A1-377[»]
    1D8EX-ray3.00A1-377[»]
    1FPPX-ray2.75A1-377[»]
    1FT1X-ray2.25A1-377[»]
    1FT2X-ray3.40A55-369[»]
    1FTImodel-A55-369[»]
    1HZ7model-A116-247[»]
    1JCRX-ray2.00A1-377[»]
    1JCSX-ray2.20A1-377[»]
    1KZOX-ray2.20A1-377[»]
    1KZPX-ray2.10A1-377[»]
    1KZRmodel-A55-377[»]
    1N4PX-ray2.65A/C/E/G/I/K1-377[»]
    1N4QX-ray2.40A/C/E/G/I/K1-377[»]
    1N4RX-ray2.80A/C/E/G/I/K1-377[»]
    1N4SX-ray2.60A/C/E/G/I/K1-377[»]
    1N94X-ray3.50A55-369[»]
    1N95X-ray2.30A55-369[»]
    1N9AX-ray3.20A55-369[»]
    1NI1X-ray2.30A55-369[»]
    1NL4X-ray2.70A55-366[»]
    1O1RX-ray2.30A1-377[»]
    1O1SX-ray2.30A1-377[»]
    1O1TX-ray2.10A1-377[»]
    1O5MX-ray2.30A1-377[»]
    1QBQX-ray2.40A45-377[»]
    1QE2model-A116-247[»]
    1S64X-ray2.55A/C/E/G/I/K1-377[»]
    1SA5X-ray2.60A1-377[»]
    1TN7X-ray2.30A1-377[»]
    1TN8X-ray2.25A1-377[»]
    1TNBX-ray2.85A/C/E/G/I/K1-377[»]
    1TNOX-ray2.70A/C/E/G/I/K1-377[»]
    1TNUX-ray2.70A/C/E/G/I/K1-377[»]
    1TNYX-ray2.70A/C/E/G/I/K1-377[»]
    1TNZX-ray2.90A/C/E/G/I/K1-377[»]
    1X81X-ray3.50A55-369[»]
    2BEDX-ray2.70A54-366[»]
    2FTImodel-A55-369[»]
    2R2LX-ray2.23A54-368[»]
    2ZIRX-ray2.40A1-377[»]
    2ZISX-ray2.60A1-377[»]
    3DPYX-ray2.70A1-377[»]
    3E30X-ray2.45A1-377[»]
    3E32X-ray2.45A1-377[»]
    3E33X-ray1.90A1-377[»]
    3E34X-ray2.05A1-377[»]
    3EU5X-ray2.80A1-377[»]
    3EUVX-ray2.75A1-377[»]
    3FTImodel-A55-369[»]
    3KSLX-ray2.05A1-377[»]
    3KSQX-ray2.10A1-377[»]
    4GTMX-ray2.20A1-377[»]
    4GTOX-ray2.15A1-377[»]
    4GTPX-ray2.75A1-377[»]
    4GTQX-ray2.60A1-377[»]
    4GTRX-ray2.20A1-377[»]
    ProteinModelPortaliQ04631.
    SMRiQ04631. Positions 55-377.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ04631.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati112 – 14635PFTA 1Add
    BLAST
    Repeati147 – 18135PFTA 2Add
    BLAST
    Repeati182 – 21433PFTA 3Add
    BLAST
    Repeati215 – 24935PFTA 4Add
    BLAST
    Repeati255 – 28935PFTA 5Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi22 – 309Pro-rich

    Sequence similaritiesi

    Contains 5 PFTA repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5536.
    HOGENOMiHOG000188957.
    HOVERGENiHBG004498.
    InParanoidiQ04631.
    KOiK05955.
    PhylomeDBiQ04631.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

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

    Q04631-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAATEGVGES APGGEPGQPE QPPPPPPPPP AQQPQEEEMA AEAGEAAASP    50
    MDDGFLSLDS PTYVLYRDRA EWADIDPVPQ NDGPSPVVQI IYSEKFRDVY 100
    DYFRAVLQRD ERSERAFKLT RDAIELNAAN YTVWHFRRVL LRSLQKDLQE 150
    EMNYIIAIIE EQPKNYQVWH HRRVLVEWLK DPSQELEFIA DILNQDAKNY 200
    HAWQHRQWVI QEFRLWDNEL QYVDQLLKED VRNNSVWNQR HFVISNTTGY 250
    SDRAVLEREV QYTLEMIKLV PHNESAWNYL KGILQDRGLS RYPNLLNQLL 300
    DLQPSHSSPY LIAFLVDIYE DMLENQCDNK EDILNKALEL CEILAKEKDT 350
    IRKEYWRYIG RSLQSKHSRE SDIPASV 377
    Length:377
    Mass (Da):44,049
    Last modified:October 1, 1993 - v1
    Checksum:iDFFFECC1B88BC080
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81225 mRNA. Translation: AAA41833.1.
    PIRiA41625.
    RefSeqiNP_036979.1. NM_012847.1.
    UniGeneiRn.5990.

    Genome annotation databases

    GeneIDi25318.
    KEGGirno:25318.
    UCSCiRGD:2625. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81225 mRNA. Translation: AAA41833.1 .
    PIRi A41625.
    RefSeqi NP_036979.1. NM_012847.1.
    UniGenei Rn.5990.

    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 A 1-377 [» ]
    1D8E X-ray 3.00 A 1-377 [» ]
    1FPP X-ray 2.75 A 1-377 [» ]
    1FT1 X-ray 2.25 A 1-377 [» ]
    1FT2 X-ray 3.40 A 55-369 [» ]
    1FTI model - A 55-369 [» ]
    1HZ7 model - A 116-247 [» ]
    1JCR X-ray 2.00 A 1-377 [» ]
    1JCS X-ray 2.20 A 1-377 [» ]
    1KZO X-ray 2.20 A 1-377 [» ]
    1KZP X-ray 2.10 A 1-377 [» ]
    1KZR model - A 55-377 [» ]
    1N4P X-ray 2.65 A/C/E/G/I/K 1-377 [» ]
    1N4Q X-ray 2.40 A/C/E/G/I/K 1-377 [» ]
    1N4R X-ray 2.80 A/C/E/G/I/K 1-377 [» ]
    1N4S X-ray 2.60 A/C/E/G/I/K 1-377 [» ]
    1N94 X-ray 3.50 A 55-369 [» ]
    1N95 X-ray 2.30 A 55-369 [» ]
    1N9A X-ray 3.20 A 55-369 [» ]
    1NI1 X-ray 2.30 A 55-369 [» ]
    1NL4 X-ray 2.70 A 55-366 [» ]
    1O1R X-ray 2.30 A 1-377 [» ]
    1O1S X-ray 2.30 A 1-377 [» ]
    1O1T X-ray 2.10 A 1-377 [» ]
    1O5M X-ray 2.30 A 1-377 [» ]
    1QBQ X-ray 2.40 A 45-377 [» ]
    1QE2 model - A 116-247 [» ]
    1S64 X-ray 2.55 A/C/E/G/I/K 1-377 [» ]
    1SA5 X-ray 2.60 A 1-377 [» ]
    1TN7 X-ray 2.30 A 1-377 [» ]
    1TN8 X-ray 2.25 A 1-377 [» ]
    1TNB X-ray 2.85 A/C/E/G/I/K 1-377 [» ]
    1TNO X-ray 2.70 A/C/E/G/I/K 1-377 [» ]
    1TNU X-ray 2.70 A/C/E/G/I/K 1-377 [» ]
    1TNY X-ray 2.70 A/C/E/G/I/K 1-377 [» ]
    1TNZ X-ray 2.90 A/C/E/G/I/K 1-377 [» ]
    1X81 X-ray 3.50 A 55-369 [» ]
    2BED X-ray 2.70 A 54-366 [» ]
    2FTI model - A 55-369 [» ]
    2R2L X-ray 2.23 A 54-368 [» ]
    2ZIR X-ray 2.40 A 1-377 [» ]
    2ZIS X-ray 2.60 A 1-377 [» ]
    3DPY X-ray 2.70 A 1-377 [» ]
    3E30 X-ray 2.45 A 1-377 [» ]
    3E32 X-ray 2.45 A 1-377 [» ]
    3E33 X-ray 1.90 A 1-377 [» ]
    3E34 X-ray 2.05 A 1-377 [» ]
    3EU5 X-ray 2.80 A 1-377 [» ]
    3EUV X-ray 2.75 A 1-377 [» ]
    3FTI model - A 55-369 [» ]
    3KSL X-ray 2.05 A 1-377 [» ]
    3KSQ X-ray 2.10 A 1-377 [» ]
    4GTM X-ray 2.20 A 1-377 [» ]
    4GTO X-ray 2.15 A 1-377 [» ]
    4GTP X-ray 2.75 A 1-377 [» ]
    4GTQ X-ray 2.60 A 1-377 [» ]
    4GTR X-ray 2.20 A 1-377 [» ]
    ProteinModelPortali Q04631.
    SMRi Q04631. Positions 55-377.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6131N.
    IntActi Q04631. 8 interactions.
    MINTi MINT-121907.
    STRINGi 10116.ENSRNOP00000019594.

    Chemistry

    BindingDBi Q04631.
    ChEMBLi CHEMBL2095197.

    PTM databases

    PhosphoSitei Q04631.

    Proteomic databases

    PaxDbi Q04631.
    PRIDEi Q04631.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 25318.
    KEGGi rno:25318.
    UCSCi RGD:2625. rat.

    Organism-specific databases

    CTDi 2339.
    RGDi 2625. Fnta.

    Phylogenomic databases

    eggNOGi COG5536.
    HOGENOMi HOG000188957.
    HOVERGENi HBG004498.
    InParanoidi Q04631.
    KOi K05955.
    PhylomeDBi Q04631.

    Enzyme and pathway databases

    SABIO-RK Q04631.

    Miscellaneous databases

    EvolutionaryTracei Q04631.
    NextBioi 606153.
    PROi Q04631.

    Gene expression databases

    Genevestigatori Q04631.

    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. "Cloning and expression of a cDNA encoding the alpha subunit of rat p21ras protein farnesyltransferase."
      Chen W.-J., Andres D.A., Goldstein J.L., Brown M.S.
      Proc. Natl. Acad. Sci. U.S.A. 88:11368-11372(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Brain.
    2. "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), SUBUNIT.
    3. Erratum
      Park H.-W., Boduluri S.R., Mooomaw J.F., Casey P.J., Beese L.S.
      Science 276:21-21(1997)
    4. "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) OF 1-377 IN COMPLEX WITH FNTB, SUBUNIT.
    5. "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 FNTB, SUBUNIT.
    6. "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) OF 45-377 IN COMPLEX WITH FNTB, SUBUNIT.
    7. Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-377 IN COMPLEX WITH FNTB, 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) OF 1-377 IN COMPLEX WITH FNTB, 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 FNTB, 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) OF 1-377 IN COMPLEX WITH FNTB, SUBUNIT.
    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 1-377 IN COMPLEX WITH FNTB, SUBUNIT.
    12. Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 55-369 IN COMPLEX WITH FNTB, SUBUNIT, CATALYTIC ACTIVITY.
    13. "Structure of mammalian protein geranylgeranyltransferase type-I."
      Taylor J.S., Reid T.S., Terry K.L., Casey P.J., Beese L.S.
      EMBO J. 22:5963-5974(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH PGGT1B, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION.
    14. "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 (2.60 ANGSTROMS) IN COMPLEX WITH FNTB, SUBUNIT.
    15. "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 FNTB, SUBUNIT.
    16. "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 FNTB, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION.
    17. Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS), SUBUNIT, CATALYTIC ACTIVITY, FUNCTION.
    18. Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH FNTB, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION.

    Entry informationi

    Entry nameiFNTA_RAT
    AccessioniPrimary (citable) accession number: Q04631
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 121 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