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P49354

- FNTA_HUMAN

UniProt

P49354 - FNTA_HUMAN

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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

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 farnesyltransferase activity Source: UniProtKB
  5. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP49354.
CleanExiHS_FNTA.
ExpressionAtlasiP49354. baseline and differential.
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. 18 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 – 683Combined sources
Helixi70 – 723Combined sources
Beta strandi87 – 904Combined sources
Helixi94 – 10916Combined sources
Helixi114 – 12613Combined sources
Helixi131 – 14313Combined sources
Helixi148 – 16114Combined sources
Helixi166 – 17914Combined sources
Helixi185 – 19511Combined sources
Helixi200 – 21314Combined sources
Helixi216 – 2183Combined sources
Helixi219 – 22911Combined sources
Helixi234 – 24613Combined sources
Helixi253 – 26917Combined sources
Helixi274 – 28411Combined sources
Turni285 – 2873Combined sources
Helixi289 – 2913Combined sources
Helixi293 – 30210Combined sources
Turni303 – 3053Combined sources
Helixi309 – 32416Combined sources
Helixi330 – 34617Combined sources
Helixi350 – 3523Combined sources
Helixi353 – 36715Combined sources

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.
GeneTreeiENSGT00550000074935.
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

        10         20         30         40         50
MAATEGVGEA AQGGEPGQPA QPPPQPHPPP PQQQHKEEMA AEAGEAVASP
60 70 80 90 100
MDDGFVSLDS PSYVLYRDRA EWADIDPVPQ NDGPNPVVQI IYSDKFRDVY
110 120 130 140 150
DYFRAVLQRD ERSERAFKLT RDAIELNAAN YTVWHFRRVL LKSLQKDLHE
160 170 180 190 200
EMNYITAIIE EQPKNYQVWH HRRVLVEWLR DPSQELEFIA DILNQDAKNY
210 220 230 240 250
HAWQHRQWVI QEFKLWDNEL QYVDQLLKED VRNNSVWNQR YFVISNTTGY
260 270 280 290 300
NDRAVLEREV QYTLEMIKLV PHNESAWNYL KGILQDRGLS KYPNLLNQLL
310 320 330 340 350
DLQPSHSSPY LIAFLVDIYE DMLENQCDNK EDILNKALEL CEILAKEKDT
360 370
IRKEYWRYIG RSLQSKHSTE NDSPTNVQQ
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. 18 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.
GeneTreei ENSGT00550000074935.
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

Bgeei P49354.
CleanExi HS_FNTA.
ExpressionAtlasi P49354. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 151 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