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P49356

- FNTB_HUMAN

UniProt

P49356 - FNTB_HUMAN

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Protein

Protein farnesyltransferase subunit beta

Gene

FNTB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

Zn2+6 PublicationsNote: 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 farnesyltransferase activity Source: UniProtKB
  3. 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
Complete GO annotation...

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
Complete GO annotation...

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.
ExpressionAtlasiP49356. baseline.
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. 34 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 – 263Combined sources
Helixi28 – 336Combined sources
Helixi43 – 6018Combined sources
Helixi75 – 8511Combined sources
Beta strandi87 – 893Combined sources
Helixi91 – 966Combined sources
Helixi100 – 11314Combined sources
Helixi120 – 13314Combined sources
Beta strandi138 – 1436Combined sources
Helixi150 – 16314Combined sources
Helixi166 – 1694Combined sources
Helixi174 – 1829Combined sources
Beta strandi191 – 1944Combined sources
Helixi201 – 21313Combined sources
Turni219 – 2246Combined sources
Helixi225 – 2328Combined sources
Beta strandi237 – 2393Combined sources
Helixi249 – 26214Combined sources
Helixi265 – 2673Combined sources
Helixi270 – 27910Combined sources
Turni283 – 2853Combined sources
Beta strandi287 – 2915Combined sources
Helixi300 – 3034Combined sources
Turni304 – 3063Combined sources
Helixi307 – 31711Combined sources
Beta strandi325 – 3273Combined sources
Helixi332 – 34211Combined sources
Helixi360 – 37415Combined sources
Beta strandi375 – 3784Combined sources
Beta strandi381 – 3844Combined sources
Helixi390 – 3923Combined sources
Turni399 – 4013Combined sources
Helixi405 – 41612Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

GeneTreeiENSGT00550000075042.
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

        10         20         30         40         50
MASPSSFTYY CPPSSSPVWS EPLYSLRPEH ARERLQDDSV ETVTSIEQAK
60 70 80 90 100
VEEKIQEVFS SYKFNHLVPR LVLQREKHFH YLKRGLRQLT DAYECLDASR
110 120 130 140 150
PWLCYWILHS LELLDEPIPQ IVATDVCQFL ELCQSPEGGF GGGPGQYPHL
160 170 180 190 200
APTYAAVNAL CIIGTEEAYD IINREKLLQY LYSLKQPDGS FLMHVGGEVD
210 220 230 240 250
VRSAYCAASV ASLTNIITPD LFEGTAEWIA RCQNWEGGIG GVPGMEAHGG
260 270 280 290 300
YTFCGLAALV ILKRERSLNL KSLLQWVTSR QMRFEGGFQG RCNKLVDGCY
310 320 330 340 350
SFWQAGLLPL LHRALHAQGD PALSMSHWMF HQQALQEYIL MCCQCPAGGL
360 370 380 390 400
LDKPGKSRDF YHTCYCLSGL SIAQHFGSGA MLHDVVLGVP ENALQPTHPV
410 420 430
YNIGPDKVIQ ATTYFLQKPV PGFEELKDET SAEPATD
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:
EMBLi
GenBanki
DDBJi
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:100529261.
hsa:2342.
UCSCiuc001xia.3. human. [P49356-1]

Polymorphism databases

DMDMi1346696.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 34 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:100529261.
hsa:2342.
UCSCi uc001xia.3. human. [P49356-1 ]

Organism-specific databases

CTDi 100529261.
2342.
GeneCardsi GC14P065381.
HGNCi HGNC:3785. FNTB.
MIMi 134636. gene.
neXtProti NX_P49356.
PharmGKBi PA28202.
GenAtlasi Search...

Phylogenomic databases

GeneTreei ENSGT00550000075042.
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.
ExpressionAtlasi P49356. baseline.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 148 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