Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha

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Reviewed, UniProtKB/Swiss-Prot P49354 (FNTA_HUMAN)

Last modified November 25, 2008. Version 87. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

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
    Ras proteins prenyltransferase alpha
    FTase-alpha
    Type I protein geranyl-geranyltransferase subunit alpha
      Short name=GGTase-I-alpha

Gene names

Name:

FNTA

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	379 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate.
Catalytic activity	Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate. Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.
Subunit structure	Heterodimer of an alpha and a beta subunit.
Sequence similarities	Belongs to the protein prenyltransferase subunit alpha family. Contains 5 PFTA repeats.

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Ontologies

Keywords
Domain	Repeat
Molecular function	Prenyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	protein amino acid farnesylation Ref.3 Traceable author statement. Source: ProtInc protein amino acid geranylgeranylation Traceable author statement. Source: ProtInc transforming growth factor beta receptor signaling pathway Traceable author statement. Source: ProtInc
Cellular component	cytosol Inferred from Experiment. Source: Reactome
Molecular function	CAAX-protein geranylgeranyltransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct protein farnesyltransferase activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
FNTB	P49356	5	EBI-602336,EBI-602349
PTP4A2	Q12974	1	EBI-602336,EBI-1046324

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 379

379

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha

PRO_0000119746

Regions

Repeat

112 – 146

PFTA 1

Repeat

147 – 180

PFTA 2

Repeat

181 – 215

PFTA 3

Repeat

216 – 249

PFTA 4

Repeat

255 – 289

PFTA 5

Compositional bias

22 – 31

Pro-rich

Amino acid modifications

Modified residue

373

Phosphoserine

Experimental info

Mutagenesis

164

K → N: Reduced activity

Mutagenesis

199

N → K: Reduced catalytic efficiency

Sequence conflict

241

Y → H Ref.2

Secondary structure

379

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P49354-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: E933CBA874AB92B9
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FASTA

379

44,409

        10         20         30         40         50         60 
MAATEGVGEA AQGGEPGQPA QPPPQPHPPP PQQQHKEEMA AEAGEAVASP MDDGFVSLDS 

        70         80         90        100        110        120 
PSYVLYRDRA EWADIDPVPQ NDGPNPVVQI IYSDKFRDVY DYFRAVLQRD ERSERAFKLT 

       130        140        150        160        170        180 
RDAIELNAAN YTVWHFRRVL LKSLQKDLHE EMNYITAIIE EQPKNYQVWH HRRVLVEWLR 

       190        200        210        220        230        240 
DPSQELEFIA DILNQDAKNY HAWQHRQWVI QEFKLWDNEL QYVDQLLKED VRNNSVWNQR 

       250        260        270        280        290        300 
YFVISNTTGY NDRAVLEREV QYTLEMIKLV PHNESAWNYL KGILQDRGLS KYPNLLNQLL 

       310        320        330        340        350        360 
DLQPSHSSPY LIAFLVDIYE DMLENQCDNK EDILNKALEL CEILAKEKDT IRKEYWRYIG 

       370 
RSLQSKHSTE NDSPTNVQQ

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8276393] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 8419339] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF LYS-164.
[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: 8494894] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF ASN-199. Tissue: Placenta.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon and Lung.
[5]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, MASS SPECTROMETRY.
[6]	"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: 11687658] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT; FARNESYL DIPHOSPHATE AND INHIBITOR L-739,750.
[7]	"3-aminopyrrolidinone farnesyltransferase inhibitors: design of macrocyclic compounds with improved pharmacokinetics and excellent cell potency." Bell I.M., Gallicchio S.N., Abrams M., Beese L.S., Beshore D.C., Bhimnathwala H., Bogusky M.J., Buser C.A., Culberson J.C., Davide J., Ellis-Hutchings M., Fernandes C., Gibbs J.B., Graham S.L., Hamilton K.A., Hartman G.D., Heimbrook D.C., Homnick C.F. Zartman C.B. J. Med. Chem. 45:2388-2409(2002) [PubMed: 12036349] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT; FARNESYL DIPHOSPHATE AND INHIBITORS.
[8]	"Dual protein farnesyltransferase-geranylgeranyltransferase-I inhibitors as potential cancer chemotherapeutic agents." deSolms S.J., Ciccarone T.M., MacTough S.C., Shaw A.W., Buser C.A., Ellis-Hutchings M., Fernandes C., Hamilton K.A., Huber H.E., Kohl N.E., Lobell R.B., Robinson R.G., Tsou N.N., Walsh E.S., Graham S.L., Beese L.S., Taylor J.S. J. Med. Chem. 46:2973-2984(2003) [PubMed: 12825937] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT; FARNESYL DIPHOSPHATE AND INHIBITOR.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

L10413 mRNA. Translation: AAA86285.1.
L00634 mRNA. Translation: AAA35853.1.
BC017029 mRNA. Translation: AAH17029.2.
BC084566 mRNA. Translation: AAH84566.1.

PIR

A47659.

RefSeq

NP_001018196.1.
NP_001018197.1.
NP_002018.1.

UniGene

Hs.370312

3D structure databases

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P49354.

PTM databases

PhosphoSite

P49354.

Genome annotation databases

Ensembl

ENSG00000168522. Homo sapiens. [Contig view]

GeneID

2339.

KEGG

hsa:2339.
son:SO_0590.

Organism-specific databases

H-InvDB

HIX0022455.

HGNC

HGNC:3782. FNTA.

HPA

CAB010149.
HPA018830.

MIM

134635. gene.

PharmGKB

PA28199.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P49354.

HOVERGEN

P49354.

Gene expression databases

ArrayExpress

P49354.

CleanEx

HS_FNTA.

GermOnline

ENSG00000168522. Homo sapiens.

Family and domain databases

InterPro

IPR002088. Prenyl_trans_a.
IPR008940. Prenyltransferase.
[Graphical view]

Gene3D

G3DSA:1.25.40.120. Prenyl_trans. 1 hit.

Pfam

PF01239. PPTA. 5 hits.
[Graphical view]

PROSITE

PS51147. PFTA. 5 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

P49354.

NextBio

9495.

SOURCE

Search...

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Entry information

Entry name

FNTA_HUMAN

Accession

Primary (citable) accession number: P49354
Secondary accession number(s): Q9UDC1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	November 25, 2008
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents