Protein farnesyltransferase subunit beta

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Q02293 (FNTB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 110. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Protein farnesyltransferase subunit beta
Short name=FTase-beta
EC=2.5.1.58

Alternative name(s):
CAAX farnesyltransferase subunit beta
Ras proteins prenyltransferase subunit beta

Gene names

Name:

Fntb

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding.
Catalytic activity	Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate.
Cofactor	Binds 1 zinc ion per subunit.
Subunit structure	Heterodimer of an alpha and a beta subunit. Ref.6
Sequence similarities	Belongs to the protein prenyltransferase subunit beta family. Contains 5 PFTB repeats.

Ontologies

Keywords
Domain	Repeat
Ligand	Metal-binding Zinc
Molecular function	Prenyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	positive regulation of cell cycle Inferred from mutant phenotype. Source: RGD positive regulation of cell proliferation Inferred from mutant phenotype. Source: RGD positive regulation of nitric-oxide synthase biosynthetic process Inferred from mutant phenotype. Source: RGD response to cytokine stimulus Inferred from mutant phenotype. Source: RGD response to inorganic substance Inferred from mutant phenotype. Source: RGD response to organic cyclic compound Inferred from mutant phenotype. Source: RGD
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein farnesyltransferase activity Inferred from direct assay Ref.1. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Fnta	Q04631	14	EBI-602454,EBI-602447

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 437

437

Protein farnesyltransferase subunit beta

PRO_0000119763

Regions

Repeat

123 – 164

PFTB 1

Repeat

174 – 215

PFTB 2

Repeat

222 – 263

PFTB 3

Repeat

270 – 312

PFTB 4

Repeat

332 – 374

PFTB 5

Sites

Metal binding

297

Zinc

Metal binding

299

Zinc

Metal binding

362

Zinc

Amino acid modifications

Modified residue

300

Phosphotyrosine By similarity

Secondary structure

437

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q02293 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 41A9D6D79CD319A8
Show »

FASTA

437

48,673

        10         20         30         40         50         60 
MASSSSFTYY CPPSSSPVWS EPLYSLRPEH ARERLQDDSV ETVTSIEQAK VEEKIQEVFS 

        70         80         90        100        110        120 
SYKFNHLVPR LVLQREKHFH YLKRGLRQLT DAYECLDASR PWLCYWILHS LELLDEPIPQ 

       130        140        150        160        170        180 
IVATDVCQFL ELCQSPDGGF GGGPGQYPHL APTYAAVNAL CIIGTEEAYN VINREKLLQY 

       190        200        210        220        230        240 
LYSLKQPDGS FLMHVGGEVD VRSAYCAASV ASLTNIITPD LFEGTAEWIA RCQNWEGGIG 

       250        260        270        280        290        300 
GVPGMEAHGG YTFCGLAALV ILKKERSLNL KSLLQWVTSR QMRFEGGFQG RCNKLVDGCY 

       310        320        330        340        350        360 
SFWQAGLLPL LHRALHAQGD PALSMSHWMF HQQALQEYIL MCCQCPAGGL LDKPGKSRDF 

       370        380        390        400        410        420 
YHTCYCLSGL SIAQHFGSGA MLHDVVMGVP ENVLQPTHPV YNIGPDKVIQ ATTHFLQKPV 

       430 
PGFEECEDAV TSDPATD

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and expression of the peptide-binding beta subunit of rat p21ras farnesyltransferase, the counterpart of yeast DPR1/RAM1." Chen W.-J., Andres D.A., Goldstein J.L., Russell D.W., Brown M.S. Cell 66:327-334(1991) [PubMed: 1855253] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Brain.
[2]	"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: Brain.
[3]	Erratum Park H.-W., Boduluri S.R., Mooomaw J.F., Casey P.J., Beese L.S. Science 276:21-21(1997)
[4]	"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: 9065406] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
[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: 9657673] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS).
[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 ALPHA SUBUNIT AND GERANYLGERANYL DIPHOSPHATE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M69056 mRNA. Translation: AAA41176.1.
BC087675 mRNA. Translation: AAH87675.1.

IPI

IPI00205139.

PIR

A40037.

RefSeq

NP_742031.1. NM_172034.2.

UniGene

Rn.8873.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D8D	X-ray	2.00	B	1-437	[»]
1D8E	X-ray	3.00	B	1-437	[»]
1FPP	X-ray	2.75	B	1-437	[»]
1FT1	X-ray	2.25	B	1-437	[»]
1FT2	X-ray	3.40	B	22-422	[»]
1FTI	model	-	B	22-422	[»]
1HZ7	model	-	B	41-406	[»]
1JCR	X-ray	2.00	B	1-437	[»]
1JCS	X-ray	2.20	B	1-437	[»]
1KZO	X-ray	2.20	B	1-437	[»]
1KZP	X-ray	2.10	B	1-437	[»]
1KZR	model	-	B	17-423	[»]
1N94	X-ray	3.50	B	22-418	[»]
1N95	X-ray	2.30	B	22-423	[»]
1N9A	X-ray	3.20	B	22-423	[»]
1NI1	X-ray	2.30	B	22-423	[»]
1NL4	X-ray	2.70	B	23-423	[»]
1O1R	X-ray	2.30	B	1-427	[»]
1O1S	X-ray	2.30	B	1-427	[»]
1O1T	X-ray	2.10	B	1-427	[»]
1O5M	X-ray	2.30	B	1-437	[»]
1QBQ	X-ray	2.40	B	1-437	[»]
1QE2	model	-	B	41-406	[»]
1SA5	X-ray	2.60	B	1-437	[»]
1TN7	X-ray	2.30	B	1-437	[»]
1TN8	X-ray	2.25	B	1-437	[»]
1X81	X-ray	3.50	B	22-418	[»]
2BED	X-ray	2.70	B	23-423	[»]
2FTI	model	-	B	22-422	[»]
2R2L	X-ray	2.23	B	23-423	[»]
2ZIR	X-ray	2.40	B	1-437	[»]
2ZIS	X-ray	2.60	B	1-437	[»]
3DPY	X-ray	2.70	B	1-437	[»]
3E30	X-ray	2.45	B	1-437	[»]
3E32	X-ray	2.45	B	1-437	[»]
3E33	X-ray	1.90	B	1-437	[»]
3E34	X-ray	2.05	B	1-437	[»]
3EU5	X-ray	2.80	B	1-427	[»]
3EUV	X-ray	2.75	B	1-427	[»]
3FTI	model	-	B	22-422	[»]
3KSL	X-ray	2.05	B	1-437	[»]
3KSQ	X-ray	2.10	B	1-437	[»]

ProteinModelPortal

Q02293.

SMR

Q02293. Positions 22-437.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6132N.

IntAct

Q02293. 1 interaction.

MINT

MINT-121917.

STRING

Q02293.

PTM databases

PhosphoSite

Q02293.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000010588; ENSRNOP00000010588; ENSRNOG00000007660.

GeneID

64511.

KEGG

rno:64511.

UCSC

NM_172034. rat.

Organism-specific databases

CTD

2342.

RGD

620119. Fntb.

Phylogenomic databases

eggNOG

roNOG14622.

GeneTree

ENSGT00550000075042.

HOVERGEN

HBG008173.

InParanoid

Q02293.

OMA

QEYILLC.

OrthoDB

EOG4KKZ33.

PhylomeDB

Q02293.

Gene expression databases

ArrayExpress

Q02293.

Genevestigator

Q02293.

GermOnline

ENSRNOG00000007660. Rattus norvegicus.

Family and domain databases

InterPro

IPR001330. Prenyltrans.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]

K05954.

Pfam

PF00432. Prenyltrans. 5 hits.
[Graphical view]

SUPFAM

SSF48239. Terp_cyc_toroid. 1 hit.

ProtoNet

Search...

Other

NextBio

613294.

Entry information

Entry name

FNTB_RAT

Accession

Primary (citable) accession number: Q02293

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	November 16, 2011
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents