Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein farnesyltransferase subunit beta

Gene

Fntb

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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.4 Publications

Catalytic activityi

Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate.5 Publications

Cofactori

Zn2+12 PublicationsNote: Binds 1 zinc ion per subunit.12 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei102Important for selectivity against geranylgeranyl diphosphateBy similarity1
Metal bindingi297Zinc; catalytic3 Publications1
Metal bindingi299Zinc; catalytic3 Publications1
Metal bindingi362Zinc; via tele nitrogen; catalytic3 Publications1

GO - Molecular functioni

GO - Biological processi

  • negative regulation of cell proliferation Source: Ensembl
  • positive regulation of cell cycle Source: RGD
  • positive regulation of cell proliferation Source: RGD
  • positive regulation of fibroblast proliferation Source: Ensembl
  • positive regulation of nitric-oxide synthase biosynthetic process Source: RGD
  • protein farnesylation Source: UniProtKB
  • response to cytokine Source: RGD
  • response to inorganic substance Source: RGD
  • response to organic cyclic compound Source: RGD
  • wound healing Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Prenyltransferase, Transferase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi2.5.1.58. 5301.
ReactomeiR-RNO-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
SABIO-RKQ02293.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi620119. Fntb.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2095197.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001197631 – 437Protein farnesyltransferase subunit betaAdd BLAST437

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei432PhosphoserineBy similarity1
Modified residuei436PhosphothreonineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ02293.
PRIDEiQ02293.

PTM databases

iPTMnetiQ02293.
PhosphoSitePlusiQ02293.

Expressioni

Gene expression databases

BgeeiENSRNOG00000007660.
GenevisibleiQ02293. RN.

Interactioni

Subunit structurei

Heterodimer of FNTA and FNTB.14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FntaQ0463114EBI-602454,EBI-602447

Protein-protein interaction databases

DIPiDIP-6132N.
IntActiQ02293. 1 interactor.
MINTiMINT-121917.
STRINGi10116.ENSRNOP00000010588.

Chemistry databases

BindingDBiQ02293.

Structurei

Secondary structure

1437
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi24 – 26Combined sources3
Helixi28 – 33Combined sources6
Helixi43 – 65Combined sources23
Helixi75 – 85Combined sources11
Helixi91 – 96Combined sources6
Helixi100 – 113Combined sources14
Helixi120 – 133Combined sources14
Beta strandi138 – 143Combined sources6
Helixi150 – 163Combined sources14
Helixi166 – 171Combined sources6
Helixi174 – 184Combined sources11
Beta strandi191 – 194Combined sources4
Helixi201 – 213Combined sources13
Turni219 – 224Combined sources6
Helixi225 – 232Combined sources8
Beta strandi237 – 239Combined sources3
Helixi249 – 261Combined sources13
Helixi265 – 267Combined sources3
Helixi270 – 278Combined sources9
Turni283 – 285Combined sources3
Beta strandi287 – 291Combined sources5
Helixi300 – 303Combined sources4
Turni304 – 306Combined sources3
Helixi307 – 317Combined sources11
Beta strandi321 – 323Combined sources3
Beta strandi325 – 327Combined sources3
Helixi332 – 342Combined sources11
Beta strandi348 – 350Combined sources3
Beta strandi352 – 355Combined sources4
Helixi360 – 374Combined sources15
Beta strandi375 – 378Combined sources4
Beta strandi381 – 384Combined sources4
Helixi390 – 392Combined sources3
Turni399 – 401Combined sources3
Helixi405 – 415Combined sources11
Helixi424 – 426Combined sources3
Helixi434 – 436Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D8DX-ray2.00B1-437[»]
1D8EX-ray3.00B1-437[»]
1FPPX-ray2.75B1-437[»]
1FT1X-ray2.25B1-437[»]
1FT2X-ray3.40B22-422[»]
1FTImodel-B22-422[»]
1HZ7model-B41-406[»]
1JCRX-ray2.00B1-437[»]
1JCSX-ray2.20B1-437[»]
1KZOX-ray2.20B1-437[»]
1KZPX-ray2.10B1-437[»]
1KZRmodel-B17-423[»]
1N94X-ray3.50B22-418[»]
1N95X-ray2.30B22-423[»]
1N9AX-ray3.20B22-423[»]
1NI1X-ray2.30B22-423[»]
1NL4X-ray2.70B23-423[»]
1O1RX-ray2.30B1-427[»]
1O1SX-ray2.30B1-427[»]
1O1TX-ray2.10B1-427[»]
1O5MX-ray2.30B1-437[»]
1QBQX-ray2.40B1-437[»]
1QE2model-B41-406[»]
1SA5X-ray2.60B1-437[»]
1TN7X-ray2.30B1-437[»]
1TN8X-ray2.25B1-437[»]
1X81X-ray3.50B22-418[»]
2BEDX-ray2.70B23-423[»]
2FTImodel-B22-422[»]
2R2LX-ray2.23B23-423[»]
2ZIRX-ray2.40B1-437[»]
2ZISX-ray2.60B1-437[»]
3DPYX-ray2.70B1-437[»]
3E30X-ray2.45B1-437[»]
3E32X-ray2.45B1-437[»]
3E33X-ray1.90B1-437[»]
3E34X-ray2.05B1-437[»]
3EU5X-ray2.80B1-427[»]
3EUVX-ray2.75B1-427[»]
3FTImodel-B22-422[»]
3KSLX-ray2.05B1-437[»]
3KSQX-ray2.10B1-437[»]
4GTMX-ray2.20B1-427[»]
4GTOX-ray2.15B1-427[»]
4GTPX-ray2.75B1-427[»]
4GTQX-ray2.60B1-427[»]
4GTRX-ray2.20B1-427[»]
ProteinModelPortaliQ02293.
SMRiQ02293.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02293.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati123 – 164PFTB 1Add BLAST42
Repeati174 – 215PFTB 2Add BLAST42
Repeati222 – 263PFTB 3Add BLAST42
Repeati270 – 312PFTB 4Add BLAST43
Repeati332 – 374PFTB 5Add BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni248 – 251Farnesyl diphosphate binding4
Regioni291 – 294Farnesyl diphosphate binding4
Regioni300 – 303Farnesyl diphosphate binding4

Sequence similaritiesi

Contains 5 PFTB repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0365. Eukaryota.
COG5029. LUCA.
GeneTreeiENSGT00550000075042.
HOGENOMiHOG000190594.
HOVERGENiHBG008173.
InParanoidiQ02293.
KOiK05954.
OMAiFMLRMKD.
OrthoDBiEOG091G08TB.
PhylomeDBiQ02293.
TreeFamiTF353162.

Family and domain databases

CDDicd02893. FTase. 1 hit.
Gene3Di1.50.10.20. 1 hit.
InterProiIPR026872. FTB.
IPR001330. PFTB_repeat.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PANTHERiPTHR11774:SF6. PTHR11774:SF6. 1 hit.
PfamiPF00432. Prenyltrans. 5 hits.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.

Sequencei

Sequence statusi: Complete.

Q02293-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSSSFTYY CPPSSSPVWS EPLYSLRPEH ARERLQDDSV ETVTSIEQAK
60 70 80 90 100
VEEKIQEVFS SYKFNHLVPR LVLQREKHFH YLKRGLRQLT DAYECLDASR
110 120 130 140 150
PWLCYWILHS LELLDEPIPQ IVATDVCQFL ELCQSPDGGF GGGPGQYPHL
160 170 180 190 200
APTYAAVNAL CIIGTEEAYN VINREKLLQY LYSLKQPDGS FLMHVGGEVD
210 220 230 240 250
VRSAYCAASV ASLTNIITPD LFEGTAEWIA RCQNWEGGIG GVPGMEAHGG
260 270 280 290 300
YTFCGLAALV ILKKERSLNL KSLLQWVTSR QMRFEGGFQG RCNKLVDGCY
310 320 330 340 350
SFWQAGLLPL LHRALHAQGD PALSMSHWMF HQQALQEYIL MCCQCPAGGL
360 370 380 390 400
LDKPGKSRDF YHTCYCLSGL SIAQHFGSGA MLHDVVMGVP ENVLQPTHPV
410 420 430
YNIGPDKVIQ ATTHFLQKPV PGFEECEDAV TSDPATD
Length:437
Mass (Da):48,673
Last modified:April 1, 1993 - v1
Checksum:i41A9D6D79CD319A8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M69056 mRNA. Translation: AAA41176.1.
BC087675 mRNA. Translation: AAH87675.1.
PIRiA40037.
RefSeqiNP_742031.1. NM_172034.2.
UniGeneiRn.8873.

Genome annotation databases

EnsembliENSRNOT00000010588; ENSRNOP00000010588; ENSRNOG00000007660.
GeneIDi64511.
KEGGirno:64511.
UCSCiRGD:620119. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M69056 mRNA. Translation: AAA41176.1.
BC087675 mRNA. Translation: AAH87675.1.
PIRiA40037.
RefSeqiNP_742031.1. NM_172034.2.
UniGeneiRn.8873.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D8DX-ray2.00B1-437[»]
1D8EX-ray3.00B1-437[»]
1FPPX-ray2.75B1-437[»]
1FT1X-ray2.25B1-437[»]
1FT2X-ray3.40B22-422[»]
1FTImodel-B22-422[»]
1HZ7model-B41-406[»]
1JCRX-ray2.00B1-437[»]
1JCSX-ray2.20B1-437[»]
1KZOX-ray2.20B1-437[»]
1KZPX-ray2.10B1-437[»]
1KZRmodel-B17-423[»]
1N94X-ray3.50B22-418[»]
1N95X-ray2.30B22-423[»]
1N9AX-ray3.20B22-423[»]
1NI1X-ray2.30B22-423[»]
1NL4X-ray2.70B23-423[»]
1O1RX-ray2.30B1-427[»]
1O1SX-ray2.30B1-427[»]
1O1TX-ray2.10B1-427[»]
1O5MX-ray2.30B1-437[»]
1QBQX-ray2.40B1-437[»]
1QE2model-B41-406[»]
1SA5X-ray2.60B1-437[»]
1TN7X-ray2.30B1-437[»]
1TN8X-ray2.25B1-437[»]
1X81X-ray3.50B22-418[»]
2BEDX-ray2.70B23-423[»]
2FTImodel-B22-422[»]
2R2LX-ray2.23B23-423[»]
2ZIRX-ray2.40B1-437[»]
2ZISX-ray2.60B1-437[»]
3DPYX-ray2.70B1-437[»]
3E30X-ray2.45B1-437[»]
3E32X-ray2.45B1-437[»]
3E33X-ray1.90B1-437[»]
3E34X-ray2.05B1-437[»]
3EU5X-ray2.80B1-427[»]
3EUVX-ray2.75B1-427[»]
3FTImodel-B22-422[»]
3KSLX-ray2.05B1-437[»]
3KSQX-ray2.10B1-437[»]
4GTMX-ray2.20B1-427[»]
4GTOX-ray2.15B1-427[»]
4GTPX-ray2.75B1-427[»]
4GTQX-ray2.60B1-427[»]
4GTRX-ray2.20B1-427[»]
ProteinModelPortaliQ02293.
SMRiQ02293.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6132N.
IntActiQ02293. 1 interactor.
MINTiMINT-121917.
STRINGi10116.ENSRNOP00000010588.

Chemistry databases

BindingDBiQ02293.
ChEMBLiCHEMBL2095197.

PTM databases

iPTMnetiQ02293.
PhosphoSitePlusiQ02293.

Proteomic databases

PaxDbiQ02293.
PRIDEiQ02293.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000010588; ENSRNOP00000010588; ENSRNOG00000007660.
GeneIDi64511.
KEGGirno:64511.
UCSCiRGD:620119. rat.

Organism-specific databases

CTDi2342.
RGDi620119. Fntb.

Phylogenomic databases

eggNOGiKOG0365. Eukaryota.
COG5029. LUCA.
GeneTreeiENSGT00550000075042.
HOGENOMiHOG000190594.
HOVERGENiHBG008173.
InParanoidiQ02293.
KOiK05954.
OMAiFMLRMKD.
OrthoDBiEOG091G08TB.
PhylomeDBiQ02293.
TreeFamiTF353162.

Enzyme and pathway databases

BRENDAi2.5.1.58. 5301.
ReactomeiR-RNO-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
SABIO-RKQ02293.

Miscellaneous databases

EvolutionaryTraceiQ02293.
PROiQ02293.

Gene expression databases

BgeeiENSRNOG00000007660.
GenevisibleiQ02293. RN.

Family and domain databases

CDDicd02893. FTase. 1 hit.
Gene3Di1.50.10.20. 1 hit.
InterProiIPR026872. FTB.
IPR001330. PFTB_repeat.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PANTHERiPTHR11774:SF6. PTHR11774:SF6. 1 hit.
PfamiPF00432. Prenyltrans. 5 hits.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFNTB_RAT
AccessioniPrimary (citable) accession number: Q02293
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: November 30, 2016
This is version 149 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.