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Protein

Geranylgeranyl transferase type-1 subunit beta

Gene

Pggt1b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of proteins with the C-terminal sequence Cys-aliphatic-aliphatic-X. Known substrates include RAC1, RAC2, RAP1A and RAP1B.1 Publication

Catalytic activityi

Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.1 Publication

Cofactori

Zn2+3 PublicationsNote: Binds 1 zinc ion per subunit.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi269 – 2691Zinc; catalytic
Metal bindingi271 – 2711Zinc; catalytic
Metal bindingi321 – 3211Zinc; via tele nitrogen; catalytic

GO - Molecular functioni

  • CAAX-protein geranylgeranyltransferase activity Source: UniProtKB
  • protein geranylgeranyltransferase activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • negative regulation of nitric-oxide synthase biosynthetic process Source: RGD
  • positive regulation of cell cycle Source: RGD
  • positive regulation of cell proliferation Source: RGD
  • protein geranylgeranylation Source: UniProtKB
  • response to cytokine Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Prenyltransferase, Transferase

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Geranylgeranyl transferase type-1 subunit beta (EC:2.5.1.59)
Alternative name(s):
Geranylgeranyl transferase type I subunit beta
Short name:
GGTase-I-beta
Type I protein geranyl-geranyltransferase subunit beta
Gene namesi
Name:Pggt1b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 18

Organism-specific databases

RGDi621754. Pggt1b.

Subcellular locationi

GO - Cellular componenti

  • CAAX-protein geranylgeranyltransferase complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2111479.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 377377Geranylgeranyl transferase type-1 subunit betaPRO_0000119771Add
BLAST

Proteomic databases

PaxDbiP53610.
PRIDEiP53610.

Expressioni

Gene expression databases

GenevisibleiP53610. RN.

Interactioni

Subunit structurei

Heterodimer of FNTA and PGGT1B. PGGT1B mediates interaction with substrate peptides.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FntaQ046315EBI-602610,EBI-602447

Protein-protein interaction databases

DIPiDIP-33953N.
IntActiP53610. 1 interaction.
STRINGi10116.ENSRNOP00000004723.

Structurei

Secondary structure

1
377
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 3413Combined sources
Helixi38 – 469Combined sources
Helixi47 – 6014Combined sources
Helixi64 – 663Combined sources
Helixi69 – 779Combined sources
Helixi90 – 923Combined sources
Beta strandi97 – 993Combined sources
Helixi122 – 13413Combined sources
Helixi144 – 15411Combined sources
Beta strandi161 – 1644Combined sources
Helixi172 – 18413Combined sources
Helixi188 – 1903Combined sources
Helixi193 – 20210Combined sources
Beta strandi208 – 2136Combined sources
Helixi220 – 23314Combined sources
Helixi236 – 2394Combined sources
Helixi242 – 25312Combined sources
Beta strandi256 – 2605Combined sources
Helixi272 – 28211Combined sources
Helixi286 – 2883Combined sources
Helixi291 – 2999Combined sources
Turni304 – 3063Combined sources
Beta strandi311 – 3155Combined sources
Helixi319 – 33113Combined sources
Turni342 – 3454Combined sources
Helixi348 – 36114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N4PX-ray2.65B/D/F/H/J/L1-377[»]
1N4QX-ray2.40B/D/F/H/J/L1-377[»]
1N4RX-ray2.80B/D/F/H/J/L1-377[»]
1N4SX-ray2.60B/D/F/H/J/L1-377[»]
1S64X-ray2.55B/D/F/H/J/L1-377[»]
1TNBX-ray2.85B/D/F/H/J/L1-377[»]
1TNOX-ray2.70B/D/F/H/J/L1-377[»]
1TNUX-ray2.70B/D/F/H/J/L1-377[»]
1TNYX-ray2.70B/D/F/H/J/L1-377[»]
1TNZX-ray2.90B/D/F/H/J/L1-377[»]
ProteinModelPortaliP53610.
SMRiP53610. Positions 18-363.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53610.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati144 – 18643PFTB 1Add
BLAST
Repeati193 – 23442PFTB 2Add
BLAST
Repeati245 – 28440PFTB 3Add
BLAST
Repeati291 – 33343PFTB 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni219 – 2213Geranylgeranyl diphosphate binding
Regioni263 – 2664Geranylgeranyl diphosphate binding
Regioni272 – 2754Geranylgeranyl diphosphate binding

Sequence similaritiesi

Contains 4 PFTB repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0367. Eukaryota.
COG5029. LUCA.
GeneTreeiENSGT00530000063392.
HOGENOMiHOG000180333.
HOVERGENiHBG008181.
InParanoidiP53610.
KOiK11713.
OMAiQMDGFQG.
OrthoDBiEOG7KDF9Z.
PhylomeDBiP53610.
TreeFamiTF105968.

Family and domain databases

Gene3Di1.50.10.20. 1 hit.
InterProiIPR001330. PFTB_repeat.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PfamiPF00432. Prenyltrans. 4 hits.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.

Sequencei

Sequence statusi: Complete.

P53610-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATEDDRLA GSGEGERLDF LRDRHVRFFQ RCLQVLPERY SSLETSRLTI
60 70 80 90 100
AFFALSGLDM LDSLDVVNKD DIIEWIYSLQ VLPTEDRSNL DRCGFRGSSY
110 120 130 140 150
LGIPFNPSKN PGTAHPYDSG HIAMTYTGLS CLIILGDDLS RVDKEACLAG
160 170 180 190 200
LRALQLEDGS FCAVPEGSEN DMRFVYCASC ICYMLNNWSG MDMKKAISYI
210 220 230 240 250
RRSMSYDNGL AQGAGLESHG GSTFCGIASL CLMGKLEEVF SEKELNRIKR
260 270 280 290 300
WCIMRQQNGY HGRPNKPVDT CYSFWVGATL KLLKIFQYTN FEKNRNYILS
310 320 330 340 350
TQDRLVGGFA KWPDSHPDAL HAYFGICGLS LMEESGICKV HPALNVSTRT
360 370
SERLRDLHQS WKTKDSKQCS DNVHISS
Length:377
Mass (Da):42,414
Last modified:October 1, 1996 - v1
Checksum:iAADEC7301A4A4011
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L24116 mRNA. Translation: AAA17756.1.
PIRiB53044.
RefSeqiNP_112344.1. NM_031082.1.
UniGeneiRn.10031.

Genome annotation databases

EnsembliENSRNOT00000004723; ENSRNOP00000004723; ENSRNOG00000003541.
GeneIDi81746.
KEGGirno:81746.
UCSCiRGD:621754. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L24116 mRNA. Translation: AAA17756.1.
PIRiB53044.
RefSeqiNP_112344.1. NM_031082.1.
UniGeneiRn.10031.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N4PX-ray2.65B/D/F/H/J/L1-377[»]
1N4QX-ray2.40B/D/F/H/J/L1-377[»]
1N4RX-ray2.80B/D/F/H/J/L1-377[»]
1N4SX-ray2.60B/D/F/H/J/L1-377[»]
1S64X-ray2.55B/D/F/H/J/L1-377[»]
1TNBX-ray2.85B/D/F/H/J/L1-377[»]
1TNOX-ray2.70B/D/F/H/J/L1-377[»]
1TNUX-ray2.70B/D/F/H/J/L1-377[»]
1TNYX-ray2.70B/D/F/H/J/L1-377[»]
1TNZX-ray2.90B/D/F/H/J/L1-377[»]
ProteinModelPortaliP53610.
SMRiP53610. Positions 18-363.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-33953N.
IntActiP53610. 1 interaction.
STRINGi10116.ENSRNOP00000004723.

Chemistry

ChEMBLiCHEMBL2111479.

Proteomic databases

PaxDbiP53610.
PRIDEiP53610.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000004723; ENSRNOP00000004723; ENSRNOG00000003541.
GeneIDi81746.
KEGGirno:81746.
UCSCiRGD:621754. rat.

Organism-specific databases

CTDi5229.
RGDi621754. Pggt1b.

Phylogenomic databases

eggNOGiKOG0367. Eukaryota.
COG5029. LUCA.
GeneTreeiENSGT00530000063392.
HOGENOMiHOG000180333.
HOVERGENiHBG008181.
InParanoidiP53610.
KOiK11713.
OMAiQMDGFQG.
OrthoDBiEOG7KDF9Z.
PhylomeDBiP53610.
TreeFamiTF105968.

Miscellaneous databases

EvolutionaryTraceiP53610.
PROiP53610.

Gene expression databases

GenevisibleiP53610. RN.

Family and domain databases

Gene3Di1.50.10.20. 1 hit.
InterProiIPR001330. PFTB_repeat.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PfamiPF00432. Prenyltrans. 4 hits.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "cDNA cloning and expression of rat and human protein geranylgeranyltransferase type-I."
    Zhang F.L., Diehl R.E., Kohl N.E., Gibbs J.B., Giros B., Casey P.J., Omer C.A.
    J. Biol. Chem. 269:3175-3180(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Structure of mammalian protein geranylgeranyltransferase type-I."
    Taylor J.S., Reid T.S., Terry K.L., Casey P.J., Beese L.S.
    EMBO J. 22:5963-5974(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS; SUBSTRATE PEPTIDE AND ISPRENOID ANALOG, SUBUNIT, COFACTOR, FUNCTION, CATALYTIC ACTIVITY.
  3. "Crystallographic analysis reveals that anticancer clinical candidate L-778,123 inhibits protein farnesyltransferase and geranylgeranyltransferase-I by different binding modes."
    Reid T.S., Long S.B., Beese L.S.
    Biochemistry 43:9000-9008(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS AND INHIBITOR, SUBUNIT, COFACTOR.
  4. "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 (2.70 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS AND SUBSTRATES, SUBUNIT, COFACTOR.

Entry informationi

Entry nameiPGTB1_RAT
AccessioniPrimary (citable) accession number: P53610
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 124 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, 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.