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P53612 (PGTB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Geranylgeranyl transferase type-2 subunit beta

EC=2.5.1.60
Alternative name(s):
Geranylgeranyl transferase type II subunit beta
Short name=GGTase-II-beta
Rab geranyl-geranyltransferase subunit beta
Short name=Rab GG transferase beta
Short name=Rab GGTase beta
Rab geranylgeranyltransferase subunit beta
Type II protein geranyl-geranyltransferase subunit beta
Gene names
Name:Rabggtb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A. Ref.5

Catalytic activity

Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate. Ref.5

Cofactor

Binds 1 zinc ion per subunit. Ref.5

Enzyme regulation

The enzymatic reaction requires the aid of a Rab escort protein (also called component A), such as CHM.

Subunit structure

Heterotrimer composed of RABGGTA, RABGGTB and CHM; within this trimer, RABGGTA and RABGGTB form the catalytic component B, while CHM (component A) mediates peptide substrate binding. The Rab GGTase dimer (RGGT) interacts with CHM (component A) prior to Rab protein binding; the association is stabilized by geranylgeranyl pyrophosphate (GGpp). The CHM:RGGT:Rab complex is destabilized by GGpp. Interaction of RABGGTB with prenylated PTP4A2 precludes its association with RABGGTA and inhibits enzyme activity By similarity. Ref.5

Tissue specificity

Ubiquitous. Detected in all the major organs in adult animals. Ref.2

Developmental stage

Specific expression was elevated in mid-gestation stages, particularly developing liver and spinal cord. Ref.2

Induction

Increased dramatically by cycloheximide (CHX) treatment within a short time (as early as 2 hours). Actinomycin D was used to determine the half-life, CHX treatment resulted in a dramatic increase of the half-life from 8 hours to greater than 12 hours. Ref.2

Sequence similarities

Belongs to the protein prenyltransferase subunit beta family.

Contains 6 PFTB repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 339339Geranylgeranyl transferase type-2 subunit beta
PRO_0000119773

Regions

Repeat28 – 6942PFTB 1
Repeat76 – 11742PFTB 2
Repeat124 – 16542PFTB 3
Repeat172 – 21342PFTB 4
Repeat220 – 26142PFTB 5
Repeat268 – 31043PFTB 6
Region198 – 2003Geranylgeranyl diphosphate binding By similarity
Region240 – 25213Geranylgeranyl diphosphate binding By similarity
Region249 – 2524Geranylgeranyl diphosphate binding By similarity

Sites

Metal binding2461Zinc; catalytic
Metal binding2481Zinc; catalytic
Metal binding2981Zinc; via tele nitrogen; catalytic

Amino acid modifications

Modified residue111Phosphothreonine By similarity

Experimental info

Sequence conflict2301R → A in AAB01502. Ref.1
Sequence conflict2361G → A in AAB01502. Ref.1
Sequence conflict2411P → R in AAB01502. Ref.1
Sequence conflict267 – 2682DR → VS in AAB01502. Ref.1

Secondary structure

............................................... 339
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53612 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 4765A39E5392B8B5

FASTA33937,803
        10         20         30         40         50         60 
MGSLLFSWKG TQQKDVTIKS DAPDTLLLEK HADYIASYGS KKDDYEYCMS EYLRMSGVYW 

        70         80         90        100        110        120 
GLTVMDLMGQ LHRMNREEIL VFIKSCQHEC GGISASIGHD PHLLYTLSAV QILTLYDSVH 

       130        140        150        160        170        180 
VINVDKVVAY VQSLQKEDGS FAGDIWGEID TRFSFCAVAT LALLGKLDAI NVEKAIEFVL 

       190        200        210        220        230        240 
SCMNFDGGFG CRPGSESHAG QIYCCTGFLA ITSQLHQVNS DLLGWWLCER QLPSGGLNGR 

       250        260        270        280        290        300 
PEKLPDVCYS WWVLASLKII GRLHWIDREK LRSFILACQD EETGGFADRP GDMVDPFHTL 

       310        320        330 
FGIAGLSLLG EEQIKPVSPV FCMPEEVLQR VNVQPELVS 

« Hide

References

« Hide 'large scale' references
[1]"Studies of cloning, chromosomal mapping, and embryonic expression of the mouse Rab geranylgeranyl transferase beta subunit."
Wei L.-N., Lee C.-H., Chinpaisal C., Copeland N.G., Gilbert D.J., Jenkins N.A., Hsu Y.-C.
Cell Growth Differ. 6:607-614(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: CD-1.
Tissue: Embryo.
[2]"Studies of the mouse Rab geranylgeranyl transferase beta subunit: gene structure, expression and regulation."
Chinpaisal C., Lee C.-H., Wei L.-N.
Gene 184:237-243(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
Strain: CD-1.
Tissue: Embryo.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"Structure-guided development of selective RabGGTase inhibitors."
Bon R.S., Guo Z., Stigter E.A., Wetzel S., Menninger S., Wolf A., Choidas A., Alexandrov K., Blankenfeldt W., Goody R.S., Waldmann H.
Angew. Chem. Int. Ed. Engl. 50:4957-4961(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 10-339 IN COMPLEX WITH ZINC AND GERANYLGERANYL DIPHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U12922 mRNA. Translation: AAB01502.1.
CH466532 Genomic DNA. Translation: EDL11902.1.
BC132473 mRNA. Translation: AAI32474.1.
BC138547 mRNA. Translation: AAI38548.1.
CCDSCCDS17923.1.
PIRI49116.
JC6177.
RefSeqNP_035361.2. NM_011231.2.
UniGeneMm.277831.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3PZ1X-ray1.95B10-339[»]
3PZ2X-ray2.35B10-339[»]
3PZ3X-ray2.00B10-339[»]
ProteinModelPortalP53612.
SMRP53612. Positions 13-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000087396.

PTM databases

PhosphoSiteP53612.

Proteomic databases

MaxQBP53612.
PaxDbP53612.
PRIDEP53612.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000167111; ENSMUSP00000129481; ENSMUSG00000038975.
GeneID19352.
KEGGmmu:19352.
UCSCuc008rug.2. mouse.

Organism-specific databases

CTD5876.
MGIMGI:99537. Rabggtb.

Phylogenomic databases

eggNOGCOG5029.
GeneTreeENSGT00530000063392.
HOGENOMHOG000180334.
HOVERGENHBG008182.
InParanoidA2RTE6.
KOK05956.
OMAESHAGLI.
TreeFamTF105762.

Gene expression databases

ArrayExpressP53612.
BgeeP53612.
CleanExMM_RABGGTB.
GenevestigatorP53612.

Family and domain databases

Gene3D1.50.10.20. 1 hit.
InterProIPR001330. Prenyltrans.
IPR026873. Ptb1.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PANTHERPTHR11774:SF9. PTHR11774:SF9. 1 hit.
PfamPF00432. Prenyltrans. 2 hits.
[Graphical view]
SUPFAMSSF48239. SSF48239. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP53612.
NextBio296383.
PROP53612.
SOURCESearch...

Entry information

Entry namePGTB2_MOUSE
AccessionPrimary (citable) accession number: P53612
Secondary accession number(s): A2RTE6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot