Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5E9B3 (PGTB2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

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

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.

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

Initiator methionine11Removed By similarity
Chain2 – 331330Geranylgeranyl transferase type-2 subunit beta
PRO_0000244433

Regions

Repeat20 – 6142PFTB 1
Repeat68 – 10942PFTB 2
Repeat116 – 15742PFTB 3
Repeat164 – 20542PFTB 4
Repeat212 – 25342PFTB 5
Repeat260 – 30243PFTB 6
Region190 – 1923Geranylgeranyl diphosphate binding By similarity
Region232 – 24413Geranylgeranyl diphosphate binding By similarity

Sites

Metal binding2381Zinc; catalytic By similarity
Metal binding2401Zinc; catalytic By similarity
Metal binding2901Zinc; via tele nitrogen; catalytic By similarity

Amino acid modifications

Modified residue21N-acetylglycine By similarity
Modified residue31Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5E9B3 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: CB554CA9B22D334A

FASTA33136,972
        10         20         30         40         50         60 
MGTPQKDVII KSDAPDTLLL EKHADYIASY GSKKDDYEYC MSEYLRMSGI YWGLTVMDLM 

        70         80         90        100        110        120 
GQLHRMNREE ILTFIKSCQH ECGGISASIG HDPHLLYTLS AVQILTLYDS INVIDINKVV 

       130        140        150        160        170        180 
EYVQSLQKED GSFAGDIWGE IDTRFSFCAV ATLALLGKLD AINVEKAIEF VLSCMNFDGG 

       190        200        210        220        230        240 
FGCRPGSESH AGQIYCCTGF LAITSQLHQV NSDLLGWWLC ERQLPSGGLN GRPEKLPDVC 

       250        260        270        280        290        300 
YSWWVLASLK IIGRLHWIDR EKLRSFILAC QDEETGGFAD RPGDMVDPFH TLFGIAGLSL 

       310        320        330 
LGEEQIKPVS PVFCMPEEVL RRVNVQPELV S 

« Hide

References

[1]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal medulla.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BT021007 mRNA. Translation: AAX09024.1.
BC147953 mRNA. Translation: AAI47954.1.
RefSeqNP_001015646.1. NM_001015646.1.
UniGeneBt.20263.

3D structure databases

ProteinModelPortalQ5E9B3.
SMRQ5E9B3. Positions 3-331.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5E9B3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID533276.
KEGGbta:533276.

Organism-specific databases

CTD5876.

Phylogenomic databases

eggNOGCOG5029.
HOGENOMHOG000180334.
HOVERGENHBG008182.
InParanoidQ5E9B3.
KOK05956.

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

NextBio20875982.

Entry information

Entry namePGTB2_BOVIN
AccessionPrimary (citable) accession number: Q5E9B3
Secondary accession number(s): A6QLG2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 15, 2005
Last modified: June 11, 2014
This is version 65 of the entry and version 1 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