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

P53611 (PGTB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. 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·Interactions·Sequence annotation·Sequences·References·Web links·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
Synonyms:GGTB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

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).

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. Ref.5 Ref.7

Sequence similarities

Belongs to the protein prenyltransferase subunit beta family.

Contains 6 PFTB repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARAFP103983EBI-536715,EBI-365961

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 331330Geranylgeranyl transferase type-2 subunit beta
PRO_0000119772

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

Amino acid modifications

Modified residue21N-acetylglycine Ref.10 Ref.11
Modified residue31Phosphothreonine Ref.8 Ref.11

Experimental info

Sequence conflict1531L → F in AAA91473. Ref.1
Sequence conflict1771F → S in CAA69383. Ref.3
Sequence conflict2111N → T in CAA69383. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P53611 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 37A8A6329146C49B

FASTA33136,924
        10         20         30         40         50         60 
MGTPQKDVII KSDAPDTLLL EKHADYIASY GSKKDDYEYC MSEYLRMSGI YWGLTVMDLM 

        70         80         90        100        110        120 
GQLHRMNREE ILAFIKSCQH ECGGISASIG HDPHLLYTLS AVQILTLYDS INVIDVNKVV 

       130        140        150        160        170        180 
EYVKGLQKED 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 EKLRNFILAC QDEETGGFAD RPGDMVDPFH TLFGIAGLSL 

       310        320        330 
LGEEQIKPVN PVFCMPEEVL QRVNVQPELV S 

« Hide

References

« Hide 'large scale' references
[1]Chang H.Y., Wu S.R., Peng H.L.
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Characterization of the interaction of the monomeric GTP-binding protein Rab3a with geranylgeranyl transferase II."
Johannes L., Perez F., Laran-Chich M.P., Henry J.P., Darchen F.
Eur. J. Biochem. 239:362-368(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"cDNA cloning and chromosomal localization of the genes encoding the alpha- and beta-subunits of human Rab geranylgeranyl transferase: the 3' end of the alpha-subunit gene overlaps with the transglutaminase 1 gene promoter."
van Bokhoven H., Rawson R.B., Merkx G.F.M., Cremers F.P.M., Seabra M.C.
Genomics 38:133-140(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetal brain.
[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: Skeletal muscle.
[5]"Interaction of farnesylated PRL-2, a protein-tyrosine phosphatase, with the beta-subunit of geranylgeranyltransferase II."
Si X., Zeng Q., Ng C.H., Hong W., Pallen C.J.
J. Biol. Chem. 276:32875-32882(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTP4A2.
[6]"Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A."
Farnsworth C.C., Seabra M.C., Ericsson L.H., Gelb M.H., Glomset J.A.
Proc. Natl. Acad. Sci. U.S.A. 91:11963-11967(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[7]"Rab geranylgeranylation occurs preferentially via the pre-formed REP-RGGT complex and is regulated by geranylgeranyl pyrophosphate."
Baron R.A., Seabra M.C.
Biochem. J. 415:67-75(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[8]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Wikipedia

Rab geranylgeranyltransferase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U49245 mRNA. Translation: AAA91473.1.
X98001 mRNA. Translation: CAA66638.1.
Y08201 mRNA. Translation: CAA69383.1.
BC020790 mRNA. Translation: AAH20790.1.
CCDSCCDS669.1.
PIRG02431.
RefSeqNP_004573.2. NM_004582.3.
UniGeneHs.78948.

3D structure databases

ProteinModelPortalP53611.
SMRP53611. Positions 5-331.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111814. 7 interactions.
IntActP53611. 2 interactions.
MINTMINT-260716.
STRING9606.ENSP00000317473.

Chemistry

BindingDBP53611.

PTM databases

PhosphoSiteP53611.

Polymorphism databases

DMDM2506788.

Proteomic databases

MaxQBP53611.
PaxDbP53611.
PRIDEP53611.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000319942; ENSP00000317473; ENSG00000137955.
GeneID5876.
KEGGhsa:5876.
UCSCuc001dgy.2. human.

Organism-specific databases

CTD5876.
GeneCardsGC01P076251.
HGNCHGNC:9796. RABGGTB.
HPAHPA026585.
HPA027167.
MIM179080. gene.
neXtProtNX_P53611.
PharmGKBPA34157.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5029.
HOGENOMHOG000180334.
HOVERGENHBG008182.
InParanoidP53611.
KOK05956.
OMAESHAGLI.
OrthoDBEOG7XSTDZ.
PhylomeDBP53611.
TreeFamTF105762.

Enzyme and pathway databases

BRENDA2.5.1.60. 2681.

Gene expression databases

ArrayExpressP53611.
BgeeP53611.
CleanExHS_RABGGTB.
GenevestigatorP53611.

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. 5 hits.
[Graphical view]
SUPFAMSSF48239. SSF48239. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRABGGTB. human.
GenomeRNAi5876.
NextBio22832.
PROP53611.
SOURCESearch...

Entry information

Entry namePGTB2_HUMAN
AccessionPrimary (citable) accession number: P53611
Secondary accession number(s): Q92697
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM