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P53609 (PGTB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PGGT1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Heterodimer of FNTA and PGGT1B. PGGT1B mediates interaction with substrate peptides. Ref.1

Sequence similarities

Belongs to the protein prenyltransferase subunit beta family.

Contains 4 PFTB repeats.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P53609-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P53609-2)

The sequence of this isoform differs from the canonical sequence as follows:
     205-281: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 377377Geranylgeranyl transferase type-1 subunit beta
PRO_0000119769

Regions

Repeat144 – 18643PFTB 1
Repeat193 – 23442PFTB 2
Repeat245 – 28440PFTB 3
Repeat291 – 33343PFTB 4
Region219 – 2213Geranylgeranyl diphosphate binding By similarity
Region263 – 2664Geranylgeranyl diphosphate binding By similarity
Region272 – 2754Geranylgeranyl diphosphate binding By similarity

Sites

Metal binding2691Zinc; catalytic By similarity
Metal binding2711Zinc; catalytic By similarity
Metal binding3211Zinc; via tele nitrogen; catalytic By similarity

Natural variations

Alternative sequence205 – 28177Missing in isoform 2.
VSP_021827
Natural variant1031I → V.
Corresponds to variant rs34918686 [ dbSNP | Ensembl ].
VAR_034381

Experimental info

Sequence conflict21A → V in AAA35888. Ref.1
Sequence conflict21A → V in AAV98360. Ref.2
Sequence conflict1261Y → C in AAV98360. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 22, 2009. Version 2.
Checksum: AA04C9B34B8A3FDC

FASTA37742,368
        10         20         30         40         50         60 
MAATEDERLA GSGEGERLDF LRDRHVRFFQ RCLQVLPERY SSLETSRLTI AFFALSGLDM 

        70         80         90        100        110        120 
LDSLDVVNKD DIIEWIYSLQ VLPTEDRSNL NRCGFRGSSY LGIPFNPSKA PGTAHPYDSG 

       130        140        150        160        170        180 
HIAMTYTGLS CLVILGDDLS RVNKEACLAG LRALQLEDGS FCAVPEGSEN DMRFVYCASC 

       190        200        210        220        230        240 
ICYMLNNWSG MDMKKAITYI RRSMSYDNGL AQGAGLESHG GSTFCGIASL CLMGKLEEVF 

       250        260        270        280        290        300 
SEKELNRIKR WCIMRQQNGY HGRPNKPVDT CYSFWVGATL KLLKIFQYTN FEKNRNYILS 

       310        320        330        340        350        360 
TQDRLVGGFA KWPDSHPDAL HAYFGICGLS LMEESGICKV HPALNVSTRT SERLLDLHQS 

       370 
WKTKDSKQCS ENVHIST 

« Hide

Isoform 2 [UniParc].

Checksum: BC6D275563263C68
Show »

FASTA30033,830

References

« Hide 'large scale' references
[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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
Tissue: Kidney and Placenta.
[2]Li H., Ke R., Nong W., Shen C., Zhong G., Zhou G., Lin L., Yang S.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[3]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L25441 mRNA. Translation: AAA35888.1.
AY780790 mRNA. Translation: AAV98360.1.
AC008494 Genomic DNA. No translation available.
PIRA53044.
RefSeqNP_005014.2. NM_005023.3.
UniGeneHs.254006.

3D structure databases

ProteinModelPortalP53609.
SMRP53609. Positions 18-363.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111250. 5 interactions.
IntActP53609. 1 interaction.
STRING9606.ENSP00000404676.

Chemistry

BindingDBP53609.
ChEMBLCHEMBL2096991.
DrugBankDB00175. Pravastatin.

PTM databases

PhosphoSiteP53609.

Polymorphism databases

DMDM259016302.

Proteomic databases

PaxDbP53609.
PRIDEP53609.

Protocols and materials databases

DNASU5229.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379615; ENSP00000368935; ENSG00000164219. [P53609-2]
ENST00000419445; ENSP00000404676; ENSG00000164219. [P53609-1]
GeneID5229.
KEGGhsa:5229.
UCSCuc003kqw.4. human. [P53609-1]
uc010jch.3. human. [P53609-2]

Organism-specific databases

CTD5229.
GeneCardsGC05M114575.
H-InvDBHIX0032034.
HGNCHGNC:8895. PGGT1B.
HPAHPA030646.
MIM602031. gene.
neXtProtNX_P53609.
PharmGKBPA33233.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5029.
HOGENOMHOG000180333.
HOVERGENHBG008181.
InParanoidP53609.
KOK11713.
OMAWIYHCQV.
OrthoDBEOG7KDF9Z.
PhylomeDBP53609.
TreeFamTF105968.

Gene expression databases

BgeeP53609.
CleanExHS_PGGT1B.
GenevestigatorP53609.

Family and domain databases

Gene3D1.50.10.20. 1 hit.
InterProIPR001330. Prenyltrans.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PfamPF00432. Prenyltrans. 4 hits.
[Graphical view]
SUPFAMSSF48239. SSF48239. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi5229.
NextBio20214.
PROP53609.
SOURCESearch...

Entry information

Entry namePGTB1_HUMAN
AccessionPrimary (citable) accession number: P53609
Secondary accession number(s): Q5MJP9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 22, 2009
Last modified: April 16, 2014
This is version 123 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM