P53609 (PGTB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

PGGT1B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Acts on the Rac1, Rac2, Rap1A and Rap1B proteins. The beta subunit is responsible for peptide-binding.
Catalytic activity	Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Heterodimer of an alpha and a beta subunit.
Sequence similarities	Belongs to the protein prenyltransferase subunit beta family. Contains 4 PFTB repeats.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	Metal-binding Zinc
Molecular function	Prenyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of nitric-oxide synthase biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of cell cycle Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara protein geranylgeranylation Traceable author statement Ref.1. Source: ProtInc response to cytokine stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	CAAX-protein geranylgeranyltransferase complex Traceable author statement Ref.1. Source: ProtInc
Molecular_function	CAAX-protein geranylgeranyltransferase activity Traceable author statement Ref.1. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 377	377	Geranylgeranyl transferase type-1 subunit beta		PRO_0000119769
Regions
	Repeat	144 – 186	43	PFTB 1
	Repeat	193 – 234	42	PFTB 2
	Repeat	245 – 284	40	PFTB 3
	Repeat	291 – 333	43	PFTB 4
Sites
	Metal binding	269	1	Zinc By similarity
	Metal binding	271	1	Zinc By similarity
	Metal binding	321	1	Zinc By similarity
Natural variations
	Alternative sequence	205 – 281	77	Missing in isoform 2.		VSP_021827
	Natural variant	103	1	I → V. Corresponds to variant rs34918686 [ dbSNP | Ensembl ].		VAR_034381
Experimental info
	Sequence conflict	2	1	A → V in AAA35888. Ref.1
	Sequence conflict	2	1	A → V in AAV98360. Ref.2
	Sequence conflict	126	1	Y → C in AAV98360. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 22, 2009. Version 2. Checksum: AA04C9B34B8A3FDC	FASTA	377	42,368
	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
	Isoform 2 [UniParc]. Checksum: BC6D275563263C68	FASTA	300	33,830
	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 RRSMLLKIFQ YTNFEKNRNY ILSTQDRLVG GFAKWPDSHP 250 260 270 280 290 300 DALHAYFGIC GLSLMEESGI CKVHPALNVS TRTSERLLDL HQSWKTKDSK QCSENVHIST

References

	« Hide 'large scale' referencesShow '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). 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. , 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.
IPI	IPI00022759. IPI00549741.
PIR	A53044.
RefSeq	NP_005014.2. NM_005023.3.
UniGene	Hs.254006.
3D structure databases
ProteinModelPortal	P53609.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000404676.
PTM databases
PhosphoSite	P53609.
Polymorphism databases
DMDM	259016302.
Proteomic databases
PaxDb	P53609.
PRIDE	P53609.
Protocols and materials databases
DNASU	5229.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000379615; ENSP00000368935; ENSG00000164219. ENST00000419445; ENSP00000404676; ENSG00000164219.
GeneID	5229.
KEGG	hsa:5229.
UCSC	uc003kqw.4. human. uc010jch.3. human.
Organism-specific databases
CTD	5229.
GeneCards	GC05M114575.
H-InvDB	HIX0032034.
HGNC	HGNC:8895. PGGT1B.
HPA	HPA030646.
MIM	602031. gene.
neXtProt	NX_P53609.
PharmGKB	PA33233.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5029.
HOGENOM	HOG000180333.
HOVERGEN	HBG008181.
InParanoid	P53609.
KO	K11713.
OMA	FILSTQD.
OrthoDB	EOG4KD6MC.
PhylomeDB	P53609.
Gene expression databases
Bgee	P53609.
CleanEx	HS_PGGT1B.
Genevestigator	P53609.
GermOnline	ENSG00000164219. Homo sapiens.
Family and domain databases
InterPro	IPR001330. Prenyltrans. IPR008930. Terpenoid_cyclase/PrenylTrfase. [Graphical view]
Pfam	PF00432. Prenyltrans. 4 hits. [Graphical view]
SUPFAM	SSF48239. Terp_cyc_toroid. 1 hit.
ProtoNet	Search...
Other
BindingDB	P53609.
ChEMBL	CHEMBL4135.
DrugBank	DB00175. Pravastatin.
GenomeRNAi	5229.
NextBio	20214.
SOURCE	Search...

Entry information

Entry name

PGTB1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.