Protein geranylgeranyltransferase type I subunit beta

PGGT1B
Identifiers
Aliases	PGGT1B, BGGI, GGTI, protein geranylgeranyltransferase type I subunit beta
External IDs	OMIM: 602031 MGI: 1917514 HomoloGene: 3685 GeneCards: PGGT1B
Gene location (Human) Chr. Chromosome 5 (human) Band 5q22.3 Start 115,204,012 bp End 115,262,877 bp
Gene location (Mouse) Chr. Chromosome 18 (mouse) Band 18|18 C Start 46,368,418 bp End 46,414,060 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in oocyte secondary oocyte monocyte palpebral conjunctiva Achilles tendon rectum islet of Langerhans amniotic fluid bronchial epithelial cell oral cavity Top expressed in hand otolith organ utricle pineal gland renal corpuscle prostate foot lacrimal gland Paneth cell ciliary body More reference expression data BioGPS n/a
Gene ontology Molecular function prenyltransferase activity zinc ion binding protein geranylgeranyltransferase activity metal ion binding catalytic activity isoprenoid binding peptide binding transferase activity CAAX-protein geranylgeranyltransferase activity Cellular component CAAX-protein geranylgeranyltransferase complex Biological process negative regulation of nitric-oxide synthase biosynthetic process positive regulation of cell cycle positive regulation of cell population proliferation response to cytokine protein geranylgeranylation protein prenylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5229 225467 Ensembl ENSG00000164219 ENSMUSG00000024477 UniProt P53609 Q8BUY9 RefSeq (mRNA) NM_005023 NM_172627 RefSeq (protein) NP_005014 NP_766215 Location (UCSC) Chr 5: 115.2 – 115.26 Mb Chr 18: 46.37 – 46.41 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Protein geranylgeranyltransferase type I subunit beta is a protein that in humans is encoded by the PGGT1B gene.

Function

Protein geranylgeranyltransferase type I (GGTase-I) transfers a geranylgeranyl group to the cysteine residue of candidate proteins containing a C-terminal CAAX motif in which 'A' is an aliphatic amino acid and 'X' is leucine (summarized by Zhang et al., 1994 [PubMed 8106351]). The enzyme is composed of a 48-kD alpha subunit (FNTA; MIM 134635) and a 43-kD beta subunit, encoded by the PGGT1B gene. The FNTA gene encodes the alpha subunit for both GGTase-I and the related enzyme farnesyltransferase.[supplied by OMIM, Mar 2010].

Further reading

• Kusama T, Mukai M, Tatsuta M, Matsumoto Y, Nakamura H, Inoue M (2003). "Selective inhibition of cancer cell invasion by a geranylgeranyltransferase-I inhibitor". Clin. Exp. Metastasis. 20 (6): 561–7. doi:10.1023/a:1025898316728. PMID 14598891. S2CID 24756418.
• Reid TS, Terry KL, Casey PJ, Beese LS (October 2004). "Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity". J. Mol. Biol. 343 (2): 417–33. doi:10.1016/j.jmb.2004.08.056. PMID 15451670.
• Comabella M, Craig DW, Morcillo-Suárez C, Río J, Navarro A, Fernández M, Martin R, Montalban X (August 2009). "Genome-wide scan of 500,000 single-nucleotide polymorphisms among responders and nonresponders to interferon beta therapy in multiple sclerosis". Arch. Neurol. 66 (8): 972–8. doi:10.1001/archneurol.2009.150. PMID 19667218.
• Lipkin SM, Chao EC, Moreno V, Rozek LS, Rennert H, Pinchev M, Dizon D, Rennert G, Kopelovich L, Gruber SB (May 2010). "Genetic variation in 3-hydroxy-3-methylglutaryl CoA reductase modifies the chemopreventive activity of statins for colorectal cancer". Cancer Prev Res (Phila). 3 (5): 597–603. doi:10.1158/1940-6207.CAPR-10-0007. PMID 20403997.
• Virtanen SS, Sandholm J, Yegutkin G, Kalervo Väänänen H, Härkönen PL (August 2010). "Inhibition of GGTase-I and FTase disrupts cytoskeletal organization of human PC-3 prostate cancer cells". Cell Biol. Int. 34 (8): 815–26. doi:10.1042/CBI20090288. PMID 20446922. S2CID 44993117.
• Ghavami S, Mutawe MM, Schaafsma D, Yeganeh B, Unruh H, Klonisch T, Halayko AJ (February 2012). "Geranylgeranyl transferase 1 modulates autophagy and apoptosis in human airway smooth muscle". Am. J. Physiol. Lung Cell Mol. Physiol. 302 (4): L420–8. doi:10.1152/ajplung.00312.2011. PMID 22160308. S2CID 13448673.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.