Protein geranylgeranyltransferase type I subunit beta

PGGT1B
Identifiers
AliasesPGGT1B, BGGI, GGTI, protein geranylgeranyltransferase type I subunit beta
External IDsOMIM: 602031 MGI: 1917514 HomoloGene: 3685 GeneCards: PGGT1B
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_005023

NM_172627

RefSeq (protein)

NP_005014

NP_766215

Location (UCSC)Chr 5: 115.2 – 115.26 MbChr 18: 46.37 – 46.41 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Protein geranylgeranyltransferase type I subunit beta is a protein that in humans is encoded by the PGGT1B gene. [5]

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].

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000164219 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024477 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Entrez Gene: Protein geranylgeranyltransferase type I subunit beta". Retrieved 2018-09-21.

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.


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