Search by BoMiProt ID - Bomi5980


Primary Information

BoMiProt ID Bomi5980
Protein Name Geranylgeranyl transferase type-2 subunit alpha/Geranylgeranyl transferase type II subunit alpha/Rab geranyl-geranyltransferase subunit alpha/Rab GG transferase alpha/Rab GGTase alpha/Rab geranylgeranyltransferase subunit alpha
Organism Bos taurus
Uniprot IdQ5EA80
Milk FractionWhey
Ref Sequence Id NP_001015614.1
Aminoacid Length 567
Molecular Weight 64945
Fasta Sequence https://www.uniprot.org/uniprot/Q5EA80.fasta
Gene Name RABGGTA
Gene Id 516619
Protein Existence Status reviewed

Secondary Information

Protein Function  Expression of DN GGTase I alpha-subunit inhibited insulin's ability to increase DNA synthesis, cell count, GGTase I activity, amounts of prenylated p21Ras and RhoA, and magnitude of phosphorylation of MAP kinase.
Biochemical Properties 7 FTase and GGTase I are heterodimers and share the same a-subunit,8 whereas the b-subunit confers substrate specificity.
PTMs Phosphorylation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|Q5EA80|PGTA_BOVIN Geranylgeranyl transferase type-2 subunit alpha OS=Bos taurus OX=9913 GN=RABGGTA PE=2 SV=1 MHGRLKVKTSEEQAEAKRLEREQKLKLYQAATQTVFQKRQAGELDESVLELTSQILGANP DFATLWNCRREVLQQLEVQKSPEELATLVKAELGFLES*98CLRVNPKSYGTWHHRCWLLSRL PEPNWARELELCARFLEVDERNFHCWDYRRFVAAQAAVPPAEELAFTDSLITRNFSNYSS WHYRSCLLPQLHPQPDSGPQGRLPEDVLLKELELVQNAFFTDPNDQSAWFYHRWLLGRAD PQDALRCLHVSRDEACLTVSFSRPLLVGSGMETLLLMVDESPLAVEWRTPEGRNRPSHIW LCDLPATSLNDQLPQHTFRVIWTAGDAQKECVLLKGRQEGWCRDSATDEQLFRCELSVEK STVLQSELESCKELQELEPENKWCLLTIILLMRALDPLQYEKETLQYFQTLKAVDPMRAA YLDDLRSKFLLENSVLKMEYAEVRVLHLGHKDLTVLCHLEQLLLVTHLDLSHNRLRALPP ALAALRCLEVLQANDNAIESLDGVTNLPRLQELILCNNRLQQPAVLQPLTSCPRLTLLNL QGNPLCQAEGSSEHLAELLPSVSSILT
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs Insulin promotes the phosphorylation and activation of FTase and GGTase I and thereby increases the amounts of prenylated p21Ras and RhoA.
Additional Comments 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.
Bibliography 1.Solomon CS, Leitner JW, Goalstone ML. Dominant negative alpha-subunit of farnesyl- and geranylgeranyl-transferase I inhibits insulin-induced differentiation of 3T3-L1 pre-adipocytes. Int J Obes Relat Metab Disord. 2003 Jan;27(1):40-7. doi: 10.1038/sj.ijo.0802189. PMID: 12532152. 2.Moores SL, Schaber MD, Mosser SD, Rands E, O’Hara MB, Garsky VM, Marshall MS, Pompliano DL, Gibbs JB. Sequence dependence of protein isoprenylation. J Biol Chem 1991; 266: 4603 – 4610. 3. Caplin BE, Hettich LA, Marshall MS. Substrate characterization of the Saccharomyces cerevisiae protein farnesyltransferase and type-I protein geranylgeranyltransferase. Biochim Biophys Acta 1994; 1205: 39 – 48. 4. Golovchenko I, Goalstone ML, Watson P, Brownlee M, Draznin B. Hyperinsulinemia enhances transcriptional activity of NFkB induced by angiotensin II, hyperglycemia and advanced glycosylation end products in vascular smooth muscle cells. Circul Res 2000; 87: 746 – 752. 5. Chappell J, Golovchenko I, Wall K, Stjernholm J, Leitner JW, Goalstone M, Draznin B. Potentiation of Rho-A-mediated lysophophatidic acid activity by hyperinsulinemia. J Biol Chem 2000; 275: 31792 – 31797.