Geranylgeranyl transferase type-2 subunit beta

Details

Name
Geranylgeranyl transferase type-2 subunit beta
Synonyms
  • 2.5.1.60
  • Geranylgeranyl transferase type II subunit beta
  • GGTase-II-beta
  • GGTB
  • Rab geranyl-geranyltransferase subunit beta
  • Rab geranylgeranyltransferase subunit beta
  • Rab GG transferase beta
  • Rab GGTase beta
  • Type II protein geranyl-geranyltransferase subunit beta
Gene Name
RABGGTB
Organism
Humans
Amino acid sequence
>lcl|BSEQ0012837|Geranylgeranyl transferase type-2 subunit beta
MGTPQKDVIIKSDAPDTLLLEKHADYIASYGSKKDDYEYCMSEYLRMSGIYWGLTVMDLM
GQLHRMNREEILAFIKSCQHECGGISASIGHDPHLLYTLSAVQILTLYDSINVIDVNKVV
EYVKGLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGG
FGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVC
YSWWVLASLKIIGRLHWIDREKLRNFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSL
LGEEQIKPVNPVFCMPEEVLQRVNVQPELVS
Number of residues
331
Molecular Weight
36924.04
Theoretical pI
4.66
GO Classification
Functions
Rab geranylgeranyltransferase activity / Rab GTPase binding / zinc ion binding
Processes
cellular protein modification process / protein geranylgeranylation / visual perception
Components
Rab-protein geranylgeranyltransferase complex
General Function
Zinc ion binding
Specific Function
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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0012838|Geranylgeranyl transferase type-2 subunit beta (RABGGTB)
ATGGGCACTCCACAGAAGGATGTTATTATCAAGTCAGATGCACCGGACACTTTGTTATTG
GAGAAACATGCAGATTATATCGCATCCTATGGCTCAAAGAAAGATGATTATGAATACTGT
ATGTCTGAGTATTTGAGAATGAGTGGCATCTATTGGGGTCTGACAGTAATGGATCTCATG
GGACAACTTCATCGCATGAATAGAGAAGAGATTCTGGCATTTATTAAGTCTTGCCAACAT
GAATGTGGTGGAATAAGTGCTAGTATCGGACATGATCCTCATCTTTTATACACTCTTAGT
GCTGTCCAGATTCTTACGCTGTATGACAGTATTAATGTTATTGACGTAAATAAAGTTGTG
GAATATGTTAAAGGTCTACAGAAAGAAGATGGTTCTTTTGCTGGAGATATTTGGGGAGAA
ATTGACACAAGATTCTCTTTTTGTGCGGTGGCAACTTTGGCTTTGTTGGGGAAGCTTGAT
GCTATTAATGTGGAAAAGGCAATCGAATTTGTTTTATCCTGTATGAACTTTGACGGTGGA
TTTGGTTGCAGACCAGGTTCTGAATCCCATGCTGGGCAGATCTATTGTTGCACAGGATTT
CTGGCAATTACAAGTCAGTTGCATCAAGTAAATTCTGATTTACTTGGCTGGTGGCTTTGT
GAACGACAATTACCCTCAGGCGGGCTCAATGGAAGGCCGGAGAAGTTACCAGATGTATGC
TACTCATGGTGGGTCCTGGCTTCCCTAAAGATAATTGGAAGACTTCATTGGATTGATAGA
GAGAAACTGCGTAATTTCATTTTAGCATGTCAAGATGAAGAAACGGGGGGATTTGCAGAC
AGGCCAGGAGATATGGTGGATCCTTTTCATACCTTATTTGGAATTGCTGGATTGTCACTT
TTGGGAGAAGAACAGATTAAACCTGTTAATCCTGTCTTTTGCATGCCTGAAGAAGTGCTT
CAGAGAGTGAATGTTCAGCCTGAGCTAGTGAGCTAG
Chromosome Location
1
Locus
1p31
External Identifiers
ResourceLink
UniProtKB IDP53611
UniProtKB Entry NamePGTB2_HUMAN
GenBank Protein ID1216504
GenBank Gene IDU49245
HGNC IDHGNC:9796
General References
  1. Johannes L, Perez F, Laran-Chich MP, Henry JP, Darchen F: Characterization of the interaction of the monomeric GTP-binding protein Rab3a with geranylgeranyl transferase II. Eur J Biochem. 1996 Jul 15;239(2):362-8. [Article]
  2. van Bokhoven H, Rawson RB, Merkx GF, Cremers FP, Seabra MC: cDNA cloning and chromosomal localization of the genes encoding the alpha- and beta-subunits of human Rab geranylgeranyl transferase: the 3' end of the alpha-subunit gene overlaps with the transglutaminase 1 gene promoter. Genomics. 1996 Dec 1;38(2):133-40. [Article]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  4. Si X, Zeng Q, Ng CH, Hong W, Pallen CJ: Interaction of farnesylated PRL-2, a protein-tyrosine phosphatase, with the beta-subunit of geranylgeranyltransferase II. J Biol Chem. 2001 Aug 31;276(35):32875-82. Epub 2001 Jul 10. [Article]
  5. Farnsworth CC, Seabra MC, Ericsson LH, Gelb MH, Glomset JA: Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A. Proc Natl Acad Sci U S A. 1994 Dec 6;91(25):11963-7. [Article]
  6. Baron RA, Seabra MC: Rab geranylgeranylation occurs preferentially via the pre-formed REP-RGGT complex and is regulated by geranylgeranyl pyrophosphate. Biochem J. 2008 Oct 1;415(1):67-75. doi: 10.1042/BJ20080662. [Article]
  7. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [Article]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [Article]
  9. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [Article]
  10. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [Article]
  11. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04464N-FormylmethionineexperimentalunknownDetails
DB07780Farnesyl diphosphateexperimentalunknownDetails
DB07841Geranylgeranyl diphosphateexperimentalunknownDetails