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
- FunctionsRab geranylgeranyltransferase activity / Rab GTPase binding / zinc ion bindingProcessescellular protein modification process / protein geranylgeranylation / visual perceptionComponentsRab-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
- Prenyltrans (PF00432)
- 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
Resource Link UniProtKB ID P53611 UniProtKB Entry Name PGTB2_HUMAN GenBank Protein ID 1216504 GenBank Gene ID U49245 HGNC ID HGNC:9796 - General References
- 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]
- 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]
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- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]