ID PGTB2_HUMAN Reviewed; 331 AA. AC P53611; Q92697; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 27-MAR-2024, entry version 195. DE RecName: Full=Geranylgeranyl transferase type-2 subunit beta; DE EC=2.5.1.60 {ECO:0000269|PubMed:7991565}; DE AltName: Full=Geranylgeranyl transferase type II subunit beta; DE Short=GGTase-II-beta; DE AltName: Full=Rab geranyl-geranyltransferase subunit beta; DE Short=Rab GG transferase beta; DE Short=Rab GGTase beta; DE AltName: Full=Rab geranylgeranyltransferase subunit beta; DE AltName: Full=Type II protein geranyl-geranyltransferase subunit beta; GN Name=RABGGTB; Synonyms=GGTB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RA Chang H.Y., Wu S.R., Peng H.L.; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=8706741; DOI=10.1111/j.1432-1033.1996.0362u.x; RA Johannes L., Perez F., Laran-Chich M.P., Henry J.P., Darchen F.; RT "Characterization of the interaction of the monomeric GTP-binding protein RT Rab3a with geranylgeranyl transferase II."; RL Eur. J. Biochem. 239:362-368(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Fetal brain; RX PubMed=8954794; DOI=10.1006/geno.1996.0608; RA van Bokhoven H., Rawson R.B., Merkx G.F.M., Cremers F.P.M., Seabra M.C.; RT "cDNA cloning and chromosomal localization of the genes encoding the RT alpha- and beta-subunits of human Rab geranylgeranyl transferase: the 3' RT end of the alpha-subunit gene overlaps with the transglutaminase 1 gene RT promoter."; RL Genomics 38:133-140(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skeletal muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP INTERACTION WITH PTP4A2. RX PubMed=11447212; DOI=10.1074/jbc.m010400200; RA Si X., Zeng Q., Ng C.H., Hong W., Pallen C.J.; RT "Interaction of farnesylated PRL-2, a protein-tyrosine phosphatase, with RT the beta-subunit of geranylgeranyltransferase II."; RL J. Biol. Chem. 276:32875-32882(2001). RN [6] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=7991565; DOI=10.1073/pnas.91.25.11963; RA Farnsworth C.C., Seabra M.C., Ericsson L.H., Gelb M.H., Glomset J.A.; RT "Rab geranylgeranyl transferase catalyzes the geranylgeranylation of RT adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A."; RL Proc. Natl. Acad. Sci. U.S.A. 91:11963-11967(1994). RN [7] RP SUBUNIT, AND ACTIVITY REGULATION. RX PubMed=18532927; DOI=10.1042/bj20080662; RA Baron R.A., Seabra M.C.; RT "Rab geranylgeranylation occurs preferentially via the pre-formed REP-RGGT RT complex and is regulated by geranylgeranyl pyrophosphate."; RL Biochem. J. 415:67-75(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT THR-3, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RAB8A. RX PubMed=26824392; DOI=10.7554/elife.12813; RA Steger M., Tonelli F., Ito G., Davies P., Trost M., Vetter M., Wachter S., RA Lorentzen E., Duddy G., Wilson S., Baptista M.A., Fiske B.K., Fell M.J., RA Morrow J.A., Reith A.D., Alessi D.R., Mann M.; RT "Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates RT a subset of Rab GTPases."; RL Elife 5:0-0(2016). CC -!- FUNCTION: Catalyzes the transfer of a geranylgeranyl moiety from CC geranylgeranyl diphosphate to both cysteines of Rab proteins with the CC C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A CC and RAB7A. {ECO:0000269|PubMed:7991565}. CC -!- CATALYTIC ACTIVITY: CC Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] = CC diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]; CC Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537, CC ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533, CC ChEBI:CHEBI:86021; EC=2.5.1.60; CC Evidence={ECO:0000269|PubMed:7991565}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:Q08603}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q08603}; CC -!- ACTIVITY REGULATION: The enzymatic reaction requires the aid of a Rab CC escort protein (also called component A). CC {ECO:0000269|PubMed:18532927}. CC -!- SUBUNIT: Heterotrimer composed of RABGGTA, RABGGTB and CHM; within this CC trimer, RABGGTA and RABGGTB form the catalytic component B, while CHM CC (component A) mediates peptide substrate binding (PubMed:18532927). The CC Rab GGTase dimer (RGGT) interacts with CHM (component A) prior to Rab CC protein binding; the association is stabilized by geranylgeranyl CC pyrophosphate (GGpp) (PubMed:18532927). The CHM:RGGT:Rab complex is CC destabilized by GGpp (PubMed:18532927). Interaction of RABGGTB with CC prenylated PTP4A2 precludes its association with RABGGTA and inhibits CC enzyme activity (PubMed:11447212). Interacts with CHODL (By CC similarity). Interacts with non-phosphorylated form of RAB8A; CC phosphorylation of RAB8A at 'Thr-72' disrupts this interaction CC (PubMed:26824392). {ECO:0000250|UniProtKB:P53612, CC ECO:0000269|PubMed:11447212, ECO:0000269|PubMed:18532927, CC ECO:0000269|PubMed:26824392}. CC -!- INTERACTION: CC P53611; P10398: ARAF; NbExp=3; IntAct=EBI-536715, EBI-365961; CC P53611; Q9UBV7: B4GALT7; NbExp=6; IntAct=EBI-536715, EBI-10319970; CC P53611; P24592: IGFBP6; NbExp=3; IntAct=EBI-536715, EBI-947015; CC P53611; Q92696: RABGGTA; NbExp=4; IntAct=EBI-536715, EBI-9104196; CC P53611; Q7Z5A9: TAFA1; NbExp=3; IntAct=EBI-536715, EBI-10257895; CC P53611; Q86YD3: TMEM25; NbExp=3; IntAct=EBI-536715, EBI-10260688; CC P53611; P57081: WDR4; NbExp=6; IntAct=EBI-536715, EBI-750427; CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta CC family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Rab geranylgeranyltransferase entry; CC URL="https://en.wikipedia.org/wiki/Rab_geranylgeranyltransferase"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U49245; AAA91473.1; -; mRNA. DR EMBL; X98001; CAA66638.1; -; mRNA. DR EMBL; Y08201; CAA69383.1; -; mRNA. DR EMBL; BC020790; AAH20790.1; -; mRNA. DR CCDS; CCDS669.1; -. DR PIR; G02431; G02431. DR RefSeq; NP_004573.2; NM_004582.3. DR PDB; 6J6X; X-ray; 2.96 A; B=1-331. DR PDB; 6J74; X-ray; 3.21 A; B=1-331. DR PDB; 6J7F; X-ray; 2.88 A; B=1-331. DR PDB; 6J7X; X-ray; 2.75 A; B=1-331. DR PDB; 6O60; X-ray; 2.50 A; B=1-331. DR PDBsum; 6J6X; -. DR PDBsum; 6J74; -. DR PDBsum; 6J7F; -. DR PDBsum; 6J7X; -. DR PDBsum; 6O60; -. DR AlphaFoldDB; P53611; -. DR SMR; P53611; -. DR BioGRID; 111814; 99. DR ComplexPortal; CPX-2919; Protein geranylgeranyltransferase type II complex. DR IntAct; P53611; 63. DR MINT; P53611; -. DR STRING; 9606.ENSP00000317473; -. DR ChEMBL; CHEMBL4523994; -. DR DrugBank; DB07780; Farnesyl diphosphate. DR DrugBank; DB07841; Geranylgeranyl diphosphate. DR DrugBank; DB04464; N-Formylmethionine. DR GlyGen; P53611; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P53611; -. DR PhosphoSitePlus; P53611; -. DR BioMuta; RABGGTB; -. DR DMDM; 2506788; -. DR EPD; P53611; -. DR jPOST; P53611; -. DR MassIVE; P53611; -. DR PaxDb; 9606-ENSP00000317473; -. DR PeptideAtlas; P53611; -. DR ProteomicsDB; 56591; -. DR Pumba; P53611; -. DR Antibodypedia; 19716; 84 antibodies from 23 providers. DR DNASU; 5876; -. DR Ensembl; ENST00000319942.8; ENSP00000317473.3; ENSG00000137955.16. DR GeneID; 5876; -. DR KEGG; hsa:5876; -. DR MANE-Select; ENST00000319942.8; ENSP00000317473.3; NM_004582.4; NP_004573.2. DR AGR; HGNC:9796; -. DR CTD; 5876; -. DR DisGeNET; 5876; -. DR GeneCards; RABGGTB; -. DR HGNC; HGNC:9796; RABGGTB. DR HPA; ENSG00000137955; Low tissue specificity. DR MIM; 179080; gene. DR neXtProt; NX_P53611; -. DR OpenTargets; ENSG00000137955; -. DR PharmGKB; PA34157; -. DR VEuPathDB; HostDB:ENSG00000137955; -. DR eggNOG; KOG0366; Eukaryota. DR GeneTree; ENSGT00950000183128; -. DR HOGENOM; CLU_028946_3_0_1; -. DR InParanoid; P53611; -. DR OMA; VKRCQCP; -. DR OrthoDB; 5478505at2759; -. DR PhylomeDB; P53611; -. DR TreeFam; TF105762; -. DR BRENDA; 2.5.1.60; 2681. DR PathwayCommons; P53611; -. DR Reactome; R-HSA-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain. DR Reactome; R-HSA-8873719; RAB geranylgeranylation. DR SignaLink; P53611; -. DR SIGNOR; P53611; -. DR BioGRID-ORCS; 5876; 827 hits in 1159 CRISPR screens. DR ChiTaRS; RABGGTB; human. DR GenomeRNAi; 5876; -. DR Pharos; P53611; Tbio. DR PRO; PR:P53611; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P53611; Protein. DR Bgee; ENSG00000137955; Expressed in secondary oocyte and 211 other cell types or tissues. DR ExpressionAtlas; P53611; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; ISS:UniProtKB. DR GO; GO:0004663; F:Rab geranylgeranyltransferase activity; ISS:UniProtKB. DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0018344; P:protein geranylgeranylation; ISS:UniProtKB. DR GO; GO:0036211; P:protein modification process; NAS:UniProtKB. DR GO; GO:0007601; P:visual perception; TAS:ProtInc. DR CDD; cd02894; GGTase-II; 1. DR Gene3D; 1.50.10.20; -; 1. DR InterPro; IPR001330; PFTB_repeat. DR InterPro; IPR045089; PGGT1B-like. DR InterPro; IPR026873; Ptb1. DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase. DR PANTHER; PTHR11774; GERANYLGERANYL TRANSFERASE TYPE BETA SUBUNIT; 1. DR PANTHER; PTHR11774:SF11; GERANYLGERANYL TRANSFERASE TYPE-2 SUBUNIT BETA; 1. DR Pfam; PF00432; Prenyltrans; 5. DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1. DR Genevisible; P53611; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Metal-binding; Phosphoprotein; KW Prenyltransferase; Reference proteome; Repeat; Transferase; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:20068231" FT CHAIN 2..331 FT /note="Geranylgeranyl transferase type-2 subunit beta" FT /id="PRO_0000119772" FT REPEAT 20..61 FT /note="PFTB 1" FT REPEAT 68..109 FT /note="PFTB 2" FT REPEAT 116..157 FT /note="PFTB 3" FT REPEAT 164..205 FT /note="PFTB 4" FT REPEAT 212..253 FT /note="PFTB 5" FT REPEAT 260..302 FT /note="PFTB 6" FT BINDING 190..192 FT /ligand="geranylgeranyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57533" FT /evidence="ECO:0000250|UniProtKB:Q08603" FT BINDING 238 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:Q08603" FT BINDING 240 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:Q08603" FT BINDING 241..244 FT /ligand="geranylgeranyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57533" FT /evidence="ECO:0000250|UniProtKB:Q08603" FT BINDING 290 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:Q08603" FT MOD_RES 2 FT /note="N-acetylglycine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:20068231" FT MOD_RES 3 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT CONFLICT 153 FT /note="L -> F (in Ref. 1; AAA91473)" FT /evidence="ECO:0000305" FT CONFLICT 177 FT /note="F -> S (in Ref. 3; CAA69383)" FT /evidence="ECO:0000305" FT CONFLICT 211 FT /note="N -> T (in Ref. 3; CAA69383)" FT /evidence="ECO:0000305" FT STRAND 12..14 FT /evidence="ECO:0007829|PDB:6J7X" FT HELIX 20..29 FT /evidence="ECO:0007829|PDB:6O60" FT HELIX 37..42 FT /evidence="ECO:0007829|PDB:6O60" FT HELIX 43..45 FT /evidence="ECO:0007829|PDB:6O60" FT HELIX 46..59 FT /evidence="ECO:0007829|PDB:6O60" FT HELIX 63..65 FT /evidence="ECO:0007829|PDB:6O60" FT HELIX 68..76 FT /evidence="ECO:0007829|PDB:6O60" FT STRAND 85..88 FT /evidence="ECO:0007829|PDB:6J7X" FT HELIX 95..107 FT /evidence="ECO:0007829|PDB:6O60" FT HELIX 111..113 FT /evidence="ECO:0007829|PDB:6O60" FT HELIX 116..125 FT /evidence="ECO:0007829|PDB:6O60" FT STRAND 129..131 FT /evidence="ECO:0007829|PDB:6J74" FT STRAND 133..136 FT /evidence="ECO:0007829|PDB:6O60" FT HELIX 143..156 FT /evidence="ECO:0007829|PDB:6O60" FT HELIX 159..161 FT /evidence="ECO:0007829|PDB:6O60" FT HELIX 164..172 FT /evidence="ECO:0007829|PDB:6O60" FT STRAND 177..179 FT /evidence="ECO:0007829|PDB:6J74" FT HELIX 191..203 FT /evidence="ECO:0007829|PDB:6O60" FT HELIX 207..209 FT /evidence="ECO:0007829|PDB:6O60" FT HELIX 212..220 FT /evidence="ECO:0007829|PDB:6O60" FT HELIX 239..251 FT /evidence="ECO:0007829|PDB:6O60" FT HELIX 255..257 FT /evidence="ECO:0007829|PDB:6O60" FT HELIX 260..269 FT /evidence="ECO:0007829|PDB:6O60" FT TURN 273..275 FT /evidence="ECO:0007829|PDB:6O60" FT STRAND 278..281 FT /evidence="ECO:0007829|PDB:6O60" FT HELIX 288..301 FT /evidence="ECO:0007829|PDB:6O60" FT STRAND 304..306 FT /evidence="ECO:0007829|PDB:6J6X" FT TURN 311..313 FT /evidence="ECO:0007829|PDB:6O60" FT STRAND 314..316 FT /evidence="ECO:0007829|PDB:6O60" FT HELIX 317..324 FT /evidence="ECO:0007829|PDB:6O60" SQ SEQUENCE 331 AA; 36924 MW; 37A8A6329146C49B CRC64; MGTPQKDVII KSDAPDTLLL EKHADYIASY GSKKDDYEYC MSEYLRMSGI YWGLTVMDLM GQLHRMNREE ILAFIKSCQH ECGGISASIG HDPHLLYTLS AVQILTLYDS INVIDVNKVV EYVKGLQKED GSFAGDIWGE IDTRFSFCAV ATLALLGKLD AINVEKAIEF VLSCMNFDGG FGCRPGSESH AGQIYCCTGF LAITSQLHQV NSDLLGWWLC ERQLPSGGLN GRPEKLPDVC YSWWVLASLK IIGRLHWIDR EKLRNFILAC QDEETGGFAD RPGDMVDPFH TLFGIAGLSL LGEEQIKPVN PVFCMPEEVL QRVNVQPELV S //