PGTB2_HUMAN
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 03-AUG-2022, entry version 186.
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";
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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; 88.
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; P53611; -.
DR PeptideAtlas; P53611; -.
DR PRIDE; P53611; -.
DR ProteomicsDB; 56591; -.
DR Antibodypedia; 19716; 72 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 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; 1042804at2759; -.
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; 792 hits in 1081 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 209 other tissues.
DR ExpressionAtlas; P53611; baseline and differential.
DR Genevisible; P53611; HS.
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:0018342; P:protein prenylation; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR CDD; cd02894; GGTase-II; 1.
DR InterPro; IPR001330; PFTB_repeat.
DR InterPro; IPR045089; PGGT1B-like.
DR InterPro; IPR026873; Ptb1.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11774; PTHR11774; 1.
DR Pfam; PF00432; Prenyltrans; 5.
DR SUPFAM; SSF48239; SSF48239; 1.
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
