Full text data of RABGGTB
RABGGTB
(GGTB)
[Confidence: low (only semi-automatic identification from reviews)]
Geranylgeranyl transferase type-2 subunit beta; 2.5.1.60 (Geranylgeranyl transferase type II subunit beta; GGTase-II-beta; Rab geranyl-geranyltransferase subunit beta; Rab GG transferase beta; Rab GGTase beta; Rab geranylgeranyltransferase subunit beta; Type II protein geranyl-geranyltransferase subunit beta)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Geranylgeranyl transferase type-2 subunit beta; 2.5.1.60 (Geranylgeranyl transferase type II subunit beta; GGTase-II-beta; Rab geranyl-geranyltransferase subunit beta; Rab GG transferase beta; Rab GGTase beta; Rab geranylgeranyltransferase subunit beta; Type II protein geranyl-geranyltransferase subunit beta)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P53611
ID PGTB2_HUMAN Reviewed; 331 AA.
AC P53611; Q92697;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1997, sequence version 2.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=Geranylgeranyl transferase type-2 subunit beta;
DE EC=2.5.1.60;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT protein 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.,
RA 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
RT 3' end of the alpha-subunit gene overlaps with the transglutaminase 1
RT gene 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
RT project: 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,
RT with the beta-subunit of geranylgeranyltransferase II.";
RL J. Biol. Chem. 276:32875-32882(2001).
RN [6]
RP CHARACTERIZATION.
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.
RX PubMed=18532927; DOI=10.1042/BJ20080662;
RA Baron R.A., Seabra M.C.;
RT "Rab geranylgeranylation occurs preferentially via the pre-formed REP-
RT RGGT 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 MASS
RP SPECTROMETRY.
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
RT the 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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT THR-3, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from
CC geranyl-geranyl pyrophosphate to both cysteines in Rab proteins
CC with an -XXCC, -XCXC and -CCXX C-terminal, such as RAB1A, RAB3A
CC and RAB5A respectively.
CC -!- CATALYTIC ACTIVITY: Geranylgeranyl diphosphate + protein-cysteine
CC = S-geranylgeranyl-protein + diphosphate.
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- ENZYME REGULATION: The enzymatic reaction requires the aid of a
CC Rab escort protein (also called component A).
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit, collectively
CC called component B. The Rab GGTase dimer (RGGT) can associate with
CC CHM (component A) prior to Rab protein binding; the association is
CC stabilized by geranylgeranyl pyrophosphate (GGpp). The
CC CHM:RGGT:Rab complex is destabilized by GGpp. Interaction of beta
CC subunit with prenylated PTP4A2 precludes its association with
CC subunit alpha, and inhibits enzyme activity.
CC -!- INTERACTION:
CC P10398:ARAF; NbExp=3; IntAct=EBI-536715, EBI-365961;
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC family.
CC -!- SIMILARITY: Contains 6 PFTB repeats.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Rab geranylgeranyltransferase
CC entry;
CC URL="http://en.wikipedia.org/wiki/Rab_geranylgeranyltransferase";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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 PIR; G02431; G02431.
DR RefSeq; NP_004573.2; NM_004582.3.
DR UniGene; Hs.78948; -.
DR ProteinModelPortal; P53611; -.
DR SMR; P53611; 5-331.
DR IntAct; P53611; 2.
DR MINT; MINT-260716; -.
DR STRING; 9606.ENSP00000317473; -.
DR BindingDB; P53611; -.
DR PhosphoSite; P53611; -.
DR DMDM; 2506788; -.
DR PaxDb; P53611; -.
DR PRIDE; P53611; -.
DR Ensembl; ENST00000319942; ENSP00000317473; ENSG00000137955.
DR GeneID; 5876; -.
DR KEGG; hsa:5876; -.
DR UCSC; uc001dgy.2; human.
DR CTD; 5876; -.
DR GeneCards; GC01P076251; -.
DR HGNC; HGNC:9796; RABGGTB.
DR HPA; HPA026585; -.
DR HPA; HPA027167; -.
DR MIM; 179080; gene.
DR neXtProt; NX_P53611; -.
DR PharmGKB; PA34157; -.
DR eggNOG; COG5029; -.
DR HOGENOM; HOG000180334; -.
DR HOVERGEN; HBG008182; -.
DR InParanoid; P53611; -.
DR KO; K05956; -.
DR OMA; ESHAGLI; -.
DR OrthoDB; EOG7XSTDZ; -.
DR PhylomeDB; P53611; -.
DR BRENDA; 2.5.1.60; 2681.
DR ChiTaRS; RABGGTB; human.
DR GenomeRNAi; 5876; -.
DR NextBio; 22832; -.
DR PRO; PR:P53611; -.
DR ArrayExpress; P53611; -.
DR Bgee; P53611; -.
DR CleanEx; HS_RABGGTB; -.
DR Genevestigator; P53611; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006464; P:cellular protein modification process; NAS:UniProtKB.
DR GO; GO:0018344; P:protein geranylgeranylation; IEA:InterPro.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR InterPro; IPR001330; Prenyltrans.
DR InterPro; IPR026873; Ptb1.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11774:SF8; PTHR11774:SF8; 1.
DR Pfam; PF00432; Prenyltrans; 5.
DR SUPFAM; SSF48239; SSF48239; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Metal-binding; Phosphoprotein;
KW Prenyltransferase; Reference proteome; Repeat; Transferase; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 331 Geranylgeranyl transferase type-2 subunit
FT beta.
FT /FTId=PRO_0000119772.
FT REPEAT 20 61 PFTB 1.
FT REPEAT 68 109 PFTB 2.
FT REPEAT 116 157 PFTB 3.
FT REPEAT 164 205 PFTB 4.
FT REPEAT 212 253 PFTB 5.
FT REPEAT 260 302 PFTB 6.
FT METAL 238 238 Zinc (By similarity).
FT METAL 240 240 Zinc (By similarity).
FT METAL 290 290 Zinc (By similarity).
FT MOD_RES 2 2 N-acetylglycine.
FT MOD_RES 3 3 Phosphothreonine.
FT CONFLICT 153 153 L -> F (in Ref. 1; AAA91473).
FT CONFLICT 177 177 F -> S (in Ref. 3; CAA69383).
FT CONFLICT 211 211 N -> T (in Ref. 3; CAA69383).
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
//
ID PGTB2_HUMAN Reviewed; 331 AA.
AC P53611; Q92697;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1997, sequence version 2.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=Geranylgeranyl transferase type-2 subunit beta;
DE EC=2.5.1.60;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT protein 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.,
RA 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
RT 3' end of the alpha-subunit gene overlaps with the transglutaminase 1
RT gene 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
RT project: 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,
RT with the beta-subunit of geranylgeranyltransferase II.";
RL J. Biol. Chem. 276:32875-32882(2001).
RN [6]
RP CHARACTERIZATION.
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.
RX PubMed=18532927; DOI=10.1042/BJ20080662;
RA Baron R.A., Seabra M.C.;
RT "Rab geranylgeranylation occurs preferentially via the pre-formed REP-
RT RGGT 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 MASS
RP SPECTROMETRY.
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
RT the 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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT THR-3, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from
CC geranyl-geranyl pyrophosphate to both cysteines in Rab proteins
CC with an -XXCC, -XCXC and -CCXX C-terminal, such as RAB1A, RAB3A
CC and RAB5A respectively.
CC -!- CATALYTIC ACTIVITY: Geranylgeranyl diphosphate + protein-cysteine
CC = S-geranylgeranyl-protein + diphosphate.
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- ENZYME REGULATION: The enzymatic reaction requires the aid of a
CC Rab escort protein (also called component A).
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit, collectively
CC called component B. The Rab GGTase dimer (RGGT) can associate with
CC CHM (component A) prior to Rab protein binding; the association is
CC stabilized by geranylgeranyl pyrophosphate (GGpp). The
CC CHM:RGGT:Rab complex is destabilized by GGpp. Interaction of beta
CC subunit with prenylated PTP4A2 precludes its association with
CC subunit alpha, and inhibits enzyme activity.
CC -!- INTERACTION:
CC P10398:ARAF; NbExp=3; IntAct=EBI-536715, EBI-365961;
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC family.
CC -!- SIMILARITY: Contains 6 PFTB repeats.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Rab geranylgeranyltransferase
CC entry;
CC URL="http://en.wikipedia.org/wiki/Rab_geranylgeranyltransferase";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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 PIR; G02431; G02431.
DR RefSeq; NP_004573.2; NM_004582.3.
DR UniGene; Hs.78948; -.
DR ProteinModelPortal; P53611; -.
DR SMR; P53611; 5-331.
DR IntAct; P53611; 2.
DR MINT; MINT-260716; -.
DR STRING; 9606.ENSP00000317473; -.
DR BindingDB; P53611; -.
DR PhosphoSite; P53611; -.
DR DMDM; 2506788; -.
DR PaxDb; P53611; -.
DR PRIDE; P53611; -.
DR Ensembl; ENST00000319942; ENSP00000317473; ENSG00000137955.
DR GeneID; 5876; -.
DR KEGG; hsa:5876; -.
DR UCSC; uc001dgy.2; human.
DR CTD; 5876; -.
DR GeneCards; GC01P076251; -.
DR HGNC; HGNC:9796; RABGGTB.
DR HPA; HPA026585; -.
DR HPA; HPA027167; -.
DR MIM; 179080; gene.
DR neXtProt; NX_P53611; -.
DR PharmGKB; PA34157; -.
DR eggNOG; COG5029; -.
DR HOGENOM; HOG000180334; -.
DR HOVERGEN; HBG008182; -.
DR InParanoid; P53611; -.
DR KO; K05956; -.
DR OMA; ESHAGLI; -.
DR OrthoDB; EOG7XSTDZ; -.
DR PhylomeDB; P53611; -.
DR BRENDA; 2.5.1.60; 2681.
DR ChiTaRS; RABGGTB; human.
DR GenomeRNAi; 5876; -.
DR NextBio; 22832; -.
DR PRO; PR:P53611; -.
DR ArrayExpress; P53611; -.
DR Bgee; P53611; -.
DR CleanEx; HS_RABGGTB; -.
DR Genevestigator; P53611; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006464; P:cellular protein modification process; NAS:UniProtKB.
DR GO; GO:0018344; P:protein geranylgeranylation; IEA:InterPro.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR InterPro; IPR001330; Prenyltrans.
DR InterPro; IPR026873; Ptb1.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11774:SF8; PTHR11774:SF8; 1.
DR Pfam; PF00432; Prenyltrans; 5.
DR SUPFAM; SSF48239; SSF48239; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Metal-binding; Phosphoprotein;
KW Prenyltransferase; Reference proteome; Repeat; Transferase; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 331 Geranylgeranyl transferase type-2 subunit
FT beta.
FT /FTId=PRO_0000119772.
FT REPEAT 20 61 PFTB 1.
FT REPEAT 68 109 PFTB 2.
FT REPEAT 116 157 PFTB 3.
FT REPEAT 164 205 PFTB 4.
FT REPEAT 212 253 PFTB 5.
FT REPEAT 260 302 PFTB 6.
FT METAL 238 238 Zinc (By similarity).
FT METAL 240 240 Zinc (By similarity).
FT METAL 290 290 Zinc (By similarity).
FT MOD_RES 2 2 N-acetylglycine.
FT MOD_RES 3 3 Phosphothreonine.
FT CONFLICT 153 153 L -> F (in Ref. 1; AAA91473).
FT CONFLICT 177 177 F -> S (in Ref. 3; CAA69383).
FT CONFLICT 211 211 N -> T (in Ref. 3; CAA69383).
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
//
MIM
179080
*RECORD*
*FIELD* NO
179080
*FIELD* TI
*179080 RAB GERANYLGERANYL TRANSFERASE, BETA SUBUNIT; RABGGTB
;;RAB GERANYLGERANYLTRANSFERASE, BETA COMPONENT;;
read moreGG TRANSFERASE, COMPONENT B; GGTB
*FIELD* TX
CLONING
By sequencing clones from a Burkitt lymphoma cDNA library, Sanders et
al. (1996) cloned RABGGTB. The cDNA showed 82.4% identity over 341 bp of
coding sequence to a rat sequence encoding the catalytic subunit of RAB
geranylgeranyl transferase. The amino acid sequences of the 2 genes are
91.1% similar.
Van Bokhoven et al. (1996) cloned the complete human cDNA of RABGGTB
from a fetal brain library and reported that it encodes a 331-amino acid
polypeptide, which is very well conserved among both mammalian and lower
eukaryotic species.
Wei et al. (1995) found that Rabggtb is ubiquitously expressed in adult
mice, but displays a varying pattern of expression during embryonic
development. Its expression was detected in whole embryos during early
embryonic stages, but was specifically concentrated in the developing
brain, heart, and liver during gestation stages E11.5 and E13.5.
GENE FUNCTION
Seabra et al. (1991) presented evidence that 2 prenyltransferases,
farnesyltransferase and geranylgeranyltransferase, are heterodimers that
share a common alpha subunit with different beta subunits. Three
distinct prenyltransferases attach polyisoprene units in thioether
linkage to cysteine residues of membrane-bound cellular proteins. The
best-characterized enzyme, protein farnesyltransferase, attaches 15
carbon farnesyl units to cysteine residues at the fourth position from
the C-terminus of p21(ras) proteins, nuclear lamins, and other proteins
that end in the so-called CAAX box, where C is cysteine, A is usually
but not always an aliphatic amino acid, and X is methionine or serine.
The CAAX farnesyltransferase is a tightly coupled heterodimer composed
of a 49-kD alpha subunit (RABGGTA; 601905) and a 46-kD beta subunit. The
other 2 known prenyltransferases transfer 20 carbon geranylgeranyl
groups. One of these enzymes resembles the CAAX farnesyltransferase
(FNTA; 134635) in recognizing a C-terminal CAAX box. Instead of
methionine or serine, the CAAX geranylgeranyl transferase (GG
transferase) prefers leucine. The third identified prenyltransferase is
a GG transferase that recognizes proteins that terminate in the sequence
cys-X-cys or cys-cys. Its substrates include a large family of related
membrane-associated GTP-binding proteins termed RAB proteins. The enzyme
from rat brain contains 2 components, A and B. Component B comprises
polypeptides of 60 and 38 kD. Seabra et al. (1992) hypothesized that
component A binds conserved sequences in RAB and that component B
transfers geranylgeranyl.
MAPPING
Sanders et al. (1996) probed a genomic Southern blot from a panel of 24
interspecies somatic cell hybrids and localized the gene to human
chromosome 1; a much fainter band was also present in the chromosome 3
somatic cell hybrid, pointing to the existence of a related gene on that
chromosome. By fluorescence in situ hybridization they further localized
the gene to chromosome 1p31-p22. Van Bokhoven et al. (1996) refined the
mapping of the RAGGTB gene to chromosome 1p31 using fluorescence in situ
hybridization.
Wei et al. (1995) mapped the mouse homolog to the distal region of mouse
chromosome 3.
*FIELD* RF
1. Sanders, R.; Islam, K. B.; Betz, R.; Larsson, C.; Smith, C. I.
E.: A human homologue of the rat Rab geranylgeranyl transferase beta
subunit on chromosome 1p22-p31. Genomics 35: 633-635, 1996.
2. Seabra, M. C.; Brown, M. S.; Slaughter, C. A.; Sudhof, T. C.; Goldstein,
J. L.: Purification of component A of Rab geranylgeranyl transferase:
possible identity with the choroideremia gene product. Cell 70:
1049-1057, 1992.
3. Seabra, M. C.; Reiss, Y.; Casey, P. J.; Brown, M. S.; Goldstein,
J. L.: Protein farnesyltransferase and geranylgeranyltransferase
share a common alpha subunit. Cell 65: 429-434, 1991.
4. van Bokhoven, H.; Rawson, R. B.; Merkx, G. F. M.; Cremers, F. P.
M.; Seabra, M. C.: cDNA cloning and chromosomal localization of the
genes encoding the alpha- and beta-subunits of human Rab geranylgeranyl
transferase: the 3-prime end of the alpha-subunit gene overlaps with
the transglutaminase 1 gene promoter. Genomics 38: 133-140, 1996.
5. Wei, L.-N.; Lee, C.-H.; Chinpaisal, C.; Copeland, N. G.; Gilbert,
D. J.; Jenkins, N. A.; Hsu, Y.-C.: Studies of cloning, chromosomal
mapping, and embryonic expression of the mouse Rab geranylgeranyl
transferase beta subunit. Cell Growth Differ. 6: 607-614, 1995.
*FIELD* CD
Victor A. McKusick: 3/27/1992
*FIELD* ED
wwang: 10/01/2008
alopez: 3/3/1998
mark: 10/6/1997
alopez: 7/14/1997
mark: 9/24/1996
terry: 8/23/1996
mark: 7/11/1995
terry: 5/16/1994
carol: 11/1/1993
carol: 2/1/1993
carol: 10/16/1992
carol: 10/12/1992
*RECORD*
*FIELD* NO
179080
*FIELD* TI
*179080 RAB GERANYLGERANYL TRANSFERASE, BETA SUBUNIT; RABGGTB
;;RAB GERANYLGERANYLTRANSFERASE, BETA COMPONENT;;
read moreGG TRANSFERASE, COMPONENT B; GGTB
*FIELD* TX
CLONING
By sequencing clones from a Burkitt lymphoma cDNA library, Sanders et
al. (1996) cloned RABGGTB. The cDNA showed 82.4% identity over 341 bp of
coding sequence to a rat sequence encoding the catalytic subunit of RAB
geranylgeranyl transferase. The amino acid sequences of the 2 genes are
91.1% similar.
Van Bokhoven et al. (1996) cloned the complete human cDNA of RABGGTB
from a fetal brain library and reported that it encodes a 331-amino acid
polypeptide, which is very well conserved among both mammalian and lower
eukaryotic species.
Wei et al. (1995) found that Rabggtb is ubiquitously expressed in adult
mice, but displays a varying pattern of expression during embryonic
development. Its expression was detected in whole embryos during early
embryonic stages, but was specifically concentrated in the developing
brain, heart, and liver during gestation stages E11.5 and E13.5.
GENE FUNCTION
Seabra et al. (1991) presented evidence that 2 prenyltransferases,
farnesyltransferase and geranylgeranyltransferase, are heterodimers that
share a common alpha subunit with different beta subunits. Three
distinct prenyltransferases attach polyisoprene units in thioether
linkage to cysteine residues of membrane-bound cellular proteins. The
best-characterized enzyme, protein farnesyltransferase, attaches 15
carbon farnesyl units to cysteine residues at the fourth position from
the C-terminus of p21(ras) proteins, nuclear lamins, and other proteins
that end in the so-called CAAX box, where C is cysteine, A is usually
but not always an aliphatic amino acid, and X is methionine or serine.
The CAAX farnesyltransferase is a tightly coupled heterodimer composed
of a 49-kD alpha subunit (RABGGTA; 601905) and a 46-kD beta subunit. The
other 2 known prenyltransferases transfer 20 carbon geranylgeranyl
groups. One of these enzymes resembles the CAAX farnesyltransferase
(FNTA; 134635) in recognizing a C-terminal CAAX box. Instead of
methionine or serine, the CAAX geranylgeranyl transferase (GG
transferase) prefers leucine. The third identified prenyltransferase is
a GG transferase that recognizes proteins that terminate in the sequence
cys-X-cys or cys-cys. Its substrates include a large family of related
membrane-associated GTP-binding proteins termed RAB proteins. The enzyme
from rat brain contains 2 components, A and B. Component B comprises
polypeptides of 60 and 38 kD. Seabra et al. (1992) hypothesized that
component A binds conserved sequences in RAB and that component B
transfers geranylgeranyl.
MAPPING
Sanders et al. (1996) probed a genomic Southern blot from a panel of 24
interspecies somatic cell hybrids and localized the gene to human
chromosome 1; a much fainter band was also present in the chromosome 3
somatic cell hybrid, pointing to the existence of a related gene on that
chromosome. By fluorescence in situ hybridization they further localized
the gene to chromosome 1p31-p22. Van Bokhoven et al. (1996) refined the
mapping of the RAGGTB gene to chromosome 1p31 using fluorescence in situ
hybridization.
Wei et al. (1995) mapped the mouse homolog to the distal region of mouse
chromosome 3.
*FIELD* RF
1. Sanders, R.; Islam, K. B.; Betz, R.; Larsson, C.; Smith, C. I.
E.: A human homologue of the rat Rab geranylgeranyl transferase beta
subunit on chromosome 1p22-p31. Genomics 35: 633-635, 1996.
2. Seabra, M. C.; Brown, M. S.; Slaughter, C. A.; Sudhof, T. C.; Goldstein,
J. L.: Purification of component A of Rab geranylgeranyl transferase:
possible identity with the choroideremia gene product. Cell 70:
1049-1057, 1992.
3. Seabra, M. C.; Reiss, Y.; Casey, P. J.; Brown, M. S.; Goldstein,
J. L.: Protein farnesyltransferase and geranylgeranyltransferase
share a common alpha subunit. Cell 65: 429-434, 1991.
4. van Bokhoven, H.; Rawson, R. B.; Merkx, G. F. M.; Cremers, F. P.
M.; Seabra, M. C.: cDNA cloning and chromosomal localization of the
genes encoding the alpha- and beta-subunits of human Rab geranylgeranyl
transferase: the 3-prime end of the alpha-subunit gene overlaps with
the transglutaminase 1 gene promoter. Genomics 38: 133-140, 1996.
5. Wei, L.-N.; Lee, C.-H.; Chinpaisal, C.; Copeland, N. G.; Gilbert,
D. J.; Jenkins, N. A.; Hsu, Y.-C.: Studies of cloning, chromosomal
mapping, and embryonic expression of the mouse Rab geranylgeranyl
transferase beta subunit. Cell Growth Differ. 6: 607-614, 1995.
*FIELD* CD
Victor A. McKusick: 3/27/1992
*FIELD* ED
wwang: 10/01/2008
alopez: 3/3/1998
mark: 10/6/1997
alopez: 7/14/1997
mark: 9/24/1996
terry: 8/23/1996
mark: 7/11/1995
terry: 5/16/1994
carol: 11/1/1993
carol: 2/1/1993
carol: 10/16/1992
carol: 10/12/1992