PGTB1_HUMAN
ID PGTB1_HUMAN Reviewed; 377 AA.
AC P53609; Q5MJP9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Geranylgeranyl transferase type-1 subunit beta;
DE EC=2.5.1.59;
DE AltName: Full=Geranylgeranyl transferase type I subunit beta;
DE Short=GGTase-I-beta;
DE AltName: Full=Type I protein geranyl-geranyltransferase subunit beta;
GN Name=PGGT1B;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBUNIT.
RC TISSUE=Kidney, and Placenta;
RX PubMed=8106351; DOI=10.1016/s0021-9258(17)41845-x;
RA Zhang F.L., Diehl R.E., Kohl N.E., Gibbs J.B., Giros B., Casey P.J.,
RA Omer C.A.;
RT "cDNA cloning and expression of rat and human protein
RT geranylgeranyltransferase type-I.";
RL J. Biol. Chem. 269:3175-3180(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Li H., Ke R., Nong W., Shen C., Zhong G., Zhou G., Lin L., Yang S.;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
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).
CC -!- FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from
CC geranyl-geranyl pyrophosphate to a cysteine at the fourth position from
CC the C-terminus of proteins having the C-terminal sequence Cys-
CC aliphatic-aliphatic-X. Known substrates include RAC1, RAC2, RAP1A and
CC RAP1B. {ECO:0000269|PubMed:8106351}.
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=2.5.1.59;
CC Evidence={ECO:0000269|PubMed:8106351};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P53610};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P53610};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P18898};
CC -!- SUBUNIT: Heterodimer of FNTA and PGGT1B. PGGT1B mediates interaction
CC with substrate peptides. {ECO:0000269|PubMed:8106351}.
CC -!- INTERACTION:
CC P53609; P49354: FNTA; NbExp=8; IntAct=EBI-8456634, EBI-602336;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P53609-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P53609-2; Sequence=VSP_021827;
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC family. {ECO:0000305}.
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DR EMBL; L25441; AAA35888.1; -; mRNA.
DR EMBL; AY780790; AAV98360.1; -; mRNA.
DR EMBL; AC008494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS4116.1; -. [P53609-1]
DR PIR; A53044; A53044.
DR RefSeq; NP_005014.2; NM_005023.3. [P53609-1]
DR AlphaFoldDB; P53609; -.
DR SMR; P53609; -.
DR BioGRID; 111250; 31.
DR ComplexPortal; CPX-2157; Protein geranylgeranyl transferase type I complex.
DR IntAct; P53609; 7.
DR MINT; P53609; -.
DR STRING; 9606.ENSP00000404676; -.
DR BindingDB; P53609; -.
DR ChEMBL; CHEMBL4135; -.
DR DrugBank; DB08180; 2-[METHYL-(5-GERANYL-4-METHYL-PENT-3-ENYL)-AMINO]-ETHYL-DIPHOSPHATE.
DR DrugBank; DB07841; Geranylgeranyl diphosphate.
DR DrugBank; DB07227; L-778123.
DR iPTMnet; P53609; -.
DR MetOSite; P53609; -.
DR PhosphoSitePlus; P53609; -.
DR BioMuta; PGGT1B; -.
DR DMDM; 259016302; -.
DR EPD; P53609; -.
DR jPOST; P53609; -.
DR MassIVE; P53609; -.
DR MaxQB; P53609; -.
DR PaxDb; P53609; -.
DR PeptideAtlas; P53609; -.
DR PRIDE; P53609; -.
DR ProteomicsDB; 56589; -. [P53609-1]
DR ProteomicsDB; 56590; -. [P53609-2]
DR Antibodypedia; 25414; 84 antibodies from 14 providers.
DR DNASU; 5229; -.
DR Ensembl; ENST00000379615.3; ENSP00000368935.3; ENSG00000164219.10. [P53609-2]
DR Ensembl; ENST00000419445.6; ENSP00000404676.1; ENSG00000164219.10. [P53609-1]
DR GeneID; 5229; -.
DR KEGG; hsa:5229; -.
DR MANE-Select; ENST00000419445.6; ENSP00000404676.1; NM_005023.4; NP_005014.2.
DR UCSC; uc003kqw.5; human. [P53609-1]
DR CTD; 5229; -.
DR DisGeNET; 5229; -.
DR GeneCards; PGGT1B; -.
DR HGNC; HGNC:8895; PGGT1B.
DR HPA; ENSG00000164219; Low tissue specificity.
DR MIM; 602031; gene.
DR neXtProt; NX_P53609; -.
DR OpenTargets; ENSG00000164219; -.
DR PharmGKB; PA33233; -.
DR VEuPathDB; HostDB:ENSG00000164219; -.
DR eggNOG; KOG0367; Eukaryota.
DR GeneTree; ENSGT00950000183128; -.
DR HOGENOM; CLU_028946_2_2_1; -.
DR InParanoid; P53609; -.
DR OMA; RWCLMRQ; -.
DR OrthoDB; 1042804at2759; -.
DR PhylomeDB; P53609; -.
DR TreeFam; TF105968; -.
DR BRENDA; 2.5.1.59; 2681.
DR PathwayCommons; P53609; -.
DR SignaLink; P53609; -.
DR BioGRID-ORCS; 5229; 330 hits in 1086 CRISPR screens.
DR GenomeRNAi; 5229; -.
DR Pharos; P53609; Tchem.
DR PRO; PR:P53609; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P53609; protein.
DR Bgee; ENSG00000164219; Expressed in oocyte and 197 other tissues.
DR Genevisible; P53609; HS.
DR GO; GO:0005953; C:CAAX-protein geranylgeranyltransferase complex; IDA:UniProtKB.
DR GO; GO:0004662; F:CAAX-protein geranylgeranyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004661; F:protein geranylgeranyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0018344; P:protein geranylgeranylation; IDA:UniProtKB.
DR GO; GO:0018342; P:protein prenylation; IBA:GO_Central.
DR CDD; cd02895; GGTase-I; 1.
DR InterPro; IPR041960; GGTase_I_beta.
DR InterPro; IPR001330; PFTB_repeat.
DR InterPro; IPR045089; PGGT1B-like.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11774; PTHR11774; 1.
DR Pfam; PF00432; Prenyltrans; 4.
DR SUPFAM; SSF48239; SSF48239; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Magnesium; Metal-binding; Prenyltransferase;
KW Reference proteome; Repeat; Transferase; Zinc.
FT CHAIN 1..377
FT /note="Geranylgeranyl transferase type-1 subunit beta"
FT /id="PRO_0000119769"
FT REPEAT 144..186
FT /note="PFTB 1"
FT REPEAT 193..234
FT /note="PFTB 2"
FT REPEAT 245..284
FT /note="PFTB 3"
FT REPEAT 291..333
FT /note="PFTB 4"
FT BINDING 219..221
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 263..266
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 272..275
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT VAR_SEQ 205..281
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_021827"
FT VARIANT 103
FT /note="I -> V (in dbSNP:rs34918686)"
FT /id="VAR_034381"
FT CONFLICT 2
FT /note="A -> V (in Ref. 1; AAA35888 and 2; AAV98360)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="Y -> C (in Ref. 2; AAV98360)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 42368 MW; AA04C9B34B8A3FDC CRC64;
MAATEDERLA GSGEGERLDF LRDRHVRFFQ RCLQVLPERY SSLETSRLTI AFFALSGLDM
LDSLDVVNKD DIIEWIYSLQ VLPTEDRSNL NRCGFRGSSY LGIPFNPSKA PGTAHPYDSG
HIAMTYTGLS CLVILGDDLS RVNKEACLAG LRALQLEDGS FCAVPEGSEN DMRFVYCASC
ICYMLNNWSG MDMKKAITYI RRSMSYDNGL AQGAGLESHG GSTFCGIASL CLMGKLEEVF
SEKELNRIKR WCIMRQQNGY HGRPNKPVDT CYSFWVGATL KLLKIFQYTN FEKNRNYILS
TQDRLVGGFA KWPDSHPDAL HAYFGICGLS LMEESGICKV HPALNVSTRT SERLLDLHQS
WKTKDSKQCS ENVHIST
