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Geranylgeranyl transferase type-1 subunit beta (EC 2.5.1.59) (Geranylgeranyl transferase type I subunit beta) (GGTase-I-beta) (Type I protein geranyl-geranyltransferase subunit beta)

 PGTB1_HUMAN             Reviewed;         377 AA.
P53609; Q5MJP9;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
22-SEP-2009, sequence version 2.
27-SEP-2017, entry version 149.
RecName: Full=Geranylgeranyl transferase type-1 subunit beta;
EC=2.5.1.59;
AltName: Full=Geranylgeranyl transferase type I subunit beta;
Short=GGTase-I-beta;
AltName: Full=Type I protein geranyl-geranyltransferase subunit beta;
Name=PGGT1B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
AND SUBUNIT.
TISSUE=Kidney, and Placenta;
PubMed=8106351;
Zhang F.L., Diehl R.E., Kohl N.E., Gibbs J.B., Giros B., Casey P.J.,
Omer C.A.;
"cDNA cloning and expression of rat and human protein
geranylgeranyltransferase type-I.";
J. Biol. Chem. 269:3175-3180(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Li H., Ke R., Nong W., Shen C., Zhong G., Zhou G., Lin L., Yang S.;
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
-!- FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from
geranyl-geranyl pyrophosphate to a cysteine at the fourth position
from the C-terminus of proteins having the C-terminal sequence
Cys-aliphatic-aliphatic-X. Known substrates include RAC1, RAC2,
RAP1A and RAP1B. {ECO:0000269|PubMed:8106351}.
-!- CATALYTIC ACTIVITY: Geranylgeranyl diphosphate + protein-cysteine
= S-geranylgeranyl-protein + diphosphate.
{ECO:0000269|PubMed:8106351}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: Heterodimer of FNTA and PGGT1B. PGGT1B mediates
interaction with substrate peptides. {ECO:0000269|PubMed:8106351}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P53609-1; Sequence=Displayed;
Name=2;
IsoId=P53609-2; Sequence=VSP_021827;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L25441; AAA35888.1; -; mRNA.
EMBL; AY780790; AAV98360.1; -; mRNA.
EMBL; AC008494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS4116.1; -. [P53609-1]
PIR; A53044; A53044.
RefSeq; NP_005014.2; NM_005023.3. [P53609-1]
UniGene; Hs.254006; -.
UniGene; Hs.594968; -.
ProteinModelPortal; P53609; -.
SMR; P53609; -.
BioGrid; 111250; 11.
IntAct; P53609; 2.
STRING; 9606.ENSP00000404676; -.
BindingDB; P53609; -.
ChEMBL; CHEMBL4135; -.
DrugBank; DB08180; 2-[METHYL-(5-GERANYL-4-METHYL-PENT-3-ENYL)-AMINO]-ETHYL-DIPHOSPHATE.
DrugBank; DB07227; 4-[(5-{[4-(3-CHLOROPHENYL)-3-OXOPIPERAZIN-1-YL]METHYL}-1H-IMIDAZOL-1-YL)METHYL]BENZONITRILE.
DrugBank; DB07841; GERANYLGERANYL DIPHOSPHATE.
iPTMnet; P53609; -.
PhosphoSitePlus; P53609; -.
BioMuta; PGGT1B; -.
DMDM; 259016302; -.
EPD; P53609; -.
MaxQB; P53609; -.
PaxDb; P53609; -.
PeptideAtlas; P53609; -.
PRIDE; P53609; -.
DNASU; 5229; -.
Ensembl; ENST00000379615; ENSP00000368935; ENSG00000164219. [P53609-2]
Ensembl; ENST00000419445; ENSP00000404676; ENSG00000164219. [P53609-1]
GeneID; 5229; -.
KEGG; hsa:5229; -.
UCSC; uc003kqw.5; human. [P53609-1]
CTD; 5229; -.
DisGeNET; 5229; -.
EuPathDB; HostDB:ENSG00000164219.9; -.
GeneCards; PGGT1B; -.
H-InvDB; HIX0032034; -.
HGNC; HGNC:8895; PGGT1B.
HPA; HPA030646; -.
MIM; 602031; gene.
neXtProt; NX_P53609; -.
OpenTargets; ENSG00000164219; -.
PharmGKB; PA33233; -.
eggNOG; KOG0367; Eukaryota.
eggNOG; COG5029; LUCA.
GeneTree; ENSGT00530000063392; -.
HOGENOM; HOG000180333; -.
HOVERGEN; HBG008181; -.
InParanoid; P53609; -.
KO; K11713; -.
OMA; LDDWSGM; -.
OrthoDB; EOG091G01YZ; -.
PhylomeDB; P53609; -.
TreeFam; TF105968; -.
GenomeRNAi; 5229; -.
PRO; PR:P53609; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000164219; -.
CleanEx; HS_PGGT1B; -.
Genevisible; P53609; HS.
GO; GO:0005953; C:CAAX-protein geranylgeranyltransferase complex; IDA:UniProtKB.
GO; GO:0004662; F:CAAX-protein geranylgeranyltransferase activity; ISS:UniProtKB.
GO; GO:0008144; F:drug binding; IEA:Ensembl.
GO; GO:0019840; F:isoprenoid binding; IEA:Ensembl.
GO; GO:0042277; F:peptide binding; IEA:Ensembl.
GO; GO:0004661; F:protein geranylgeranyltransferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0051771; P:negative regulation of nitric-oxide synthase biosynthetic process; IEA:Ensembl.
GO; GO:0045787; P:positive regulation of cell cycle; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0018344; P:protein geranylgeranylation; IDA:UniProtKB.
GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
InterPro; IPR001330; PFTB_repeat.
InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
Pfam; PF00432; Prenyltrans; 4.
SUPFAM; SSF48239; SSF48239; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Metal-binding; Polymorphism;
Prenyltransferase; Reference proteome; Repeat; Transferase; Zinc.
CHAIN 1 377 Geranylgeranyl transferase type-1 subunit
beta.
/FTId=PRO_0000119769.
REPEAT 144 186 PFTB 1.
REPEAT 193 234 PFTB 2.
REPEAT 245 284 PFTB 3.
REPEAT 291 333 PFTB 4.
REGION 219 221 Geranylgeranyl diphosphate binding.
{ECO:0000250}.
REGION 263 266 Geranylgeranyl diphosphate binding.
{ECO:0000250}.
REGION 272 275 Geranylgeranyl diphosphate binding.
{ECO:0000250}.
METAL 269 269 Zinc; catalytic. {ECO:0000250}.
METAL 271 271 Zinc; catalytic. {ECO:0000250}.
METAL 321 321 Zinc; via tele nitrogen; catalytic.
{ECO:0000250}.
VAR_SEQ 205 281 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_021827.
VARIANT 103 103 I -> V (in dbSNP:rs34918686).
/FTId=VAR_034381.
CONFLICT 2 2 A -> V (in Ref. 1; AAA35888 and 2;
AAV98360). {ECO:0000305}.
CONFLICT 126 126 Y -> C (in Ref. 2; AAV98360).
{ECO:0000305}.
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


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