(data stored in ACNUC14511 zone)

HOGENOM: HS1_PE4938

ID   HS1_PE4938                           STANDARD;      PRT;   419 AA.
AC   HS1_PE4938; P14324; D3DV91; Q96G29;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Farnesyl pyrophosphate synthase; Short=FPP synthase;
DE   Short=FPS; EC=2.5.1.10;AltName: Full=(2E,6E)-farnesyl diphosphate
DE   synthase;AltName: Full=Dimethylallyltranstransferase; EC=2.5.1 1;AltName:
DE   Full=Farnesyl diphosphate synthase;AltName: Full=Geranyltranstransferase;
DE   (HS1.PE4938).
GN   Name=FDPS; Synonyms=FPS, KIAA1293;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS1.PE4938.
CC       Homo sapiens chromosome 1 GRCh37  sequence 1..249240621 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:FPPS_HUMAN
CC   -!- FUNCTION: Key enzyme in isoprenoid biosynthesis which catalyzes
CC       the formation of farnesyl diphosphate (FPP), a precursor for
CC       several classes of essential metabolites including sterols,
CC       dolichols, carotenoids, and ubiquinones. FPP also serves as
CC       substrate for protein farnesylation and geranylgeranylation.
CC       Catalyzes the sequential condensation of isopentenyl pyrophosphate
CC       with the allylic pyrophosphates, dimethylallyl pyrophosphate, and
CC       then with the resultant geranylpyrophosphate to the ultimate
CC       product farnesyl pyrophosphate.
CC   -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + isopentenyl
CC       diphosphate = diphosphate + geranyl diphosphate.
CC   -!- CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate
CC       = diphosphate + (2E,6E)-farnesyl diphosphate.
CC   -!- COFACTOR: Binds 3 magnesium ions per subunit.
CC   -!- ENZYME REGULATION: Inactivated by interferon-induced RSAD2. This
CC       inactivation may result of disruption of lipid rafts at the plasma
CC       membrane, and thus have an antiviral effect since many envelopped
CC       viruses need lipid rafts to bud efficiently out of the cell.
CC   -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate
CC       biosynthesis; farnesyl diphosphate from geranyl diphosphate and
CC       isopentenyl diphosphate: step 1/1.
CC   -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate
CC       biosynthesis; geranyl diphosphate from dimethylallyl diphosphate
CC       and isopentenyl diphosphate: step 1/1.
CC   -!- SUBUNIT: Homodimer. Interacts with RSAD2. Interacts with HTLV-1
CC       protein p13(II).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-67 is the initiator.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA52423.1; Type=Erroneous initiation;
CC       Sequence=BAA03523.2; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000160912 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000160752;ENST00000368356;ENSP00000357340.
DR   EMBL; AK291084; - ;
DR   EMBL; AL139410; - ;
DR   EMBL; BC010004; - ;
DR   EMBL; CH471121; - ;
DR   EMBL; D14697; - ;
DR   EMBL; J05262; - ;
DR   EMBL; M29863; - ;
DR   EMBL; Z47055; - ;
DR   UniProtKB/Swiss-Prot; P14324; D3DV91; Q96G29; -.
DR   EMBL; D14697; BAA03523.2; ALT_INIT; mRNA.
DR   EMBL; AK291084; BAF83773.1; -; mRNA.
DR   EMBL; AL139410; CAI12715.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW53076.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW53077.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW53078.1; -; Genomic_DNA.
DR   EMBL; BC010004; AAH10004.1; -; mRNA.
DR   EMBL; J05262; AAA52423.1; ALT_INIT; mRNA.
DR   EMBL; M29863; AAA35820.1; -; mRNA.
DR   IPI; IPI00914566; -.
DR   PIR; A35726; A35726.
DR   RefSeq; NP_001129293.1; NM_001135821.1.
DR   RefSeq; NP_001129294.1; NM_001135822.1.
DR   RefSeq; NP_001995.1; NM_002004.3.
DR   UniGene; Hs.335918; -.
DR   PDB; 1YQ7; X-ray; 2.20 A; A=67-419.
DR   PDB; 1YV5; X-ray; 2.00 A; A=67-419.
DR   PDB; 1ZW5; X-ray; 2.30 A; A=67-419.
DR   PDB; 2F7M; X-ray; 2.30 A; F=72-419.
DR   PDB; 2F89; X-ray; 2.60 A; F=72-419.
DR   PDB; 2F8C; X-ray; 2.20 A; F=72-419.
DR   PDB; 2F8Z; X-ray; 2.60 A; F=72-419.
DR   PDB; 2F92; X-ray; 2.15 A; F=72-419.
DR   PDB; 2F94; X-ray; 1.94 A; F=72-419.
DR   PDB; 2F9K; X-ray; 2.06 A; F=72-419.
DR   PDB; 2OPM; X-ray; 2.40 A; A=67-419.
DR   PDB; 2OPN; X-ray; 2.70 A; A=67-419.
DR   PDB; 2QIS; X-ray; 1.80 A; A=67-419.
DR   PDB; 2RAH; X-ray; 2.00 A; A=67-419.
DR   PDB; 2VF6; X-ray; 2.10 A; A=67-419.
DR   PDB; 3B7L; X-ray; 1.95 A; A=67-419.
DR   PDB; 3CP6; X-ray; 1.95 A; A=67-419.
DR   PDB; 3N1V; X-ray; 2.18 A; F=72-419.
DR   PDB; 3N1W; X-ray; 2.56 A; F=72-419.
DR   PDB; 3N3L; X-ray; 2.74 A; F=72-419.
DR   PDB; 3N45; X-ray; 1.88 A; F=72-419.
DR   PDB; 3N46; X-ray; 2.35 A; F=72-419.
DR   PDB; 3N49; X-ray; 2.50 A; F=72-419.
DR   PDB; 3N5H; X-ray; 2.20 A; F=72-419.
DR   PDB; 3N5J; X-ray; 2.35 A; F=72-419.
DR   PDB; 3N6K; X-ray; 2.25 A; F=72-419.
DR   PDB; 3RYE; X-ray; 2.10 A; A=72-419.
DR   PDB; 3S4J; X-ray; 1.95 A; A=72-419.
DR   PDBsum; 1YQ7; -.
DR   PDBsum; 1YV5; -.
DR   PDBsum; 1ZW5; -.
DR   PDBsum; 2F7M; -.
DR   PDBsum; 2F89; -.
DR   PDBsum; 2F8C; -.
DR   PDBsum; 2F8Z; -.
DR   PDBsum; 2F92; -.
DR   PDBsum; 2F94; -.
DR   PDBsum; 2F9K; -.
DR   PDBsum; 2OPM; -.
DR   PDBsum; 2OPN; -.
DR   PDBsum; 2QIS; -.
DR   PDBsum; 2RAH; -.
DR   PDBsum; 2VF6; -.
DR   PDBsum; 3B7L; -.
DR   PDBsum; 3CP6; -.
DR   PDBsum; 3N1V; -.
DR   PDBsum; 3N1W; -.
DR   PDBsum; 3N3L; -.
DR   PDBsum; 3N45; -.
DR   PDBsum; 3N46; -.
DR   PDBsum; 3N49; -.
DR   PDBsum; 3N5H; -.
DR   PDBsum; 3N5J; -.
DR   PDBsum; 3N6K; -.
DR   PDBsum; 3RYE; -.
DR   PDBsum; 3S4J; -.
DR   ProteinModelPortal; P14324; -.
DR   SMR; P14324; 74-416.
DR   IntAct; P14324; 5.
DR   MINT; MINT-2858951; -.
DR   STRING; P14324; -.
DR   PhosphoSite; P14324; -.
DR   PRIDE; P14324; -.
DR   Ensembl; ENST00000356657; ENSP00000349078; ENSG00000160752.
DR   Ensembl; ENST00000368356; ENSP00000357340; ENSG00000160752.
DR   GeneID; 2224; -.
DR   KEGG; hsa:2224; -.
DR   UCSC; uc001fkd.1; human.
DR   CTD; 2224; -.
DR   GeneCards; GC01P126640; -.
DR   H-InvDB; HIX0199817; -.
DR   HGNC; HGNC:3631; FDPS.
DR   HPA; HPA028200; -.
DR   MIM; 134629; gene.
DR   neXtProt; NX_P14324; -.
DR   PharmGKB; PA28075; -.
DR   eggNOG; prNOG17911; -.
DR   InParanoid; P14324; -.
DR   OMA; RDFMAVF; -.
DR   OrthoDB; EOG4ZGPCS; -.
DR   PhylomeDB; P14324; -.
DR   BioCyc; MetaCyc:ENSG00000160752-MON; -.
DR   Reactome; REACT_22258; Metabolism of lipids and lipoproteins.
DR   DrugBank; DB00630; Alendronate.
DR   DrugBank; DB00710; Ibandronate.
DR   DrugBank; DB00282; Pamidronate.
DR   DrugBank; DB00884; Risedronate.
DR   DrugBank; DB00399; Zoledronate.
DR   ArrayExpress; P14324; -.
DR   Bgee; P14324; -.
DR   CleanEx; HS_FDPS; -.
DR   Genevestigator; P14324; -.
DR   GermOnline; ENSG00000160752; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:EC.
DR   GO; GO:0004337; F:geranyltranstransferase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; TAS:Reactome.
DR   GO; GO:0044419; P:interspecies interaction between organisms; IEA:UniProtKB-KW.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR008949; Terpenoid_synth.
DR   Gene3D; G3DSA:1.10.600.10; Terpenoid_synth; 1.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   SUPFAM; SSF48576; Terpenoid_synth; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
DR   HOGENOMDNA; HS1.PE4938; -.
KW   ENSG000001607521755old_1320000031; ENSP000003573407901old_1320000031;
KW   D3DV91_HUMAN; Q14329_HUMAN; AK291084; AL139410; BC010004; CH471121;
KW   J05262; M29863; Z47055;
KW   3D-structure; Acetylation; Cholesterol biosynthesis;
KW   Complete proteome; Cytoplasm; Host-virus interaction;
KW   Isoprene biosynthesis; Lipid synthesis; Magnesium; Metal-binding;
KW   Polymorphism; Reference proteome; Steroid biosynthesis;
KW   Sterol biosynthesis; Transferase.
SQ   SEQUENCE   419 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPLSRWLRSV GVFLLPAPYW APRERWLGSL RRPSLVHGYP VLAWHSARCW CQAWTEEPRA
     LCSSLRMNGD QNSDVYAQEK QDFVQHFSQI VRVLTEDEMG HPEIGDAIAR LKEVLEYNAI
     GGKYNRGLTV VVAFRELVEP RKQDADSLQR AWTVGWCVEL LQAFFLVADD IMDSSLTRRG
     QICWYQKPGV GLDAINDANL LEACIYRLLK LYCREQPYYL NLIELFLQSS YQTEIGQTLD
     LLTAPQGNVD LVRFTEKRYK SIVKYKTAFY SFYLPIAAAM YMAGIDGEKE HANAKKILLE
     MGEFFQIQDD YLDLFGDPSV TGKIGTDIQD NKCSWLVVQC LQRATPEQYQ ILKENYGQKE
     AEKVARVKAL YEELDLPAVF LQYEEDSYSH IMALIEQYAA PLPPAVFLGL ARKIYKRRK
//

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