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Q08603

- PGTB2_RAT

UniProt

Q08603 - PGTB2_RAT

Protein

Geranylgeranyl transferase type-2 subunit beta

Gene

Rabggtb

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A.6 Publications

    Catalytic activityi

    Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.6 Publications

    Cofactori

    Binds 1 zinc ion per subunit.7 Publications

    Enzyme regulationi

    The enzymatic reaction requires the aid of a Rab escort protein (also called component A), such as CHM.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi238 – 2381Zinc; catalytic
    Metal bindingi240 – 2401Zinc; catalytic
    Metal bindingi290 – 2901Zinc; via tele nitrogen; catalytic

    GO - Molecular functioni

    1. Rab geranylgeranyltransferase activity Source: UniProtKB
    2. Rab GTPase binding Source: UniProtKB
    3. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. protein geranylgeranylation Source: UniProtKB

    Keywords - Molecular functioni

    Prenyltransferase, Transferase

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Geranylgeranyl transferase type-2 subunit beta (EC:2.5.1.60)
    Alternative name(s):
    Geranylgeranyl transferase type II subunit beta
    Short name:
    GGTase-II-beta
    Rab geranyl-geranyltransferase subunit beta
    Short name:
    Rab GG transferase beta
    Short name:
    Rab GGTase beta
    Rab geranylgeranyltransferase subunit beta
    Type II protein geranyl-geranyltransferase subunit beta
    Gene namesi
    Name:Rabggtb
    Synonyms:Ggtb
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3530. Rabggtb.

    Subcellular locationi

    GO - Cellular componenti

    1. Rab-protein geranylgeranyltransferase complex Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 331330Geranylgeranyl transferase type-2 subunit betaPRO_0000119774Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylglycineBy similarity
    Modified residuei3 – 31PhosphothreonineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ08603.
    PRIDEiQ08603.

    Expressioni

    Tissue specificityi

    Most abundant in the heart, brain, spleen and liver. Less in the lung, muscle, kidney and testis; in these tissues, more abundant than the subunit alpha.

    Gene expression databases

    GenevestigatoriQ08603.

    Interactioni

    Subunit structurei

    Heterotrimer composed of RABGGTA, RABGGTB and CHM; within this trimer, RABGGTA and RABGGTB form the catalytic component B, while CHM (component A) mediates peptide substrate binding. The Rab GGTase dimer (RGGT) interacts with CHM (component A) prior to Rab protein binding; the association is stabilized by geranylgeranyl pyrophosphate (GGpp). The CHM:RGGT:Rab complex is destabilized by GGpp. Interaction of RABGGTB with prenylated PTP4A2 precludes its association with RABGGTA and inhibits enzyme activity.9 Publications

    Protein-protein interaction databases

    DIPiDIP-6138N.

    Structurei

    Secondary structure

    1
    331
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi20 – 2910
    Beta strandi32 – 343
    Helixi36 – 383
    Helixi40 – 456
    Helixi46 – 5914
    Helixi63 – 653
    Helixi68 – 7710
    Beta strandi85 – 884
    Helixi95 – 10713
    Helixi111 – 1133
    Helixi116 – 12510
    Beta strandi133 – 1364
    Helixi143 – 15614
    Helixi159 – 1613
    Helixi164 – 1729
    Helixi191 – 20313
    Helixi207 – 2093
    Helixi212 – 2209
    Beta strandi231 – 2344
    Helixi239 – 25113
    Helixi255 – 2573
    Helixi260 – 26910
    Turni273 – 2753
    Beta strandi278 – 2814
    Helixi288 – 30013
    Turni311 – 3133
    Beta strandi314 – 3163
    Helixi317 – 3237

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DCEX-ray2.00B/D1-331[»]
    1LTXX-ray2.70B1-331[»]
    3C72X-ray2.30B1-331[»]
    3DSSX-ray1.80B1-331[»]
    3DSTX-ray1.90B1-331[»]
    3DSUX-ray1.90B1-331[»]
    3DSVX-ray2.10B1-331[»]
    3DSWX-ray2.15B1-331[»]
    3DSXX-ray2.10B1-331[»]
    3HXBX-ray2.25B1-331[»]
    3HXCX-ray1.95B1-331[»]
    3HXDX-ray1.95B1-331[»]
    3HXEX-ray1.95B1-331[»]
    3HXFX-ray1.90B1-331[»]
    4EHMX-ray2.20B2-331[»]
    4GTSX-ray2.45B2-331[»]
    4GTTX-ray2.05B2-331[»]
    4GTVX-ray1.95B2-331[»]
    ProteinModelPortaliQ08603.
    SMRiQ08603. Positions 3-331.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ08603.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati20 – 6142PFTB 1Add
    BLAST
    Repeati68 – 10942PFTB 2Add
    BLAST
    Repeati116 – 15742PFTB 3Add
    BLAST
    Repeati164 – 20542PFTB 4Add
    BLAST
    Repeati212 – 25342PFTB 5Add
    BLAST
    Repeati260 – 30243PFTB 6Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni190 – 1923Geranylgeranyl diphosphate binding
    Regioni232 – 24413Geranylgeranyl diphosphate bindingAdd
    BLAST

    Sequence similaritiesi

    Contains 6 PFTB repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5029.
    HOVERGENiHBG008182.
    InParanoidiQ08603.
    KOiK05956.
    PhylomeDBiQ08603.

    Family and domain databases

    Gene3Di1.50.10.20. 1 hit.
    InterProiIPR001330. Prenyltrans.
    IPR026873. Ptb1.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [Graphical view]
    PANTHERiPTHR11774:SF9. PTHR11774:SF9. 1 hit.
    PfamiPF00432. Prenyltrans. 2 hits.
    [Graphical view]
    SUPFAMiSSF48239. SSF48239. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q08603-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGTQQKDVTI KSDAPDTLLL EKHADYIASY GSKKDDYEYC MSEYLRMSGV    50
    YWGLTVMDLM GQLHRMNKEE ILVFIKSCQH ECGGVSASIG HDPHLLYTLS 100
    AVQILTLYDS IHVINVDKVV AYVQSLQKED GSFAGDIWGE IDTRFSFCAV 150
    ATLALLGKLD AINVEKAIEF VLSCMNFDGG FGCRPGSESH AGQIYCCTGF 200
    LAITSQLHQV NSDLLGWWLC ERQLPSGGLN GRPEKLPDVC YSWWVLASLK 250
    IIGRLHWIDR EKLRSFILAC QDEETGGFAD RPGDMVDPFH TLFGIAGLSL 300
    LGEEQIKPVS PVFCMPEEVL QRVNVQPELV S 331
    Length:331
    Mass (Da):36,856
    Last modified:February 1, 1995 - v1
    Checksum:i4B12DEC0245979D6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L10416 mRNA. Translation: AAA41999.1.
    S62097 mRNA. Translation: AAB27019.1.
    PIRiB45977.
    RefSeqiNP_619715.1. NM_138708.2.
    UniGeneiRn.107818.

    Genome annotation databases

    GeneIDi25533.
    KEGGirno:25533.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L10416 mRNA. Translation: AAA41999.1 .
    S62097 mRNA. Translation: AAB27019.1 .
    PIRi B45977.
    RefSeqi NP_619715.1. NM_138708.2.
    UniGenei Rn.107818.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DCE X-ray 2.00 B/D 1-331 [» ]
    1LTX X-ray 2.70 B 1-331 [» ]
    3C72 X-ray 2.30 B 1-331 [» ]
    3DSS X-ray 1.80 B 1-331 [» ]
    3DST X-ray 1.90 B 1-331 [» ]
    3DSU X-ray 1.90 B 1-331 [» ]
    3DSV X-ray 2.10 B 1-331 [» ]
    3DSW X-ray 2.15 B 1-331 [» ]
    3DSX X-ray 2.10 B 1-331 [» ]
    3HXB X-ray 2.25 B 1-331 [» ]
    3HXC X-ray 1.95 B 1-331 [» ]
    3HXD X-ray 1.95 B 1-331 [» ]
    3HXE X-ray 1.95 B 1-331 [» ]
    3HXF X-ray 1.90 B 1-331 [» ]
    4EHM X-ray 2.20 B 2-331 [» ]
    4GTS X-ray 2.45 B 2-331 [» ]
    4GTT X-ray 2.05 B 2-331 [» ]
    4GTV X-ray 1.95 B 2-331 [» ]
    ProteinModelPortali Q08603.
    SMRi Q08603. Positions 3-331.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6138N.

    Proteomic databases

    PaxDbi Q08603.
    PRIDEi Q08603.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 25533.
    KEGGi rno:25533.

    Organism-specific databases

    CTDi 5876.
    RGDi 3530. Rabggtb.

    Phylogenomic databases

    eggNOGi COG5029.
    HOVERGENi HBG008182.
    InParanoidi Q08603.
    KOi K05956.
    PhylomeDBi Q08603.

    Miscellaneous databases

    EvolutionaryTracei Q08603.
    NextBioi 607037.
    PROi Q08603.

    Gene expression databases

    Genevestigatori Q08603.

    Family and domain databases

    Gene3Di 1.50.10.20. 1 hit.
    InterProi IPR001330. Prenyltrans.
    IPR026873. Ptb1.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [Graphical view ]
    PANTHERi PTHR11774:SF9. PTHR11774:SF9. 1 hit.
    Pfami PF00432. Prenyltrans. 2 hits.
    [Graphical view ]
    SUPFAMi SSF48239. SSF48239. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning and expression of the alpha and beta subunits of rat Rab geranylgeranyl transferase."
      Armstrong S.A., Seabra M.C., Suedhof T.C., Goldstein J.L., Brown M.S.
      J. Biol. Chem. 268:12221-12229(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT, CATALYTIC ACTIVITY.
      Tissue: Brain.
    2. "Phosphoisoprenoids modulate association of Rab geranylgeranyltransferase with REP-1."
      Thoma N.H., Iakovenko A., Goody R.S., Alexandrov K.
      J. Biol. Chem. 276:48637-48643(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    3. "Crystal structure of Rab geranylgeranyltransferase at 2.0 A resolution."
      Zhang H., Seabra M.C., Deisenhofer J.
      Structure 8:241-251(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH RABGGTA AND ZINC IONS, SUBUNIT, COFACTOR.
    4. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS; GERANYGERANYL PHOSHATE ANALOG; RAB7A; RABGGTA AND CHM, SUBUNIT, COFACTOR.
    5. "Development of selective RabGGTase inhibitors and crystal structure of a RabGGTase-inhibitor complex."
      Guo Z., Wu Y.W., Tan K.T., Bon R.S., Guiu-Rozas E., Delon C., Nguyen T.U., Wetzel S., Arndt S., Goody R.S., Blankenfeldt W., Alexandrov K., Waldmann H.
      Angew. Chem. Int. Ed. Engl. 47:3747-3750(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH RABGGTA; INHIBITOR AND ZINC IONS, FUNCTION, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY.
    6. "Structures of RabGGTase-substrate/product complexes provide insights into the evolution of protein prenylation."
      Guo Z., Wu Y.W., Das D., Delon C., Cramer J., Yu S., Thuns S., Lupilova N., Waldmann H., Brunsveld L., Goody R.S., Alexandrov K., Blankenfeldt W.
      EMBO J. 27:2444-2456(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEXES WITH RABGGTA; RAB7A; GERANYLGERANYL DIPHOSPHATE AND ZINC IONS, COFACTOR, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY.
    7. "Design, synthesis, and characterization of peptide-based rab geranylgeranyl transferase inhibitors."
      Tan K.T., Guiu-Rozas E., Bon R.S., Guo Z., Delon C., Wetzel S., Arndt S., Alexandrov K., Waldmann H., Goody R.S., Wu Y.W., Blankenfeldt W.
      J. Med. Chem. 52:8025-8037(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH RABGGTA; ZINC IONS AND INHIBITOR, SUBUNIT, COFACTOR, FUNCTION, CATALYTIC ACTIVITY.
    8. "Psoromic acid is a selective and covalent Rab-prenylation inhibitor targeting autoinhibited RabGGTase."
      Deraeve C., Guo Z., Bon R.S., Blankenfeldt W., DiLucrezia R., Wolf A., Menninger S., Stigter E.A., Wetzel S., Choidas A., Alexandrov K., Waldmann H., Goody R.S., Wu Y.W.
      J. Am. Chem. Soc. 134:7384-7391(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH RABGGTA; ZINC IONS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, FUNCTION.
    9. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH RABGGTA; ZINC IONS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, FUNCTION.

    Entry informationi

    Entry nameiPGTB2_RAT
    AccessioniPrimary (citable) accession number: Q08603
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3