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Q5E9B3

- PGTB2_BOVIN

UniProt

Q5E9B3 - PGTB2_BOVIN

Protein

Geranylgeranyl transferase type-2 subunit beta

Gene

RABGGTB

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (15 Mar 2005)
      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.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Enzyme regulationi

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

    Sites

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

    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
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    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_0000244433Add
    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

    PRIDEiQ5E9B3.

    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 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ5E9B3.
    SMRiQ5E9B3. Positions 3-331.
    ModBaseiSearch...
    MobiDBiSearch...

    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 bindingBy similarity
    Regioni232 – 24413Geranylgeranyl diphosphate bindingBy similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 6 PFTB repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5029.
    HOGENOMiHOG000180334.
    HOVERGENiHBG008182.
    InParanoidiQ5E9B3.
    KOiK05956.

    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.

    Q5E9B3-1 [UniParc]FASTAAdd to Basket

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    MGTPQKDVII KSDAPDTLLL EKHADYIASY GSKKDDYEYC MSEYLRMSGI    50
    YWGLTVMDLM GQLHRMNREE ILTFIKSCQH ECGGISASIG HDPHLLYTLS 100
    AVQILTLYDS INVIDINKVV EYVQSLQKED GSFAGDIWGE IDTRFSFCAV 150
    ATLALLGKLD AINVEKAIEF VLSCMNFDGG FGCRPGSESH AGQIYCCTGF 200
    LAITSQLHQV NSDLLGWWLC ERQLPSGGLN GRPEKLPDVC YSWWVLASLK 250
    IIGRLHWIDR EKLRSFILAC QDEETGGFAD RPGDMVDPFH TLFGIAGLSL 300
    LGEEQIKPVS PVFCMPEEVL RRVNVQPELV S 331
    Length:331
    Mass (Da):36,972
    Last modified:March 15, 2005 - v1
    Checksum:iCB554CA9B22D334A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT021007 mRNA. Translation: AAX09024.1.
    BC147953 mRNA. Translation: AAI47954.1.
    RefSeqiNP_001015646.1. NM_001015646.1.
    UniGeneiBt.20263.

    Genome annotation databases

    GeneIDi533276.
    KEGGibta:533276.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT021007 mRNA. Translation: AAX09024.1 .
    BC147953 mRNA. Translation: AAI47954.1 .
    RefSeqi NP_001015646.1. NM_001015646.1.
    UniGenei Bt.20263.

    3D structure databases

    ProteinModelPortali Q5E9B3.
    SMRi Q5E9B3. Positions 3-331.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q5E9B3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 533276.
    KEGGi bta:533276.

    Organism-specific databases

    CTDi 5876.

    Phylogenomic databases

    eggNOGi COG5029.
    HOGENOMi HOG000180334.
    HOVERGENi HBG008182.
    InParanoidi Q5E9B3.
    KOi K05956.

    Miscellaneous databases

    NextBioi 20875982.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Fetal medulla.

    Entry informationi

    Entry nameiPGTB2_BOVIN
    AccessioniPrimary (citable) accession number: Q5E9B3
    Secondary accession number(s): A6QLG2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2006
    Last sequence update: March 15, 2005
    Last modified: October 1, 2014
    This is version 66 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3