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P53612

- PGTB2_MOUSE

UniProt

P53612 - PGTB2_MOUSE

Protein

Geranylgeranyl transferase type-2 subunit beta

Gene

Rabggtb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      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.1 Publication

    Catalytic activityi

    Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.1 Publication

    Cofactori

    Binds 1 zinc ion per subunit.1 Publication

    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 bindingi246 – 2461Zinc; catalytic1 Publication
    Metal bindingi248 – 2481Zinc; catalytic1 Publication
    Metal bindingi298 – 2981Zinc; via tele nitrogen; catalytic1 Publication

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:99537. Rabggtb.

    Subcellular locationi

    GO - Cellular componenti

    1. Rab-protein geranylgeranyltransferase complex Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 339339Geranylgeranyl transferase type-2 subunit betaPRO_0000119773Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei11 – 111PhosphothreonineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP53612.
    PaxDbiP53612.
    PRIDEiP53612.

    PTM databases

    PhosphoSiteiP53612.

    Expressioni

    Tissue specificityi

    Ubiquitous. Detected in all the major organs in adult animals.1 Publication

    Developmental stagei

    Specific expression was elevated in mid-gestation stages, particularly developing liver and spinal cord.1 Publication

    Inductioni

    Increased dramatically by cycloheximide (CHX) treatment within a short time (as early as 2 hours). Actinomycin D was used to determine the half-life, CHX treatment resulted in a dramatic increase of the half-life from 8 hours to greater than 12 hours.1 Publication

    Gene expression databases

    ArrayExpressiP53612.
    BgeeiP53612.
    CleanExiMM_RABGGTB.
    GenevestigatoriP53612.

    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

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000087396.

    Structurei

    Secondary structure

    1
    339
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi28 – 3710
    Helixi45 – 484
    Helixi49 – 535
    Helixi54 – 6714
    Helixi71 – 733
    Helixi76 – 8510
    Beta strandi93 – 964
    Helixi103 – 11513
    Helixi119 – 1213
    Helixi124 – 13310
    Beta strandi141 – 1444
    Helixi151 – 16414
    Helixi167 – 1693
    Helixi172 – 1809
    Helixi199 – 21113
    Helixi215 – 2173
    Helixi220 – 2289
    Helixi249 – 25911
    Helixi263 – 2653
    Helixi268 – 27710
    Turni281 – 2833
    Helixi296 – 30813
    Turni319 – 3213
    Beta strandi322 – 3243
    Helixi325 – 3317

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3PZ1X-ray1.95B10-339[»]
    3PZ2X-ray2.35B10-339[»]
    3PZ3X-ray2.00B10-339[»]
    ProteinModelPortaliP53612.
    SMRiP53612. Positions 13-339.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53612.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati28 – 6942PFTB 1Add
    BLAST
    Repeati76 – 11742PFTB 2Add
    BLAST
    Repeati124 – 16542PFTB 3Add
    BLAST
    Repeati172 – 21342PFTB 4Add
    BLAST
    Repeati220 – 26142PFTB 5Add
    BLAST
    Repeati268 – 31043PFTB 6Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni198 – 2003Geranylgeranyl diphosphate bindingBy similarity
    Regioni240 – 25213Geranylgeranyl diphosphate bindingBy similarityAdd
    BLAST
    Regioni249 – 2524Geranylgeranyl diphosphate bindingBy similarity

    Sequence similaritiesi

    Contains 6 PFTB repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5029.
    GeneTreeiENSGT00530000063392.
    HOGENOMiHOG000180334.
    HOVERGENiHBG008182.
    InParanoidiA2RTE6.
    KOiK05956.
    OMAiESHAGLI.
    TreeFamiTF105762.

    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.

    P53612-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSLLFSWKG TQQKDVTIKS DAPDTLLLEK HADYIASYGS KKDDYEYCMS    50
    EYLRMSGVYW GLTVMDLMGQ LHRMNREEIL VFIKSCQHEC GGISASIGHD 100
    PHLLYTLSAV QILTLYDSVH VINVDKVVAY VQSLQKEDGS FAGDIWGEID 150
    TRFSFCAVAT LALLGKLDAI NVEKAIEFVL SCMNFDGGFG CRPGSESHAG 200
    QIYCCTGFLA ITSQLHQVNS DLLGWWLCER QLPSGGLNGR PEKLPDVCYS 250
    WWVLASLKII GRLHWIDREK LRSFILACQD EETGGFADRP GDMVDPFHTL 300
    FGIAGLSLLG EEQIKPVSPV FCMPEEVLQR VNVQPELVS 339
    Length:339
    Mass (Da):37,803
    Last modified:July 27, 2011 - v2
    Checksum:i4765A39E5392B8B5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti230 – 2301R → A in AAB01502. (PubMed:7544156)Curated
    Sequence conflicti236 – 2361G → A in AAB01502. (PubMed:7544156)Curated
    Sequence conflicti241 – 2411P → R in AAB01502. (PubMed:7544156)Curated
    Sequence conflicti267 – 2682DR → VS in AAB01502. (PubMed:7544156)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U12922 mRNA. Translation: AAB01502.1.
    CH466532 Genomic DNA. Translation: EDL11902.1.
    BC132473 mRNA. Translation: AAI32474.1.
    BC138547 mRNA. Translation: AAI38548.1.
    CCDSiCCDS17923.1.
    PIRiI49116.
    JC6177.
    RefSeqiNP_035361.2. NM_011231.2.
    UniGeneiMm.277831.

    Genome annotation databases

    EnsembliENSMUST00000167111; ENSMUSP00000129481; ENSMUSG00000038975.
    GeneIDi19352.
    KEGGimmu:19352.
    UCSCiuc008rug.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U12922 mRNA. Translation: AAB01502.1 .
    CH466532 Genomic DNA. Translation: EDL11902.1 .
    BC132473 mRNA. Translation: AAI32474.1 .
    BC138547 mRNA. Translation: AAI38548.1 .
    CCDSi CCDS17923.1.
    PIRi I49116.
    JC6177.
    RefSeqi NP_035361.2. NM_011231.2.
    UniGenei Mm.277831.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3PZ1 X-ray 1.95 B 10-339 [» ]
    3PZ2 X-ray 2.35 B 10-339 [» ]
    3PZ3 X-ray 2.00 B 10-339 [» ]
    ProteinModelPortali P53612.
    SMRi P53612. Positions 13-339.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000087396.

    PTM databases

    PhosphoSitei P53612.

    Proteomic databases

    MaxQBi P53612.
    PaxDbi P53612.
    PRIDEi P53612.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000167111 ; ENSMUSP00000129481 ; ENSMUSG00000038975 .
    GeneIDi 19352.
    KEGGi mmu:19352.
    UCSCi uc008rug.2. mouse.

    Organism-specific databases

    CTDi 5876.
    MGIi MGI:99537. Rabggtb.

    Phylogenomic databases

    eggNOGi COG5029.
    GeneTreei ENSGT00530000063392.
    HOGENOMi HOG000180334.
    HOVERGENi HBG008182.
    InParanoidi A2RTE6.
    KOi K05956.
    OMAi ESHAGLI.
    TreeFami TF105762.

    Miscellaneous databases

    EvolutionaryTracei P53612.
    NextBioi 296383.
    PROi P53612.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P53612.
    Bgeei P53612.
    CleanExi MM_RABGGTB.
    Genevestigatori P53612.

    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. "Studies of cloning, chromosomal mapping, and embryonic expression of the mouse Rab geranylgeranyl transferase beta subunit."
      Wei L.-N., Lee C.-H., Chinpaisal C., Copeland N.G., Gilbert D.J., Jenkins N.A., Hsu Y.-C.
      Cell Growth Differ. 6:607-614(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: CD-1.
      Tissue: Embryo.
    2. "Studies of the mouse Rab geranylgeranyl transferase beta subunit: gene structure, expression and regulation."
      Chinpaisal C., Lee C.-H., Wei L.-N.
      Gene 184:237-243(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
      Strain: CD-1.
      Tissue: Embryo.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 10-339 IN COMPLEX WITH ZINC AND GERANYLGERANYL DIPHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.

    Entry informationi

    Entry nameiPGTB2_MOUSE
    AccessioniPrimary (citable) accession number: P53612
    Secondary accession number(s): A2RTE6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 110 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3