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P53611

- PGTB2_HUMAN

UniProt

P53611 - PGTB2_HUMAN

Protein

Geranylgeranyl transferase type-2 subunit beta

Gene

RABGGTB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      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.

    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).

    Sites

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular protein modification process Source: UniProtKB
    2. protein geranylgeranylation Source: UniProtKB
    3. visual perception Source: ProtInc

    Keywords - Molecular functioni

    Prenyltransferase, Transferase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi2.5.1.60. 2681.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9796. RABGGTB.

    Subcellular locationi

    GO - Cellular componenti

    1. Rab-protein geranylgeranyltransferase complex Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34157.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 331330Geranylgeranyl transferase type-2 subunit betaPRO_0000119772Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylglycine2 Publications
    Modified residuei3 – 31Phosphothreonine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP53611.
    PaxDbiP53611.
    PRIDEiP53611.

    PTM databases

    PhosphoSiteiP53611.

    Expressioni

    Gene expression databases

    ArrayExpressiP53611.
    BgeeiP53611.
    CleanExiHS_RABGGTB.
    GenevestigatoriP53611.

    Organism-specific databases

    HPAiHPA026585.
    HPA027167.

    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.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARAFP103983EBI-536715,EBI-365961

    Protein-protein interaction databases

    BioGridi111814. 7 interactions.
    IntActiP53611. 2 interactions.
    MINTiMINT-260716.
    STRINGi9606.ENSP00000317473.

    Structurei

    3D structure databases

    ProteinModelPortaliP53611.
    SMRiP53611. Positions 5-331.
    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.
    InParanoidiP53611.
    KOiK05956.
    OMAiESHAGLI.
    OrthoDBiEOG7XSTDZ.
    PhylomeDBiP53611.
    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. 5 hits.
    [Graphical view]
    SUPFAMiSSF48239. SSF48239. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P53611-1 [UniParc]FASTAAdd to Basket

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    MGTPQKDVII KSDAPDTLLL EKHADYIASY GSKKDDYEYC MSEYLRMSGI    50
    YWGLTVMDLM GQLHRMNREE ILAFIKSCQH ECGGISASIG HDPHLLYTLS 100
    AVQILTLYDS INVIDVNKVV EYVKGLQKED GSFAGDIWGE IDTRFSFCAV 150
    ATLALLGKLD AINVEKAIEF VLSCMNFDGG FGCRPGSESH AGQIYCCTGF 200
    LAITSQLHQV NSDLLGWWLC ERQLPSGGLN GRPEKLPDVC YSWWVLASLK 250
    IIGRLHWIDR EKLRNFILAC QDEETGGFAD RPGDMVDPFH TLFGIAGLSL 300
    LGEEQIKPVN PVFCMPEEVL QRVNVQPELV S 331
    Length:331
    Mass (Da):36,924
    Last modified:November 1, 1997 - v2
    Checksum:i37A8A6329146C49B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti153 – 1531L → F in AAA91473. 1 PublicationCurated
    Sequence conflicti177 – 1771F → S in CAA69383. (PubMed:8954794)Curated
    Sequence conflicti211 – 2111N → T in CAA69383. (PubMed:8954794)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49245 mRNA. Translation: AAA91473.1.
    X98001 mRNA. Translation: CAA66638.1.
    Y08201 mRNA. Translation: CAA69383.1.
    BC020790 mRNA. Translation: AAH20790.1.
    CCDSiCCDS669.1.
    PIRiG02431.
    RefSeqiNP_004573.2. NM_004582.3.
    UniGeneiHs.78948.

    Genome annotation databases

    EnsembliENST00000319942; ENSP00000317473; ENSG00000137955.
    GeneIDi5876.
    KEGGihsa:5876.
    UCSCiuc001dgy.2. human.

    Polymorphism databases

    DMDMi2506788.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Rab geranylgeranyltransferase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49245 mRNA. Translation: AAA91473.1 .
    X98001 mRNA. Translation: CAA66638.1 .
    Y08201 mRNA. Translation: CAA69383.1 .
    BC020790 mRNA. Translation: AAH20790.1 .
    CCDSi CCDS669.1.
    PIRi G02431.
    RefSeqi NP_004573.2. NM_004582.3.
    UniGenei Hs.78948.

    3D structure databases

    ProteinModelPortali P53611.
    SMRi P53611. Positions 5-331.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111814. 7 interactions.
    IntActi P53611. 2 interactions.
    MINTi MINT-260716.
    STRINGi 9606.ENSP00000317473.

    Chemistry

    BindingDBi P53611.

    PTM databases

    PhosphoSitei P53611.

    Polymorphism databases

    DMDMi 2506788.

    Proteomic databases

    MaxQBi P53611.
    PaxDbi P53611.
    PRIDEi P53611.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000319942 ; ENSP00000317473 ; ENSG00000137955 .
    GeneIDi 5876.
    KEGGi hsa:5876.
    UCSCi uc001dgy.2. human.

    Organism-specific databases

    CTDi 5876.
    GeneCardsi GC01P076251.
    HGNCi HGNC:9796. RABGGTB.
    HPAi HPA026585.
    HPA027167.
    MIMi 179080. gene.
    neXtProti NX_P53611.
    PharmGKBi PA34157.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5029.
    HOGENOMi HOG000180334.
    HOVERGENi HBG008182.
    InParanoidi P53611.
    KOi K05956.
    OMAi ESHAGLI.
    OrthoDBi EOG7XSTDZ.
    PhylomeDBi P53611.
    TreeFami TF105762.

    Enzyme and pathway databases

    BRENDAi 2.5.1.60. 2681.

    Miscellaneous databases

    ChiTaRSi RABGGTB. human.
    GenomeRNAii 5876.
    NextBioi 22832.
    PROi P53611.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P53611.
    Bgeei P53611.
    CleanExi HS_RABGGTB.
    Genevestigatori P53611.

    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. 5 hits.
    [Graphical view ]
    SUPFAMi SSF48239. SSF48239. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Chang H.Y., Wu S.R., Peng H.L.
      Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "Characterization of the interaction of the monomeric GTP-binding protein Rab3a with geranylgeranyl transferase II."
      Johannes L., Perez F., Laran-Chich M.P., Henry J.P., Darchen F.
      Eur. J. Biochem. 239:362-368(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    3. "cDNA cloning and chromosomal localization of the genes encoding the alpha- and beta-subunits of human Rab geranylgeranyl transferase: the 3' end of the alpha-subunit gene overlaps with the transglutaminase 1 gene promoter."
      van Bokhoven H., Rawson R.B., Merkx G.F.M., Cremers F.P.M., Seabra M.C.
      Genomics 38:133-140(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal brain.
    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: Skeletal muscle.
    5. "Interaction of farnesylated PRL-2, a protein-tyrosine phosphatase, with the beta-subunit of geranylgeranyltransferase II."
      Si X., Zeng Q., Ng C.H., Hong W., Pallen C.J.
      J. Biol. Chem. 276:32875-32882(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTP4A2.
    6. "Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A."
      Farnsworth C.C., Seabra M.C., Ericsson L.H., Gelb M.H., Glomset J.A.
      Proc. Natl. Acad. Sci. U.S.A. 91:11963-11967(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    7. "Rab geranylgeranylation occurs preferentially via the pre-formed REP-RGGT complex and is regulated by geranylgeranyl pyrophosphate."
      Baron R.A., Seabra M.C.
      Biochem. J. 415:67-75(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPGTB2_HUMAN
    AccessioniPrimary (citable) accession number: P53611
    Secondary accession number(s): Q92697
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3