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Q92696

- PGTA_HUMAN

UniProt

Q92696 - PGTA_HUMAN

Protein

Geranylgeranyl transferase type-2 subunit alpha

Gene

RABGGTA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (15 Jul 1999)
      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

    Enzyme regulationi

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

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Prenyltransferase, Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Geranylgeranyl transferase type-2 subunit alpha (EC:2.5.1.60)
    Alternative name(s):
    Geranylgeranyl transferase type II subunit alpha
    Rab geranyl-geranyltransferase subunit alpha
    Short name:
    Rab GG transferase alpha
    Short name:
    Rab GGTase alpha
    Rab geranylgeranyltransferase subunit alpha
    Gene namesi
    Name:RABGGTA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:9795. RABGGTA.

    Subcellular locationi

    GO - Cellular componenti

    1. Rab-protein geranylgeranyltransferase complex Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34156.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 567567Geranylgeranyl transferase type-2 subunit alphaPRO_0000119757Add
    BLAST

    Proteomic databases

    MaxQBiQ92696.
    PaxDbiQ92696.
    PRIDEiQ92696.

    PTM databases

    PhosphoSiteiQ92696.

    Expressioni

    Gene expression databases

    ArrayExpressiQ92696.
    BgeeiQ92696.
    CleanExiHS_RABGGTA.
    GenevestigatoriQ92696.

    Organism-specific databases

    HPAiHPA043488.

    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.2 Publications

    Protein-protein interaction databases

    BioGridi111813. 7 interactions.
    STRINGi9606.ENSP00000216840.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92696.
    SMRiQ92696. Positions 2-567.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati44 – 7835PFTA 1Add
    BLAST
    Repeati88 – 12235PFTA 2Add
    BLAST
    Repeati124 – 15835PFTA 3Add
    BLAST
    Repeati159 – 19335PFTA 4Add
    BLAST
    Repeati207 – 24135PFTA 5Add
    BLAST
    Repeati363 – 39735PFTA 6Add
    BLAST
    Repeati442 – 46322LRR 1Add
    BLAST
    Repeati464 – 48623LRR 2Add
    BLAST
    Repeati487 – 50822LRR 3Add
    BLAST
    Repeati509 – 53022LRR 4Add
    BLAST
    Repeati534 – 55522LRR 5Add
    BLAST

    Sequence similaritiesi

    Contains 5 LRR (leucine-rich) repeats.Curated
    Contains 6 PFTA repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Leucine-rich repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG5536.
    HOGENOMiHOG000007845.
    HOVERGENiHBG002171.
    InParanoidiQ92696.
    KOiK14050.
    OMAiWNCRREV.
    OrthoDBiEOG7PP56C.
    PhylomeDBiQ92696.
    TreeFamiTF315057.

    Family and domain databases

    Gene3Di2.60.40.1130. 1 hit.
    InterProiIPR001611. Leu-rich_rpt.
    IPR002088. Prenyl_trans_a.
    IPR009087. RabGGT_asu_insert-domain.
    [Graphical view]
    PfamiPF00560. LRR_1. 1 hit.
    PF01239. PPTA. 5 hits.
    PF07711. RabGGT_insert. 1 hit.
    [Graphical view]
    ProDomiPD331837. RabGG_trans_A. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF49594. SSF49594. 1 hit.
    PROSITEiPS51450. LRR. 5 hits.
    PS51147. PFTA. 6 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q92696-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHGRLKVKTS EEQAEAKRLE REQKLKLYQS ATQAVFQKRQ AGELDESVLE    50
    LTSQILGANP DFATLWNCRR EVLQQLETQK SPEELAALVK AELGFLESCL 100
    RVNPKSYGTW HHRCWLLGRL PEPNWTRELE LCARFLEVDE RNFHCWDYRR 150
    FVATQAAVPP AEELAFTDSL ITRNFSNYSS WHYRSCLLPQ LHPQPDSGPQ 200
    GRLPEDVLLK ELELVQNAFF TDPNDQSAWF YHRWLLGRAD PQDALRCLHV 250
    SRDEACLTVS FSRPLLVGSR MEILLLMVDD SPLIVEWRTP DGRNRPSHVW 300
    LCDLPAASLN DQLPQHTFRV IWTAGDVQKE CVLLKGRQEG WCRDSTTDEQ 350
    LFRCELSVEK STVLQSELES CKELQELEPE NKWCLLTIIL LMRALDPLLY 400
    EKETLQYFQT LKAVDPMRAT YLDDLRSKFL LENSVLKMEY AEVRVLHLAH 450
    KDLTVLCHLE QLLLVTHLDL SHNRLRTLPP ALAALRCLEV LQASDNAIES 500
    LDGVTNLPRL QELLLCNNRL QQPAVLQPLA SCPRLVLLNL QGNPLCQAVG 550
    ILEQLAELLP SVSSVLT 567
    Length:567
    Mass (Da):65,072
    Last modified:July 15, 1999 - v2
    Checksum:iABA1AFFC8A496C5F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti420 – 4201T → A.1 Publication
    Corresponds to variant rs729421 [ dbSNP | Ensembl ].
    VAR_020406

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08200 mRNA. Translation: CAA69382.1.
    AK291347 mRNA. Translation: BAF84036.1.
    AK292613 mRNA. Translation: BAF85302.1.
    CH471078 Genomic DNA. Translation: EAW66044.1.
    CH471078 Genomic DNA. Translation: EAW66045.1.
    BC003093 mRNA. Translation: AAH03093.1.
    CCDSiCCDS45088.1.
    PIRiJC5538.
    RefSeqiNP_004572.3. NM_004581.5.
    NP_878256.1. NM_182836.2.
    UniGeneiHs.377992.

    Genome annotation databases

    EnsembliENST00000216840; ENSP00000216840; ENSG00000100949.
    ENST00000399409; ENSP00000382341; ENSG00000100949.
    GeneIDi5875.
    KEGGihsa:5875.
    UCSCiuc001wof.4. human.

    Polymorphism databases

    DMDMi6093707.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08200 mRNA. Translation: CAA69382.1 .
    AK291347 mRNA. Translation: BAF84036.1 .
    AK292613 mRNA. Translation: BAF85302.1 .
    CH471078 Genomic DNA. Translation: EAW66044.1 .
    CH471078 Genomic DNA. Translation: EAW66045.1 .
    BC003093 mRNA. Translation: AAH03093.1 .
    CCDSi CCDS45088.1.
    PIRi JC5538.
    RefSeqi NP_004572.3. NM_004581.5.
    NP_878256.1. NM_182836.2.
    UniGenei Hs.377992.

    3D structure databases

    ProteinModelPortali Q92696.
    SMRi Q92696. Positions 2-567.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111813. 7 interactions.
    STRINGi 9606.ENSP00000216840.

    Chemistry

    BindingDBi Q92696.

    PTM databases

    PhosphoSitei Q92696.

    Polymorphism databases

    DMDMi 6093707.

    Proteomic databases

    MaxQBi Q92696.
    PaxDbi Q92696.
    PRIDEi Q92696.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216840 ; ENSP00000216840 ; ENSG00000100949 .
    ENST00000399409 ; ENSP00000382341 ; ENSG00000100949 .
    GeneIDi 5875.
    KEGGi hsa:5875.
    UCSCi uc001wof.4. human.

    Organism-specific databases

    CTDi 5875.
    GeneCardsi GC14M024734.
    HGNCi HGNC:9795. RABGGTA.
    HPAi HPA043488.
    MIMi 601905. gene.
    neXtProti NX_Q92696.
    PharmGKBi PA34156.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5536.
    HOGENOMi HOG000007845.
    HOVERGENi HBG002171.
    InParanoidi Q92696.
    KOi K14050.
    OMAi WNCRREV.
    OrthoDBi EOG7PP56C.
    PhylomeDBi Q92696.
    TreeFami TF315057.

    Miscellaneous databases

    GenomeRNAii 5875.
    NextBioi 22826.
    PROi Q92696.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92696.
    Bgeei Q92696.
    CleanExi HS_RABGGTA.
    Genevestigatori Q92696.

    Family and domain databases

    Gene3Di 2.60.40.1130. 1 hit.
    InterProi IPR001611. Leu-rich_rpt.
    IPR002088. Prenyl_trans_a.
    IPR009087. RabGGT_asu_insert-domain.
    [Graphical view ]
    Pfami PF00560. LRR_1. 1 hit.
    PF01239. PPTA. 5 hits.
    PF07711. RabGGT_insert. 1 hit.
    [Graphical view ]
    ProDomi PD331837. RabGG_trans_A. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF49594. SSF49594. 1 hit.
    PROSITEi PS51450. LRR. 5 hits.
    PS51147. PFTA. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. van Bokhoven H.
      Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "The genes encoding geranylgeranyl transferase alpha-subunit and transglutaminase 1 are very closely linked but not functionally related in terminally differentiating keratinocytes."
      Song H.-J., Rossi A., Ceci R., Kim I.-G., Anzano M.A., Jang S.-I., De Laurenzi V., Steinert P.M.
      Biochem. Biophys. Res. Commun. 235:10-14(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-420.
      Tissue: Thymus and Tongue.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Lung.
    7. "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: FUNCTION, SUBUNIT, CATALYTIC ACTIVITY.
    8. "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.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPGTA_HUMAN
    AccessioniPrimary (citable) accession number: Q92696
    Secondary accession number(s): A8K5N2, D3DS69
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 15, 1999
    Last modified: October 1, 2014
    This is version 133 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 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3