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Q92696 (PGTA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:RABGGTA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length567 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Catalytic activity

Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate. Ref.7

Enzyme regulation

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

Subunit structure

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. Ref.7 Ref.8

Sequence similarities

Belongs to the protein prenyltransferase subunit alpha family.

Contains 5 LRR (leucine-rich) repeats.

Contains 6 PFTA repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 567567Geranylgeranyl transferase type-2 subunit alpha
PRO_0000119757

Regions

Repeat44 – 7835PFTA 1
Repeat88 – 12235PFTA 2
Repeat124 – 15835PFTA 3
Repeat159 – 19335PFTA 4
Repeat207 – 24135PFTA 5
Repeat363 – 39735PFTA 6
Repeat442 – 46322LRR 1
Repeat464 – 48623LRR 2
Repeat487 – 50822LRR 3
Repeat509 – 53022LRR 4
Repeat534 – 55522LRR 5

Natural variations

Natural variant4201T → A. Ref.4
Corresponds to variant rs729421 [ dbSNP | Ensembl ].
VAR_020406

Sequences

Sequence LengthMass (Da)Tools
Q92696 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: ABA1AFFC8A496C5F

FASTA56765,072
        10         20         30         40         50         60 
MHGRLKVKTS EEQAEAKRLE REQKLKLYQS ATQAVFQKRQ AGELDESVLE LTSQILGANP 

        70         80         90        100        110        120 
DFATLWNCRR EVLQQLETQK SPEELAALVK AELGFLESCL RVNPKSYGTW HHRCWLLGRL 

       130        140        150        160        170        180 
PEPNWTRELE LCARFLEVDE RNFHCWDYRR FVATQAAVPP AEELAFTDSL ITRNFSNYSS 

       190        200        210        220        230        240 
WHYRSCLLPQ LHPQPDSGPQ GRLPEDVLLK ELELVQNAFF TDPNDQSAWF YHRWLLGRAD 

       250        260        270        280        290        300 
PQDALRCLHV SRDEACLTVS FSRPLLVGSR MEILLLMVDD SPLIVEWRTP DGRNRPSHVW 

       310        320        330        340        350        360 
LCDLPAASLN DQLPQHTFRV IWTAGDVQKE CVLLKGRQEG WCRDSTTDEQ LFRCELSVEK 

       370        380        390        400        410        420 
STVLQSELES CKELQELEPE NKWCLLTIIL LMRALDPLLY EKETLQYFQT LKAVDPMRAT 

       430        440        450        460        470        480 
YLDDLRSKFL LENSVLKMEY AEVRVLHLAH KDLTVLCHLE QLLLVTHLDL SHNRLRTLPP 

       490        500        510        520        530        540 
ALAALRCLEV LQASDNAIES LDGVTNLPRL QELLLCNNRL QQPAVLQPLA SCPRLVLLNL 

       550        560 
QGNPLCQAVG ILEQLAELLP SVSSVLT 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS45088.1.
PIRJC5538.
RefSeqNP_004572.3. NM_004581.5.
NP_878256.1. NM_182836.2.
UniGeneHs.377992.

3D structure databases

ProteinModelPortalQ92696.
SMRQ92696. Positions 2-567.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111813. 7 interactions.
STRING9606.ENSP00000216840.

Chemistry

BindingDBQ92696.

PTM databases

PhosphoSiteQ92696.

Polymorphism databases

DMDM6093707.

Proteomic databases

MaxQBQ92696.
PaxDbQ92696.
PRIDEQ92696.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216840; ENSP00000216840; ENSG00000100949.
ENST00000399409; ENSP00000382341; ENSG00000100949.
GeneID5875.
KEGGhsa:5875.
UCSCuc001wof.4. human.

Organism-specific databases

CTD5875.
GeneCardsGC14M024734.
HGNCHGNC:9795. RABGGTA.
HPAHPA043488.
MIM601905. gene.
neXtProtNX_Q92696.
PharmGKBPA34156.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5536.
HOGENOMHOG000007845.
HOVERGENHBG002171.
InParanoidQ92696.
KOK14050.
OMAWNCRREV.
OrthoDBEOG7PP56C.
PhylomeDBQ92696.
TreeFamTF315057.

Gene expression databases

ArrayExpressQ92696.
BgeeQ92696.
CleanExHS_RABGGTA.
GenevestigatorQ92696.

Family and domain databases

Gene3D2.60.40.1130. 1 hit.
InterProIPR001611. Leu-rich_rpt.
IPR002088. Prenyl_trans_a.
IPR009087. RabGGT_asu_insert-domain.
[Graphical view]
PfamPF00560. LRR_1. 1 hit.
PF01239. PPTA. 5 hits.
PF07711. RabGGT_insert. 1 hit.
[Graphical view]
ProDomPD331837. RabGG_trans_A. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF49594. SSF49594. 1 hit.
PROSITEPS51450. LRR. 5 hits.
PS51147. PFTA. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi5875.
NextBio22826.
PROQ92696.
SOURCESearch...

Entry information

Entry namePGTA_HUMAN
AccessionPrimary (citable) accession number: Q92696
Secondary accession number(s): A8K5N2, D3DS69
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1999
Last modified: July 9, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM