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Q92696

- PGTA_HUMAN

UniProt

Q92696 - PGTA_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ92696.
CleanExiHS_RABGGTA.
ExpressionAtlasiQ92696. baseline and differential.
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. 13 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.
GeneTreeiENSGT00550000075121.
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

        10         20         30         40         50
MHGRLKVKTS EEQAEAKRLE REQKLKLYQS ATQAVFQKRQ AGELDESVLE
60 70 80 90 100
LTSQILGANP DFATLWNCRR EVLQQLETQK SPEELAALVK AELGFLESCL
110 120 130 140 150
RVNPKSYGTW HHRCWLLGRL PEPNWTRELE LCARFLEVDE RNFHCWDYRR
160 170 180 190 200
FVATQAAVPP AEELAFTDSL ITRNFSNYSS WHYRSCLLPQ LHPQPDSGPQ
210 220 230 240 250
GRLPEDVLLK ELELVQNAFF TDPNDQSAWF YHRWLLGRAD PQDALRCLHV
260 270 280 290 300
SRDEACLTVS FSRPLLVGSR MEILLLMVDD SPLIVEWRTP DGRNRPSHVW
310 320 330 340 350
LCDLPAASLN DQLPQHTFRV IWTAGDVQKE CVLLKGRQEG WCRDSTTDEQ
360 370 380 390 400
LFRCELSVEK STVLQSELES CKELQELEPE NKWCLLTIIL LMRALDPLLY
410 420 430 440 450
EKETLQYFQT LKAVDPMRAT YLDDLRSKFL LENSVLKMEY AEVRVLHLAH
460 470 480 490 500
KDLTVLCHLE QLLLVTHLDL SHNRLRTLPP ALAALRCLEV LQASDNAIES
510 520 530 540 550
LDGVTNLPRL QELLLCNNRL QQPAVLQPLA SCPRLVLLNL QGNPLCQAVG
560
ILEQLAELLP SVSSVLT
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 13 interactions.
STRINGi 9606.ENSP00000216840.

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.
GeneTreei ENSGT00550000075121.
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

Bgeei Q92696.
CleanExi HS_RABGGTA.
ExpressionAtlasi Q92696. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 135 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