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Protein

Geranylgeranyl transferase type-2 subunit alpha

Gene

Rabggta

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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.6 Publications

Catalytic activityi

Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.4 Publications

Enzyme regulationi

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

GO - Molecular functioni

  • Rab geranylgeranyltransferase activity Source: UniProtKB
  • Rab GTPase binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • protein geranylgeranylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Prenyltransferase, Transferase

Enzyme and pathway databases

ReactomeiR-RNO-6803205. TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.

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
Synonyms:Ggta
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 15

Organism-specific databases

RGDi621697. Rabggta.

Subcellular locationi

GO - Cellular componenti

  • Rab-protein geranylgeranyltransferase complex Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001197591 – 567Geranylgeranyl transferase type-2 subunit alphaAdd BLAST567

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei98PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ08602.
PRIDEiQ08602.

Expressioni

Tissue specificityi

Most abundant in the heart, brain, spleen and liver. Less in the lung, muscle, kidney and testis; in these tissues less abundant than the beta subunit.

Gene expression databases

BgeeiENSRNOG00000030483.
GenevisibleiQ08602. RN.

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.9 Publications

GO - Molecular functioni

  • Rab GTPase binding Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-6137N.
STRINGi10116.ENSRNOP00000049261.

Structurei

Secondary structure

1567
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 40Combined sources28
Helixi46 – 56Combined sources11
Helixi63 – 79Combined sources17
Helixi82 – 102Combined sources21
Helixi107 – 119Combined sources13
Beta strandi120 – 122Combined sources3
Helixi125 – 138Combined sources14
Helixi143 – 155Combined sources13
Helixi160 – 173Combined sources14
Helixi178 – 191Combined sources14
Beta strandi197 – 199Combined sources3
Helixi205 – 221Combined sources17
Helixi226 – 237Combined sources12
Beta strandi245 – 251Combined sources7
Turni252 – 255Combined sources4
Beta strandi256 – 265Combined sources10
Beta strandi267 – 269Combined sources3
Beta strandi274 – 283Combined sources10
Beta strandi296 – 303Combined sources8
Helixi306 – 308Combined sources3
Beta strandi313 – 322Combined sources10
Turni323 – 326Combined sources4
Beta strandi327 – 334Combined sources8
Beta strandi338 – 343Combined sources6
Turni347 – 350Combined sources4
Helixi353 – 355Combined sources3
Helixi358 – 377Combined sources20
Helixi382 – 395Combined sources14
Turni397 – 400Combined sources4
Helixi401 – 414Combined sources14
Helixi416 – 418Combined sources3
Helixi419 – 438Combined sources20
Beta strandi444 – 447Combined sources4
Helixi459 – 462Combined sources4
Beta strandi467 – 469Combined sources3
Helixi480 – 484Combined sources5
Beta strandi490 – 492Combined sources3
Helixi502 – 504Combined sources3
Beta strandi512 – 514Combined sources3
Beta strandi522 – 524Combined sources3
Helixi527 – 531Combined sources5
Beta strandi537 – 539Combined sources3
Helixi544 – 547Combined sources4
Beta strandi548 – 550Combined sources3
Helixi554 – 558Combined sources5
Beta strandi563 – 566Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DCEX-ray2.00A/C1-567[»]
1LTXX-ray2.70A1-567[»]
3C72X-ray2.30A1-236[»]
A353-441[»]
3DSSX-ray1.80A1-237[»]
A353-441[»]
3DSTX-ray1.90A1-237[»]
A353-441[»]
3DSUX-ray1.90A1-237[»]
A353-441[»]
3DSVX-ray2.10A1-237[»]
A353-441[»]
3DSWX-ray2.15A1-237[»]
A353-441[»]
3DSXX-ray2.10A1-237[»]
A353-441[»]
3HXBX-ray2.25A1-237[»]
A353-441[»]
3HXCX-ray1.95A1-237[»]
A353-441[»]
3HXDX-ray1.95A1-237[»]
A353-441[»]
3HXEX-ray1.95A1-237[»]
A353-441[»]
3HXFX-ray1.90A1-237[»]
A353-441[»]
3PZ1X-ray1.95A1-237[»]
A353-441[»]
3PZ2X-ray2.35A1-237[»]
A353-441[»]
3PZ3X-ray2.00A1-237[»]
A353-441[»]
4EHMX-ray2.20A1-237[»]
A353-441[»]
4GTSX-ray2.45A1-237[»]
A353-441[»]
4GTTX-ray2.05A1-237[»]
A353-441[»]
4GTVX-ray1.95A1-237[»]
A353-441[»]
ProteinModelPortaliQ08602.
SMRiQ08602.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08602.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati44 – 78PFTA 1Add BLAST35
Repeati88 – 122PFTA 2Add BLAST35
Repeati124 – 158PFTA 3Add BLAST35
Repeati159 – 193PFTA 4Add BLAST35
Repeati207 – 241PFTA 5Add BLAST35
Repeati363 – 397PFTA 6Add BLAST35
Repeati442 – 463LRR 1Add BLAST22
Repeati464 – 486LRR 2Add BLAST23
Repeati487 – 508LRR 3Add BLAST22
Repeati509 – 530LRR 4Add BLAST22
Repeati534 – 555LRR 5Add BLAST22

Sequence similaritiesi

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

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiKOG0529. Eukaryota.
COG5536. LUCA.
GeneTreeiENSGT00550000075121.
HOGENOMiHOG000007845.
HOVERGENiHBG002171.
InParanoidiQ08602.
KOiK14050.
OMAiMRAAYLD.
OrthoDBiEOG091G0L9H.
PhylomeDBiQ08602.
TreeFamiTF315057.

Family and domain databases

Gene3Di2.60.40.1130. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR002088. Prenyl_trans_a.
IPR009087. RabGGT_asu_insert-domain.
IPR032955. RabGGTase_alpha.
[Graphical view]
PANTHERiPTHR11129:SF2. PTHR11129:SF2. 2 hits.
PfamiPF01239. PPTA. 4 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.
SSF52058. SSF52058. 1 hit.
PROSITEiPS51147. PFTA. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q08602-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHGRLKVKTS EEQAEAKRLE REQKLKLYQS ATQAVFQKRQ AGELDESVLE
60 70 80 90 100
LTSQILGANP DFATLWNCRR EVLQHLETEK SPEESAALVK AELGFLESCL
110 120 130 140 150
RVNPKSYGTW HHRCWLLSRL PEPNWARELE LCARFLEADE RNFHCWDYRR
160 170 180 190 200
FVAAQAAVAP AEELAFTDSL ITRNFSNYSS WHYRSCLLPQ LHPQPDSGPQ
210 220 230 240 250
GRLPENVLLK ELELVQNAFF TDPNDQSAWF YHRWLLGRAE PHDVLCCVHV
260 270 280 290 300
SREEACLSVC FSRPLTVGSR MGTLLLMVDE APLSVEWRTP DGRNRPSHVW
310 320 330 340 350
LCDLPAASLN DQLPQHTFRV IWTGSDSQKE CVLLKDRPEC WCRDSATDEQ
360 370 380 390 400
LFRCELSVEK STVLQSELES CKELQELEPE NKWCLLTIIL LMRALDPLLY
410 420 430 440 450
EKETLQYFST LKAVDPMRAA YLDDLRSKFL LENSVLKMEY ADVRVLHLAH
460 470 480 490 500
KDLTVLCHLE QLLLVTHLDL SHNRLRALPP ALAALRCLEV LQASDNALEN
510 520 530 540 550
VDGVANLPRL QELLLCNNRL QQSAAIQPLV SCPRLVLLNL QGNSLCQEEG
560
IQERLAEMLP SVSSILT
Length:567
Mass (Da):64,904
Last modified:February 1, 1995 - v1
Checksum:i1F9D235F973EABD5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti169S → D AA sequence (PubMed:8505342).Curated1
Sequence conflicti227S → Q AA sequence (PubMed:8505342).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10415 mRNA. Translation: AAA41998.1.
S62096 mRNA. Translation: AAB27018.1.
BC086547 mRNA. Translation: AAH86547.1.
PIRiA45977.
RefSeqiNP_113842.1. NM_031654.2.
XP_006252071.1. XM_006252009.3.
XP_006252072.1. XM_006252010.3.
UniGeneiRn.29434.

Genome annotation databases

EnsembliENSRNOT00000048455; ENSRNOP00000049261; ENSRNOG00000030483.
GeneIDi58983.
KEGGirno:58983.
UCSCiRGD:621697. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10415 mRNA. Translation: AAA41998.1.
S62096 mRNA. Translation: AAB27018.1.
BC086547 mRNA. Translation: AAH86547.1.
PIRiA45977.
RefSeqiNP_113842.1. NM_031654.2.
XP_006252071.1. XM_006252009.3.
XP_006252072.1. XM_006252010.3.
UniGeneiRn.29434.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DCEX-ray2.00A/C1-567[»]
1LTXX-ray2.70A1-567[»]
3C72X-ray2.30A1-236[»]
A353-441[»]
3DSSX-ray1.80A1-237[»]
A353-441[»]
3DSTX-ray1.90A1-237[»]
A353-441[»]
3DSUX-ray1.90A1-237[»]
A353-441[»]
3DSVX-ray2.10A1-237[»]
A353-441[»]
3DSWX-ray2.15A1-237[»]
A353-441[»]
3DSXX-ray2.10A1-237[»]
A353-441[»]
3HXBX-ray2.25A1-237[»]
A353-441[»]
3HXCX-ray1.95A1-237[»]
A353-441[»]
3HXDX-ray1.95A1-237[»]
A353-441[»]
3HXEX-ray1.95A1-237[»]
A353-441[»]
3HXFX-ray1.90A1-237[»]
A353-441[»]
3PZ1X-ray1.95A1-237[»]
A353-441[»]
3PZ2X-ray2.35A1-237[»]
A353-441[»]
3PZ3X-ray2.00A1-237[»]
A353-441[»]
4EHMX-ray2.20A1-237[»]
A353-441[»]
4GTSX-ray2.45A1-237[»]
A353-441[»]
4GTTX-ray2.05A1-237[»]
A353-441[»]
4GTVX-ray1.95A1-237[»]
A353-441[»]
ProteinModelPortaliQ08602.
SMRiQ08602.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6137N.
STRINGi10116.ENSRNOP00000049261.

Proteomic databases

PaxDbiQ08602.
PRIDEiQ08602.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000048455; ENSRNOP00000049261; ENSRNOG00000030483.
GeneIDi58983.
KEGGirno:58983.
UCSCiRGD:621697. rat.

Organism-specific databases

CTDi5875.
RGDi621697. Rabggta.

Phylogenomic databases

eggNOGiKOG0529. Eukaryota.
COG5536. LUCA.
GeneTreeiENSGT00550000075121.
HOGENOMiHOG000007845.
HOVERGENiHBG002171.
InParanoidiQ08602.
KOiK14050.
OMAiMRAAYLD.
OrthoDBiEOG091G0L9H.
PhylomeDBiQ08602.
TreeFamiTF315057.

Enzyme and pathway databases

ReactomeiR-RNO-6803205. TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.

Miscellaneous databases

EvolutionaryTraceiQ08602.
PROiQ08602.

Gene expression databases

BgeeiENSRNOG00000030483.
GenevisibleiQ08602. RN.

Family and domain databases

Gene3Di2.60.40.1130. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR002088. Prenyl_trans_a.
IPR009087. RabGGT_asu_insert-domain.
IPR032955. RabGGTase_alpha.
[Graphical view]
PANTHERiPTHR11129:SF2. PTHR11129:SF2. 2 hits.
PfamiPF01239. PPTA. 4 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.
SSF52058. SSF52058. 1 hit.
PROSITEiPS51147. PFTA. 6 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPGTA_RAT
AccessioniPrimary (citable) accession number: Q08602
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.