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Protein

Geranylgeranyl transferase type-2 subunit beta

Gene

Rabggtb

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.6 Publications

Cofactori

Zn2+7 PublicationsNote: Binds 1 zinc ion per subunit.7 Publications

Enzyme regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi238Zinc; catalytic1
Metal bindingi240Zinc; catalytic1
Metal bindingi290Zinc; via tele nitrogen; catalytic1

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Prenyltransferase, Transferase

Keywords - Ligandi

Metal-binding, Zinc

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3530. Rabggtb.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001197742 – 331Geranylgeranyl transferase type-2 subunit betaAdd BLAST330

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylglycineBy similarity1
Modified residuei3PhosphothreonineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ08603.
PRIDEiQ08603.

Expressioni

Tissue specificityi

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

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.9 Publications

GO - Molecular functioni

  • Rab GTPase binding Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-6138N.
STRINGi10116.ENSRNOP00000061541.

Structurei

Secondary structure

1331
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi20 – 29Combined sources10
Beta strandi32 – 34Combined sources3
Helixi36 – 38Combined sources3
Helixi40 – 45Combined sources6
Helixi46 – 59Combined sources14
Helixi63 – 65Combined sources3
Helixi68 – 77Combined sources10
Beta strandi85 – 88Combined sources4
Helixi95 – 107Combined sources13
Helixi111 – 113Combined sources3
Helixi116 – 125Combined sources10
Beta strandi133 – 136Combined sources4
Helixi143 – 156Combined sources14
Helixi159 – 161Combined sources3
Helixi164 – 172Combined sources9
Helixi191 – 203Combined sources13
Helixi207 – 209Combined sources3
Helixi212 – 220Combined sources9
Beta strandi231 – 234Combined sources4
Helixi239 – 251Combined sources13
Helixi255 – 257Combined sources3
Helixi260 – 269Combined sources10
Turni273 – 275Combined sources3
Beta strandi278 – 281Combined sources4
Helixi288 – 300Combined sources13
Turni311 – 313Combined sources3
Beta strandi314 – 316Combined sources3
Helixi317 – 323Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DCEX-ray2.00B/D1-331[»]
1LTXX-ray2.70B1-331[»]
3C72X-ray2.30B1-331[»]
3DSSX-ray1.80B1-331[»]
3DSTX-ray1.90B1-331[»]
3DSUX-ray1.90B1-331[»]
3DSVX-ray2.10B1-331[»]
3DSWX-ray2.15B1-331[»]
3DSXX-ray2.10B1-331[»]
3HXBX-ray2.25B1-331[»]
3HXCX-ray1.95B1-331[»]
3HXDX-ray1.95B1-331[»]
3HXEX-ray1.95B1-331[»]
3HXFX-ray1.90B1-331[»]
4EHMX-ray2.20B2-331[»]
4GTSX-ray2.45B2-331[»]
4GTTX-ray2.05B2-331[»]
4GTVX-ray1.95B2-331[»]
ProteinModelPortaliQ08603.
SMRiQ08603.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08603.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati20 – 61PFTB 1Add BLAST42
Repeati68 – 109PFTB 2Add BLAST42
Repeati116 – 157PFTB 3Add BLAST42
Repeati164 – 205PFTB 4Add BLAST42
Repeati212 – 253PFTB 5Add BLAST42
Repeati260 – 302PFTB 6Add BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni190 – 192Geranylgeranyl diphosphate binding3
Regioni232 – 244Geranylgeranyl diphosphate bindingAdd BLAST13

Sequence similaritiesi

Contains 6 PFTB repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0366. Eukaryota.
COG5029. LUCA.
HOVERGENiHBG008182.
InParanoidiQ08603.
KOiK05956.
PhylomeDBiQ08603.

Family and domain databases

CDDicd02894. GGTase-II. 1 hit.
Gene3Di1.50.10.20. 1 hit.
InterProiIPR001330. PFTB_repeat.
IPR026873. Ptb1.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PANTHERiPTHR11774:SF11. PTHR11774:SF11. 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.

Q08603-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTQQKDVTI KSDAPDTLLL EKHADYIASY GSKKDDYEYC MSEYLRMSGV
60 70 80 90 100
YWGLTVMDLM GQLHRMNKEE ILVFIKSCQH ECGGVSASIG HDPHLLYTLS
110 120 130 140 150
AVQILTLYDS IHVINVDKVV AYVQSLQKED GSFAGDIWGE IDTRFSFCAV
160 170 180 190 200
ATLALLGKLD AINVEKAIEF VLSCMNFDGG FGCRPGSESH AGQIYCCTGF
210 220 230 240 250
LAITSQLHQV NSDLLGWWLC ERQLPSGGLN GRPEKLPDVC YSWWVLASLK
260 270 280 290 300
IIGRLHWIDR EKLRSFILAC QDEETGGFAD RPGDMVDPFH TLFGIAGLSL
310 320 330
LGEEQIKPVS PVFCMPEEVL QRVNVQPELV S
Length:331
Mass (Da):36,856
Last modified:February 1, 1995 - v1
Checksum:i4B12DEC0245979D6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10416 mRNA. Translation: AAA41999.1.
S62097 mRNA. Translation: AAB27019.1.
PIRiB45977.
RefSeqiNP_619715.1. NM_138708.2.
UniGeneiRn.107818.

Genome annotation databases

GeneIDi25533.
KEGGirno:25533.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10416 mRNA. Translation: AAA41999.1.
S62097 mRNA. Translation: AAB27019.1.
PIRiB45977.
RefSeqiNP_619715.1. NM_138708.2.
UniGeneiRn.107818.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DCEX-ray2.00B/D1-331[»]
1LTXX-ray2.70B1-331[»]
3C72X-ray2.30B1-331[»]
3DSSX-ray1.80B1-331[»]
3DSTX-ray1.90B1-331[»]
3DSUX-ray1.90B1-331[»]
3DSVX-ray2.10B1-331[»]
3DSWX-ray2.15B1-331[»]
3DSXX-ray2.10B1-331[»]
3HXBX-ray2.25B1-331[»]
3HXCX-ray1.95B1-331[»]
3HXDX-ray1.95B1-331[»]
3HXEX-ray1.95B1-331[»]
3HXFX-ray1.90B1-331[»]
4EHMX-ray2.20B2-331[»]
4GTSX-ray2.45B2-331[»]
4GTTX-ray2.05B2-331[»]
4GTVX-ray1.95B2-331[»]
ProteinModelPortaliQ08603.
SMRiQ08603.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6138N.
STRINGi10116.ENSRNOP00000061541.

Proteomic databases

PaxDbiQ08603.
PRIDEiQ08603.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25533.
KEGGirno:25533.

Organism-specific databases

CTDi5876.
RGDi3530. Rabggtb.

Phylogenomic databases

eggNOGiKOG0366. Eukaryota.
COG5029. LUCA.
HOVERGENiHBG008182.
InParanoidiQ08603.
KOiK05956.
PhylomeDBiQ08603.

Miscellaneous databases

EvolutionaryTraceiQ08603.
PROiQ08603.

Family and domain databases

CDDicd02894. GGTase-II. 1 hit.
Gene3Di1.50.10.20. 1 hit.
InterProiIPR001330. PFTB_repeat.
IPR026873. Ptb1.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PANTHERiPTHR11774:SF11. PTHR11774:SF11. 1 hit.
PfamiPF00432. Prenyltrans. 5 hits.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPGTB2_RAT
AccessioniPrimary (citable) accession number: Q08603
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 120 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.