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Q08603

- PGTB2_RAT

UniProt

Q08603 - PGTB2_RAT

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Protein

Geranylgeranyl transferase type-2 subunit beta

Gene

Rabggtb

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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

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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi238 – 2381Zinc; catalytic
Metal bindingi240 – 2401Zinc; catalytic
Metal bindingi290 – 2901Zinc; via tele nitrogen; catalytic

GO - Molecular functioni

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

GO - Biological processi

  1. 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
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi3530. Rabggtb.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 331330Geranylgeranyl transferase type-2 subunit betaPRO_0000119774Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycineBy similarity
Modified residuei3 – 31PhosphothreonineBy similarity

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.

Gene expression databases

GenevestigatoriQ08603.

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

Protein-protein interaction databases

DIPiDIP-6138N.

Structurei

Secondary structure

1
331
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 2910
Beta strandi32 – 343
Helixi36 – 383
Helixi40 – 456
Helixi46 – 5914
Helixi63 – 653
Helixi68 – 7710
Beta strandi85 – 884
Helixi95 – 10713
Helixi111 – 1133
Helixi116 – 12510
Beta strandi133 – 1364
Helixi143 – 15614
Helixi159 – 1613
Helixi164 – 1729
Helixi191 – 20313
Helixi207 – 2093
Helixi212 – 2209
Beta strandi231 – 2344
Helixi239 – 25113
Helixi255 – 2573
Helixi260 – 26910
Turni273 – 2753
Beta strandi278 – 2814
Helixi288 – 30013
Turni311 – 3133
Beta strandi314 – 3163
Helixi317 – 3237

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 3-331.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08603.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati20 – 6142PFTB 1Add
BLAST
Repeati68 – 10942PFTB 2Add
BLAST
Repeati116 – 15742PFTB 3Add
BLAST
Repeati164 – 20542PFTB 4Add
BLAST
Repeati212 – 25342PFTB 5Add
BLAST
Repeati260 – 30243PFTB 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni190 – 1923Geranylgeranyl diphosphate binding
Regioni232 – 24413Geranylgeranyl diphosphate bindingAdd
BLAST

Sequence similaritiesi

Contains 6 PFTB repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5029.
HOVERGENiHBG008182.
InParanoidiQ08603.
KOiK05956.
PhylomeDBiQ08603.

Family and domain databases

Gene3Di1.50.10.20. 1 hit.
InterProiIPR001330. Prenyltrans.
IPR026873. Ptb1.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PANTHERiPTHR11774:SF9. PTHR11774:SF9. 1 hit.
PfamiPF00432. Prenyltrans. 2 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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
L10416 mRNA. Translation: AAA41999.1 .
S62097 mRNA. Translation: AAB27019.1 .
PIRi B45977.
RefSeqi NP_619715.1. NM_138708.2.
UniGenei Rn.107818.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DCE X-ray 2.00 B/D 1-331 [» ]
1LTX X-ray 2.70 B 1-331 [» ]
3C72 X-ray 2.30 B 1-331 [» ]
3DSS X-ray 1.80 B 1-331 [» ]
3DST X-ray 1.90 B 1-331 [» ]
3DSU X-ray 1.90 B 1-331 [» ]
3DSV X-ray 2.10 B 1-331 [» ]
3DSW X-ray 2.15 B 1-331 [» ]
3DSX X-ray 2.10 B 1-331 [» ]
3HXB X-ray 2.25 B 1-331 [» ]
3HXC X-ray 1.95 B 1-331 [» ]
3HXD X-ray 1.95 B 1-331 [» ]
3HXE X-ray 1.95 B 1-331 [» ]
3HXF X-ray 1.90 B 1-331 [» ]
4EHM X-ray 2.20 B 2-331 [» ]
4GTS X-ray 2.45 B 2-331 [» ]
4GTT X-ray 2.05 B 2-331 [» ]
4GTV X-ray 1.95 B 2-331 [» ]
ProteinModelPortali Q08603.
SMRi Q08603. Positions 3-331.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6138N.

Proteomic databases

PaxDbi Q08603.
PRIDEi Q08603.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 25533.
KEGGi rno:25533.

Organism-specific databases

CTDi 5876.
RGDi 3530. Rabggtb.

Phylogenomic databases

eggNOGi COG5029.
HOVERGENi HBG008182.
InParanoidi Q08603.
KOi K05956.
PhylomeDBi Q08603.

Miscellaneous databases

EvolutionaryTracei Q08603.
NextBioi 607037.
PROi Q08603.

Gene expression databases

Genevestigatori Q08603.

Family and domain databases

Gene3Di 1.50.10.20. 1 hit.
InterProi IPR001330. Prenyltrans.
IPR026873. Ptb1.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view ]
PANTHERi PTHR11774:SF9. PTHR11774:SF9. 1 hit.
Pfami PF00432. Prenyltrans. 2 hits.
[Graphical view ]
SUPFAMi SSF48239. SSF48239. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "cDNA cloning and expression of the alpha and beta subunits of rat Rab geranylgeranyl transferase."
    Armstrong S.A., Seabra M.C., Suedhof T.C., Goldstein J.L., Brown M.S.
    J. Biol. Chem. 268:12221-12229(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT, CATALYTIC ACTIVITY.
    Tissue: Brain.
  2. "Phosphoisoprenoids modulate association of Rab geranylgeranyltransferase with REP-1."
    Thoma N.H., Iakovenko A., Goody R.S., Alexandrov K.
    J. Biol. Chem. 276:48637-48643(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  3. "Crystal structure of Rab geranylgeranyltransferase at 2.0 A resolution."
    Zhang H., Seabra M.C., Deisenhofer J.
    Structure 8:241-251(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH RABGGTA AND ZINC IONS, SUBUNIT, COFACTOR.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS; GERANYGERANYL PHOSHATE ANALOG; RAB7A; RABGGTA AND CHM, SUBUNIT, COFACTOR.
  5. "Development of selective RabGGTase inhibitors and crystal structure of a RabGGTase-inhibitor complex."
    Guo Z., Wu Y.W., Tan K.T., Bon R.S., Guiu-Rozas E., Delon C., Nguyen T.U., Wetzel S., Arndt S., Goody R.S., Blankenfeldt W., Alexandrov K., Waldmann H.
    Angew. Chem. Int. Ed. Engl. 47:3747-3750(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH RABGGTA; INHIBITOR AND ZINC IONS, FUNCTION, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY.
  6. "Structures of RabGGTase-substrate/product complexes provide insights into the evolution of protein prenylation."
    Guo Z., Wu Y.W., Das D., Delon C., Cramer J., Yu S., Thuns S., Lupilova N., Waldmann H., Brunsveld L., Goody R.S., Alexandrov K., Blankenfeldt W.
    EMBO J. 27:2444-2456(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEXES WITH RABGGTA; RAB7A; GERANYLGERANYL DIPHOSPHATE AND ZINC IONS, COFACTOR, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY.
  7. "Design, synthesis, and characterization of peptide-based rab geranylgeranyl transferase inhibitors."
    Tan K.T., Guiu-Rozas E., Bon R.S., Guo Z., Delon C., Wetzel S., Arndt S., Alexandrov K., Waldmann H., Goody R.S., Wu Y.W., Blankenfeldt W.
    J. Med. Chem. 52:8025-8037(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH RABGGTA; ZINC IONS AND INHIBITOR, SUBUNIT, COFACTOR, FUNCTION, CATALYTIC ACTIVITY.
  8. "Psoromic acid is a selective and covalent Rab-prenylation inhibitor targeting autoinhibited RabGGTase."
    Deraeve C., Guo Z., Bon R.S., Blankenfeldt W., DiLucrezia R., Wolf A., Menninger S., Stigter E.A., Wetzel S., Choidas A., Alexandrov K., Waldmann H., Goody R.S., Wu Y.W.
    J. Am. Chem. Soc. 134:7384-7391(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH RABGGTA; ZINC IONS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, FUNCTION.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH RABGGTA; ZINC IONS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, FUNCTION.

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: October 1, 2014
This is version 109 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

External Data

Dasty 3