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Protein

Geranylgeranyl transferase type-2 subunit beta

Gene

RABGGTB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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.

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Enzyme regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi238ZincBy similarity1
Metal bindingi238Zinc; catalyticBy similarity1
Metal bindingi240ZincBy similarity1
Metal bindingi240Zinc; catalyticBy similarity1
Metal bindingi290ZincBy similarity1
Metal bindingi290Zinc; via tele nitrogen; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

  • cellular protein modification process Source: UniProtKB
  • post-translational protein modification Source: Reactome
  • protein geranylgeranylation Source: UniProtKB
  • regulation of apoptotic process Source: Reactome
  • visual perception Source: ProtInc

Keywordsi

Molecular functionPrenyltransferase, Transferase
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDAi2.5.1.60 2681
ReactomeiR-HSA-6803205 TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain
R-HSA-8873719 RAB geranylgeranylation

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000137955.15
HGNCiHGNC:9796 RABGGTB
MIMi179080 gene
neXtProtiNX_P53611

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Organism-specific databases

DisGeNETi5876
OpenTargetsiENSG00000137955
PharmGKBiPA34157

Chemistry databases

DrugBankiDB07780 FARNESYL DIPHOSPHATE
DB07841 GERANYLGERANYL DIPHOSPHATE
DB04464 N-Formylmethionine

Polymorphism and mutation databases

DMDMi2506788

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001197722 – 331Geranylgeranyl transferase type-2 subunit betaAdd BLAST330

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylglycineCombined sources1
Modified residuei3PhosphothreonineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP53611
PaxDbiP53611
PeptideAtlasiP53611
PRIDEiP53611

PTM databases

iPTMnetiP53611
PhosphoSitePlusiP53611

Expressioni

Gene expression databases

BgeeiENSG00000137955
CleanExiHS_RABGGTB
ExpressionAtlasiP53611 baseline and differential
GenevisibleiP53611 HS

Organism-specific databases

HPAiHPA026585
HPA027167
HPA030793

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. Interacts with CHODL.By similarity2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi11181471 interactors.
IntActiP53611 11 interactors.
STRINGi9606.ENSP00000317473

Structurei

3D structure databases

ProteinModelPortaliP53611
SMRiP53611
ModBaseiSearch...
MobiDBiSearch...

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 bindingBy similarity3
Regioni232 – 244Geranylgeranyl diphosphate bindingBy similarityAdd BLAST13

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0366 Eukaryota
COG5029 LUCA
GeneTreeiENSGT00530000063392
HOGENOMiHOG000180334
HOVERGENiHBG008182
InParanoidiP53611
KOiK05956
OMAiWGEEDTR
OrthoDBiEOG091G0DXU
PhylomeDBiP53611
TreeFamiTF105762

Family and domain databases

CDDicd02894 GGTase-II, 1 hit
InterProiView protein in InterPro
IPR001330 PFTB_repeat
IPR026873 Ptb1
IPR008930 Terpenoid_cyclase/PrenylTrfase
PfamiView protein in Pfam
PF00432 Prenyltrans, 5 hits
SUPFAMiSSF48239 SSF48239, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P53611-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTPQKDVII KSDAPDTLLL EKHADYIASY GSKKDDYEYC MSEYLRMSGI
60 70 80 90 100
YWGLTVMDLM GQLHRMNREE ILAFIKSCQH ECGGISASIG HDPHLLYTLS
110 120 130 140 150
AVQILTLYDS INVIDVNKVV EYVKGLQKED 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 EKLRNFILAC QDEETGGFAD RPGDMVDPFH TLFGIAGLSL
310 320 330
LGEEQIKPVN PVFCMPEEVL QRVNVQPELV S
Length:331
Mass (Da):36,924
Last modified:November 1, 1997 - v2
Checksum:i37A8A6329146C49B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti153L → F in AAA91473 (Ref. 1) Curated1
Sequence conflicti177F → S in CAA69383 (PubMed:8954794).Curated1
Sequence conflicti211N → T in CAA69383 (PubMed:8954794).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49245 mRNA Translation: AAA91473.1
X98001 mRNA Translation: CAA66638.1
Y08201 mRNA Translation: CAA69383.1
BC020790 mRNA Translation: AAH20790.1
CCDSiCCDS669.1
PIRiG02431
RefSeqiNP_004573.2, NM_004582.3
UniGeneiHs.78948

Genome annotation databases

EnsembliENST00000319942; ENSP00000317473; ENSG00000137955
GeneIDi5876
KEGGihsa:5876

Similar proteinsi

Entry informationi

Entry nameiPGTB2_HUMAN
AccessioniPrimary (citable) accession number: P53611
Secondary accession number(s): Q92697
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: February 28, 2018
This is version 159 of the entry and version 2 of the sequence. See 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