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Protein

Geranylgeranyl transferase type-2 subunit beta

Gene

RABGGTB

Organism
Homo sapiens (Human)
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.

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
  • protein geranylgeranylation Source: UniProtKB
  • regulation of apoptotic process Source: Reactome
  • visual perception Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Prenyltransferase, Transferase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:HS06425-MONOMER.
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.

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

HGNCiHGNC:9796. RABGGTB.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

DisGeNETi5876.
OpenTargetsiENSG00000137955.
PharmGKBiPA34157.

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARAFP103983EBI-536715,EBI-365961
B4GALT7Q9UBV75EBI-536715,EBI-10319970
FAM19A1Q7Z5A93EBI-536715,EBI-10257895
TMEM25Q86YD33EBI-536715,EBI-10260688
WDR4P570813EBI-536715,EBI-750427

GO - Molecular functioni

Protein-protein interaction databases

BioGridi111814. 63 interactors.
IntActiP53611. 10 interactors.
MINTiMINT-260716.
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

Contains 6 PFTB repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

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

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.

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.

Cross-referencesi

Web resourcesi

Wikipedia

Rab geranylgeranyltransferase entry

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.

3D structure databases

ProteinModelPortaliP53611.
SMRiP53611.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111814. 63 interactors.
IntActiP53611. 10 interactors.
MINTiMINT-260716.
STRINGi9606.ENSP00000317473.

PTM databases

iPTMnetiP53611.
PhosphoSitePlusiP53611.

Polymorphism and mutation databases

DMDMi2506788.

Proteomic databases

EPDiP53611.
PaxDbiP53611.
PeptideAtlasiP53611.
PRIDEiP53611.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000319942; ENSP00000317473; ENSG00000137955.
GeneIDi5876.
KEGGihsa:5876.

Organism-specific databases

CTDi5876.
DisGeNETi5876.
GeneCardsiRABGGTB.
HGNCiHGNC:9796. RABGGTB.
HPAiHPA026585.
HPA027167.
HPA030793.
MIMi179080. gene.
neXtProtiNX_P53611.
OpenTargetsiENSG00000137955.
PharmGKBiPA34157.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:HS06425-MONOMER.
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.

Miscellaneous databases

ChiTaRSiRABGGTB. human.
GenomeRNAii5876.
PROiP53611.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000137955.
CleanExiHS_RABGGTB.
ExpressionAtlasiP53611. baseline and differential.
GenevisibleiP53611. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: P53611
Secondary accession number(s): Q92697
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 151 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.