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P53611

- PGTB2_HUMAN

UniProt

P53611 - PGTB2_HUMAN

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Protein
Geranylgeranyl transferase type-2 subunit beta
Gene
RABGGTB, GGTB
Organism
Homo sapiens (Human)
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.

Catalytic activityi

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

Cofactori

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

GO - Molecular functioni

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

GO - Biological processi

  1. cellular protein modification process Source: UniProtKB
  2. protein geranylgeranylation Source: UniProtKB
  3. visual perception Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Prenyltransferase, Transferase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi2.5.1.60. 2681.

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
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9796. RABGGTB.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34157.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 331330Geranylgeranyl transferase type-2 subunit beta
PRO_0000119772Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycine2 Publications
Modified residuei3 – 31Phosphothreonine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP53611.
PaxDbiP53611.
PRIDEiP53611.

PTM databases

PhosphoSiteiP53611.

Expressioni

Gene expression databases

ArrayExpressiP53611.
BgeeiP53611.
CleanExiHS_RABGGTB.
GenevestigatoriP53611.

Organism-specific databases

HPAiHPA026585.
HPA027167.

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

Protein-protein interaction databases

BioGridi111814. 7 interactions.
IntActiP53611. 2 interactions.
MINTiMINT-260716.
STRINGi9606.ENSP00000317473.

Structurei

3D structure databases

ProteinModelPortaliP53611.
SMRiP53611. Positions 5-331.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Contains 6 PFTB repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5029.
HOGENOMiHOG000180334.
HOVERGENiHBG008182.
InParanoidiP53611.
KOiK05956.
OMAiESHAGLI.
OrthoDBiEOG7XSTDZ.
PhylomeDBiP53611.
TreeFamiTF105762.

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. 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

MGTPQKDVII KSDAPDTLLL EKHADYIASY GSKKDDYEYC MSEYLRMSGI    50
YWGLTVMDLM GQLHRMNREE ILAFIKSCQH ECGGISASIG HDPHLLYTLS 100
AVQILTLYDS INVIDVNKVV EYVKGLQKED GSFAGDIWGE IDTRFSFCAV 150
ATLALLGKLD AINVEKAIEF VLSCMNFDGG FGCRPGSESH AGQIYCCTGF 200
LAITSQLHQV NSDLLGWWLC ERQLPSGGLN GRPEKLPDVC YSWWVLASLK 250
IIGRLHWIDR EKLRNFILAC QDEETGGFAD RPGDMVDPFH TLFGIAGLSL 300
LGEEQIKPVN PVFCMPEEVL QRVNVQPELV S 331
Length:331
Mass (Da):36,924
Last modified:November 1, 1997 - v2
Checksum:i37A8A6329146C49B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1531L → F in AAA91473. 1 Publication
Sequence conflicti177 – 1771F → S in CAA69383. 1 Publication
Sequence conflicti211 – 2111N → T in CAA69383. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
UCSCiuc001dgy.2. human.

Polymorphism databases

DMDMi2506788.

Cross-referencesi

Web resourcesi

Wikipedia

Rab geranylgeranyltransferase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U49245 mRNA. Translation: AAA91473.1 .
X98001 mRNA. Translation: CAA66638.1 .
Y08201 mRNA. Translation: CAA69383.1 .
BC020790 mRNA. Translation: AAH20790.1 .
CCDSi CCDS669.1.
PIRi G02431.
RefSeqi NP_004573.2. NM_004582.3.
UniGenei Hs.78948.

3D structure databases

ProteinModelPortali P53611.
SMRi P53611. Positions 5-331.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111814. 7 interactions.
IntActi P53611. 2 interactions.
MINTi MINT-260716.
STRINGi 9606.ENSP00000317473.

Chemistry

BindingDBi P53611.

PTM databases

PhosphoSitei P53611.

Polymorphism databases

DMDMi 2506788.

Proteomic databases

MaxQBi P53611.
PaxDbi P53611.
PRIDEi P53611.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000319942 ; ENSP00000317473 ; ENSG00000137955 .
GeneIDi 5876.
KEGGi hsa:5876.
UCSCi uc001dgy.2. human.

Organism-specific databases

CTDi 5876.
GeneCardsi GC01P076251.
HGNCi HGNC:9796. RABGGTB.
HPAi HPA026585.
HPA027167.
MIMi 179080. gene.
neXtProti NX_P53611.
PharmGKBi PA34157.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5029.
HOGENOMi HOG000180334.
HOVERGENi HBG008182.
InParanoidi P53611.
KOi K05956.
OMAi ESHAGLI.
OrthoDBi EOG7XSTDZ.
PhylomeDBi P53611.
TreeFami TF105762.

Enzyme and pathway databases

BRENDAi 2.5.1.60. 2681.

Miscellaneous databases

ChiTaRSi RABGGTB. human.
GenomeRNAii 5876.
NextBioi 22832.
PROi P53611.
SOURCEi Search...

Gene expression databases

ArrayExpressi P53611.
Bgeei P53611.
CleanExi HS_RABGGTB.
Genevestigatori P53611.

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. 5 hits.
[Graphical view ]
SUPFAMi SSF48239. SSF48239. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Chang H.Y., Wu S.R., Peng H.L.
    Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Characterization of the interaction of the monomeric GTP-binding protein Rab3a with geranylgeranyl transferase II."
    Johannes L., Perez F., Laran-Chich M.P., Henry J.P., Darchen F.
    Eur. J. Biochem. 239:362-368(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "cDNA cloning and chromosomal localization of the genes encoding the alpha- and beta-subunits of human Rab geranylgeranyl transferase: the 3' end of the alpha-subunit gene overlaps with the transglutaminase 1 gene promoter."
    van Bokhoven H., Rawson R.B., Merkx G.F.M., Cremers F.P.M., Seabra M.C.
    Genomics 38:133-140(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal brain.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skeletal muscle.
  5. "Interaction of farnesylated PRL-2, a protein-tyrosine phosphatase, with the beta-subunit of geranylgeranyltransferase II."
    Si X., Zeng Q., Ng C.H., Hong W., Pallen C.J.
    J. Biol. Chem. 276:32875-32882(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTP4A2.
  6. "Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A."
    Farnsworth C.C., Seabra M.C., Ericsson L.H., Gelb M.H., Glomset J.A.
    Proc. Natl. Acad. Sci. U.S.A. 91:11963-11967(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "Rab geranylgeranylation occurs preferentially via the pre-formed REP-RGGT complex and is regulated by geranylgeranyl pyrophosphate."
    Baron R.A., Seabra M.C.
    Biochem. J. 415:67-75(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: July 9, 2014
This is version 131 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

External Data

Dasty 3

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