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P53612

- PGTB2_MOUSE

UniProt

P53612 - PGTB2_MOUSE

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Protein

Geranylgeranyl transferase type-2 subunit beta

Gene

Rabggtb

Organism
Mus musculus (Mouse)
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.1 Publication

Catalytic activityi

Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.1 Publication

Cofactori

Binds 1 zinc ion per subunit.1 Publication

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 bindingi246 – 2461Zinc; catalytic1 Publication
Metal bindingi248 – 2481Zinc; catalytic1 Publication
Metal bindingi298 – 2981Zinc; via tele nitrogen; catalytic1 Publication

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:99537. 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
Chaini1 – 339339Geranylgeranyl transferase type-2 subunit betaPRO_0000119773Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53612.
PaxDbiP53612.
PRIDEiP53612.

PTM databases

PhosphoSiteiP53612.

Expressioni

Tissue specificityi

Ubiquitous. Detected in all the major organs in adult animals.1 Publication

Developmental stagei

Specific expression was elevated in mid-gestation stages, particularly developing liver and spinal cord.1 Publication

Inductioni

Increased dramatically by cycloheximide (CHX) treatment within a short time (as early as 2 hours). Actinomycin D was used to determine the half-life, CHX treatment resulted in a dramatic increase of the half-life from 8 hours to greater than 12 hours.1 Publication

Gene expression databases

BgeeiP53612.
CleanExiMM_RABGGTB.
ExpressionAtlasiP53612. baseline and differential.
GenevestigatoriP53612.

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 By similarity.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000087396.

Structurei

Secondary structure

1
339
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi28 – 3710
Helixi45 – 484
Helixi49 – 535
Helixi54 – 6714
Helixi71 – 733
Helixi76 – 8510
Beta strandi93 – 964
Helixi103 – 11513
Helixi119 – 1213
Helixi124 – 13310
Beta strandi141 – 1444
Helixi151 – 16414
Helixi167 – 1693
Helixi172 – 1809
Helixi199 – 21113
Helixi215 – 2173
Helixi220 – 2289
Helixi249 – 25911
Helixi263 – 2653
Helixi268 – 27710
Turni281 – 2833
Helixi296 – 30813
Turni319 – 3213
Beta strandi322 – 3243
Helixi325 – 3317

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PZ1X-ray1.95B10-339[»]
3PZ2X-ray2.35B10-339[»]
3PZ3X-ray2.00B10-339[»]
ProteinModelPortaliP53612.
SMRiP53612. Positions 13-339.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53612.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati28 – 6942PFTB 1Add
BLAST
Repeati76 – 11742PFTB 2Add
BLAST
Repeati124 – 16542PFTB 3Add
BLAST
Repeati172 – 21342PFTB 4Add
BLAST
Repeati220 – 26142PFTB 5Add
BLAST
Repeati268 – 31043PFTB 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 2003Geranylgeranyl diphosphate bindingBy similarity
Regioni240 – 25213Geranylgeranyl diphosphate bindingBy similarityAdd
BLAST
Regioni249 – 2524Geranylgeranyl diphosphate bindingBy similarity

Sequence similaritiesi

Contains 6 PFTB repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5029.
GeneTreeiENSGT00530000063392.
HOGENOMiHOG000180334.
HOVERGENiHBG008182.
InParanoidiP53612.
KOiK05956.
OMAiESHAGLI.
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. 2 hits.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.

Sequencei

Sequence statusi: Complete.

P53612-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSLLFSWKG TQQKDVTIKS DAPDTLLLEK HADYIASYGS KKDDYEYCMS
60 70 80 90 100
EYLRMSGVYW GLTVMDLMGQ LHRMNREEIL VFIKSCQHEC GGISASIGHD
110 120 130 140 150
PHLLYTLSAV QILTLYDSVH VINVDKVVAY VQSLQKEDGS FAGDIWGEID
160 170 180 190 200
TRFSFCAVAT LALLGKLDAI NVEKAIEFVL SCMNFDGGFG CRPGSESHAG
210 220 230 240 250
QIYCCTGFLA ITSQLHQVNS DLLGWWLCER QLPSGGLNGR PEKLPDVCYS
260 270 280 290 300
WWVLASLKII GRLHWIDREK LRSFILACQD EETGGFADRP GDMVDPFHTL
310 320 330
FGIAGLSLLG EEQIKPVSPV FCMPEEVLQR VNVQPELVS
Length:339
Mass (Da):37,803
Last modified:July 27, 2011 - v2
Checksum:i4765A39E5392B8B5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti230 – 2301R → A in AAB01502. (PubMed:7544156)Curated
Sequence conflicti236 – 2361G → A in AAB01502. (PubMed:7544156)Curated
Sequence conflicti241 – 2411P → R in AAB01502. (PubMed:7544156)Curated
Sequence conflicti267 – 2682DR → VS in AAB01502. (PubMed:7544156)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U12922 mRNA. Translation: AAB01502.1.
CH466532 Genomic DNA. Translation: EDL11902.1.
BC132473 mRNA. Translation: AAI32474.1.
BC138547 mRNA. Translation: AAI38548.1.
CCDSiCCDS17923.1.
PIRiI49116.
JC6177.
RefSeqiNP_035361.2. NM_011231.2.
UniGeneiMm.277831.

Genome annotation databases

EnsembliENSMUST00000167111; ENSMUSP00000129481; ENSMUSG00000038975.
GeneIDi19352.
KEGGimmu:19352.
UCSCiuc008rug.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U12922 mRNA. Translation: AAB01502.1 .
CH466532 Genomic DNA. Translation: EDL11902.1 .
BC132473 mRNA. Translation: AAI32474.1 .
BC138547 mRNA. Translation: AAI38548.1 .
CCDSi CCDS17923.1.
PIRi I49116.
JC6177.
RefSeqi NP_035361.2. NM_011231.2.
UniGenei Mm.277831.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3PZ1 X-ray 1.95 B 10-339 [» ]
3PZ2 X-ray 2.35 B 10-339 [» ]
3PZ3 X-ray 2.00 B 10-339 [» ]
ProteinModelPortali P53612.
SMRi P53612. Positions 13-339.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000087396.

PTM databases

PhosphoSitei P53612.

Proteomic databases

MaxQBi P53612.
PaxDbi P53612.
PRIDEi P53612.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000167111 ; ENSMUSP00000129481 ; ENSMUSG00000038975 .
GeneIDi 19352.
KEGGi mmu:19352.
UCSCi uc008rug.2. mouse.

Organism-specific databases

CTDi 5876.
MGIi MGI:99537. Rabggtb.

Phylogenomic databases

eggNOGi COG5029.
GeneTreei ENSGT00530000063392.
HOGENOMi HOG000180334.
HOVERGENi HBG008182.
InParanoidi P53612.
KOi K05956.
OMAi ESHAGLI.
TreeFami TF105762.

Miscellaneous databases

EvolutionaryTracei P53612.
NextBioi 296383.
PROi P53612.
SOURCEi Search...

Gene expression databases

Bgeei P53612.
CleanExi MM_RABGGTB.
ExpressionAtlasi P53612. baseline and differential.
Genevestigatori P53612.

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

« Hide 'large scale' publications
  1. "Studies of cloning, chromosomal mapping, and embryonic expression of the mouse Rab geranylgeranyl transferase beta subunit."
    Wei L.-N., Lee C.-H., Chinpaisal C., Copeland N.G., Gilbert D.J., Jenkins N.A., Hsu Y.-C.
    Cell Growth Differ. 6:607-614(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: CD-1.
    Tissue: Embryo.
  2. "Studies of the mouse Rab geranylgeranyl transferase beta subunit: gene structure, expression and regulation."
    Chinpaisal C., Lee C.-H., Wei L.-N.
    Gene 184:237-243(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
    Strain: CD-1.
    Tissue: Embryo.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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: Brain.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 10-339 IN COMPLEX WITH ZINC AND GERANYLGERANYL DIPHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiPGTB2_MOUSE
AccessioniPrimary (citable) accession number: P53612
Secondary accession number(s): A2RTE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3