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Q9JHK4

- PGTA_MOUSE

UniProt

Q9JHK4 - PGTA_MOUSE

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Protein

Geranylgeranyl transferase type-2 subunit alpha

Gene

Rabggta

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript 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.

Enzyme regulationi

The enzymatic reaction requires the aid of a Rab escort protein (also called component A), such as CHM.By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. protein geranylgeranylation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Prenyltransferase, Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Geranylgeranyl transferase type-2 subunit alpha (EC:2.5.1.60)
Alternative name(s):
Geranylgeranyl transferase type II subunit alpha
Rab geranyl-geranyltransferase subunit alpha
Short name:
Rab GG transferase alpha
Short name:
Rab GGTase alpha
Rab geranylgeranyltransferase subunit alpha
Gene namesi
Name:Rabggta
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:1860443. Rabggta.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Defects in Rabggta are the cause of the gunmetal (gm) phenotype. Mice homozygous for gm have prolonged bleeding, thrombocytopenia and reduced platelet alpha- and delta-granule contents.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 567567Geranylgeranyl transferase type-2 subunit alphaPRO_0000119758Add
BLAST

Proteomic databases

MaxQBiQ9JHK4.
PaxDbiQ9JHK4.
PRIDEiQ9JHK4.

PTM databases

PhosphoSiteiQ9JHK4.

Expressioni

Gene expression databases

BgeeiQ9JHK4.
CleanExiMM_RABGGTA.
GenevestigatoriQ9JHK4.

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi207827. 1 interaction.
IntActiQ9JHK4. 1 interaction.
STRINGi10090.ENSMUSP00000061498.

Structurei

3D structure databases

ProteinModelPortaliQ9JHK4.
SMRiQ9JHK4. Positions 2-567.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JHK4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati44 – 7835PFTA 1Add
BLAST
Repeati88 – 12235PFTA 2Add
BLAST
Repeati124 – 15835PFTA 3Add
BLAST
Repeati159 – 19335PFTA 4Add
BLAST
Repeati207 – 24135PFTA 5Add
BLAST
Repeati363 – 39735PFTA 6Add
BLAST
Repeati442 – 46322LRR 1Add
BLAST
Repeati464 – 48623LRR 2Add
BLAST
Repeati487 – 50822LRR 3Add
BLAST
Repeati509 – 53022LRR 4Add
BLAST
Repeati534 – 55522LRR 5Add
BLAST

Sequence similaritiesi

Contains 5 LRR (leucine-rich) repeats.Curated
Contains 6 PFTA repeats.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiCOG5536.
GeneTreeiENSGT00550000075121.
HOGENOMiHOG000007845.
HOVERGENiHBG002171.
InParanoidiQ9JHK4.
KOiK14050.
OMAiWNCRREV.
OrthoDBiEOG7PP56C.
PhylomeDBiQ9JHK4.
TreeFamiTF315057.

Family and domain databases

Gene3Di2.60.40.1130. 1 hit.
InterProiIPR001611. Leu-rich_rpt.
IPR002088. Prenyl_trans_a.
IPR009087. RabGGT_asu_insert-domain.
[Graphical view]
PfamiPF00560. LRR_1. 1 hit.
PF01239. PPTA. 5 hits.
PF07711. RabGGT_insert. 1 hit.
[Graphical view]
ProDomiPD331837. RabGG_trans_A. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF49594. SSF49594. 1 hit.
PROSITEiPS51147. PFTA. 6 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9JHK4-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MHGRLKVKTS EEQAEAKRLE REQKLKLYQS ATQAVFQKRE AGELDESVLE
60 70 80 90 100
LTSQILGANP DFATLWNCRR EVLQQLETQK SPEELAALVK AELGFLESCL
110 120 130 140 150
RVNPKSYGTW HHRCWLLSRL PEPNWARELE LCARFLEADE RNFHCWDYRR
160 170 180 190 200
FVAAQAAVAP AEELAFTDSL ITRNFSNYSS WHYRSCLLPQ LHPQPDSGPQ
210 220 230 240 250
GRLPENVLLR ELELVQNAFF TDPNDQSAWF YHRWLLGRAE PHDVLCCLHV
260 270 280 290 300
SREEACLSVC FSRPLIVGSK MGTLLLTVDE APLSVEWRTP DGRNRPSHVW
310 320 330 340 350
LCDLPAASLN DHLPQHTFRV IWTGSDTQKE CVLLKGHQEC WCRDSATDEQ
360 370 380 390 400
LFRCELSVEK STVLQSELES CKELQELEPE NKWCLLTIIL LMRALDPLLY
410 420 430 440 450
EKETLEYFST LKAVDPMRAA YLDDLRSKFL VENSVLKMEY ADVRVLHLAH
460 470 480 490 500
KDLTVLCHLE QLLLVTHLDL SHNRLRALPP ALAALRCLEV LQASDNVLEN
510 520 530 540 550
LDGVANLPRL RELLLCNNRL QQSAALQTLA SCPRLVFLNL QGNSLCQEEG
560
IRERLAEMLP SVSSILT
Length:567
Mass (Da):64,989
Last modified:October 1, 2000 - v1
Checksum:i387DA2DAC12C4C0D
GO
Isoform 2 (identifier: Q9JHK4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     337-339: HQE → DAV
     340-567: Missing.

Show »
Length:339
Mass (Da):38,943
Checksum:iB68BCAADA15ED4D2
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei337 – 3393HQE → DAV in isoform 2. 1 PublicationVSP_009113
Alternative sequencei340 – 567228Missing in isoform 2. 1 PublicationVSP_009114Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF127654 Genomic DNA. Translation: AAF65918.1.
AF127655 Genomic DNA. Translation: AAF65919.1.
AF127656 mRNA. Translation: AAF65920.1.
AF127658 mRNA. Translation: AAF65921.1.
AF127659 mRNA. Translation: AAF65922.1.
AF127660 mRNA. Translation: AAF65923.1.
AF127662 mRNA. Translation: AAF65924.1.
AK002625 mRNA. Translation: BAB22240.1.
CCDSiCCDS36933.1. [Q9JHK4-1]
RefSeqiNP_062392.1. NM_019519.2. [Q9JHK4-1]
XP_006519357.1. XM_006519294.1. [Q9JHK4-1]
XP_006519358.1. XM_006519295.1. [Q9JHK4-1]
UniGeneiMm.87216.

Genome annotation databases

EnsembliENSMUST00000062861; ENSMUSP00000061498; ENSMUSG00000040472. [Q9JHK4-1]
ENSMUST00000163889; ENSMUSP00000128668; ENSMUSG00000040472. [Q9JHK4-1]
ENSMUST00000169237; ENSMUSP00000133032; ENSMUSG00000040472. [Q9JHK4-1]
GeneIDi56187.
KEGGimmu:56187.
UCSCiuc007uai.1. mouse. [Q9JHK4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF127654 Genomic DNA. Translation: AAF65918.1 .
AF127655 Genomic DNA. Translation: AAF65919.1 .
AF127656 mRNA. Translation: AAF65920.1 .
AF127658 mRNA. Translation: AAF65921.1 .
AF127659 mRNA. Translation: AAF65922.1 .
AF127660 mRNA. Translation: AAF65923.1 .
AF127662 mRNA. Translation: AAF65924.1 .
AK002625 mRNA. Translation: BAB22240.1 .
CCDSi CCDS36933.1. [Q9JHK4-1 ]
RefSeqi NP_062392.1. NM_019519.2. [Q9JHK4-1 ]
XP_006519357.1. XM_006519294.1. [Q9JHK4-1 ]
XP_006519358.1. XM_006519295.1. [Q9JHK4-1 ]
UniGenei Mm.87216.

3D structure databases

ProteinModelPortali Q9JHK4.
SMRi Q9JHK4. Positions 2-567.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 207827. 1 interaction.
IntActi Q9JHK4. 1 interaction.
STRINGi 10090.ENSMUSP00000061498.

PTM databases

PhosphoSitei Q9JHK4.

Proteomic databases

MaxQBi Q9JHK4.
PaxDbi Q9JHK4.
PRIDEi Q9JHK4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000062861 ; ENSMUSP00000061498 ; ENSMUSG00000040472 . [Q9JHK4-1 ]
ENSMUST00000163889 ; ENSMUSP00000128668 ; ENSMUSG00000040472 . [Q9JHK4-1 ]
ENSMUST00000169237 ; ENSMUSP00000133032 ; ENSMUSG00000040472 . [Q9JHK4-1 ]
GeneIDi 56187.
KEGGi mmu:56187.
UCSCi uc007uai.1. mouse. [Q9JHK4-1 ]

Organism-specific databases

CTDi 5875.
MGIi MGI:1860443. Rabggta.

Phylogenomic databases

eggNOGi COG5536.
GeneTreei ENSGT00550000075121.
HOGENOMi HOG000007845.
HOVERGENi HBG002171.
InParanoidi Q9JHK4.
KOi K14050.
OMAi WNCRREV.
OrthoDBi EOG7PP56C.
PhylomeDBi Q9JHK4.
TreeFami TF315057.

Miscellaneous databases

EvolutionaryTracei Q9JHK4.
NextBioi 311974.
PROi Q9JHK4.
SOURCEi Search...

Gene expression databases

Bgeei Q9JHK4.
CleanExi MM_RABGGTA.
Genevestigatori Q9JHK4.

Family and domain databases

Gene3Di 2.60.40.1130. 1 hit.
InterProi IPR001611. Leu-rich_rpt.
IPR002088. Prenyl_trans_a.
IPR009087. RabGGT_asu_insert-domain.
[Graphical view ]
Pfami PF00560. LRR_1. 1 hit.
PF01239. PPTA. 5 hits.
PF07711. RabGGT_insert. 1 hit.
[Graphical view ]
ProDomi PD331837. RabGG_trans_A. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF49594. SSF49594. 1 hit.
PROSITEi PS51147. PFTA. 6 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Rab geranylgeranyl transferase alpha mutation in the gunmetal mouse reduces Rab prenylation and platelet synthesis."
    Detter J.C., Zhang Q., Mules E.H., Novack E.K., Mishra V.S., Li W., McMurtrie E.B., Tchernev V.T., Wallace M.R., Seabra M.C., Swank R.T., Kingsmore S.K.
    Proc. Natl. Acad. Sci. U.S.A. 97:4144-4149(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), DISEASE, FUNCTION.
    Strain: C57BL/6J and C57BL/6J-GM/GM.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Kidney.

Entry informationi

Entry nameiPGTA_MOUSE
AccessioniPrimary (citable) accession number: Q9JHK4
Secondary accession number(s): Q9JLX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2000
Last modified: October 1, 2014
This is version 110 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

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3