Q92696 (PGTA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

RABGGTA

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	567 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to both cysteines in Rab proteins with an -XXCC, -XCXC and -CCXX C-terminal, such as RAB1A, RAB3A and RAB5A respectively.
Catalytic activity	Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.
Cofactor	Binds 1 zinc ion per dimer By similarity.
Enzyme regulation	The enzymatic reaction requires the aid of a Rab escort protein (also called component A).
Subunit structure	Heterodimer of an alpha and a beta subunit, collectively called component B.
Sequence similarities	Belongs to the protein prenyltransferase subunit alpha family. Contains 5 LRR (leucine-rich) repeats. Contains 6 PFTA repeats.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Domain	Leucine-rich repeat Repeat
Ligand	Metal-binding Zinc
Molecular function	Prenyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	visual perception Traceable author statement. Source: ProtInc
Molecular function	Rab geranylgeranyltransferase activity Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 567	567	Geranylgeranyl transferase type-2 subunit alpha		PRO_0000119757
Regions
	Repeat	44 – 78	35	PFTA 1
	Repeat	88 – 122	35	PFTA 2
	Repeat	124 – 158	35	PFTA 3
	Repeat	159 – 193	35	PFTA 4
	Repeat	207 – 241	35	PFTA 5
	Repeat	363 – 397	35	PFTA 6
	Repeat	442 – 463	22	LRR 1
	Repeat	464 – 486	23	LRR 2
	Repeat	487 – 508	22	LRR 3
	Repeat	509 – 530	22	LRR 4
	Repeat	534 – 555	22	LRR 5
Sites
	Metal binding	2	1	Zinc By similarity
Natural variations
	Natural variant	420	1	T → A. Ref.4 Corresponds to variant rs729421 [ dbSNP | Ensembl ].		VAR_020406

Sequences

	Sequence		Length	Mass (Da)
	Q92696 [UniParc]. Last modified July 15, 1999. Version 2. Checksum: ABA1AFFC8A496C5F	FASTA	567	65,072
	10 20 30 40 50 60 MHGRLKVKTS EEQAEAKRLE REQKLKLYQS ATQAVFQKRQ AGELDESVLE LTSQILGANP 70 80 90 100 110 120 DFATLWNCRR EVLQQLETQK SPEELAALVK AELGFLESCL RVNPKSYGTW HHRCWLLGRL 130 140 150 160 170 180 PEPNWTRELE LCARFLEVDE RNFHCWDYRR FVATQAAVPP AEELAFTDSL ITRNFSNYSS 190 200 210 220 230 240 WHYRSCLLPQ LHPQPDSGPQ GRLPEDVLLK ELELVQNAFF TDPNDQSAWF YHRWLLGRAD 250 260 270 280 290 300 PQDALRCLHV SRDEACLTVS FSRPLLVGSR MEILLLMVDD SPLIVEWRTP DGRNRPSHVW 310 320 330 340 350 360 LCDLPAASLN DQLPQHTFRV IWTAGDVQKE CVLLKGRQEG WCRDSTTDEQ LFRCELSVEK 370 380 390 400 410 420 STVLQSELES CKELQELEPE NKWCLLTIIL LMRALDPLLY EKETLQYFQT LKAVDPMRAT 430 440 450 460 470 480 YLDDLRSKFL LENSVLKMEY AEVRVLHLAH KDLTVLCHLE QLLLVTHLDL SHNRLRTLPP 490 500 510 520 530 540 ALAALRCLEV LQASDNAIES LDGVTNLPRL QELLLCNNRL QQPAVLQPLA SCPRLVLLNL 550 560 QGNPLCQAVG ILEQLAELLP SVSSVLT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 8954794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal brain.
[2]	van Bokhoven H. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"The genes encoding geranylgeranyl transferase alpha-subunit and transglutaminase 1 are very closely linked but not functionally related in terminally differentiating keratinocytes." Song H.-J., Rossi A., Ceci R., Kim I.-G., Anzano M.A., Jang S.-I., De Laurenzi V., Steinert P.M. Biochem. Biophys. Res. Commun. 235:10-14(1997) [PubMed: 9196026] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-420. Tissue: Thymus and Tongue.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[7]	"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: 7991565] [Abstract] Cited for: CHARACTERIZATION.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y08200 mRNA. Translation: CAA69382.1. AK291347 mRNA. Translation: BAF84036.1. AK292613 mRNA. Translation: BAF85302.1. CH471078 Genomic DNA. Translation: EAW66044.1. CH471078 Genomic DNA. Translation: EAW66045.1. BC003093 mRNA. Translation: AAH03093.1.
IPI	IPI00022664.
PIR	JC5538.
RefSeq	NP_004572.3. NM_004581.3. NP_878256.1. NM_182836.1.
UniGene	Hs.377992.
3D structure databases
ProteinModelPortal	Q92696.
SMR	Q92696. Positions 2-567.
ModBase	Search...
Protein-protein interaction databases
STRING	Q92696.
PTM databases
PhosphoSite	Q92696.
Polymorphism databases
DMDM	6093707.
Proteomic databases
PRIDE	Q92696.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000216840; ENSP00000216840; ENSG00000100949. ENST00000399409; ENSP00000382341; ENSG00000100949.
GeneID	5875.
KEGG	hsa:5875.
UCSC	uc001wof.1. human.
Organism-specific databases
CTD	5875.
GeneCards	GC14M024734.
H-InvDB	HIX0011565.
HGNC	HGNC:9795. RABGGTA.
HPA	HPA043488.
MIM	601905. gene.
neXtProt	NX_Q92696.
PharmGKB	PA34156.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10945.
GeneTree	ENSGT00550000075121.
HOGENOM	HBG444904.
HOVERGEN	HBG002171.
InParanoid	Q92696.
OMA	QSELESC.
OrthoDB	EOG4FXR7F.
PhylomeDB	Q92696.
Enzyme and pathway databases
Pathway_Interaction_DB	prlsignalingeventspathway. Signaling events mediated by PRL.
Gene expression databases
ArrayExpress	Q92696.
Bgee	Q92696.
CleanEx	HS_RABGGTA.
Genevestigator	Q92696.
GermOnline	ENSG00000100949. Homo sapiens.
Family and domain databases
InterPro	IPR001611. Leu-rich_rpt. IPR002088. Prenyl_trans_a. IPR008940. Prenyltransferase. IPR009087. RabGGT_asu_insert-domain. [Graphical view]
Gene3D	G3DSA:1.25.40.120. Prenyl_trans. 2 hits. G3DSA:2.60.40.1130. RabGGT_asu_insert-domain. 1 hit.
KO	K14050.
Pfam	PF00560. LRR_1. 1 hit. PF01239. PPTA. 5 hits. PF07711. RabGGT_insert. 1 hit. [Graphical view]
ProDom	PD331837. RabGG_trans_A. 1 hit. [Graphical view] [Entries sharing at least one domain]
SUPFAM	SSF49594. RabGG_trans_A. 1 hit.
PROSITE	PS51450. LRR. 5 hits. PS51147. PFTA. 6 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	22826.
SOURCE	Search...

Entry information

Entry name

PGTA_HUMAN

Accession

Primary (citable) accession number: Q92696
Secondary accession number(s): A8K5N2, D3DS69

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 15, 1999
Last modified:	January 25, 2012
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.