Reviewed, UniProtKB/Swiss-Prot Q92696 (PGTA_HUMAN)

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 geranylgeranyltransferase subunit alpha
    Rab geranyl-geranyltransferase subunit alpha
      Short name=Rab GG transferase alpha
      Short name=Rab GGTase alpha

Gene names

Name:

RABGGTA

Organism

Homo sapiens (Human) [Complete proteome]

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 6 PFTA repeats.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	Metal-binding Zinc
Molecular function	Prenyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	visual perception Traceable author statement. Source: ProtInc
Molecular function	Rab geranylgeranyltransferase activity Traceable author statement. Source: ProtInc protein binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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
Sites
	Metal binding	2	1	Zinc By similarity
Natural variations
	Natural variant	420	1	T → A: dbSNP rs729421. Ref.4		VAR_020406

Sequences

	Sequence		Length	Mass (Da)
	Q92696-1 [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]	"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.
[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: 7991565] [Abstract] Cited for: CHARACTERIZATION.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y08200 mRNA. Translation: CAA69382.1. AK291347 mRNA. Translation: BAF84036.1. AK292613 mRNA. Translation: BAF85302.1. BC003093 mRNA. Translation: AAH03093.1.
IPI	IPI00022664.
PIR	JC5538.
RefSeq	NP_004572.3. NP_878256.1.
UniGene	Hs.377992
3D structure databases
SMR	Q92696. Positions 2-567.
ModBase	Search...
Protein-protein interaction databases
STRING	Q92696.
Proteomic databases
PRIDE	Q92696.
Genome annotation databases
Ensembl	ENST00000216840; ENSP00000216840; ENSG00000100949; Homo sapiens. [Genome view] ENST00000399409; ENSP00000382341; ENSG00000100949; Homo sapiens. [Genome view]
GeneID	5875.
KEGG	hsa:5875.
UCSC	uc001wof.1. human.
Organism-specific databases
CTD	5875.
GeneCards	GC14M023804.
H-InvDB	HIX0011565.
HGNC	HGNC:9795. RABGGTA.
MIM	601905. gene.
PharmGKB	PA34156.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10945.
HOGENOM	HBG444904.
HOVERGEN	Q92696.
InParanoid	Q92696.
OMA	WHYRSCL.
OrthoDB	EOG9909VB.
PhylomeDB	Q92696.
Enzyme and pathway databases
BRENDA	2.5.1.60. 247.
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. RabGG_trans_A. [Graphical view]
Gene3D	G3DSA:1.25.40.120. Prenyl_trans. 1 hit.
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]
PROSITE	PS51450. LRR. 5 hits. PS51147. PFTA. 6 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	22826.
SOURCE	Search...

Entry information

Entry name

PGTA_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 15, 1999
Last modified:	February 9, 2010
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.