Reviewed, UniProtKB/Swiss-Prot P53611 (PGTB2_HUMAN)

Names and origin

Protein names

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
    Type II protein geranyl-geranyltransferase subunit beta
    Rab geranylgeranyltransferase subunit beta
    Rab geranyl-geranyltransferase subunit beta
      Short name=Rab GG transferase beta
      Short name=Rab GGTase beta

Gene names

Name:	RABGGTB
Synonyms:	GGTB

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	331 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 subunit 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. Interaction of beta subunit with prenylated PTP4A2 precludes its association with subunit alpha, and inhibits enzyme activity.
Sequence similarities	Belongs to the protein prenyltransferase subunit beta family. Contains 6 PFTB repeats.

Ontologies

Keywords
Domain	Repeat
Ligand	Metal-binding Zinc
Molecular function	Prenyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein modification process Non-traceable author statement. Source: UniProtKB visual perception Traceable author statement. Source: ProtInc
Molecular function	Rab geranylgeranyltransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARAF	P10398	3	EBI-536715,EBI-365961

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 331	331	Geranylgeranyl transferase type-2 subunit beta		PRO_0000119772
Regions
	Repeat	20 – 61	42	PFTB 1
	Repeat	68 – 109	42	PFTB 2
	Repeat	116 – 157	42	PFTB 3
	Repeat	164 – 205	42	PFTB 4
	Repeat	212 – 253	42	PFTB 5
	Repeat	260 – 302	43	PFTB 6
Sites
	Metal binding	238	1	Zinc By similarity
	Metal binding	240	1	Zinc By similarity
	Metal binding	290	1	Zinc By similarity
Amino acid modifications
	Modified residue	3	1	Phosphothreonine Ref.7 Ref.8 Ref.9
Experimental info
	Sequence conflict	153	1	L → F in AAA91473. Ref.1
	Sequence conflict	177	1	F → S in CAA69383. Ref.3
	Sequence conflict	211	1	N → T in CAA69383. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P53611-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 37A8A6329146C49B	FASTA	331	36,924
	10 20 30 40 50 60 MGTPQKDVII KSDAPDTLLL EKHADYIASY GSKKDDYEYC MSEYLRMSGI YWGLTVMDLM 70 80 90 100 110 120 GQLHRMNREE ILAFIKSCQH ECGGISASIG HDPHLLYTLS AVQILTLYDS INVIDVNKVV 130 140 150 160 170 180 EYVKGLQKED GSFAGDIWGE IDTRFSFCAV ATLALLGKLD AINVEKAIEF VLSCMNFDGG 190 200 210 220 230 240 FGCRPGSESH AGQIYCCTGF LAITSQLHQV NSDLLGWWLC ERQLPSGGLN GRPEKLPDVC 250 260 270 280 290 300 YSWWVLASLK IIGRLHWIDR EKLRNFILAC QDEETGGFAD RPGDMVDPFH TLFGIAGLSL 310 320 330 LGEEQIKPVN PVFCMPEEVL QRVNVQPELV S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8706741] [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: 8954794] [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: 15489334] [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: 11447212] [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: 7991565] [Abstract] Cited for: CHARACTERIZATION.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, MASS SPECTROMETRY. Tissue: Epithelium.
[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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, MASS SPECTROMETRY.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, MASS SPECTROMETRY.
[10]	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
EMBLGenBankDDBJ	U49245 mRNA. Translation: AAA91473.1. X98001 mRNA. Translation: CAA66638.1. Y08201 mRNA. Translation: CAA69383.1. BC020790 mRNA. Translation: AAH20790.1.
IPI	IPI00295849.
PIR	G02431.
RefSeq	NP_004573.2.
UniGene	Hs.78948
3D structure databases
HSSP	HSSP built from PDB template 1LTX based on UniProtKB Q08603.
SMR	P53611. Positions 3-331.
ModBase	Search...
Protein-protein interaction databases
IntAct	P53611. 1 interaction.
PTM databases
PhosphoSite	P53611.
Proteomic databases
PRIDE	P53611.
Genome annotation databases
Ensembl	ENSG00000137955. Homo sapiens. [Contig view]
GeneID	5876.
KEGG	hsa:5876.
UCSC	uc001dgy.1. human.
Organism-specific databases
GeneCards	GC01P075963.
H-InvDB	HIX0000707. HIX0077640.
HGNC	HGNC:9796. RABGGTB.
MIM	179080. gene.
PharmGKB	PA34157.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P53611.
OMA	P53611. YWGLTAL.
Enzyme and pathway databases
BRENDA	2.5.1.60. 247.
Pathway_Interaction_DB	prlsignalingeventspathway. Signaling events mediated by PRL.
Gene expression databases
ArrayExpress	P53611.
Bgee	P53611.
CleanEx	HS_RABGGTB.
Family and domain databases
InterPro	IPR001330. Prenyltrans. [Graphical view]
Pfam	PF00432. Prenyltrans. 5 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	22832.
SOURCE	Search...

Entry information

Entry name

PGTB2_HUMAN

Accession

Primary (citable) accession number: P53611
Secondary accession number(s): Q92697

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 1, 1997
Last modified:	July 7, 2009
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)