P50395 (GDIB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rab GDP dissociation inhibitor beta
Short name=Rab GDI beta

Alternative name(s):
Guanosine diphosphate dissociation inhibitor 2
Short name=GDI-2

Gene names

Name:	GDI2
Synonyms:	RABGDIB

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	445 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them.
Subunit structure	Interacts with RHOH. Ref.7
Subcellular location	Cytoplasm By similarity. Membrane; Peripheral membrane protein By similarity.
Tissue specificity	Ubiquitous. Ref.6
Sequence similarities	Belongs to the Rab GDI family.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Molecular function	GTPase activation
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein transport Inferred from electronic annotation. Source: InterPro small GTPase mediated signal transduction Traceable author statement. Source: Reactome
Cellular component	cell surface Inferred from direct assay. Source: UniProtKB cytosol Traceable author statement. Source: Reactome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	Rab GDP-dissociation inhibitor activity Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction Ref.7. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 445	445	Rab GDP dissociation inhibitor beta		PRO_0000056679
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.10
	Modified residue	61	1	Phosphoserine Ref.9 Ref.10
	Modified residue	112	1	N6-acetyllysine Ref.11
	Modified residue	203	1	Phosphotyrosine Ref.8
	Modified residue	269	1	N6-acetyllysine Ref.11
Experimental info
	Sequence conflict	2	1	N → D in BAA03095. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P50395 [UniParc]. Last modified April 27, 2001. Version 2. Checksum: CE186A2E3A47FCC9	FASTA	445	50,663
	10 20 30 40 50 60 MNEEYDVIVL GTGLTECILS GIMSVNGKKV LHMDRNPYYG GESASITPLE DLYKRFKIPG 70 80 90 100 110 120 SPPESMGRGR DWNVDLIPKF LMANGQLVKM LLYTEVTRYL DFKVTEGSFV YKGGKIYKVP 130 140 150 160 170 180 STEAEALASS LMGLFEKRRF RKFLVYVANF DEKDPRTFEG IDPKKTTMRD VYKKFDLGQD 190 200 210 220 230 240 VIDFTGHALA LYRTDDYLDQ PCYETINRIK LYSESLARYG KSPYLYPLYG LGELPQGFAR 250 260 270 280 290 300 LSAIYGGTYM LNKPIEEIIV QNGKVIGVKS EGEIARCKQL ICDPSYVKDR VEKVGQVIRV 310 320 330 340 350 360 ICILSHPIKN TNDANSCQII IPQNQVNRKS DIYVCMISFA HNVAAQGKYI AIVSTTVETK 370 380 390 400 410 420 EPEKEIRPAL ELLEPIEQKF VSISDLLVPK DLGTESQIFI SRTYDATTHF ETTCDDIKNI 430 440 YKRMTGSEFD FEEMKRKKND IYGED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Asada M., Kaibuchi K., Takai Y. Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"The human rab GDI beta gene with long retroposon-rich introns maps to 10p15 and its pseudogene to 7p11-p13." Sedlacek Z., Munstermann E., Mincheva A., Lichter P., Poutska A. Mamm. Genome 9:78-80(1998) [PubMed: 9434952] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: Placenta.
[5]	"Impairment of bile salt-dependent lipase secretion in human pancreatic tumoral SOJ-6 cells." Caillol N., Pasqualini E., Lloubes R., Lombardo D. J. Cell. Biochem. 79:628-647(2000) [PubMed: 10996854] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 81-439. Tissue: Pancreas.
[6]	"Expression patterns of two human genes coding for different rab GDP-dissociation inhibitors (GDIs), extremely conserved proteins involved in cellular transport." Bachner D., Sedlacek Z., Korn B., Hameister H., Poustka A. Hum. Mol. Genet. 4:701-708(1995) [PubMed: 7543319] [Abstract] Cited for: TISSUE SPECIFICITY.
[7]	"The hematopoiesis-specific GTP-binding protein RhoH is GTPase deficient and modulates activities of other Rho GTPases by an inhibitory function." Li X., Bu X., Lu B., Avraham H., Flavell R.A., Lim B. Mol. Cell. Biol. 22:1158-1171(2002) [PubMed: 11809807] [Abstract] Cited for: INTERACTION WITH RHOH.
[8]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-203, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[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 SER-61, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112 AND LYS-269, MASS SPECTROMETRY.
[12]	"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	D13988 mRNA. Translation: BAA03095.1. Y13286 mRNA. Translation: CAA73734.1. Y13287 , Y13288, Y13289, Y13290, Y13291, Y13292, Y13293, Y13294, Y13295, Y13296, Y13297 Genomic DNA. Translation: CAA73735.1. BT006868 mRNA. Translation: AAP35514.1. BC005145 mRNA. Translation: AAH05145.1. AF144713 mRNA. Translation: AAD34588.1.
IPI	IPI00940148.
RefSeq	NP_001108628.1. NM_001115156.1. NP_001485.2. NM_001494.3.
UniGene	Hs.299055.
3D structure databases
ProteinModelPortal	P50395.
SMR	P50395. Positions 1-430.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-50593N.
IntAct	P50395. 9 interactions.
STRING	P50395.
PTM databases
PhosphoSite	P50395.
Polymorphism databases
DMDM	13638228.
2D gel databases
OGP	P50395.
REPRODUCTION-2DPAGE	IPI00031461. P50395.
Proteomic databases
PRIDE	P50395.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000380191; ENSP00000369538; ENSG00000057608.
GeneID	2665.
KEGG	hsa:2665.
UCSC	uc001iil.2. human.
Organism-specific databases
CTD	2665.
GeneCards	GC10M005807.
H-InvDB	HIX0008614.
HGNC	HGNC:4227. GDI2.
MIM	600767. gene.
neXtProt	NX_P50395.
PharmGKB	PA28642.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18194.
HOVERGEN	HBG000839.
InParanoid	P50395.
OrthoDB	EOG4H19VS.
PhylomeDB	P50395.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	P50395.
Bgee	P50395.
CleanEx	HS_GDI2.
Genevestigator	P50395.
GermOnline	ENSG00000057608. Homo sapiens.
Family and domain databases
InterPro	IPR018203. GDP_dissociation_inhibitor. IPR000806. RabGDI. [Graphical view]
Pfam	PF00996. GDI. 1 hit. [Graphical view]
PRINTS	PR00892. RABGDI. PR00891. RABGDIREP.
ProtoNet	Search...
Other
NextBio	10516.
SOURCE	Search...

Entry information

Entry name

GDIB_HUMAN

Accession

Primary (citable) accession number: P50395
Secondary accession number(s): O43928, Q9UQM6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	April 27, 2001
Last modified:	January 25, 2012
This is version 105 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.