P31150 (GDIA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Guanosine diphosphate dissociation inhibitor 1
Short name=GDI-1
Oligophrenin-2
Protein XAP-4

Gene names

Name:	GDI1
Synonyms:	GDIL, OPHN2, RABGDIA, XAP4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	447 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. Interacts with RAB10; negatively regulates RAB10 association with membranes and activation. Ref.16 Ref.17
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Brain; predominant in neural and sensory tissues. Ref.15
Involvement in disease	Mental retardation, X-linked 41 (MRX41) [MIM:300849]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19 Ref.20
Sequence similarities	Belongs to the Rab GDI family.

Ontologies

Keywords
Cellular component	Cytoplasm
Disease	Disease mutation Mental retardation
Molecular function	GTPase activation
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of axonogenesis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of GTPase activity Inferred from electronic annotation. Source: GOC protein transport Inferred from electronic annotation. Source: InterPro regulation of small GTPase mediated signal transduction Traceable author statement. Source: Reactome response to calcium ion Inferred from electronic annotation. Source: Compara small GTPase mediated signal transduction Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome midbody Inferred from direct assay PubMed 15166316. Source: UniProtKB neuron projection Inferred from electronic annotation. Source: Compara protein complex Inferred from electronic annotation. Source: Compara
Molecular_function	GDP-dissociation inhibitor activity Traceable author statement Ref.1. Source: ProtInc GTPase activator activity Inferred from electronic annotation. Source: UniProtKB-KW Rab GDP-dissociation inhibitor activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Rab10	P61027	3	EBI-946999,EBI-911581	From a different organism.
RAB4A	P20338	2	EBI-946999,EBI-722284

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 447	447	Rab GDP dissociation inhibitor alpha		PRO_0000056671
Amino acid modifications
	Modified residue	339	1	Phosphotyrosine By similarity
Natural variations
	Natural variant	92	1	L → P in MRX41; causes reduced binding and recycling of RAB3A. Ref.19		VAR_008130
	Natural variant	423	1	R → P in MRX41. Ref.20		VAR_008131
Experimental info
	Sequence conflict	34	1	D → G in BAA08078. Ref.2
	Sequence conflict	36	1	N → K in BAA08078. Ref.2
	Sequence conflict	149 – 151	3	NFD → GTY in BAA08078. Ref.2
	Sequence conflict	347	1	G → V in AAC15851. Ref.13
	Sequence conflict	409	1	H → Q in AAC15851. Ref.13
	Sequence conflict	416	1	D → G in AAC15851. Ref.13
	Sequence conflict	442	1	F → S in BAA08078. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P31150 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: BC283A445E50A652	FASTA	447	50,583
	10 20 30 40 50 60 MDEEYDVIVL GTGLTECILS GIMSVNGKKV LHMDRNPYYG GESSSITPLE ELYKRFQLLE 70 80 90 100 110 120 GPPESMGRGR DWNVDLIPKF LMANGQLVKM LLYTEVTRYL DFKVVEGSFV YKGGKIYKVP 130 140 150 160 170 180 STETEALASN LMGMFEKRRF RKFLVFVANF DENDPKTFEG VDPQTTSMRD VYRKFDLGQD 190 200 210 220 230 240 VIDFTGHALA LYRTDDYLDQ PCLETVNRIK LYSESLARYG KSPYLYPLYG LGELPQGFAR 250 260 270 280 290 300 LSAIYGGTYM LNKPVDDIIM ENGKVVGVKS EGEVARCKQL ICDPSYIPDR VRKAGQVIRI 310 320 330 340 350 360 ICILSHPIKN TNDANSCQII IPQNQVNRKS DIYVCMISYA HNVAAQGKYI AIASTTVETT 370 380 390 400 410 420 DPEKEVEPAL ELLEPIDQKF VAISDLYEPI DDGCESQVFC SCSYDATTHF ETTCNDIKDI 430 440 YKRMAGTAFD FENMKRKQND VFGEAEQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evolutionary conservation and genomic organization of XAP-4, an Xq28 located gene coding for a human rab GDP-dissociation inhibitor (GDI)." Sedlacek Z., Konecki D.S., Korn B., Klauck S.M., Poustka A. Mamm. Genome 5:633-639(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]	"Cloning of a brain-type isoform of human Rab GDI and its expression in human neuroblastoma cell lines and tumor specimens." Nishimura N., Goji J., Nakamura H., Orita S., Takai Y., Sano K. Cancer Res. 55:5445-5450(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Retina.
[3]	"Long-range sequence analysis in Xq28: thirteen known and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci." Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L., Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M. Hum. Mol. Genet. 5:659-668(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[4]	Feng Z., Zhang B., Zhou Y., Peng X., Yuan J., Qiang B. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"Gene diversity patterns at 10 X-chromosomal loci in humans and chimpanzees." Kitano T., Schwarz C., Nickel B., Paeaebo S. Mol. Biol. Evol. 20:1281-1289(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[6]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"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 (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	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].
[10]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Lung.
[11]	"Rapid identification of gene sequences for transcriptional map assembly by direct cDNA screening of genomic reference libraries." Hochgeschwender U. Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 143-181.
[12]	Lubec G., Vishwanath V. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 143-156; 174-193 AND 222-240, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[13]	Bhat K.S. Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 328-436.
[14]	"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes." Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J. Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 349-361. Tissue: Keratinocyte.
[15]	"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] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[16]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RHOH.
[17]	"GDI-1 preferably interacts with Rab10 in insulin-stimulated GLUT4 translocation." Chen Y., Deng Y., Zhang J., Yang L., Xie X., Xu T. Biochem. J. 422:229-235(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAB10.
[18]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"Mutations in GDI1 are responsible for X-linked non-specific mental retardation." D'Adamo P., Menegon A., Lo Nigro C., Grasso M., Gulisano M., Tamanini F., Bienvenu T., Gedeon A.K., Oostra B., Wu S.-K., Tandon A., Valtorta F., Balch W.E., Chelly J., Toniolo D. Nat. Genet. 19:134-139(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MRX41 PRO-92.
[20]	"Non-specific X-linked semidominant mental retardation by mutations in a Rab GDP-dissociation inhibitor." Bienvenu T., Des Portes V., Saint Martin A., McDonell N., Billuart P., Carrie A., Vinet M.-C., Couvert P., Toniolo D., Ropers H.-H., Moraine C., van Bokhoven H., Fryns J.-P., Kahn A., Beldjord C., Chelly J. Hum. Mol. Genet. 7:1311-1315(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MRX41 PRO-423.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	X79353 mRNA. Translation: CAA55908.1. X79354 , X79355, X79356, X79357, X79358, X79359, X79360, X79364, X79361, X79362, X79363 Genomic DNA. Translation: CAA55909.1. D45021 mRNA. Translation: BAA08078.1. L44140 Genomic DNA. Translation: AAA92648.1. AF400433 mRNA. Translation: AAK92482.1. AB101741 Genomic DNA. Translation: BAC80330.1. AB101742 Genomic DNA. Translation: BAC80331.1. AB101743 Genomic DNA. Translation: BAC80332.1. AB101744 Genomic DNA. Translation: BAC80333.1. AB101745 Genomic DNA. Translation: BAC80334.1. AB101746 Genomic DNA. Translation: BAC80335.1. AB101747 Genomic DNA. Translation: BAC80336.1. AB101748 Genomic DNA. Translation: BAC80337.1. AB101749 Genomic DNA. Translation: BAC80338.1. AB101750 Genomic DNA. Translation: BAC80339.1. AB101751 Genomic DNA. Translation: BAC80340.1. AB101752 Genomic DNA. Translation: BAC80341.1. AB101753 Genomic DNA. Translation: BAC80342.1. AB101754 Genomic DNA. Translation: BAC80343.1. AB101755 Genomic DNA. Translation: BAC80344.1. AB101756 Genomic DNA. Translation: BAC80345.1. AB101757 Genomic DNA. Translation: BAC80346.1. AB101758 Genomic DNA. Translation: BAC80347.1. AB101759 Genomic DNA. Translation: BAC80348.1. AB101760 Genomic DNA. Translation: BAC80349.1. AB101771 Genomic DNA. Translation: BAC80360.1. AB101772 Genomic DNA. Translation: BAC80361.1. AB101773 Genomic DNA. Translation: BAC80362.1. AB101774 Genomic DNA. Translation: BAC80363.1. AB101775 Genomic DNA. Translation: BAC80364.1. AB101776 Genomic DNA. Translation: BAC80365.1. AB101777 Genomic DNA. Translation: BAC80366.1. AB101778 Genomic DNA. Translation: BAC80367.1. AB101779 Genomic DNA. Translation: BAC80368.1. AB101780 Genomic DNA. Translation: BAC80369.1. AB101781 Genomic DNA. Translation: BAC80370.1. AB101782 Genomic DNA. Translation: BAC80371.1. AB101783 Genomic DNA. Translation: BAC80372.1. AB101784 Genomic DNA. Translation: BAC80373.1. AB101785 Genomic DNA. Translation: BAC80374.1. AB101786 Genomic DNA. Translation: BAC80375.1. AB101787 Genomic DNA. Translation: BAC80376.1. AB101788 Genomic DNA. Translation: BAC80377.1. AB101789 Genomic DNA. Translation: BAC80378.1. AB101790 Genomic DNA. Translation: BAC80379.1. AB101801 Genomic DNA. Translation: BAC80390.1. AB101802 Genomic DNA. Translation: BAC80391.1. AB101803 Genomic DNA. Translation: BAC80392.1. AB101804 Genomic DNA. Translation: BAC80393.1. AB101805 Genomic DNA. Translation: BAC80394.1. AB101806 Genomic DNA. Translation: BAC80395.1. AB101807 Genomic DNA. Translation: BAC80396.1. AB101808 Genomic DNA. Translation: BAC80397.1. AB101809 Genomic DNA. Translation: BAC80398.1. AB101810 Genomic DNA. Translation: BAC80399.1. AB101811 Genomic DNA. Translation: BAC80400.1. AB101812 Genomic DNA. Translation: BAC80401.1. AB101813 Genomic DNA. Translation: BAC80402.1. AB101814 Genomic DNA. Translation: BAC80403.1. AB101815 Genomic DNA. Translation: BAC80404.1. AB101816 Genomic DNA. Translation: BAC80405.1. AB101817 Genomic DNA. Translation: BAC80406.1. AB101818 Genomic DNA. Translation: BAC80407.1. AB101819 Genomic DNA. Translation: BAC80408.1. AB101820 Genomic DNA. Translation: BAC80409.1. AB101831 Genomic DNA. Translation: BAC80420.1. AB101832 Genomic DNA. Translation: BAC80421.1. AB101833 Genomic DNA. Translation: BAC80422.1. AB101834 Genomic DNA. Translation: BAC80423.1. AB101835 Genomic DNA. Translation: BAC80424.1. AB101836 Genomic DNA. Translation: BAC80425.1. AB101837 Genomic DNA. Translation: BAC80426.1. AB101838 Genomic DNA. Translation: BAC80427.1. AB101839 Genomic DNA. Translation: BAC80428.1. AB101840 Genomic DNA. Translation: BAC80429.1. AB101841 Genomic DNA. Translation: BAC80430.1. AB101842 Genomic DNA. Translation: BAC80431.1. AB101843 Genomic DNA. Translation: BAC80432.1. AB101844 Genomic DNA. Translation: BAC80433.1. AB101845 Genomic DNA. Translation: BAC80434.1. AB101846 Genomic DNA. Translation: BAC80435.1. AB101847 Genomic DNA. Translation: BAC80436.1. AB101848 Genomic DNA. Translation: BAC80437.1. AB101849 Genomic DNA. Translation: BAC80438.1. AB101850 Genomic DNA. Translation: BAC80439.1. AB102647 mRNA. Translation: BAC81116.1. CR542258 mRNA. Translation: CAG47054.1. CR542276 mRNA. Translation: CAG47072.1. BT019884 mRNA. Translation: AAV38687.1. BX936385 Genomic DNA. Translation: CAI95780.1. CH471172 Genomic DNA. Translation: EAW72710.1. BC000317 mRNA. Translation: AAH00317.1. BC012201 mRNA. Translation: AAH12201.1. U14623 Genomic DNA. Translation: AAA21558.1. L05086 mRNA. Translation: AAC15851.1.
IPI	IPI00010154.
PIR	I37082.
RefSeq	NP_001484.1. NM_001493.2.
UniGene	Hs.595950. Hs.74576.
3D structure databases
ProteinModelPortal	P31150.
ModBase	Search...
Protein-protein interaction databases
IntAct	P31150. 8 interactions.
MINT	MINT-2859157.
STRING	9606.ENSP00000394071.
PTM databases
PhosphoSite	P31150.
Polymorphism databases
DMDM	1707886.
2D gel databases
OGP	P31150.
REPRODUCTION-2DPAGE	IPI00010154.
UCD-2DPAGE	P31150.
Proteomic databases
PaxDb	P31150.
PeptideAtlas	P31150.
PRIDE	P31150.
Protocols and materials databases
DNASU	2664.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000447750; ENSP00000394071; ENSG00000203879. ENST00000601899; ENSP00000471186; ENSG00000268690.
GeneID	2664.
KEGG	hsa:2664.
UCSC	uc004fli.4. human.
Organism-specific databases
CTD	2664.
GeneCards	GC0XP153665.
H-InvDB	HIX0056464.
HGNC	HGNC:4226. GDI1.
HPA	CAB012979. HPA049290.
MIM	300104. gene. 300849. phenotype.
neXtProt	NX_P31150.
Orphanet	777. X-linked nonsyndromic intellectual deficit.
PharmGKB	PA28641.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5044.
HOVERGEN	HBG000839.
InParanoid	P31150.
OMA	FGLDKNT.
OrthoDB	EOG4H19VS.
Enzyme and pathway databases
Pathway_Interaction_DB	p38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	P31150.
Bgee	P31150.
CleanEx	HS_GDI1.
Genevestigator	P31150.
GermOnline	ENSG00000203879. 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
ChiTaRS	GDI1. human.
GenomeRNAi	2664.
NextBio	10512.
SOURCE	Search...

Entry information

Entry name

GDIA_HUMAN

Accession

Primary (citable) accession number: P31150
Secondary accession number(s): P50394 , Q6FG50, Q7Z2G6, Q7Z2G9, Q7Z2H5, Q7Z2I6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 137 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.