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P31150 (GDIA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Promotes the dissociation of GDP-bound Rab proteins from the membrane and inhibits their activation. Promotes the dissociation of RAB1A, RAB3A, RAB5A and RAB10 from membranes. Ref.19

Subunit structure

Interacts with RHOH. Interacts with RAB1A, RAB3A, RAB5A and RAB10. Ref.16 Ref.17 Ref.19

Subcellular location

Cytoplasm. Golgi apparatustrans-Golgi network Ref.17.

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 adaptive 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.20 Ref.21

Sequence similarities

Belongs to the Rab GDI family.

Ontologies

Keywords
   Cellular componentCytoplasm
Golgi apparatus
   DiseaseDisease mutation
Mental retardation
   Molecular functionGTPase activation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRab protein signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of axonogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein targeting to membrane

Inferred from mutant phenotype Ref.19. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: InterPro

regulation of catalytic activity

Inferred from sequence or structural similarity. Source: GOC

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

response to calcium ion

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.15. Source: ProtInc

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay. Source: LIFEdb

cytosol

Traceable author statement. Source: Reactome

midbody

Inferred from direct assay PubMed 15166316. Source: UniProtKB

neuron projection

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGDP-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 sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Rab10P610273EBI-946999,EBI-911581From a different organism.
RAB4AP203382EBI-946999,EBI-722284

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 447447Rab GDP dissociation inhibitor alpha
PRO_0000056671

Natural variations

Natural variant921L → P in MRX41; causes reduced binding and recycling of RAB3A. Ref.20
VAR_008130
Natural variant4231R → P in MRX41. Ref.21
VAR_008131

Experimental info

Sequence conflict341D → G in BAA08078. Ref.2
Sequence conflict361N → K in BAA08078. Ref.2
Sequence conflict149 – 1513NFD → GTY in BAA08078. Ref.2
Sequence conflict3471G → V in AAC15851. Ref.13
Sequence conflict4091H → Q in AAC15851. Ref.13
Sequence conflict4161D → G in AAC15851. Ref.13
Sequence conflict4421F → S in BAA08078. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P31150 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: BC283A445E50A652

FASTA44750,583
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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, SUBCELLULAR LOCATION.
[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]"Rab1a and Rab5a preferentially bind to binary lipid compositions with higher stored curvature elastic energy."
Kirsten M.L., Baron R.A., Seabra M.C., Ces O.
Mol. Membr. Biol. 30:303-314(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB1A AND RAB5A, FUNCTION.
[20]"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.
[21]"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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X79353 mRNA. Translation: CAA55908.1.
X79354 expand/collapse EMBL AC list , 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.
PIRI37082.
RefSeqNP_001484.1. NM_001493.2.
UniGeneHs.595950.
Hs.74576.

3D structure databases

ProteinModelPortalP31150.
SMRP31150. Positions 1-430.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108932. 31 interactions.
IntActP31150. 11 interactions.
MINTMINT-2859157.
STRING9606.ENSP00000394071.

PTM databases

PhosphoSiteP31150.

Polymorphism databases

DMDM1707886.

2D gel databases

OGPP31150.
REPRODUCTION-2DPAGEIPI00010154.
UCD-2DPAGEP31150.

Proteomic databases

PaxDbP31150.
PeptideAtlasP31150.
PRIDEP31150.

Protocols and materials databases

DNASU2664.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000447750; ENSP00000394071; ENSG00000203879.
ENST00000601899; ENSP00000471186; ENSG00000268690.
GeneID2664.
KEGGhsa:2664.
UCSCuc004fli.4. human.

Organism-specific databases

CTD2664.
GeneCardsGC0XP153665.
H-InvDBHIX0056464.
HGNCHGNC:4226. GDI1.
HPACAB012979.
HPA049290.
MIM300104. gene.
300849. phenotype.
neXtProtNX_P31150.
Orphanet777. X-linked non-syndromic intellectual deficit.
PharmGKBPA28641.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5044.
HOVERGENHBG000839.
InParanoidP31150.
KOK17255.
OMAFGLDKNT.
PhylomeDBP31150.
TreeFamTF300449.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressP31150.
BgeeP31150.
CleanExHS_GDI1.
GenevestigatorP31150.

Family and domain databases

InterProIPR018203. GDP_dissociation_inhibitor.
IPR000806. RabGDI.
[Graphical view]
PfamPF00996. GDI. 1 hit.
[Graphical view]
PRINTSPR00892. RABGDI.
PR00891. RABGDIREP.
ProtoNetSearch...

Other

ChiTaRSGDI1. human.
GeneWikiGDI1.
GenomeRNAi2664.
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Entry information

Entry nameGDIA_HUMAN
AccessionPrimary (citable) accession number: P31150
Secondary accession number(s): P50394 expand/collapse secondary AC list , Q6FG50, Q7Z2G6, Q7Z2G9, Q7Z2H5, Q7Z2I6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM