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P52565 (GDIR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rho GDP-dissociation inhibitor 1

Short name=Rho GDI 1
Alternative name(s):
Rho-GDI alpha
Gene names
Name:ARHGDIA
Synonyms:GDIA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length204 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Controls Rho proteins homeostasis. Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1. Ref.20 Ref.24

Subunit structure

Monomer. Interacts with FER. Interacts with PLXNB3 By similarity. Forms a heterodimer with RAC1. Interacts with RHOA, the affinity is increased by three orders of magnitude when RHOA is prenylated. Interacts with PSMD10; the interaction increases ARHGDIA association with RHOA, leading to ARHGDIA-mediated inactivation of RHOA and ROCK and prolonged AKT activation. Interacts with RHOC and CDC42. Ref.18 Ref.19 Ref.20 Ref.24

Subcellular location

Cytoplasm Ref.24.

Involvement in disease

Nephrotic syndrome 8 (NPHS8) [MIM:615244]: A form of nephrotic syndrome, a renal disease clinically characterized by progressive renal failure, severe proteinuria, hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show diffuse mesangial sclerosis, with small glomeruli, hypercellularity, increased extracellular matrix, and contracted/collapsed glomerular tufts surrounded by immature or abnormal podocytes.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.24

Sequence similarities

Belongs to the Rho GDI family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   Molecular functionGTPase activation
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRho protein signal transduction

Traceable author statement Ref.1. Source: ProtInc

cellular component movement

Traceable author statement PubMed 16130169. Source: UniProtKB

negative regulation of apoptotic process

Traceable author statement PubMed 16130169. Source: UniProtKB

negative regulation of axonogenesis

Traceable author statement. Source: Reactome

negative regulation of cell adhesion

Traceable author statement Ref.1. Source: ProtInc

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of axonogenesis

Traceable author statement. Source: Reactome

regulation of axonogenesis

Traceable author statement. Source: Reactome

regulation of catalytic activity

Traceable author statement Ref.1. Source: GOC

regulation of protein localization

Inferred from electronic annotation. Source: Ensembl

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

   Cellular_componentcytoskeleton

Traceable author statement PubMed 16130169. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337PubMed 23376485. Source: UniProt

immunological synapse

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGTPase activator activity

Inferred from electronic annotation. Source: UniProtKB-KW

Rho GDP-dissociation inhibitor activity

Traceable author statement Ref.1. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 10489445PubMed 11513578PubMed 17245428PubMed 20711218PubMed 21900206PubMed 22157745. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P52565-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P52565-2)

The sequence of this isoform differs from the canonical sequence as follows:
     139-183: IDKTDYMVGSYGPRAEEYEFLTPVEEAPKGMLARGSYSIKSRFTD → N

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 204203Rho GDP-dissociation inhibitor 1
PRO_0000219013

Amino acid modifications

Modified residue21N-acetylalanine Ref.12 Ref.16 Ref.21
Modified residue341Phosphoserine By similarity
Modified residue431N6-acetyllysine By similarity
Modified residue1051N6-acetyllysine Ref.17
Modified residue1271N6-acetyllysine Ref.17
Modified residue1411N6-acetyllysine; alternate Ref.15 Ref.17
Modified residue1411N6-succinyllysine; alternate By similarity
Modified residue1781N6-acetyllysine Ref.17

Natural variations

Alternative sequence139 – 18345IDKTD…SRFTD → N in isoform 2.
VSP_046699
Natural variant1851Missing in NPHS8; produces mislocalization into the nucleus, hyperactivation of Rho-GTPases RHOA, RAC1 and CDC42 and impaired cell motility. Ref.24
VAR_069814

Experimental info

Mutagenesis451D → A: Loss of RHOA interaction; when associated with A-185. Ref.20
Mutagenesis1851D → A: Loss of RHOA interaction; when associated with A-45. Ref.20
Sequence conflict1391I → V in CAA45344. Ref.3
Sequence conflict1391I → V in BAG35268. Ref.5
Sequence conflict1881D → R AA sequence Ref.13

Secondary structure

............................. 204
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 59CB6F42E3B3BCCA

FASTA20423,207
        10         20         30         40         50         60 
MAEQEPTAEQ LAQIAAENEE DEHSVNYKPP AQKSIQEIQE LDKDDESLRK YKEALLGRVA 

        70         80         90        100        110        120 
VSADPNVPNV VVTGLTLVCS SAPGPLELDL TGDLESFKKQ SFVLKEGVEY RIKISFRVNR 

       130        140        150        160        170        180 
EIVSGMKYIQ HTYRKGVKID KTDYMVGSYG PRAEEYEFLT PVEEAPKGML ARGSYSIKSR 

       190        200 
FTDDDKTDHL SWEWNLTIKK DWKD 

« Hide

Isoform 2 [UniParc].

Checksum: 0E14B24C9B7AFCA2
Show »

FASTA16018,233

References

« Hide 'large scale' references
[1]"Identification of two human Rho GDP dissociation inhibitor proteins whose overexpression leads to disruption of the actin cytoskeleton."
Leffers H., Nielsen M.S., Andersen A.H., Honore B., Madsen P., Vandekerckhove J., Celis J.E.
Exp. Cell Res. 209:165-174(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Molecular cloning of human rho GDI."
Maeda A., Kaibuchi K., Takai Y.
Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"cDNA sequence of human rho GDP dissociation inhibitor."
Chuang T.H., Bokoch G.M.
Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Genomic sequence of a human rho GDP dissociation inhibitor (GDI)."
Mulheron J.G., Schwinn D.A., Caron M.G., Liggett S.B.
Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[5]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain cortex and Neuroblastoma.
[6]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]"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] (ISOFORM 1).
[9]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"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] (ISOFORM 1).
Tissue: Colon, Lung, Muscle, Skin, Tonsil and Uterus.
[12]Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
Submitted (MAY-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-42, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: T-cell.
[13]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 34-50; 139-167 AND 181-199, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[14]"Regulation of the human neutrophil NADPH oxidase by rho-related G-proteins."
Kwong C.H., Malech H.L., Rotrosen D., Leto T.L.
Biochemistry 32:5711-5717(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 34-37; 136-142 AND 181-199.
Tissue: Neutrophil.
[15]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105; LYS-127; LYS-141 AND LYS-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"The Fer tyrosine kinase regulates interactions of Rho GDP-Dissociation Inhibitor alpha with the small GTPase Rac."
Fei F., Kweon S.M., Haataja L., De Sepulveda P., Groffen J., Heisterkamp N.
BMC Biochem. 11:48-48(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FER.
[19]"Gankyrin plays an essential role in Ras-induced tumorigenesis through regulation of the RhoA/ROCK pathway in mammalian cells."
Man J.H., Liang B., Gu Y.X., Zhou T., Li A.L., Li T., Jin B.F., Bai B., Zhang H.Y., Zhang W.N., Li W.H., Gong W.L., Li H.Y., Zhang X.M.
J. Clin. Invest. 120:2829-2841(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSMD10 AND RHOA.
[20]"Regulation of Rho GTPase crosstalk, degradation and activity by RhoGDI1."
Boulter E., Garcia-Mata R., Guilluy C., Dubash A., Rossi G., Brennwald P.J., Burridge K.
Nat. Cell Biol. 12:477-483(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RHOA AND RHOC, MUTAGENESIS OF ASP-45 AND ASP-185.
[21]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"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].
[23]"A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm."
Keep N.H., Barnes M., Barsukov I., Badii R., Lian L.-Y., Segal A.W., Moody P.C.E., Roberts G.C.K.
Structure 5:623-633(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 59-204.
[24]"ARHGDIA: a novel gene implicated in nephrotic syndrome."
Gupta I.R., Baldwin C., Auguste D., Ha K.C., El Andalousi J., Fahiminiya S., Bitzan M., Bernard C., Akbari M.R., Narod S.A., Rosenblatt D.S., Majewski J., Takano T.
J. Med. Genet. 50:330-338(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NPHS8 ASP-185 DEL, CHARACTERIZATION OF VARIANT NPHS8 ASP-185 DEL, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAC1; RHOA AND CDC42.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X69550 mRNA. Translation: CAA49281.1.
D13989 mRNA. Translation: BAA03096.1.
M97579 mRNA. Translation: AAA36566.1.
X63863 Genomic DNA. Translation: CAA45344.1.
AK300816 mRNA. Translation: BAG62471.1.
AK312347 mRNA. Translation: BAG35268.1.
AF498926 mRNA. Translation: AAM21074.1.
BT006884 mRNA. Translation: AAP35530.1.
CR456777 mRNA. Translation: CAG33058.1.
AC145207 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89697.1.
BC005851 mRNA. Translation: AAH05851.1.
BC005875 mRNA. Translation: AAH05875.1.
BC008701 mRNA. Translation: AAH08701.1.
BC009759 mRNA. Translation: AAH09759.1.
BC016031 mRNA. Translation: AAH16031.1.
BC016185 mRNA. Translation: AAH16185.1.
BC024258 mRNA. Translation: AAH24258.1.
BC027730 mRNA. Translation: AAH27730.1.
BC075827 mRNA. Translation: AAH75827.1.
BC106044 mRNA. Translation: AAI06045.1.
CCDSCCDS11788.1. [P52565-1]
CCDS58609.1. [P52565-2]
PIRI38156.
RefSeqNP_001172006.1. NM_001185077.1. [P52565-1]
NP_001172007.1. NM_001185078.1. [P52565-2]
NP_004300.1. NM_004309.4. [P52565-1]
UniGeneHs.159161.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CC0X-ray5.00E/F1-204[»]
1FSOX-ray2.00A67-204[»]
1FSTX-ray2.70A/B24-204[»]
1FT0X-ray2.60A/B67-204[»]
1FT3X-ray2.80A/B67-204[»]
1HH4X-ray2.70D/E1-204[»]
1KMTX-ray1.30A/B67-204[»]
1QVYX-ray1.60A/B/C/D67-204[»]
1RHOX-ray2.50A/B/C59-203[»]
2BXWX-ray2.40A/B67-204[»]
2JHSX-ray1.95A67-202[»]
2JHTX-ray1.88A/B/C/D67-202[»]
2JHUX-ray1.65A/B67-202[»]
2JHVX-ray2.07A/B/C/D/E/F67-202[»]
2JHWX-ray2.50A/B67-202[»]
2JHXX-ray1.60A/B67-202[»]
2JHYX-ray1.90A67-202[»]
2JHZX-ray2.20A/B67-202[»]
2JI0X-ray2.10A67-202[»]
ProteinModelPortalP52565.
SMRP52565. Positions 23-202.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106889. 62 interactions.
IntActP52565. 32 interactions.
MINTMINT-93856.
STRING9606.ENSP00000269321.

PTM databases

PhosphoSiteP52565.

Polymorphism databases

DMDM1707892.

2D gel databases

DOSAC-COBS-2DPAGEP52565.
OGPP52565.
REPRODUCTION-2DPAGEIPI00003815.

Proteomic databases

MaxQBP52565.
PaxDbP52565.
PRIDEP52565.

Protocols and materials databases

DNASU396.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000269321; ENSP00000269321; ENSG00000141522. [P52565-1]
ENST00000400721; ENSP00000383556; ENSG00000141522. [P52565-2]
ENST00000541078; ENSP00000441348; ENSG00000141522. [P52565-1]
ENST00000580685; ENSP00000464205; ENSG00000141522. [P52565-1]
GeneID396.
KEGGhsa:396.
UCSCuc002kbq.3. human. [P52565-1]

Organism-specific databases

CTD396.
GeneCardsGC17M079825.
HGNCHGNC:678. ARHGDIA.
HPACAB010005.
HPA021407.
MIM601925. gene.
615244. phenotype.
neXtProtNX_P52565.
Orphanet93217. Familial idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial sclerosis.
PharmGKBPA24963.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG289931.
HOGENOMHOG000175765.
HOVERGENHBG000206.
InParanoidP52565.
KOK12462.
OMAEGVEYQI.
OrthoDBEOG72JWH9.
PhylomeDBP52565.
TreeFamTF105387.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressP52565.
BgeeP52565.
CleanExHS_ARHGDIA.
GenevestigatorP52565.

Family and domain databases

Gene3D2.70.50.30. 1 hit.
InterProIPR014756. Ig_E-set.
IPR000406. Rho_GDI.
IPR024792. RhoGDI_domain.
[Graphical view]
PANTHERPTHR10980. PTHR10980. 1 hit.
PfamPF02115. Rho_GDI. 1 hit.
[Graphical view]
PRINTSPR00492. RHOGDI.
SUPFAMSSF81296. SSF81296. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP52565.
GeneWikiARHGDIA.
GenomeRNAi396.
NextBio1661.
PROP52565.
SOURCESearch...

Entry information

Entry nameGDIR1_HUMAN
AccessionPrimary (citable) accession number: P52565
Secondary accession number(s): A8MXW0 expand/collapse secondary AC list , B2R5X1, B4DDD3, B4DUV9, Q6IBM5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 145 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM