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P52565

- GDIR1_HUMAN

UniProt

P52565 - GDIR1_HUMAN

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Protein

Rho GDP-dissociation inhibitor 1

Gene

ARHGDIA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 RAC1.2 Publications

GO - Molecular functioni

  1. GTPase activator activity Source: UniProtKB-KW
  2. Rho GDP-dissociation inhibitor activity Source: ProtInc

GO - Biological processi

  1. cellular component movement Source: UniProtKB
  2. negative regulation of apoptotic process Source: UniProtKB
  3. negative regulation of axonogenesis Source: Reactome
  4. negative regulation of cell adhesion Source: ProtInc
  5. neurotrophin TRK receptor signaling pathway Source: Reactome
  6. positive regulation of axonogenesis Source: Reactome
  7. regulation of axonogenesis Source: Reactome
  8. regulation of protein localization Source: Ensembl
  9. regulation of small GTPase mediated signal transduction Source: Reactome
  10. Rho protein signal transduction Source: ProtInc
  11. semaphorin-plexin signaling pathway Source: UniProtKB
  12. small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_13779. Axonal growth stimulation.
REACT_13815. Axonal growth inhibition (RHOA activation).

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GDP-dissociation inhibitor 1
Short name:
Rho GDI 1
Alternative name(s):
Rho-GDI alpha
Gene namesi
Name:ARHGDIA
Synonyms:GDIA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:678. ARHGDIA.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoskeleton Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. immunological synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti185 – 1851Missing in NPHS8; produces mislocalization into the nucleus, hyperactivation of Rho-GTPases RHOA, RAC1 and CDC42 and impaired cell motility. 1 Publication
VAR_069814

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi45 – 451D → A: Loss of RHOA interaction; when associated with A-185. 1 Publication
Mutagenesisi185 – 1851D → A: Loss of RHOA interaction; when associated with A-45. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615244. phenotype.
Orphaneti93217. Familial idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial sclerosis.
PharmGKBiPA24963.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 204203Rho GDP-dissociation inhibitor 1PRO_0000219013Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei34 – 341PhosphoserineBy similarity
Modified residuei43 – 431N6-acetyllysineBy similarity
Modified residuei105 – 1051N6-acetyllysine1 Publication
Modified residuei127 – 1271N6-acetyllysine1 Publication
Modified residuei141 – 1411N6-acetyllysine; alternate2 Publications
Modified residuei141 – 1411N6-succinyllysine; alternateBy similarity
Modified residuei178 – 1781N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP52565.
PaxDbiP52565.
PRIDEiP52565.

2D gel databases

DOSAC-COBS-2DPAGEP52565.
OGPiP52565.
REPRODUCTION-2DPAGEIPI00003815.

PTM databases

PhosphoSiteiP52565.

Expressioni

Gene expression databases

BgeeiP52565.
CleanExiHS_ARHGDIA.
ExpressionAtlasiP52565. baseline and differential.
GenevestigatoriP52565.

Organism-specific databases

HPAiCAB010005.
HPA021407.

Interactioni

Subunit structurei

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.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RAC1P630006EBI-712693,EBI-413628
RHOAP615862EBI-712693,EBI-446668

Protein-protein interaction databases

BioGridi106889. 65 interactions.
IntActiP52565. 32 interactions.
MINTiMINT-93856.
STRINGi9606.ENSP00000269321.

Structurei

Secondary structure

1
204
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 395Combined sources
Helixi46 – 5611Combined sources
Beta strandi69 – 7810Combined sources
Beta strandi82 – 843Combined sources
Beta strandi87 – 893Combined sources
Helixi94 – 996Combined sources
Beta strandi102 – 1054Combined sources
Beta strandi109 – 11810Combined sources
Beta strandi123 – 13412Combined sources
Beta strandi137 – 14913Combined sources
Beta strandi156 – 1594Combined sources
Turni169 – 1713Combined sources
Beta strandi173 – 18210Combined sources
Beta strandi189 – 20012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP52565.
SMRiP52565. Positions 23-202.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52565.

Family & Domainsi

Sequence similaritiesi

Belongs to the Rho GDI family.Curated

Phylogenomic databases

eggNOGiNOG289931.
GeneTreeiENSGT00390000006233.
HOGENOMiHOG000175765.
HOVERGENiHBG000206.
InParanoidiP52565.
KOiK12462.
OMAiEGVEYQI.
OrthoDBiEOG72JWH9.
PhylomeDBiP52565.
TreeFamiTF105387.

Family and domain databases

Gene3Di2.70.50.30. 1 hit.
InterProiIPR014756. Ig_E-set.
IPR000406. Rho_GDI.
IPR024792. RhoGDI_domain.
[Graphical view]
PANTHERiPTHR10980. PTHR10980. 1 hit.
PfamiPF02115. Rho_GDI. 1 hit.
[Graphical view]
PRINTSiPR00492. RHOGDI.
SUPFAMiSSF81296. SSF81296. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P52565-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAEQEPTAEQ LAQIAAENEE DEHSVNYKPP AQKSIQEIQE LDKDDESLRK
60 70 80 90 100
YKEALLGRVA VSADPNVPNV VVTGLTLVCS SAPGPLELDL TGDLESFKKQ
110 120 130 140 150
SFVLKEGVEY RIKISFRVNR EIVSGMKYIQ HTYRKGVKID KTDYMVGSYG
160 170 180 190 200
PRAEEYEFLT PVEEAPKGML ARGSYSIKSR FTDDDKTDHL SWEWNLTIKK

DWKD
Length:204
Mass (Da):23,207
Last modified:January 23, 2007 - v3
Checksum:i59CB6F42E3B3BCCA
GO
Isoform 2 (identifier: P52565-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:160
Mass (Da):18,233
Checksum:i0E14B24C9B7AFCA2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1391I → V in CAA45344. 1 PublicationCurated
Sequence conflicti139 – 1391I → V in BAG35268. (PubMed:14702039)Curated
Sequence conflicti188 – 1881D → R AA sequence 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti185 – 1851Missing in NPHS8; produces mislocalization into the nucleus, hyperactivation of Rho-GTPases RHOA, RAC1 and CDC42 and impaired cell motility. 1 Publication
VAR_069814

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei139 – 18345IDKTD…SRFTD → N in isoform 2. 1 PublicationVSP_046699Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11788.1. [P52565-1]
CCDS58609.1. [P52565-2]
PIRiI38156.
RefSeqiNP_001172006.1. NM_001185077.2. [P52565-1]
NP_001172007.1. NM_001185078.2. [P52565-2]
NP_001288169.1. NM_001301240.1.
NP_001288170.1. NM_001301241.1.
NP_001288171.1. NM_001301242.1.
NP_001288172.1. NM_001301243.1.
NP_004300.1. NM_004309.5. [P52565-1]
UniGeneiHs.159161.
Hs.599508.
Hs.728006.

Genome annotation databases

EnsembliENST00000269321; ENSP00000269321; ENSG00000141522. [P52565-1]
ENST00000400721; ENSP00000383556; ENSG00000141522. [P52565-2]
ENST00000541078; ENSP00000441348; ENSG00000141522. [P52565-1]
ENST00000580685; ENSP00000464205; ENSG00000141522. [P52565-1]
GeneIDi396.
KEGGihsa:396.
UCSCiuc002kbq.3. human. [P52565-1]
uc021ufg.1. human.

Polymorphism databases

DMDMi1707892.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS11788.1. [P52565-1 ]
CCDS58609.1. [P52565-2 ]
PIRi I38156.
RefSeqi NP_001172006.1. NM_001185077.2. [P52565-1 ]
NP_001172007.1. NM_001185078.2. [P52565-2 ]
NP_001288169.1. NM_001301240.1.
NP_001288170.1. NM_001301241.1.
NP_001288171.1. NM_001301242.1.
NP_001288172.1. NM_001301243.1.
NP_004300.1. NM_004309.5. [P52565-1 ]
UniGenei Hs.159161.
Hs.599508.
Hs.728006.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CC0 X-ray 5.00 E/F 1-204 [» ]
1FSO X-ray 2.00 A 67-204 [» ]
1FST X-ray 2.70 A/B 24-204 [» ]
1FT0 X-ray 2.60 A/B 67-204 [» ]
1FT3 X-ray 2.80 A/B 67-204 [» ]
1HH4 X-ray 2.70 D/E 1-204 [» ]
1KMT X-ray 1.30 A/B 67-204 [» ]
1QVY X-ray 1.60 A/B/C/D 67-204 [» ]
1RHO X-ray 2.50 A/B/C 59-203 [» ]
2BXW X-ray 2.40 A/B 67-204 [» ]
2JHS X-ray 1.95 A 67-202 [» ]
2JHT X-ray 1.88 A/B/C/D 67-202 [» ]
2JHU X-ray 1.65 A/B 67-202 [» ]
2JHV X-ray 2.07 A/B/C/D/E/F 67-202 [» ]
2JHW X-ray 2.50 A/B 67-202 [» ]
2JHX X-ray 1.60 A/B 67-202 [» ]
2JHY X-ray 1.90 A 67-202 [» ]
2JHZ X-ray 2.20 A/B 67-202 [» ]
2JI0 X-ray 2.10 A 67-202 [» ]
ProteinModelPortali P52565.
SMRi P52565. Positions 23-202.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106889. 65 interactions.
IntActi P52565. 32 interactions.
MINTi MINT-93856.
STRINGi 9606.ENSP00000269321.

Chemistry

BindingDBi P52565.

PTM databases

PhosphoSitei P52565.

Polymorphism databases

DMDMi 1707892.

2D gel databases

DOSAC-COBS-2DPAGE P52565.
OGPi P52565.
REPRODUCTION-2DPAGE IPI00003815.

Proteomic databases

MaxQBi P52565.
PaxDbi P52565.
PRIDEi P52565.

Protocols and materials databases

DNASUi 396.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000269321 ; ENSP00000269321 ; ENSG00000141522 . [P52565-1 ]
ENST00000400721 ; ENSP00000383556 ; ENSG00000141522 . [P52565-2 ]
ENST00000541078 ; ENSP00000441348 ; ENSG00000141522 . [P52565-1 ]
ENST00000580685 ; ENSP00000464205 ; ENSG00000141522 . [P52565-1 ]
GeneIDi 396.
KEGGi hsa:396.
UCSCi uc002kbq.3. human. [P52565-1 ]
uc021ufg.1. human.

Organism-specific databases

CTDi 396.
GeneCardsi GC17M079825.
HGNCi HGNC:678. ARHGDIA.
HPAi CAB010005.
HPA021407.
MIMi 601925. gene.
615244. phenotype.
neXtProti NX_P52565.
Orphaneti 93217. Familial idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial sclerosis.
PharmGKBi PA24963.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG289931.
GeneTreei ENSGT00390000006233.
HOGENOMi HOG000175765.
HOVERGENi HBG000206.
InParanoidi P52565.
KOi K12462.
OMAi EGVEYQI.
OrthoDBi EOG72JWH9.
PhylomeDBi P52565.
TreeFami TF105387.

Enzyme and pathway databases

Reactomei REACT_11051. Rho GTPase cycle.
REACT_13779. Axonal growth stimulation.
REACT_13815. Axonal growth inhibition (RHOA activation).

Miscellaneous databases

EvolutionaryTracei P52565.
GeneWikii ARHGDIA.
GenomeRNAii 396.
NextBioi 1661.
PROi P52565.
SOURCEi Search...

Gene expression databases

Bgeei P52565.
CleanExi HS_ARHGDIA.
ExpressionAtlasi P52565. baseline and differential.
Genevestigatori P52565.

Family and domain databases

Gene3Di 2.70.50.30. 1 hit.
InterProi IPR014756. Ig_E-set.
IPR000406. Rho_GDI.
IPR024792. RhoGDI_domain.
[Graphical view ]
PANTHERi PTHR10980. PTHR10980. 1 hit.
Pfami PF02115. Rho_GDI. 1 hit.
[Graphical view ]
PRINTSi PR00492. RHOGDI.
SUPFAMi SSF81296. SSF81296. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. Cited for: VARIANT NPHS8 ASP-185 DEL, CHARACTERIZATION OF VARIANT NPHS8 ASP-185 DEL, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAC1; RHOA AND CDC42.

Entry informationi

Entry nameiGDIR1_HUMAN
AccessioniPrimary (citable) accession number: P52565
Secondary accession number(s): A8MXW0
, B2R5X1, B4DDD3, B4DUV9, Q6IBM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3