P52565 (GDIR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rho GDP-dissociation inhibitor 1
Short name=Rho GDI 1

Alternative name(s):
Rho-GDI alpha

Gene names

Name:	ARHGDIA
Synonyms:	GDIA1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	204 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the Rho GDI family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	GTPase activation
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	Rho protein signal transduction Traceable author statement. Source: ProtInc anti-apoptosis Traceable author statement. Source: UniProtKB cellular component movement Traceable author statement. Source: UniProtKB negative regulation of axonogenesis Traceable author statement. Source: Reactome negative regulation of cell adhesion Traceable author statement. Source: ProtInc nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome positive regulation of axonogenesis Traceable author statement. Source: Reactome regulation of small GTPase mediated signal transduction Traceable author statement. Source: Reactome
Cellular component	cytoskeleton Traceable author statement. Source: UniProtKB cytosol Traceable author statement. Source: Reactome
Molecular function	GTPase activator activity Inferred from electronic annotation. Source: UniProtKB-KW Rho GDP-dissociation inhibitor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.11

Chain

2 – 204

203

Rho GDP-dissociation inhibitor 1

PRO_0000219013

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.11 Ref.15

Modified residue

105

1

N6-acetyllysine Ref.16

Modified residue

127

1

N6-acetyllysine Ref.16

Modified residue

141

1

N6-acetyllysine Ref.14 Ref.16

Modified residue

178

1

N6-acetyllysine Ref.16

Experimental info

Sequence conflict

139

1

I → V in CAA45344. Ref.3

Sequence conflict

139

1

I → V in BAG35268. Ref.5

Sequence conflict

188

1

D → R AA sequence Ref.13

Secondary structure

1

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204

Helix Strand Turn

Details...

Helix

35 – 39

5

Beta strand

69 – 78

10

Beta strand

82 – 84

3

Beta strand

87 – 89

3

Helix

94 – 99

6

Beta strand

102 – 105

4

Beta strand

109 – 118

10

Beta strand

123 – 134

12

Beta strand

137 – 149

13

Beta strand

156 – 159

4

Turn

169 – 171

3

Beta strand

173 – 182

10

Beta strand

189 – 200

12

Sequences

	Sequence		Length	Mass (Da)
	P52565 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 59CB6F42E3B3BCCA	FASTA	204	23,207
	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

References

	« Hide 'large scale' referencesShow '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: 8262133] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
[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].
[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].
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex.
[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]. 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].
[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].
[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 (JUL-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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon, Lung, Muscle, Skin, Tonsil and Uterus.
[11]	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, MASS SPECTROMETRY. Tissue: T-cell.
[12]	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, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[13]	"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: 8504089] [Abstract] Cited for: PROTEIN SEQUENCE OF 34-37; 136-142 AND 181-199. Tissue: Neutrophil.
[14]	"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: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-141, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105; LYS-127; LYS-141 AND LYS-178, MASS SPECTROMETRY.
[17]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"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: 9195882] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 59-204.
+	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.
AK312347 mRNA. Translation: BAG35268.1.
AF498926 mRNA. Translation: AAM21074.1.
BT006884 mRNA. Translation: AAP35530.1.
CR456777 mRNA. Translation: CAG33058.1.
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.

IPI

IPI00003815.

PIR

I38156.

RefSeq

NP_001172006.1. NM_001185077.1.
NP_001172007.1. NM_001185078.1.
NP_004300.1. NM_004309.4.

UniGene

Hs.159161.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P52565.

SMR

P52565. Positions 23-202.

ModBase

Search...

Protein-protein interaction databases

IntAct

P52565. 17 interactions.

MINT

MINT-93856.

STRING

P52565.

PTM databases

PhosphoSite

P52565.

Polymorphism databases

DMDM

1707892.

2D gel databases

Aarhus/Ghent-2DPAGE

8118. IEF.

Cornea-2DPAGE

P52565.

DOSAC-COBS-2DPAGE

P52565.

OGP

P52565.

REPRODUCTION-2DPAGE

IPI00003815.

Proteomic databases

PRIDE

P52565.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000269321; ENSP00000269321; ENSG00000141522.

GeneID

396.

KEGG

hsa:396.

UCSC

uc002kbp.1. human.

Organism-specific databases

CTD

396.

GeneCards

GC17M079825.

H-InvDB

HIX0014259.

HGNC

HGNC:678. ARHGDIA.

HPA

CAB004561.
CAB010005.
HPA021407.

MIM

601925. gene.

neXtProt

NX_P52565.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00390000006233.

HOVERGEN

HBG000206.

InParanoid

P52565.

OMA

RIKISFK.

OrthoDB

EOG4Q58QJ.

PhylomeDB

P52565.

Enzyme and pathway databases

Pathway_Interaction_DB

p75ntrpathway. p75(NTR)-mediated signaling.

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

P52565.

Bgee

P52565.

CleanEx

HS_ARHGDIA.

Genevestigator

P52565.

GermOnline

ENSG00000141522. Homo sapiens.

Family and domain databases

InterPro

IPR014756. Ig_E-set.
IPR000406. Rho_GDI.
IPR024792. RhoGDI_domain.
[Graphical view]

Gene3D

G3DSA:2.70.50.30. Rho_GDI. 1 hit.

KO

K12462.

PANTHER

PTHR10980. Rho_GDI. 1 hit.

Pfam

PF02115. Rho_GDI. 1 hit.
[Graphical view]

PRINTS

PR00492. RHOGDI.

SUPFAM

SSF81296. Ig_E-set. 1 hit.

ProtoNet

Search...

Other

NextBio

1661.

SOURCE

Search...

Entry information

Entry name

GDIR1_HUMAN

Accession

Primary (citable) accession number: P52565
Secondary accession number(s): B2R5X1, Q6IBM5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 118 of the entry and version 3 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.