P52566 (GDIR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rho GDP-dissociation inhibitor 2
Short name=Rho GDI 2

Alternative name(s):
Ly-GDI
Rho-GDI beta

Gene names

Name:	ARHGDIB
Synonyms:	GDIA2, GDID4, RAP1GN1

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	201 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.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the Rho GDI family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	GTPase activation
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Rho protein signal transduction Traceable author statement Ref.1. Source: ProtInc actin cytoskeleton organization Traceable author statement Ref.2. Source: ProtInc cellular component movement Traceable author statement PubMed 16130169. Source: UniProtKB immune response Traceable author statement Ref.1. Source: ProtInc multicellular organismal development Traceable author statement Ref.3. Source: ProtInc negative regulation of cell adhesion Traceable author statement PubMed 9113980. Source: ProtInc positive regulation of GTPase activity Inferred from electronic annotation. Source: GOC regulation of small GTPase mediated signal transduction Traceable author statement. Source: Reactome
Cellular_component	cytoplasmic membrane-bounded vesicle Traceable author statement PubMed 9113980. Source: ProtInc cytoskeleton Traceable author statement PubMed 16130169. 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 Ref.2. 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.8

Chain

2 – 201

200

Rho GDP-dissociation inhibitor 2

PRO_0000219016

Amino acid modifications

Modified residue

2

1

N-acetylthreonine Ref.8

Modified residue

21

1

N6-acetyllysine Ref.12

Modified residue

24

1

Phosphotyrosine Ref.10

Modified residue

25

1

N6-acetyllysine Ref.12

Modified residue

40

1

N6-acetyllysine Ref.12

Modified residue

47

1

N6-acetyllysine Ref.12

Modified residue

102

1

N6-acetyllysine Ref.12

Modified residue

124

1

N6-acetyllysine Ref.12

Modified residue

145

1

Phosphoserine Ref.11

Modified residue

175

1

N6-acetyllysine Ref.12

Experimental info

Sequence conflict

153

1

Y → V AA sequence Ref.9

Sequence conflict

169 – 170

2

RG → QD in L07916. Ref.3

Secondary structure

1

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201

Helix Strand Turn

Details...

Helix

32 – 37

6

Turn

38 – 41

4

Helix

43 – 52

10

Beta strand

62 – 64

3

Beta strand

69 – 75

7

Beta strand

84 – 86

3

Helix

91 – 96

6

Beta strand

98 – 102

5

Beta strand

106 – 113

8

Beta strand

120 – 131

12

Beta strand

134 – 146

13

Beta strand

153 – 156

4

Turn

166 – 168

3

Beta strand

170 – 179

10

Beta strand

187 – 198

12

Sequences

	Sequence		Length	Mass (Da)
	P52566 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: F1E840134F643E5F	FASTA	201	22,988
	10 20 30 40 50 60 MTEKAPEPHV EEDDDDELDS KLNYKPPPQK SLKELQEMDK DDESLIKYKK TLLGDGPVVT 70 80 90 100 110 120 DPKAPNVVVT RLTLVCESAP GPITMDLTGD LEALKKETIV LKEGSEYRVK IHFKVNRDIV 130 140 150 160 170 180 SGLKYVQHTY RTGVKVDKAT FMVGSYGPRP EEYEFLTPVE EAPKGMLARG TYHNKSFFTD 190 200 DDKQDHLSWE WNLSIKKEWT E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Ly-GDI, a GDP-dissociation inhibitor of the RhoA GTP-binding protein, is expressed preferentially in lymphocytes." Scherle P., Behrens T., Staudt L.M. Proc. Natl. Acad. Sci. U.S.A. 90:7568-7572(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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].
[3]	"cDNA cloning of a human mRNA preferentially expressed in hematopoietic cells and with homology to a GDP-dissociation inhibitor for the rho GTP-binding proteins." Lelias J.M., Adra C.N., Wulf G.M., Guillemot J.-C., Caput D., Lim B. Proc. Natl. Acad. Sci. U.S.A. 90:1479-1483(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"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.
[5]	"Human protein factory for converting the transcriptome into an in vitro-expressed proteome." Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N. Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	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].
[7]	"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: Lymph.
[8]	Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M. Submitted (MAY-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-20; 33-46 AND 50-62, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, MASS SPECTROMETRY. Tissue: T-cell.
[9]	"Sequence analysis of proteins separated by polyacrylamide gel electrophoresis: towards an integrated protein database." Aebersold R., Leavitt J. Electrophoresis 11:517-527(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 10-19; 21-25; 51-58; 142-148 AND 150-156.
[10]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24, MASS SPECTROMETRY.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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-21; LYS-25; LYS-40; LYS-47; LYS-102; LYS-124 AND LYS-175, MASS SPECTROMETRY.
[13]	"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].
[14]	"The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI." Scheffzek K., Stephan I., Jensen O.N., Illenberger D., Gierschik P. Nat. Struct. Biol. 7:122-126(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF COMPLEX WITH RAC2.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L20688 mRNA. Translation: AAA59539.1.
X69549 mRNA. Translation: CAA49280.1.
L07916 mRNA. No translation available.
AF498927 mRNA. Translation: AAM21075.1.
AB451315 mRNA. Translation: BAG70129.1.
AB451445 mRNA. Translation: BAG70259.1.
CH471094 Genomic DNA. Translation: EAW96336.1.
BC009200 mRNA. Translation: AAH09200.1.

IPI

IPI00003817.

PIR

A47742.

RefSeq

NP_001166.3. NM_001175.4.

UniGene

Hs.504877.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DS6	X-ray	2.35	B	23-199	[»]

ProteinModelPortal

P52566.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-40959N.

IntAct

P52566. 5 interactions.

MINT

MINT-1616342.

STRING

9606.ENSP00000228945.

PTM databases

PhosphoSite

P52566.

Polymorphism databases

DMDM

1707893.

2D gel databases

OGP

P52566.

SWISS-2DPAGE

P52566.

Proteomic databases

PaxDb

P52566.

PRIDE

P52566.

Protocols and materials databases

DNASU

397.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000228945; ENSP00000228945; ENSG00000111348.
ENST00000541546; ENSP00000440560; ENSG00000111348.
ENST00000541644; ENSP00000444860; ENSG00000111348.

GeneID

397.

KEGG

hsa:397.

UCSC

uc001rcq.1. human.

Organism-specific databases

CTD

397.

GeneCards

GC12M015094.

H-InvDB

HIX0036989.

HGNC

HGNC:679. ARHGDIB.

HPA

CAB018584.

MIM

602843. gene.

neXtProt

NX_P52566.

PharmGKB

PA24964.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG253438.

HOGENOM

HOG000175765.

HOVERGEN

HBG000206.

InParanoid

P52566.

KO

K12462.

OMA

LSIKKDW.

OrthoDB

EOG4Q58QJ.

PhylomeDB

P52566.

Enzyme and pathway databases

Pathway_Interaction_DB

caspase_pathway. Caspase cascade in apoptosis.
faspathway. FAS signaling pathway (CD95).

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

P52566.

Bgee

P52566.

CleanEx

HS_ARHGDIB.

Genevestigator

P52566.

GermOnline

ENSG00000111348. Homo sapiens.

Family and domain databases

Gene3D

2.70.50.30. 1 hit.

InterPro

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

PANTHER

PTHR10980. PTHR10980. 1 hit.

Pfam

PF02115. Rho_GDI. 1 hit.
[Graphical view]

PRINTS

PR00492. RHOGDI.

SUPFAM

SSF81296. Ig_E-set. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P52566.

GenomeRNAi

397.

NextBio

1665.

PMAP-CutDB

P52566.

SOURCE

Search...

Entry information

Entry name

GDIR2_HUMAN

Accession

Primary (citable) accession number: P52566
Secondary accession number(s): B5BU79

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 127 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.