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P52566 (GDIR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Subunit structure

Interacts with RHOA. Ref.13

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the Rho GDI family.

Ontologies

Keywords
   Cellular componentCytoplasm
   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

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

regulation of catalytic activity

Traceable author statement Ref.2. Source: GOC

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Traceable author statement PubMed 16130169. Source: UniProtKB

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

extracellular vesicular exosome

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

   Molecular_functionGTPase 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 201200Rho GDP-dissociation inhibitor 2
PRO_0000219016

Amino acid modifications

Modified residue21N-acetylthreonine Ref.8
Modified residue211N6-acetyllysine Ref.12
Modified residue241Phosphotyrosine Ref.10
Modified residue251N6-acetyllysine Ref.12
Modified residue401N6-acetyllysine Ref.12
Modified residue471N6-acetyllysine Ref.12
Modified residue1021N6-acetyllysine Ref.12
Modified residue1241N6-acetyllysine Ref.12
Modified residue1451Phosphoserine Ref.11
Modified residue1751N6-acetyllysine Ref.12

Experimental info

Sequence conflict1531Y → V AA sequence Ref.9
Sequence conflict169 – 1702RG → QD in L07916. Ref.3

Secondary structure

.............................. 201
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52566 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F1E840134F643E5F

FASTA20122,988
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. 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].
[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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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: INTERACTION WITH RHOA.
[14]"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].
[15]"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.
CCDSCCDS8671.1.
PIRA47742.
RefSeqNP_001166.3. NM_001175.5.
UniGeneHs.504877.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DS6X-ray2.35B23-199[»]
ProteinModelPortalP52566.
SMRP52566. Positions 23-199.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106890. 13 interactions.
DIPDIP-40959N.
IntActP52566. 8 interactions.
MINTMINT-1616342.
STRING9606.ENSP00000228945.

PTM databases

PhosphoSiteP52566.

2D gel databases

OGPP52566.
SWISS-2DPAGEP52566.

Proteomic databases

MaxQBP52566.
PaxDbP52566.
PRIDEP52566.

Protocols and materials databases

DNASU397.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000228945; ENSP00000228945; ENSG00000111348.
ENST00000541546; ENSP00000440560; ENSG00000111348.
ENST00000541644; ENSP00000444860; ENSG00000111348.
GeneID397.
KEGGhsa:397.
UCSCuc001rcq.1. human.

Organism-specific databases

CTD397.
GeneCardsGC12M015094.
H-InvDBHIX0036989.
HGNCHGNC:679. ARHGDIB.
HPACAB018584.
HPA051235.
MIM602843. gene.
neXtProtNX_P52566.
PharmGKBPA24964.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG253438.
HOGENOMHOG000175765.
HOVERGENHBG000206.
InParanoidP52566.
KOK12462.
OMAEIKKDWA.
OrthoDBEOG72JWH9.
PhylomeDBP52566.
TreeFamTF105387.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressP52566.
BgeeP52566.
CleanExHS_ARHGDIB.
GenevestigatorP52566.

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

EvolutionaryTraceP52566.
GeneWikiARHGDIB.
GenomeRNAi397.
NextBio1665.
PMAP-CutDBP52566.
PROP52566.
SOURCESearch...

Entry information

Entry nameGDIR2_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 137 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 chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM