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Protein

Rho GDP-dissociation inhibitor 2

Gene

ARHGDIB

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

Functioni

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.

GO - Molecular functioni

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

GO - Biological processi

  1. actin cytoskeleton organization Source: ProtInc
  2. immune response Source: ProtInc
  3. movement of cell or subcellular component Source: UniProtKB
  4. multicellular organismal development Source: ProtInc
  5. negative regulation of cell adhesion Source: ProtInc
  6. regulation of catalytic activity Source: GOC
  7. regulation of small GTPase mediated signal transduction Source: Reactome
  8. Rho protein signal transduction Source: ProtInc
  9. small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GDP-dissociation inhibitor 2
Short name:
Rho GDI 2
Alternative name(s):
Ly-GDI
Rho-GDI beta
Gene namesi
Name:ARHGDIB
Synonyms:GDIA2, GDID4, RAP1GN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:679. ARHGDIB.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic membrane-bounded vesicle Source: ProtInc
  3. cytoskeleton Source: UniProtKB
  4. cytosol Source: Reactome
  5. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24964.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 201200Rho GDP-dissociation inhibitor 2PRO_0000219016Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication
Modified residuei21 – 211N6-acetyllysine1 Publication
Modified residuei24 – 241Phosphotyrosine1 Publication
Modified residuei25 – 251N6-acetyllysine1 Publication
Modified residuei40 – 401N6-acetyllysine1 Publication
Modified residuei47 – 471N6-acetyllysine1 Publication
Modified residuei102 – 1021N6-acetyllysine1 Publication
Modified residuei124 – 1241N6-acetyllysine1 Publication
Modified residuei145 – 1451Phosphoserine1 Publication
Modified residuei175 – 1751N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP52566.
PaxDbiP52566.
PRIDEiP52566.

2D gel databases

OGPiP52566.
SWISS-2DPAGEP52566.

PTM databases

PhosphoSiteiP52566.

Miscellaneous databases

PMAP-CutDBP52566.

Expressioni

Gene expression databases

BgeeiP52566.
CleanExiHS_ARHGDIB.
ExpressionAtlasiP52566. baseline and differential.
GenevestigatoriP52566.

Organism-specific databases

HPAiCAB018584.
HPA051235.

Interactioni

Subunit structurei

Interacts with RHOA.1 Publication

Protein-protein interaction databases

BioGridi106890. 13 interactions.
DIPiDIP-40959N.
IntActiP52566. 8 interactions.
MINTiMINT-1616342.
STRINGi9606.ENSP00000228945.

Structurei

Secondary structure

1
201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 376Combined sources
Turni38 – 414Combined sources
Helixi43 – 5210Combined sources
Beta strandi62 – 643Combined sources
Beta strandi69 – 757Combined sources
Beta strandi84 – 863Combined sources
Helixi91 – 966Combined sources
Beta strandi98 – 1025Combined sources
Beta strandi106 – 1138Combined sources
Beta strandi120 – 13112Combined sources
Beta strandi134 – 14613Combined sources
Beta strandi153 – 1564Combined sources
Turni166 – 1683Combined sources
Beta strandi170 – 17910Combined sources
Beta strandi187 – 19812Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DS6X-ray2.35B23-199[»]
ProteinModelPortaliP52566.
SMRiP52566. Positions 23-199.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52566.

Family & Domainsi

Sequence similaritiesi

Belongs to the Rho GDI family.Curated

Phylogenomic databases

eggNOGiNOG253438.
GeneTreeiENSGT00390000006233.
HOGENOMiHOG000175765.
HOVERGENiHBG000206.
InParanoidiP52566.
KOiK12462.
OMAiVWKTAVK.
OrthoDBiEOG72JWH9.
PhylomeDBiP52566.
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.

Sequencei

Sequence statusi: Complete.

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

P52566-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEKAPEPHV EEDDDDELDS KLNYKPPPQK SLKELQEMDK DDESLIKYKK
60 70 80 90 100
TLLGDGPVVT DPKAPNVVVT RLTLVCESAP GPITMDLTGD LEALKKETIV
110 120 130 140 150
LKEGSEYRVK IHFKVNRDIV SGLKYVQHTY RTGVKVDKAT FMVGSYGPRP
160 170 180 190 200
EEYEFLTPVE EAPKGMLARG TYHNKSFFTD DDKQDHLSWE WNLSIKKEWT

E
Length:201
Mass (Da):22,988
Last modified:January 23, 2007 - v3
Checksum:iF1E840134F643E5F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1531Y → V AA sequence (PubMed:2226408).Curated
Sequence conflicti169 – 1702RG → QD in L07916 (PubMed:8434008).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS8671.1.
PIRiA47742.
RefSeqiNP_001166.3. NM_001175.5.
UniGeneiHs.504877.

Genome annotation databases

EnsembliENST00000228945; ENSP00000228945; ENSG00000111348.
ENST00000541546; ENSP00000440560; ENSG00000111348.
ENST00000541644; ENSP00000444860; ENSG00000111348.
GeneIDi397.
KEGGihsa:397.
UCSCiuc001rcq.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS8671.1.
PIRiA47742.
RefSeqiNP_001166.3. NM_001175.5.
UniGeneiHs.504877.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DS6X-ray2.35B23-199[»]
ProteinModelPortaliP52566.
SMRiP52566. Positions 23-199.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106890. 13 interactions.
DIPiDIP-40959N.
IntActiP52566. 8 interactions.
MINTiMINT-1616342.
STRINGi9606.ENSP00000228945.

PTM databases

PhosphoSiteiP52566.

2D gel databases

OGPiP52566.
SWISS-2DPAGEP52566.

Proteomic databases

MaxQBiP52566.
PaxDbiP52566.
PRIDEiP52566.

Protocols and materials databases

DNASUi397.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000228945; ENSP00000228945; ENSG00000111348.
ENST00000541546; ENSP00000440560; ENSG00000111348.
ENST00000541644; ENSP00000444860; ENSG00000111348.
GeneIDi397.
KEGGihsa:397.
UCSCiuc001rcq.1. human.

Organism-specific databases

CTDi397.
GeneCardsiGC12M015094.
H-InvDBHIX0036989.
HGNCiHGNC:679. ARHGDIB.
HPAiCAB018584.
HPA051235.
MIMi602843. gene.
neXtProtiNX_P52566.
PharmGKBiPA24964.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG253438.
GeneTreeiENSGT00390000006233.
HOGENOMiHOG000175765.
HOVERGENiHBG000206.
InParanoidiP52566.
KOiK12462.
OMAiVWKTAVK.
OrthoDBiEOG72JWH9.
PhylomeDBiP52566.
TreeFamiTF105387.

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.

Miscellaneous databases

ChiTaRSiARHGDIB. human.
EvolutionaryTraceiP52566.
GeneWikiiARHGDIB.
GenomeRNAii397.
NextBioi1665.
PMAP-CutDBP52566.
PROiP52566.
SOURCEiSearch...

Gene expression databases

BgeeiP52566.
CleanExiHS_ARHGDIB.
ExpressionAtlasiP52566. baseline and differential.
GenevestigatoriP52566.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1992) [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(1992) [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(1992) [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 (MAR-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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. 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(2003) [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 (APR-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(1989) [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(2004) [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(2008) [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(2008) [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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RHOA.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF COMPLEX WITH RAC2.

Entry informationi

Entry nameiGDIR2_HUMAN
AccessioniPrimary (citable) accession number: P52566
Secondary accession number(s): B5BU79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 143 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 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.