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Protein

Rho GDP-dissociation inhibitor 2

Gene

Arhgdib

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiREACT_297947. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GDP-dissociation inhibitor 2
Short name:
Rho GDI 2
Alternative name(s):
D4
Rho-GDI beta
Gene namesi
Name:Arhgdib
Synonyms:Gdid4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:101940. Arhgdib.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 200199Rho GDP-dissociation inhibitor 2PRO_0000219017Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Modified residuei20 – 201N6-acetyllysineBy similarity
Modified residuei23 – 231PhosphotyrosineBy similarity
Modified residuei24 – 241N6-acetyllysineBy similarity
Modified residuei39 – 391N6-acetyllysineBy similarity
Modified residuei46 – 461N6-acetyllysineBy similarity
Modified residuei101 – 1011N6-acetyllysineBy similarity
Modified residuei123 – 1231N6-acetyllysineBy similarity
Modified residuei144 – 1441PhosphoserineBy similarity
Modified residuei174 – 1741N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ61599.
PaxDbiQ61599.
PRIDEiQ61599.

2D gel databases

COMPLUYEAST-2DPAGEQ61599.

PTM databases

PhosphoSiteiQ61599.

Expressioni

Tissue specificityi

Preferentially expressed in hematopoietic cells.

Gene expression databases

BgeeiQ61599.
CleanExiMM_ARHGDIB.
ExpressionAtlasiQ61599. baseline and differential.
GenevisibleiQ61599. MM.

Interactioni

Subunit structurei

Interacts with RHOA.By similarity

Protein-protein interaction databases

BioGridi198201. 7 interactions.
IntActiQ61599. 3 interactions.
MINTiMINT-1613948.
STRINGi10090.ENSMUSP00000032344.

Structurei

3D structure databases

ProteinModelPortaliQ61599.
SMRiQ61599. Positions 22-198.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Rho GDI family.Curated

Phylogenomic databases

eggNOGiNOG253438.
GeneTreeiENSGT00390000006233.
HOGENOMiHOG000175765.
HOVERGENiHBG000206.
InParanoidiQ61599.
KOiK12462.
OMAiAPEPHLE.
OrthoDBiEOG72JWH9.
PhylomeDBiQ61599.
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.

Q61599-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEKDAQPQL EEADDDLDSK LNYKPPPQKS LKELQEMDKD DESLTKYKKT
60 70 80 90 100
LLGDVPVVAD PTVPNVTVTR LSLVCDSAPG PITMDLTGDL EALKKDTFVL
110 120 130 140 150
KEGIEYRVKI NFKVNKDIVS GLKYVQHTYR TGMRVDKATF MVGSYGPRPE
160 170 180 190 200
EYEFLTPVEE APKGMLARGT YHNKSFFTDD DKQDHLTWEW NLAIKKDWTE
Length:200
Mass (Da):22,851
Last modified:January 23, 2007 - v3
Checksum:iEA78C965F1AB6F5C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07918 mRNA. Translation: AAA61613.1.
AK002516 mRNA. Translation: BAB22155.1.
AK169733 mRNA. Translation: BAE41335.1.
BC031763 mRNA. Translation: AAH31763.1.
CCDSiCCDS20661.1.
PIRiI49687.
RefSeqiNP_001288230.1. NM_001301301.1.
NP_001288232.1. NM_001301303.1.
NP_001288234.1. NM_001301305.1.
NP_001288237.1. NM_001301308.1.
NP_001288238.1. NM_001301309.1.
NP_031512.1. NM_007486.5.
XP_006505467.1. XM_006505404.2.
UniGeneiMm.2241.

Genome annotation databases

EnsembliENSMUST00000032344; ENSMUSP00000032344; ENSMUSG00000030220.
ENSMUST00000111891; ENSMUSP00000107522; ENSMUSG00000030220.
ENSMUST00000111892; ENSMUSP00000107523; ENSMUSG00000030220.
GeneIDi11857.
KEGGimmu:11857.
UCSCiuc009emo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07918 mRNA. Translation: AAA61613.1.
AK002516 mRNA. Translation: BAB22155.1.
AK169733 mRNA. Translation: BAE41335.1.
BC031763 mRNA. Translation: AAH31763.1.
CCDSiCCDS20661.1.
PIRiI49687.
RefSeqiNP_001288230.1. NM_001301301.1.
NP_001288232.1. NM_001301303.1.
NP_001288234.1. NM_001301305.1.
NP_001288237.1. NM_001301308.1.
NP_001288238.1. NM_001301309.1.
NP_031512.1. NM_007486.5.
XP_006505467.1. XM_006505404.2.
UniGeneiMm.2241.

3D structure databases

ProteinModelPortaliQ61599.
SMRiQ61599. Positions 22-198.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198201. 7 interactions.
IntActiQ61599. 3 interactions.
MINTiMINT-1613948.
STRINGi10090.ENSMUSP00000032344.

PTM databases

PhosphoSiteiQ61599.

2D gel databases

COMPLUYEAST-2DPAGEQ61599.

Proteomic databases

MaxQBiQ61599.
PaxDbiQ61599.
PRIDEiQ61599.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032344; ENSMUSP00000032344; ENSMUSG00000030220.
ENSMUST00000111891; ENSMUSP00000107522; ENSMUSG00000030220.
ENSMUST00000111892; ENSMUSP00000107523; ENSMUSG00000030220.
GeneIDi11857.
KEGGimmu:11857.
UCSCiuc009emo.2. mouse.

Organism-specific databases

CTDi397.
MGIiMGI:101940. Arhgdib.

Phylogenomic databases

eggNOGiNOG253438.
GeneTreeiENSGT00390000006233.
HOGENOMiHOG000175765.
HOVERGENiHBG000206.
InParanoidiQ61599.
KOiK12462.
OMAiAPEPHLE.
OrthoDBiEOG72JWH9.
PhylomeDBiQ61599.
TreeFamiTF105387.

Enzyme and pathway databases

ReactomeiREACT_297947. Rho GTPase cycle.

Miscellaneous databases

ChiTaRSiArhgdib. mouse.
NextBioi279847.
PROiQ61599.
SOURCEiSearch...

Gene expression databases

BgeeiQ61599.
CleanExiMM_ARHGDIB.
ExpressionAtlasiQ61599. baseline and differential.
GenevisibleiQ61599. MM.

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. "Identification of a novel protein with GDP dissociation inhibitor activity for the ras-like proteins CDC42Hs and rac I."
    Adra C.N., Ko J., Leonard D., Wirth L.J., Cerione R.A., Lim B.
    Genes Chromosomes Cancer 8:253-261(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: NIH Swiss.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Kidney and Thymus.
  3. "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].
    Strain: FVB/N.
    Tissue: Salivary gland.

Entry informationi

Entry nameiGDIR2_MOUSE
AccessioniPrimary (citable) accession number: Q61599
Secondary accession number(s): Q3TEB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.