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Q61599 (GDIR2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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):
D4
Rho-GDI beta
Gene names
Name:Arhgdib
Synonyms:Gdid4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length200 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 By similarity.

Subcellular location

Cytoplasm.

Tissue specificity

Preferentially expressed in hematopoietic cells.

Sequence similarities

Belongs to the Rho GDI family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionGTPase activation
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTPase activator activity

Inferred from electronic annotation. Source: UniProtKB-KW

Rho GDP-dissociation inhibitor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 200199Rho GDP-dissociation inhibitor 2
PRO_0000219017

Amino acid modifications

Modified residue21N-acetylthreonine By similarity
Modified residue201N6-acetyllysine By similarity
Modified residue231Phosphotyrosine By similarity
Modified residue241N6-acetyllysine By similarity
Modified residue391N6-acetyllysine By similarity
Modified residue461N6-acetyllysine By similarity
Modified residue1011N6-acetyllysine By similarity
Modified residue1231N6-acetyllysine By similarity
Modified residue1441Phosphoserine By similarity
Modified residue1741N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q61599 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: EA78C965F1AB6F5C

FASTA20022,851
        10         20         30         40         50         60 
MTEKDAQPQL EEADDDLDSK LNYKPPPQKS LKELQEMDKD DESLTKYKKT LLGDVPVVAD 

        70         80         90        100        110        120 
PTVPNVTVTR LSLVCDSAPG PITMDLTGDL EALKKDTFVL KEGIEYRVKI NFKVNKDIVS 

       130        140        150        160        170        180 
GLKYVQHTYR TGMRVDKATF MVGSYGPRPE EYEFLTPVEE APKGMLARGT YHNKSFFTDD 

       190        200 
DKQDHLTWEW NLAIKKDWTE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07918 mRNA. Translation: AAA61613.1.
AK002516 mRNA. Translation: BAB22155.1.
AK169733 mRNA. Translation: BAE41335.1.
BC031763 mRNA. Translation: AAH31763.1.
CCDSCCDS20661.1.
PIRI49687.
RefSeqNP_031512.1. NM_007486.4.
XP_006505466.1. XM_006505403.1.
XP_006505467.1. XM_006505404.1.
XP_006505468.1. XM_006505405.1.
XP_006505469.1. XM_006505406.1.
UniGeneMm.2241.

3D structure databases

ProteinModelPortalQ61599.
SMRQ61599. Positions 22-198.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198201. 6 interactions.
IntActQ61599. 3 interactions.
MINTMINT-1613948.

PTM databases

PhosphoSiteQ61599.

2D gel databases

COMPLUYEAST-2DPAGEQ61599.

Proteomic databases

MaxQBQ61599.
PaxDbQ61599.
PRIDEQ61599.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032344; ENSMUSP00000032344; ENSMUSG00000030220.
ENSMUST00000111891; ENSMUSP00000107522; ENSMUSG00000030220.
ENSMUST00000111892; ENSMUSP00000107523; ENSMUSG00000030220.
GeneID11857.
KEGGmmu:11857.
UCSCuc009emo.1. mouse.

Organism-specific databases

CTD397.
MGIMGI:101940. Arhgdib.

Phylogenomic databases

eggNOGNOG253438.
GeneTreeENSGT00390000006233.
HOGENOMHOG000175765.
HOVERGENHBG000206.
InParanoidQ61599.
KOK12462.
OMAQDHLTWE.
OrthoDBEOG72JWH9.
PhylomeDBQ61599.
TreeFamTF105387.

Gene expression databases

BgeeQ61599.
CleanExMM_ARHGDIB.
GenevestigatorQ61599.

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

ChiTaRSARHGDIB. mouse.
NextBio279847.
PROQ61599.
SOURCESearch...

Entry information

Entry nameGDIR2_MOUSE
AccessionPrimary (citable) accession number: Q61599
Secondary accession number(s): Q3TEB3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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