Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9D3G9 (RHOH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. 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-related GTP-binding protein RhoH
Gene names
Name:Rhoh
Synonyms:Arhh
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length191 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins. Inhibits the activation of NF-kappa-B by TNF and IKKB and the activation of CRK/p38 by TNF. Inhibits activities of RAC1, RHOA and CDC42. Negatively regulates leukotriene production in neutrophils By similarity. Negative regulator of hematopoietic progenitor cell proliferation, survival and migration. Critical regulator of thymocyte development and T-cell antigen receptor (TCR) signaling by mediating recruitment and activation of ZAP70. Required for phosphorylation of CD3Z, membrane translocation of ZAP70 and subsequent activation of the ZAP70-mediated pathways. Essential for efficient beta-selection and positive selection by promoting the ZAP70-dependent phosphorylation of the LAT signalosome during pre-TCR and TCR signaling. Crucial for thymocyte maturation during DN3 to DN4 transition and during positive selection. Plays critical roles in mast cell function by facilitating phosphorylation of SYK in Fc epsilon RI-mediated signal transduction. Essential for the phosphorylation of LAT, LCP2, PLCG1 and PLCG2 and for Ca2+ mobilization in mast cells. Ref.1 Ref.3 Ref.4 Ref.5

Subunit structure

Interacts with GDI1 and GDI2 By similarity. Interacts with ZAP70 (via SH2 domains) and the interaction is enhanced by its phosphorylation by LCK. Interacts with SYK and the interaction is enhanced by its phosphorylation by FYN. Ref.3 Ref.5

Subcellular location

Cytoplasm. Cell membrane; Lipid-anchor; Cytoplasmic side. Note: Colocalizes together with ZAP70 in the immunological synapse. Ref.3

Tissue specificity

Expression is widespread in hematopoietic cells, including in bone marrow progenitor cells and in differentiated myeloid as well as lymphoid cells. Expressed at high levels in the thymus and mast cells, found in spleen and low-density bone marrow (LDBM) cells and is detected at a low level in neutrophils. In the thymus it is detected in thymocytes of the thymic cortex but not in non-lymphoid cells of fibrovascular and fibroadipose tissues. Expressed in T-cells, B-cells and mast cells. Ref.1 Ref.5

Developmental stage

Expressed at all stages of thymocyte development, with relative peaks at the DN3 and DP stages. Ref.4

Domain

The region involved in interaction with ZAP70 is a non-canonical immunoreceptor tyrosine-based activation motif (ITAM).

Post-translational modification

Phosphorylated on tyrosine by LCK. Phosphorylated by FYN. Phosphorylation enhances the interactions with ZAP70 and SYK and is critical for its function in thymocyte development. Ref.3

Disruption phenotype

Mice show impaired passive systemic anaphylaxis and histamine release upon challenge with the specific antigen and impaired T-cell differentiation. Ref.4 Ref.5

Sequence similarities

Belongs to the small GTPase superfamily. Rho family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 188188Rho-related GTP-binding protein RhoH
PRO_0000198868
Propeptide189 – 1913Removed in mature form By similarity
PRO_0000281219

Regions

Nucleotide binding11 – 188GTP By similarity
Nucleotide binding58 – 625GTP By similarity
Nucleotide binding116 – 1194GTP By similarity
Region73 – 8614Interaction with ZAP70
Motif33 – 419Effector region By similarity

Amino acid modifications

Modified residue1881Cysteine methyl ester By similarity
Lipidation1881S-geranylgeranyl cysteine By similarity

Experimental info

Mutagenesis731Y → F: Abolishes interaction with ZAP70; when associated with F-83. Ref.3
Mutagenesis831Y → F: Abolishes interaction with ZAP70; when associated with F-73. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9D3G9 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 18845201F647D539

FASTA19121,324
        10         20         30         40         50         60 
MLSSIKCVLV GDSAVGKTSL LVRFTSETFP EAYKPTVYEN TGVDVFMDGI QISLGLWDTA 

        70         80         90        100        110        120 
GNDAFRSIRP LSYQQADVVL MCYSVANHNS FLNLKNKWIS EIRSNLPCTP VLVVATQTDQ 

       130        140        150        160        170        180 
REVGPHRASC INAIEGKRLA QDVRAKGYLE CSALSNRGVQ QVFECAVRTA VNQARRRNRR 

       190 
KLFSINECKI F 

« Hide

References

« Hide 'large scale' references
[1]"RhoH, a hematopoietic-specific Rho GTPase, regulates proliferation, survival, migration, and engraftment of hematopoietic progenitor cells."
Gu Y., Jasti A.C., Jansen M., Siefring J.E.
Blood 105:1467-1475(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[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.
Tissue: Thymus.
[3]"RhoH GTPase recruits and activates Zap70 required for T cell receptor signaling and thymocyte development."
Gu Y., Chae H.-D., Siefring J.E., Jasti A.C., Hildeman D.A., Williams D.A.
Nat. Immunol. 7:1182-1190(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ZAP70, SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF TYR-73 AND TYR-83.
[4]"RhoH is important for positive thymocyte selection and T-cell receptor signaling."
Dorn T., Kuhn U., Bungartz G., Stiller S., Bauer M., Ellwart J., Peters T., Scharffetter-Kochanek K., Semmrich M., Laschinger M., Holzmann B., Klinkert W.E.F., Straten P.T., Kollgaard T., Sixt M., Brakebusch C.
Blood 109:2346-2355(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
[5]"RhoH plays critical roles in Fc epsilon RI-dependent signal transduction in mast cells."
Oda H., Fujimoto M., Patrick M.S., Chida D., Sato Y., Azuma Y., Aoki H., Abe T., Suzuki H., Shirai M.
J. Immunol. 182:957-962(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH SYK, TISSUE SPECIFICITY.
[6]"RhoH/TTF negatively regulates leukotriene production in neutrophils."
Daryadel A., Yousefi S., Troi D., Schmid I., Schmidt-Mende J., Mordasini C., Dahinden C.A., Ziemiecki A., Simon H.-U.
J. Immunol. 182:6527-6532(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK017885 mRNA. Translation: BAB30987.1.
RefSeqNP_001074574.1. NM_001081105.1.
UniGeneMm.20323.

3D structure databases

ProteinModelPortalQ9D3G9.
SMRQ9D3G9. Positions 4-168.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid216981. 1 interaction.
STRING10090.ENSMUSP00000031106.

Proteomic databases

PRIDEQ9D3G9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031106; ENSMUSP00000031106; ENSMUSG00000029204.
GeneID74734.
KEGGmmu:74734.
UCSCuc008xoc.1. mouse.

Organism-specific databases

CTD399.
MGIMGI:1921984. Rhoh.

Phylogenomic databases

eggNOGCOG1100.
GeneTreeENSGT00720000108472.
HOGENOMHOG000233974.
HOVERGENHBG009351.
InParanoidQ9D3G9.
KOK07873.
OMAASCINAI.
OrthoDBEOG7TJ3K0.
PhylomeDBQ9D3G9.
TreeFamTF331219.

Gene expression databases

ArrayExpressQ9D3G9.
BgeeQ9D3G9.
CleanExMM_RHOH.
GenevestigatorQ9D3G9.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio341522.
PROQ9D3G9.
SOURCESearch...

Entry information

Entry nameRHOH_MOUSE
AccessionPrimary (citable) accession number: Q9D3G9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 96 of the entry and version 1 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