SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9D3G9

- RHOH_MOUSE

UniProt

Q9D3G9 - RHOH_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Rho-related GTP-binding protein RhoH
Gene
Rhoh, Arhh
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 188GTP By similarity
Nucleotide bindingi58 – 625GTP By similarity
Nucleotide bindingi116 – 1194GTP By similarity

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. kinase inhibitor activity Source: Ensembl
  3. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. T cell differentiation Source: UniProtKB
  2. mast cell activation Source: UniProtKB
  3. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  4. small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_210090. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho-related GTP-binding protein RhoH
Gene namesi
Name:Rhoh
Synonyms:Arhh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1921984. Rhoh.

Subcellular locationi

Cytoplasm. Cell membrane; Lipid-anchor; Cytoplasmic side
Note: Colocalizes together with ZAP70 in the immunological synapse.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. immunological synapse Source: UniProtKB
  3. mitochondrion Source: Ensembl
  4. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice show impaired passive systemic anaphylaxis and histamine release upon challenge with the specific antigen and impaired T-cell differentiation.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi73 – 731Y → F: Abolishes interaction with ZAP70; when associated with F-83. 1 Publication
Mutagenesisi83 – 831Y → F: Abolishes interaction with ZAP70; when associated with F-73. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 188188Rho-related GTP-binding protein RhoH
PRO_0000198868Add
BLAST
Propeptidei189 – 1913Removed in mature form By similarity
PRO_0000281219

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei188 – 1881Cysteine methyl ester By similarity
Lipidationi188 – 1881S-geranylgeranyl cysteine By similarity

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

PRIDEiQ9D3G9.

Expressioni

Tissue specificityi

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.2 Publications

Developmental stagei

Expressed at all stages of thymocyte development, with relative peaks at the DN3 and DP stages.1 Publication

Gene expression databases

ArrayExpressiQ9D3G9.
BgeeiQ9D3G9.
CleanExiMM_RHOH.
GenevestigatoriQ9D3G9.

Interactioni

Subunit structurei

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.2 Publications

Protein-protein interaction databases

BioGridi216981. 1 interaction.
STRINGi10090.ENSMUSP00000031106.

Structurei

3D structure databases

ProteinModelPortaliQ9D3G9.
SMRiQ9D3G9. Positions 4-168.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni73 – 8614Interaction with ZAP70
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi33 – 419Effector region By similarity

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00720000108472.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiQ9D3G9.
KOiK07873.
OMAiASCINAI.
OrthoDBiEOG7TJ3K0.
PhylomeDBiQ9D3G9.
TreeFamiTF331219.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9D3G9-1 [UniParc]FASTAAdd to Basket

« Hide

MLSSIKCVLV GDSAVGKTSL LVRFTSETFP EAYKPTVYEN TGVDVFMDGI    50
QISLGLWDTA GNDAFRSIRP LSYQQADVVL MCYSVANHNS FLNLKNKWIS 100
EIRSNLPCTP VLVVATQTDQ REVGPHRASC INAIEGKRLA QDVRAKGYLE 150
CSALSNRGVQ QVFECAVRTA VNQARRRNRR KLFSINECKI F 191
Length:191
Mass (Da):21,324
Last modified:June 1, 2001 - v1
Checksum:i18845201F647D539
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK017885 mRNA. Translation: BAB30987.1.
CCDSiCCDS39100.1.
RefSeqiNP_001074574.1. NM_001081105.1.
UniGeneiMm.20323.

Genome annotation databases

EnsembliENSMUST00000031106; ENSMUSP00000031106; ENSMUSG00000029204.
GeneIDi74734.
KEGGimmu:74734.
UCSCiuc008xoc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK017885 mRNA. Translation: BAB30987.1 .
CCDSi CCDS39100.1.
RefSeqi NP_001074574.1. NM_001081105.1.
UniGenei Mm.20323.

3D structure databases

ProteinModelPortali Q9D3G9.
SMRi Q9D3G9. Positions 4-168.
ModBasei Search...

Protein-protein interaction databases

BioGridi 216981. 1 interaction.
STRINGi 10090.ENSMUSP00000031106.

Proteomic databases

PRIDEi Q9D3G9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000031106 ; ENSMUSP00000031106 ; ENSMUSG00000029204 .
GeneIDi 74734.
KEGGi mmu:74734.
UCSCi uc008xoc.1. mouse.

Organism-specific databases

CTDi 399.
MGIi MGI:1921984. Rhoh.

Phylogenomic databases

eggNOGi COG1100.
GeneTreei ENSGT00720000108472.
HOGENOMi HOG000233974.
HOVERGENi HBG009351.
InParanoidi Q9D3G9.
KOi K07873.
OMAi ASCINAI.
OrthoDBi EOG7TJ3K0.
PhylomeDBi Q9D3G9.
TreeFami TF331219.

Enzyme and pathway databases

Reactomei REACT_210090. Rho GTPase cycle.

Miscellaneous databases

NextBioi 341522.
PROi Q9D3G9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9D3G9.
Bgeei Q9D3G9.
CleanExi MM_RHOH.
Genevestigatori Q9D3G9.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view ]
Pfami PF00071. Ras. 1 hit.
[Graphical view ]
PRINTSi PR00449. RASTRNSFRMNG.
SMARTi SM00174. RHO. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51420. RHO. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: INDUCTION.

Entry informationi

Entry nameiRHOH_MOUSE
AccessioniPrimary (citable) accession number: Q9D3G9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: June 1, 2001
Last modified: September 3, 2014
This is version 99 of the entry and version 1 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