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Protein

RAS guanyl-releasing protein 1

Gene

Rasgrp1

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

Functioni

Functions as a calcium- and diacylglycerol (DAG)-regulated nucleotide exchange factor specifically activating Ras through the exchange of bound GDP for GTP. Activates the Erk/MAP kinase cascade. Regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. Regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways (By similarity). Functions in mast cell degranulation and cytokine secretion, regulating FcERI-evoked allergic responses (PubMed:17190838). May also function in differentiation of other cell types. Proto-oncogene, which promotes T-cell lymphomagenesis when its expression is deregulated (PubMed:15829980, PubMed:17210708).By similarity13 Publications

Enzyme regulationi

Autoinhibited. Activated by diacylglycerol and calcium binding, which induces a conformational change releasing the autoinhibitory state. Regulated by DGKA. Regulated by DGKZ. Regulated by PLC gamma and F-actin polymerization (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi483 – 49412PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri541 – 59151Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • activation of GTPase activity Source: CACAO
  • cell differentiation Source: UniProtKB-KW
  • cytokine production Source: MGI
  • inflammatory response to antigenic stimulus Source: MGI
  • mast cell degranulation Source: MGI
  • positive regulation of ERK1 and ERK2 cascade Source: MGI
  • positive regulation of granulocyte macrophage colony-stimulating factor production Source: MGI
  • positive regulation of GTPase activity Source: MGI
  • positive regulation of interferon-gamma secretion Source: MGI
  • positive regulation of JNK cascade Source: MGI
  • positive regulation of MAP kinase activity Source: MGI
  • positive regulation of natural killer cell activation Source: CACAO
  • positive regulation of natural killer cell differentiation Source: CACAO
  • positive regulation of natural killer cell mediated cytotoxicity Source: MGI
  • positive regulation of protein phosphorylation Source: MGI
  • positive regulation of Ras protein signal transduction Source: MGI
  • positive regulation of T cell differentiation in thymus Source: CACAO
  • positive regulation of tumor necrosis factor production Source: MGI
  • protein oligomerization Source: MGI
  • Ras protein signal transduction Source: InterPro
  • regulation of ERK1 and ERK2 cascade Source: MGI
  • regulation of phosphatidylinositol 3-kinase signaling Source: MGI
  • secretory granule localization Source: MGI
  • vesicle transport along microtubule Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Biological processi

Differentiation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-1169092. Activation of RAS in B cells.
R-MMU-354192. Integrin alphaIIb beta3 signaling.
R-MMU-392517. Rap1 signalling.
R-MMU-5673001. RAF/MAP kinase cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
RAS guanyl-releasing protein 1
Alternative name(s):
Calcium and DAG-regulated guanine nucleotide exchange factor II
Short name:
CalDAG-GEFII
Ras guanyl-releasing protein
Gene namesi
Name:Rasgrp1
Synonyms:Rasgrp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1314635. Rasgrp1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • Golgi apparatus Source: MGI
  • Golgi membrane Source: UniProtKB-SubCell
  • mast cell granule Source: GOC
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice fail to mount anaphylactic allergic reactions and display chronic T-cell immunodeficiencies. Lag (lymphoproliferation-autoimmunity-glomerulonephritis) mice do not express Rasgrp1 and display a systemic lupus erythematosus-like phenotype.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi271 – 2711R → E: Loss of function and transforming activity. 2 Publications

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 795795RAS guanyl-releasing protein 1PRO_0000316979Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei184 – 1841Phosphothreonine; by PKCBy similarity
Modified residuei597 – 5971PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9Z1S3.
MaxQBiQ9Z1S3.
PaxDbiQ9Z1S3.
PRIDEiQ9Z1S3.

PTM databases

iPTMnetiQ9Z1S3.
PhosphoSiteiQ9Z1S3.

Expressioni

Tissue specificityi

Detected in spleen and thymus. Expressed by mature thymocytes and to a lower extent by bone marrow-derived mast cells (at protein level). Detected in B-cells and keratinocytes (at protein level).6 Publications

Inductioni

Up-regulated at the double-negative to double-positive transition during thymocyte development. Down-regulated by 12-O-tetradecanoylphorbol-13-acetate (TPA).2 Publications

Gene expression databases

BgeeiQ9Z1S3.
CleanExiMM_RASGRP1.
ExpressionAtlasiQ9Z1S3. baseline and differential.
GenevisibleiQ9Z1S3. MM.

Interactioni

Subunit structurei

Homodimer. Forms a signaling complex with DGKZ and HRAS. Interacts with F-actin. Interacts with SKAP1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000099593.

Structurei

3D structure databases

ProteinModelPortaliQ9Z1S3.
SMRiQ9Z1S3. Positions 53-593, 743-784.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 176124N-terminal Ras-GEFPROSITE-ProRule annotationAdd
BLAST
Domaini205 – 436232Ras-GEFPROSITE-ProRule annotationAdd
BLAST
Domaini470 – 50536EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini497 – 53236EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni57 – 11054Ras exchanger motif region; required for transforming activityAdd
BLAST
Regioni686 – 6949Suppress the PT region-mediated translocation to plasma membrane
Regioni717 – 79579PT region; mediates the BCR-dependent translocation to plasma membraneAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili738 – 77942Sequence analysisAdd
BLAST

Domaini

The phorbol-ester/DAG-type zinc finger is the principal mediator of the targeting to membranes and is required for functional activation through DAG-binding.
Two EF-hand domains are present. However, only EF-hand 1 (and not EF-hand 2) binds calcium.By similarity

Sequence similaritiesi

Belongs to the RASGRP family.Curated
Contains 2 EF-hand domains.PROSITE-ProRule annotation
Contains 1 N-terminal Ras-GEF domain.PROSITE-ProRule annotation
Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 Ras-GEF domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri541 – 59151Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IQ6J. Eukaryota.
ENOG410ZKZ2. LUCA.
GeneTreeiENSGT00810000125357.
HOGENOMiHOG000293171.
HOVERGENiHBG007513.
InParanoidiQ9Z1S3.
KOiK04350.
OMAiEGPFTFP.
OrthoDBiEOG72G16V.
PhylomeDBiQ9Z1S3.
TreeFamiTF312918.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
1.10.840.10. 1 hit.
InterProiIPR020454. DAG/PE-bd.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR002219. PE/DAG-bd.
IPR000651. Ras-like_Gua-exchang_fac_N.
IPR023578. Ras_GEF_dom.
IPR001895. RASGEF_cat_dom.
IPR029647. RasGRP1.
[Graphical view]
PANTHERiPTHR23113:SF174. PTHR23113:SF174. 1 hit.
PfamiPF00130. C1_1. 1 hit.
PF13202. EF-hand_5. 1 hit.
PF00617. RasGEF. 1 hit.
PF00618. RasGEF_N. 1 hit.
[Graphical view]
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00054. EFh. 1 hit.
SM00147. RasGEF. 1 hit.
SM00229. RasGEFN. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 2 hits.
SSF48366. SSF48366. 1 hit.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS50009. RASGEF_CAT. 1 hit.
PS50212. RASGEF_NTER. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Z1S3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTLGKAREA PRKPCHGSRA GPKARLEAKS TNSPLPAQPS LAQITQFRMM
60 70 80 90 100
VSLGHLAKGA SLDDLIDSCI QSFDADGNLC RNNQLLQVML TMHRIIISSA
110 120 130 140 150
ELLQKVMNLY KDALEKNSPG VCLKICYFVR YWITEFWIMF KMDASLTSTM
160 170 180 190 200
EEFQDLVKAN GEETHCHLID TTQINSRDWS RKLTQRIKSN TSKKRKVSLL
210 220 230 240 250
FDHLEPEELS EHLTYLEFKS FRRISFSDYQ NYLVNSCVKE NPTMERSIAL
260 270 280 290 300
CNGISQWVQL MVLSRPTPQL RAEVFIKFIH VAQKLHQLQN FNTLMAVIGG
310 320 330 340 350
LCHSSISRLK ETSSHVPHEI NKVLGEMTEL LSSCRNYDNY RRAYGECTHF
360 370 380 390 400
KIPILGVHLK DLISLYEAMP DYLEDGKVNV QKLLALYNHI NELVQLQEMA
410 420 430 440 450
PPLDANKDLV HLLTLSLDLY YTEDEIYELS YAREPRNHRA PPLTPSKPPV
460 470 480 490 500
VVDWASGVSP KPDPKTISKH VQRMVDSVFK NYDLDQDGYI SQEEFEKIAA
510 520 530 540 550
SFPFSFCVMD KDREGLISRD EITAYFMRAS SIYSKLGLGF PHNFQETTYL
560 570 580 590 600
KPTFCDNCAG FLWGVIKQGY RCKDCGMNCH KQCKDLVVFE CKKRIKSPAI
610 620 630 640 650
STENISSVVP MSTLCPLGTK DLLHAPEEGS FIFQNGEIVD HSEESKDRTI
660 670 680 690 700
MLLGVSSQKI SVRLKRTVAH KSTQTESFPW VGGETTPGHF VLSSPRKSAQ
710 720 730 740 750
GALYVHSPAS PCPSPALVRK RAFVKWENKE SLIKPKPELH LRLRTYQELE
760 770 780 790
QEINTLKADN DALKIQLKYA QKKIESLQLG KSNHVLAQMD HGDSA
Length:795
Mass (Da):90,304
Last modified:May 1, 1999 - v1
Checksum:iE2096D985DFB79A0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti171 – 1711T → R in BAE24718 (PubMed:16141072).Curated
Sequence conflicti472 – 4721Q → K in BAE20439 (PubMed:16141072).Curated
Sequence conflicti485 – 4851D → E in BAE20439 (PubMed:16141072).Curated
Sequence conflicti501 – 5011S → T in BAE20439 (PubMed:16141072).Curated
Sequence conflicti520 – 5201D → H in BAE20439 (PubMed:16141072).Curated
Sequence conflicti768 – 7681K → R in BAC33100 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF106070 mRNA. Translation: AAC97348.1.
AK028308 mRNA. Translation: BAE20439.1.
AK047613 mRNA. Translation: BAC33100.1.
AK141524 mRNA. Translation: BAE24718.1.
AL844579, AL928959 Genomic DNA. Translation: CAM17832.1.
AL928959, AL844579 Genomic DNA. Translation: CAM26780.1.
BC057120 mRNA. Translation: AAH57120.1.
BC057341 mRNA. Translation: AAH57341.1.
CCDSiCCDS16572.1.
RefSeqiNP_035376.1. NM_011246.2.
UniGeneiMm.42150.

Genome annotation databases

EnsembliENSMUST00000102534; ENSMUSP00000099593; ENSMUSG00000027347.
ENSMUST00000178884; ENSMUSP00000136423; ENSMUSG00000027347.
GeneIDi19419.
KEGGimmu:19419.
UCSCiuc033hpk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF106070 mRNA. Translation: AAC97348.1.
AK028308 mRNA. Translation: BAE20439.1.
AK047613 mRNA. Translation: BAC33100.1.
AK141524 mRNA. Translation: BAE24718.1.
AL844579, AL928959 Genomic DNA. Translation: CAM17832.1.
AL928959, AL844579 Genomic DNA. Translation: CAM26780.1.
BC057120 mRNA. Translation: AAH57120.1.
BC057341 mRNA. Translation: AAH57341.1.
CCDSiCCDS16572.1.
RefSeqiNP_035376.1. NM_011246.2.
UniGeneiMm.42150.

3D structure databases

ProteinModelPortaliQ9Z1S3.
SMRiQ9Z1S3. Positions 53-593, 743-784.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000099593.

PTM databases

iPTMnetiQ9Z1S3.
PhosphoSiteiQ9Z1S3.

Proteomic databases

EPDiQ9Z1S3.
MaxQBiQ9Z1S3.
PaxDbiQ9Z1S3.
PRIDEiQ9Z1S3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102534; ENSMUSP00000099593; ENSMUSG00000027347.
ENSMUST00000178884; ENSMUSP00000136423; ENSMUSG00000027347.
GeneIDi19419.
KEGGimmu:19419.
UCSCiuc033hpk.1. mouse.

Organism-specific databases

CTDi10125.
MGIiMGI:1314635. Rasgrp1.

Phylogenomic databases

eggNOGiENOG410IQ6J. Eukaryota.
ENOG410ZKZ2. LUCA.
GeneTreeiENSGT00810000125357.
HOGENOMiHOG000293171.
HOVERGENiHBG007513.
InParanoidiQ9Z1S3.
KOiK04350.
OMAiEGPFTFP.
OrthoDBiEOG72G16V.
PhylomeDBiQ9Z1S3.
TreeFamiTF312918.

Enzyme and pathway databases

ReactomeiR-MMU-1169092. Activation of RAS in B cells.
R-MMU-354192. Integrin alphaIIb beta3 signaling.
R-MMU-392517. Rap1 signalling.
R-MMU-5673001. RAF/MAP kinase cascade.

Miscellaneous databases

NextBioi296563.
PROiQ9Z1S3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z1S3.
CleanExiMM_RASGRP1.
ExpressionAtlasiQ9Z1S3. baseline and differential.
GenevisibleiQ9Z1S3. MM.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
1.10.840.10. 1 hit.
InterProiIPR020454. DAG/PE-bd.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR002219. PE/DAG-bd.
IPR000651. Ras-like_Gua-exchang_fac_N.
IPR023578. Ras_GEF_dom.
IPR001895. RASGEF_cat_dom.
IPR029647. RasGRP1.
[Graphical view]
PANTHERiPTHR23113:SF174. PTHR23113:SF174. 1 hit.
PfamiPF00130. C1_1. 1 hit.
PF13202. EF-hand_5. 1 hit.
PF00617. RasGEF. 1 hit.
PF00618. RasGEF_N. 1 hit.
[Graphical view]
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00054. EFh. 1 hit.
SM00147. RasGEF. 1 hit.
SM00229. RasGEFN. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 2 hits.
SSF48366. SSF48366. 1 hit.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS50009. RASGEF_CAT. 1 hit.
PS50212. RASGEF_NTER. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "RasGRP, a Ras activator: mouse and human cDNA sequences and chromosomal positions."
    Bottorff D.A., Ebinu J.O., Stone J.C.
    Mamm. Genome 10:358-361(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X C3H.
    Tissue: Brain.
  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: Brain, Corpus striatum and Hippocampus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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: C57BL/6J.
    Tissue: Fetal brain.
  5. "Regulation of RasGRP via a phorbol ester-responsive C1 domain."
    Tognon C.E., Kirk H.E., Passmore L.A., Whitehead I.P., Der C.J., Kay R.J.
    Mol. Cell. Biol. 18:6995-7008(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ARG-271, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "RasGRP is essential for mouse thymocyte differentiation and TCR signaling."
    Dower N.A., Stang S.L., Bottorff D.A., Ebinu J.O., Dickie P., Ostergaard H.L., Stone J.C.
    Nat. Immunol. 1:317-321(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN T-CELL ACTIVATION, TISSUE SPECIFICITY.
  7. "RasGRP1 transduces low-grade TCR signals which are critical for T cell development, homeostasis, and differentiation."
    Priatel J.J., Teh S.-J., Dower N.A., Stone J.C., Teh H.-S.
    Immunity 17:617-627(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  8. Cited for: FUNCTION.
  9. "RasGRP1 represents a novel non-protein kinase C phorbol ester signaling pathway in mouse epidermal keratinocytes."
    Rambaratsingh R.A., Stone J.C., Blumberg P.M., Lorenzo P.S.
    J. Biol. Chem. 278:52792-52801(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, INDUCTION BY TPA.
  10. "Transgenic expression of RasGRP1 induces the maturation of double-negative thymocytes and enhances the production of CD8 single-positive thymocytes."
    Norment A.M., Bogatzki L.Y., Klinger M.B., Ojala E.W., Bevan M.J., Kay R.J.
    J. Immunol. 170:1141-1149(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  11. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  12. "RasGRP1 sensitizes an immature B cell line to antigen receptor-induced apoptosis."
    Guilbault B., Kay R.J.
    J. Biol. Chem. 279:19523-19530(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN B-CELLS, TISSUE SPECIFICITY, MUTAGENESIS OF ARG-271.
  13. "RasGRP1 and RasGRP3 regulate B cell proliferation by facilitating B cell receptor-Ras signaling."
    Coughlin J.J., Stang S.L., Dower N.A., Stone J.C.
    J. Immunol. 175:7179-7184(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Deregulated expression of RasGRP1 initiates thymic lymphomagenesis independently of T-cell receptors."
    Klinger M.B., Guilbault B., Goulding R.E., Kay R.J.
    Oncogene 24:2695-2704(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "RasGRP1 transmits prodifferentiation TCR signaling that is crucial for CD4 T cell development."
    Priatel J.J., Chen X., Dhanji S., Abraham N., Teh H.-S.
    J. Immunol. 177:1470-1480(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  16. "Differential membrane binding and diacylglycerol recognition by C1 domains of RasGRPs."
    Johnson J.E., Goulding R.E., Ding Z., Partovi A., Anthony K.V., Beaulieu N., Tazmini G., Cornell R.B., Kay R.J.
    Biochem. J. 406:223-236(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DIACYLGLYCEROL-BINDING, SUBCELLULAR LOCATION.
  17. "Transgenic overexpression of RasGRP1 in mouse epidermis results in spontaneous tumors of the skin."
    Oki-Idouchi C.E., Lorenzo P.S.
    Cancer Res. 67:276-280(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "An essential role for RasGRP1 in mast cell function and IgE-mediated allergic response."
    Liu Y., Zhu M., Nishida K., Hirano T., Zhang W.
    J. Exp. Med. 204:93-103(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MAST CELL ACTIVATION, TISSUE SPECIFICITY.
  19. "Chronic immunodeficiency in mice lacking RasGRP1 results in CD4 T cell immune activation and exhaustion."
    Priatel J.J., Chen X., Zenewicz L.A., Shen H., Harder K.W., Horwitz M.S., Teh H.-S.
    J. Immunol. 179:2143-2152(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  20. "Regulation of RasGRP1 by B cell antigen receptor requires cooperativity between three domains controlling translocation to the plasma membrane."
    Beaulieu N., Zahedi B., Goulding R.E., Tazmini G., Anthony K.V., Omeis S.L., de Jong D.R., Kay R.J.
    Mol. Biol. Cell 18:3156-3168(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiGRP1_MOUSE
AccessioniPrimary (citable) accession number: Q9Z1S3
Secondary accession number(s): Q3URH0, Q3V401, Q8BQP6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 1, 1999
Last modified: May 11, 2016
This is version 138 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

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 one 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.