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O95267

- GRP1_HUMAN

UniProt

O95267 - GRP1_HUMAN

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Protein

RAS guanyl-releasing protein 1

Gene
RASGRP1, RASGRP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Functions as a diacylglycerol (DAG)-regulated nucleotide exchange factor specifically activating Ras through the exchange of bound GDP for GTP. Activates the Erk/MAP kinase cascade. Couples T-lymphocytes and B-lymphocytes antigen receptors to the activation of Ras. Hence, regulates T-cells and B-cells development, homeostasis and differentiation. Functions also in FcERI-evoked degranulation and cytokine secretion by mast cells, regulating allergic responses. May also function in other cell types differentiation.7 Publications

Enzyme regulationi

Probably regulated by calcium By similarity. Regulated by PLC gamma, DGKA, DGKZ and by F-actin polymerization.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi483 – 494121 Reviewed predictionAdd
BLAST
Calcium bindingi510 – 521122 Reviewed predictionAdd
BLAST
Zinc fingeri541 – 59151Phorbol-ester/DAG-typeAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: ProtInc
  2. guanyl-nucleotide exchange factor activity Source: Reactome
  3. lipid binding Source: ProtInc

GO - Biological processi

  1. activation of Rho GTPase activity Source: Ensembl
  2. blood coagulation Source: Reactome
  3. cell differentiation Source: UniProtKB-KW
  4. cytokine production Source: Ensembl
  5. Fc-epsilon receptor signaling pathway Source: Reactome
  6. inflammatory response to antigenic stimulus Source: Ensembl
  7. innate immune response Source: Reactome
  8. mast cell degranulation Source: Ensembl
  9. platelet activation Source: Reactome
  10. Ras protein signal transduction Source: ProtInc
  11. regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
  12. secretory granule localization Source: Ensembl
  13. signal transduction Source: ProtInc
  14. vesicle transport along microtubule Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Biological processi

Differentiation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118778. Activation of RAS in B cells.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_163994. FCERI mediated NF-kB activation.
REACT_2202. Effects of PIP2 hydrolysis.
REACT_23898. Rap1 signalling.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:9878. RASGRP1.

Subcellular locationi

Cytoplasmcytosol. Cell membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein
Note: Found both in the cytosol and associated with membranes. Relocalization to the cell membrane upon activation is F-actin-dependent. Translocates to the Golgi in response to phorbol ester or nerve growth factor. Localizes to somata and dendrites but not to axons of hippocampal pyramidal cells By similarity.4 Publications

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. Golgi membrane Source: UniProtKB-SubCell
  4. mast cell granule Source: GOC
  5. membrane Source: ProtInc
  6. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Systemic lupus erythematosus (SLE) [MIM:152700]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Aberrantly spliced isoforms and/or diminished levels of RASGRP1 are found in a cohort of SLE patients raising the possibility that dysregulation of this signaling protein contributes to the development of autoimmunity in a subset of SLE patients.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi271 – 2711R → E: Loss of function; prevents Ras activation. 1 Publication
Mutagenesisi549 – 5491Y → F: Loss of localization to the endoplasmic reticulum and the Golgi apparatus. 1 Publication

Keywords - Diseasei

Systemic lupus erythematosus

Organism-specific databases

MIMi152700. phenotype.
PharmGKBiPA34240.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 797797RAS guanyl-releasing protein 1PRO_0000316978Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei184 – 1841Phosphothreonine; by PKC2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO95267.
PaxDbiO95267.
PRIDEiO95267.

PTM databases

PhosphoSiteiO95267.

Expressioni

Tissue specificityi

Expressed in brain with higher expression in cerebellum, cerebral cortex and amygdala. Expressed in the hematopoietic system. Expressed in T-cells (at protein level).3 Publications

Developmental stagei

Expressed in fetal brain and kidney.1 Publication

Gene expression databases

ArrayExpressiO95267.
BgeeiO95267.
GenevestigatoriO95267.

Interactioni

Subunit structurei

Forms a signaling complex with DGKZ and HRAS. Interacts with F-actin. Interacts with SKAP1.3 Publications

Protein-protein interaction databases

BioGridi115429. 5 interactions.
IntActiO95267. 1 interaction.
MINTiMINT-7970969.

Structurei

Secondary structure

1
797
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi62 – 7110
Helixi84 – 929
Helixi93 – 953
Helixi99 – 11517
Helixi119 – 13517
Helixi138 – 1425
Helixi144 – 16017
Helixi164 – 1685
Helixi172 – 1798
Beta strandi201 – 2033
Helixi206 – 22217
Helixi226 – 2349
Helixi242 – 26423
Turni267 – 2693
Helixi270 – 28718
Helixi291 – 30111
Helixi304 – 3074
Helixi310 – 3156
Helixi318 – 33114
Turni335 – 3373
Helixi338 – 3458
Helixi355 – 36814
Beta strandi376 – 3783
Helixi380 – 39516
Helixi396 – 3983
Helixi407 – 41610
Helixi423 – 43311
Helixi464 – 48219
Helixi492 – 5009
Helixi519 – 53315
Beta strandi544 – 5474
Turni556 – 5583
Beta strandi564 – 5663
Beta strandi569 – 5724
Turni573 – 5753
Turni581 – 5833
Beta strandi584 – 5863
Helixi748 – 78235
Turni783 – 7853
Helixi788 – 7914

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4L9MX-ray3.00A50-607[»]
4L9UX-ray1.60A/B739-793[»]
ProteinModelPortaliO95267.
SMRiO95267. Positions 53-593, 745-793.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni57 – 11054Ras exchanger motif region; required for transforming activity By similarityAdd
BLAST
Regioni686 – 6949Suppress the PT region-mediated translocation to plasma membrane By similarity
Regioni718 – 79780PT region; mediates the BCR-dependent translocation to plasma membrane By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili746 – 78641 Reviewed predictionAdd
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.

Sequence similaritiesi

Belongs to the RASGRP family.
Contains 2 EF-hand domains.
Contains 1 Ras-GEF domain.

Zinc finger

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

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG256085.
HOVERGENiHBG007513.
InParanoidiO95267.
KOiK04350.
OrthoDBiEOG72G16V.
PhylomeDBiO95267.
TreeFamiTF312918.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
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. Prot_Kinase_C-like_PE/DAG-bd.
IPR000651. Ras-like_Gua-exchang_fac_N.
IPR023578. Ras_GEF_dom.
IPR001895. RasGRF_CDC25.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF13405. EF-hand_6. 1 hit.
PF00617. RasGEF. 1 hit.
PF00618. RasGEF_N. 1 hit.
[Graphical view]
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00147. RasGEF. 1 hit.
SM00229. RasGEFN. 1 hit.
[Graphical view]
SUPFAMiSSF48366. 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]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist. Several splicing events may be used independently in a modular way.

Isoform 1 (identifier: O95267-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MGTLGKAREA PRKPSHGCRA ASKARLEAKP ANSPFPSHPS LAHITQFRMM    50
VSLGHLAKGA SLDDLIDSCI QSFDADGNLC RSNQLLQVML TMHRIVISSA 100
ELLQKVITLY KDALAKNSPG LCLKICYFVR YWITEFWVMF KMDASLTDTM 150
EEFQELVKAK GEELHCRLID TTQINARDWS RKLTQRIKSN TSKKRKVSLL 200
FDHLEPEELS EHLTYLEFKS FRRISFSDYQ NYLVNSCVKE NPTMERSIAL 250
CNGISQWVQL MVLSRPTPQL RAEVFIKFIQ VAQKLHQLQN FNTLMAVIGG 300
LCHSSISRLK ETSSHVPHEI NKVLGEMTEL LSSSRNYDNY RRAYGECTDF 350
KIPILGVHLK DLISLYEAMP DYLEDGKVNV HKLLALYNHI SELVQLQEVA 400
PPLEANKDLV HLLTLSLDLY YTEDEIYELS YAREPRNHRA PPLTPSKPPV 450
VVDWASGVSP KPDPKTISKH VQRMVDSVFK NYDHDQDGYI SQEEFEKIAA 500
SFPFSFCVMD KDREGLISRD EITAYFMRAS SIYSKLGLGF PHNFQETTYL 550
KPTFCDNCAG FLWGVIKQGY RCKDCGMNCH KQCKDLVVFE CKKRAKNPVA 600
PTENNTSVGP VSNLCSLGAK DLLHAPEEGP FTFPNGEAVE HGEESKDRTI 650
MLMGVSSQKI SLRLKRAVAH KATQTESQPW IGSEGPSGPF VLSSPRKTAQ 700
DTLYVLPSPT SPCPSPVLVR KRAFVKWENK DSLIKSKEEL RHLRLPTYQE 750
LEQEINTLKA DNDALKIQLK YAQKKIESLQ LEKSNHVLAQ MEQGDCS 797
Length:797
Mass (Da):90,402
Last modified:February 5, 2008 - v2
Checksum:i8ACDCF0F715ABAA9
GO
Isoform 2 (identifier: O95267-2) [UniParc]FASTAAdd to Basket

Also known as: A

The sequence of this isoform differs from the canonical sequence as follows:
     442-476: Missing.

Show »
Length:762
Mass (Da):86,625
Checksum:iC3ACFFF5888E3236
GO
Isoform 3 (identifier: O95267-3) [UniParc]FASTAAdd to Basket

Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     442-476: Missing.
     625-632: APEEGPFT → GNKYSESR
     633-797: Missing.

Show »
Length:597
Mass (Da):68,170
Checksum:i979AEA31D0FBE5DC
GO
Isoform 4 (identifier: O95267-4) [UniParc]FASTAAdd to Basket

Also known as: C

The sequence of this isoform differs from the canonical sequence as follows:
     442-476: Missing.
     513-516: REGL → SSGE
     517-797: Missing.

Show »
Length:481
Mass (Da):55,100
Checksum:i11408850F4E84118
GO
Isoform 5 (identifier: O95267-5) [UniParc]FASTAAdd to Basket

Also known as: D

The sequence of this isoform differs from the canonical sequence as follows:
     442-476: Missing.
     574-581: DCGMNCHK → GNKYSESR
     582-797: Missing.

Note: No experimental confirmation available.

Show »
Length:546
Mass (Da):62,674
Checksum:i54018A113532AF92
GO

Sequence cautioni

The sequence AAH67298.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei442 – 47635Missing in isoform 2, isoform 3, isoform 4 and isoform 5. VSP_030836Add
BLAST
Alternative sequencei513 – 5164REGL → SSGE in isoform 4. VSP_030837
Alternative sequencei517 – 797281Missing in isoform 4. VSP_030838Add
BLAST
Alternative sequencei574 – 5818DCGMNCHK → GNKYSESR in isoform 5. VSP_030839
Alternative sequencei582 – 797216Missing in isoform 5. VSP_030840Add
BLAST
Alternative sequencei625 – 6328APEEGPFT → GNKYSESR in isoform 3. VSP_030841
Alternative sequencei633 – 797165Missing in isoform 3. VSP_030842Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti374 – 3741E → G in AAC79699. 1 Publication
Sequence conflicti374 – 3741E → G in AAF21898. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF081195 mRNA. Translation: AAC79699.1.
AF081197 mRNA. Translation: AAF21898.1.
AF106071 mRNA. Translation: AAC97349.1.
AY634315 mRNA. Translation: AAT47482.2.
AY858556 mRNA. Translation: AAW32406.2.
AY954625 mRNA. Translation: AAX54699.4.
AY966005 mRNA. Translation: AAX76907.1.
BC067298 mRNA. Translation: AAH67298.1. Sequence problems.
BC109296 mRNA. Translation: AAI09297.1.
BC109297 mRNA. Translation: AAI09298.1.
AB208848 mRNA. Translation: BAD92085.1.
CCDSiCCDS45221.1. [O95267-2]
CCDS45222.1. [O95267-1]
RefSeqiNP_001122074.1. NM_001128602.1. [O95267-2]
NP_005730.2. NM_005739.3. [O95267-1]
UniGeneiHs.591127.

Genome annotation databases

EnsembliENST00000310803; ENSP00000310244; ENSG00000172575. [O95267-1]
ENST00000414708; ENSP00000413105; ENSG00000172575. [O95267-4]
ENST00000450598; ENSP00000388540; ENSG00000172575. [O95267-2]
ENST00000558164; ENSP00000454164; ENSG00000172575. [O95267-5]
ENST00000559830; ENSP00000452721; ENSG00000172575. [O95267-3]
GeneIDi10125.
KEGGihsa:10125.
UCSCiuc001zkd.4. human. [O95267-2]
uc001zke.4. human. [O95267-1]
uc010bbf.3. human. [O95267-3]
uc010bbg.3. human. [O95267-5]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF081195 mRNA. Translation: AAC79699.1 .
AF081197 mRNA. Translation: AAF21898.1 .
AF106071 mRNA. Translation: AAC97349.1 .
AY634315 mRNA. Translation: AAT47482.2 .
AY858556 mRNA. Translation: AAW32406.2 .
AY954625 mRNA. Translation: AAX54699.4 .
AY966005 mRNA. Translation: AAX76907.1 .
BC067298 mRNA. Translation: AAH67298.1 . Sequence problems.
BC109296 mRNA. Translation: AAI09297.1 .
BC109297 mRNA. Translation: AAI09298.1 .
AB208848 mRNA. Translation: BAD92085.1 .
CCDSi CCDS45221.1. [O95267-2 ]
CCDS45222.1. [O95267-1 ]
RefSeqi NP_001122074.1. NM_001128602.1. [O95267-2 ]
NP_005730.2. NM_005739.3. [O95267-1 ]
UniGenei Hs.591127.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4L9M X-ray 3.00 A 50-607 [» ]
4L9U X-ray 1.60 A/B 739-793 [» ]
ProteinModelPortali O95267.
SMRi O95267. Positions 53-593, 745-793.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115429. 5 interactions.
IntActi O95267. 1 interaction.
MINTi MINT-7970969.

Chemistry

ChEMBLi CHEMBL5953.

PTM databases

PhosphoSitei O95267.

Proteomic databases

MaxQBi O95267.
PaxDbi O95267.
PRIDEi O95267.

Protocols and materials databases

DNASUi 10125.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000310803 ; ENSP00000310244 ; ENSG00000172575 . [O95267-1 ]
ENST00000414708 ; ENSP00000413105 ; ENSG00000172575 . [O95267-4 ]
ENST00000450598 ; ENSP00000388540 ; ENSG00000172575 . [O95267-2 ]
ENST00000558164 ; ENSP00000454164 ; ENSG00000172575 . [O95267-5 ]
ENST00000559830 ; ENSP00000452721 ; ENSG00000172575 . [O95267-3 ]
GeneIDi 10125.
KEGGi hsa:10125.
UCSCi uc001zkd.4. human. [O95267-2 ]
uc001zke.4. human. [O95267-1 ]
uc010bbf.3. human. [O95267-3 ]
uc010bbg.3. human. [O95267-5 ]

Organism-specific databases

CTDi 10125.
GeneCardsi GC15M038780.
H-InvDB HIX0038076.
HGNCi HGNC:9878. RASGRP1.
MIMi 152700. phenotype.
603962. gene.
neXtProti NX_O95267.
PharmGKBi PA34240.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG256085.
HOVERGENi HBG007513.
InParanoidi O95267.
KOi K04350.
OrthoDBi EOG72G16V.
PhylomeDBi O95267.
TreeFami TF312918.

Enzyme and pathway databases

Reactomei REACT_118778. Activation of RAS in B cells.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_163994. FCERI mediated NF-kB activation.
REACT_2202. Effects of PIP2 hydrolysis.
REACT_23898. Rap1 signalling.

Miscellaneous databases

GeneWikii RASGRP1.
GenomeRNAii 10125.
NextBioi 38299.
PROi O95267.
SOURCEi Search...

Gene expression databases

ArrayExpressi O95267.
Bgeei O95267.
Genevestigatori O95267.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
1.10.840.10. 1 hit.
InterProi IPR020454. DAG/PE-bd.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000651. Ras-like_Gua-exchang_fac_N.
IPR023578. Ras_GEF_dom.
IPR001895. RasGRF_CDC25.
[Graphical view ]
Pfami PF00130. C1_1. 1 hit.
PF13405. EF-hand_6. 1 hit.
PF00617. RasGEF. 1 hit.
PF00618. RasGEF_N. 1 hit.
[Graphical view ]
PRINTSi PR00008. DAGPEDOMAIN.
SMARTi SM00109. C1. 1 hit.
SM00147. RasGEF. 1 hit.
SM00229. RasGEFN. 1 hit.
[Graphical view ]
SUPFAMi SSF48366. SSF48366. 1 hit.
PROSITEi PS00018. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Frontal cortex.
  2. "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] (ISOFORM 1).
    Tissue: T-cell.
  3. "Defective expression of ras guanyl nucleotide-releasing protein 1 in a subset of patients with systemic lupus erythematosus."
    Yasuda S., Stevens R.L., Terada T., Takeda M., Hashimoto T., Fukae J., Horita T., Kataoka H., Atsumi T., Koike T.
    J. Immunol. 179:4890-4900(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), INVOLVEMENT IN SYSTEMIC LUPUS ERYTHEMATOSUS, TISSUE SPECIFICITY.
    Tissue: Peripheral blood.
  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] (ISOFORM 1).
    Tissue: Testis.
  5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 233-797 (ISOFORM 2).
    Tissue: Brain.
  6. "RasGRP links T-cell receptor signaling to Ras."
    Ebinu J.O., Stang S.L., Teixeira C., Bottorff D.A., Hooton J., Blumberg P.M., Barry M., Bleakley R.C., Ostergaard H.L., Stone J.C.
    Blood 95:3199-3203(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN T-CELL RECEPTOR SIGNALING, TOPOLOGY, TISSUE SPECIFICITY.
  7. "Diacylglycerol kinase zeta regulates Ras activation by a novel mechanism."
    Topham M.K., Prescott S.M.
    J. Cell Biol. 152:1135-1143(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH DGKZ AND HRAS, ENZYME REGULATION.
  8. "Expression of a catalytically inactive form of diacylglycerol kinase alpha induces sustained signaling through RasGRP."
    Jones D.R., Sanjuan M.A., Stone J.C., Merida I.
    FASEB J. 16:595-597(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  9. "Vav mediates Ras stimulation by direct activation of the GDP/GTP exchange factor Ras GRP1."
    Caloca M.J., Zugaza J.L., Matallanas D., Crespo P., Bustelo X.R.
    EMBO J. 22:3326-3336(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN B-CELLS, SUBCELLULAR LOCATION, INTERACTION WITH F-ACTIN, ENZYME REGULATION.
  10. "Exchange factors of the RasGRP family mediate Ras activation in the Golgi."
    Caloca M.J., Zugaza J.L., Bustelo X.R.
    J. Biol. Chem. 278:33465-33473(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-549.
  11. Cited for: FUNCTION, MUTAGENESIS OF ARG-271.
  12. "Ras activation in Jurkat T cells following low-grade stimulation of the T-cell receptor is specific to N-Ras and occurs only on the Golgi apparatus."
    Perez de Castro I., Bivona T.G., Philips M.R., Pellicer A.
    Mol. Cell. Biol. 24:3485-3496(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. "Inverted signaling hierarchy between RAS and RAC in T-lymphocytes."
    Zugaza J.L., Caloca M.J., Bustelo X.R.
    Oncogene 23:5823-5833(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  14. "Phosphorylation of RasGRP3 on threonine 133 provides a mechanistic link between PKC and Ras signaling systems in B cells."
    Zheng Y., Liu H., Coughlin J.J., Zheng J., Li L., Stone J.C.
    Blood 105:3648-3654(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-184 BY PKC.
  15. "A diacylglycerol-protein kinase C-RasGRP1 pathway directs Ras activation upon antigen receptor stimulation of T cells."
    Roose J.P., Mollenauer M., Gupta V.A., Stone J.C., Weiss A.
    Mol. Cell. Biol. 25:4426-4441(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-184.
  16. "SKAP55 modulates T cell antigen receptor-induced activation of the Ras-Erk-AP1 pathway by binding RasGRP1."
    Kosco K.A., Cerignoli F., Williams S., Abraham R.T., Mustelin T.
    Mol. Immunol. 45:510-522(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SKAP1.

Entry informationi

Entry nameiGRP1_HUMAN
AccessioniPrimary (citable) accession number: O95267
Secondary accession number(s): Q56CZ0
, Q58G75, Q59HB1, Q5I3A8, Q6GV31, Q6NX39, Q7LDG6, Q9UI94, Q9UNN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: September 3, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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