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Protein

RAS guanyl-releasing protein 1

Gene

RASGRP1

Organism
Homo sapiens (Human)
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 (PubMed:15899849, PubMed:23908768). Activates the Erk/MAP kinase cascade (PubMed:15899849). Regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras (PubMed:10807788, PubMed:12839994). Regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways (PubMed:19933860). Functions in mast cell degranulation and cytokine secretion, regulating FcERI-evoked allergic responses (By similarity). May also function in differentiation of other cell types (PubMed:12845332).By similarity9 Publications

Enzyme regulationi

Autoinhibited. Activated by diacylglycerol and calcium binding, which induces a conformational change releasing the autoinhibitory state (PubMed:23908768). Regulated by DGKA (PubMed:11919165). Regulated by DGKZ (PubMed:11257115). Regulated by PLC gamma and F-actin polymerization (PubMed:12839994).4 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi483 – 494PROSITE-ProRule annotationAdd BLAST12
Zinc fingeri541 – 591Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST51

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • diacylglycerol binding Source: UniProtKB
  • guanyl-nucleotide exchange factor activity Source: Reactome
  • lipid binding Source: ProtInc
  • phosphatidylcholine binding Source: UniProtKB
  • phosphatidylserine binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • Ras guanyl-nucleotide exchange factor activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

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

BioCyciZFISH:ENSG00000172575-MONOMER.
ReactomeiR-HSA-114508. Effects of PIP2 hydrolysis.
R-HSA-1169092. Activation of RAS in B cells.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-354192. Integrin alphaIIb beta3 signaling.
R-HSA-392517. Rap1 signalling.
R-HSA-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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:9878. RASGRP1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • Golgi apparatus Source: CACAO
  • Golgi membrane Source: UniProtKB-SubCell
  • mast cell granule Source: GOC
  • membrane Source: ProtInc
  • 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)1 Publication
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.
Disease descriptionA 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.
See also OMIM:152700

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi271R → E: Loss of function; prevents Ras activation. 2 Publications1
Mutagenesisi483 – 487DHDQD → AHAQA: Decrease of Ras activation indicated by decrease of ERK phosphorylation. 1 Publication5
Mutagenesisi494E → A: Decrease of Ras activation indicated by decrease of ERK phosphorylation. 1 Publication1
Mutagenesisi506F → D: Increase of Ras activation indicated by increase of ERK phosphorylation. 1 Publication1
Mutagenesisi508V → D: Increase of Ras activation indicated by increase of ERK phosphorylation. 1 Publication1
Mutagenesisi549Y → F: Loss of localization to the endoplasmic reticulum and the Golgi apparatus. 1 Publication1

Keywords - Diseasei

Systemic lupus erythematosus

Organism-specific databases

DisGeNETi10125.
MIMi152700. phenotype.
OpenTargetsiENSG00000172575.
PharmGKBiPA34240.

Chemistry databases

ChEMBLiCHEMBL5953.

Polymorphism and mutation databases

BioMutaiRASGRP1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003169781 – 797RAS guanyl-releasing protein 1Add BLAST797

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei184Phosphothreonine; by PKC2 Publications1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO95267.
PaxDbiO95267.
PeptideAtlasiO95267.
PRIDEiO95267.

PTM databases

iPTMnetiO95267.
PhosphoSitePlusiO95267.

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). Expressed in NK cells (at protein level) (PubMed:19933860).4 Publications

Developmental stagei

Expressed in fetal brain and kidney.1 Publication

Gene expression databases

BgeeiENSG00000172575.
ExpressionAtlasiO95267. baseline and differential.
GenevisibleiO95267. HS.

Organism-specific databases

HPAiCAB009204.

Interactioni

Subunit structurei

Homodimer (PubMed:23908768). Forms a signaling complex with DGKZ and HRAS (PubMed:11257115). Interacts with F-actin (PubMed:12839994). Interacts with SKAP1 (PubMed:17658605).4 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi115429. 5 interactors.
IntActiO95267. 1 interactor.
MINTiMINT-7970969.
STRINGi9606.ENSP00000310244.

Chemistry databases

BindingDBiO95267.

Structurei

Secondary structure

1797
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi62 – 71Combined sources10
Helixi84 – 92Combined sources9
Helixi93 – 95Combined sources3
Helixi99 – 115Combined sources17
Helixi119 – 135Combined sources17
Helixi138 – 142Combined sources5
Helixi144 – 160Combined sources17
Helixi164 – 168Combined sources5
Helixi172 – 179Combined sources8
Beta strandi201 – 203Combined sources3
Helixi206 – 222Combined sources17
Helixi226 – 234Combined sources9
Helixi242 – 264Combined sources23
Turni267 – 269Combined sources3
Helixi270 – 287Combined sources18
Helixi291 – 301Combined sources11
Helixi304 – 307Combined sources4
Helixi310 – 315Combined sources6
Helixi318 – 331Combined sources14
Turni335 – 337Combined sources3
Helixi338 – 345Combined sources8
Helixi355 – 368Combined sources14
Beta strandi376 – 378Combined sources3
Helixi380 – 395Combined sources16
Helixi396 – 398Combined sources3
Helixi407 – 416Combined sources10
Helixi423 – 433Combined sources11
Helixi464 – 482Combined sources19
Helixi492 – 500Combined sources9
Helixi519 – 533Combined sources15
Beta strandi544 – 547Combined sources4
Turni556 – 558Combined sources3
Beta strandi564 – 566Combined sources3
Beta strandi569 – 572Combined sources4
Turni573 – 575Combined sources3
Turni581 – 583Combined sources3
Beta strandi584 – 586Combined sources3
Helixi748 – 782Combined sources35
Turni783 – 785Combined sources3
Helixi788 – 791Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4L9MX-ray3.00A50-607[»]
4L9UX-ray1.60A/B739-793[»]
ProteinModelPortaliO95267.
SMRiO95267.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini53 – 176N-terminal Ras-GEFPROSITE-ProRule annotationAdd BLAST124
Domaini205 – 436Ras-GEFPROSITE-ProRule annotationAdd BLAST232
Domaini470 – 505EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini497 – 532EF-hand 2PROSITE-ProRule annotationAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni57 – 110Ras exchanger motif region; required for transforming activityBy similarityAdd BLAST54
Regioni686 – 694Suppress the PT region-mediated translocation to plasma membraneBy similarity9
Regioni718 – 797PT region; mediates the BCR-dependent translocation to plasma membraneBy similarityAdd BLAST80

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili746 – 786Sequence analysisAdd BLAST41

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.1 Publication

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)DescriptionActionsGraphical viewLength
Zinc fingeri541 – 591Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST51

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IQ6J. Eukaryota.
ENOG410ZKZ2. LUCA.
GeneTreeiENSGT00850000132267.
HOVERGENiHBG007513.
InParanoidiO95267.
KOiK04350.
PhylomeDBiO95267.
TreeFamiTF312918.

Family and domain databases

CDDicd00029. C1. 1 hit.
cd00155. RasGEF. 1 hit.
cd06224. REM. 1 hit.
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.
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]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

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

        10         20         30         40         50
MGTLGKAREA PRKPSHGCRA ASKARLEAKP ANSPFPSHPS LAHITQFRMM
60 70 80 90 100
VSLGHLAKGA SLDDLIDSCI QSFDADGNLC RSNQLLQVML TMHRIVISSA
110 120 130 140 150
ELLQKVITLY KDALAKNSPG LCLKICYFVR YWITEFWVMF KMDASLTDTM
160 170 180 190 200
EEFQELVKAK GEELHCRLID TTQINARDWS RKLTQRIKSN TSKKRKVSLL
210 220 230 240 250
FDHLEPEELS EHLTYLEFKS FRRISFSDYQ NYLVNSCVKE NPTMERSIAL
260 270 280 290 300
CNGISQWVQL MVLSRPTPQL RAEVFIKFIQ VAQKLHQLQN FNTLMAVIGG
310 320 330 340 350
LCHSSISRLK ETSSHVPHEI NKVLGEMTEL LSSSRNYDNY RRAYGECTDF
360 370 380 390 400
KIPILGVHLK DLISLYEAMP DYLEDGKVNV HKLLALYNHI SELVQLQEVA
410 420 430 440 450
PPLEANKDLV HLLTLSLDLY YTEDEIYELS YAREPRNHRA PPLTPSKPPV
460 470 480 490 500
VVDWASGVSP KPDPKTISKH VQRMVDSVFK NYDHDQDGYI SQEEFEKIAA
510 520 530 540 550
SFPFSFCVMD KDREGLISRD EITAYFMRAS SIYSKLGLGF PHNFQETTYL
560 570 580 590 600
KPTFCDNCAG FLWGVIKQGY RCKDCGMNCH KQCKDLVVFE CKKRAKNPVA
610 620 630 640 650
PTENNTSVGP VSNLCSLGAK DLLHAPEEGP FTFPNGEAVE HGEESKDRTI
660 670 680 690 700
MLMGVSSQKI SLRLKRAVAH KATQTESQPW IGSEGPSGPF VLSSPRKTAQ
710 720 730 740 750
DTLYVLPSPT SPCPSPVLVR KRAFVKWENK DSLIKSKEEL RHLRLPTYQE
760 770 780 790
LEQEINTLKA DNDALKIQLK YAQKKIESLQ LEKSNHVLAQ MEQGDCS
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 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti374E → G in AAC79699 (PubMed:9789079).Curated1
Sequence conflicti374E → G in AAF21898 (PubMed:9789079).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_030836442 – 476Missing in isoform 2, isoform 3, isoform 4 and isoform 5. 2 PublicationsAdd BLAST35
Alternative sequenceiVSP_030837513 – 516REGL → SSGE in isoform 4. 1 Publication4
Alternative sequenceiVSP_030838517 – 797Missing in isoform 4. 1 PublicationAdd BLAST281
Alternative sequenceiVSP_030839574 – 581DCGMNCHK → GNKYSESR in isoform 5. 1 Publication8
Alternative sequenceiVSP_030840582 – 797Missing in isoform 5. 1 PublicationAdd BLAST216
Alternative sequenceiVSP_030841625 – 632APEEGPFT → GNKYSESR in isoform 3. 1 Publication8
Alternative sequenceiVSP_030842633 – 797Missing in isoform 3. 1 PublicationAdd BLAST165

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS76733.1. [O95267-3]
RefSeqiNP_001122074.1. NM_001128602.1. [O95267-2]
NP_001293015.1. NM_001306086.1. [O95267-3]
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.5. human. [O95267-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS76733.1. [O95267-3]
RefSeqiNP_001122074.1. NM_001128602.1. [O95267-2]
NP_001293015.1. NM_001306086.1. [O95267-3]
NP_005730.2. NM_005739.3. [O95267-1]
UniGeneiHs.591127.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4L9MX-ray3.00A50-607[»]
4L9UX-ray1.60A/B739-793[»]
ProteinModelPortaliO95267.
SMRiO95267.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115429. 5 interactors.
IntActiO95267. 1 interactor.
MINTiMINT-7970969.
STRINGi9606.ENSP00000310244.

Chemistry databases

BindingDBiO95267.
ChEMBLiCHEMBL5953.

PTM databases

iPTMnetiO95267.
PhosphoSitePlusiO95267.

Polymorphism and mutation databases

BioMutaiRASGRP1.

Proteomic databases

MaxQBiO95267.
PaxDbiO95267.
PeptideAtlasiO95267.
PRIDEiO95267.

Protocols and materials databases

DNASUi10125.
Structural Biology KnowledgebaseSearch...

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.5. human. [O95267-1]

Organism-specific databases

CTDi10125.
DisGeNETi10125.
GeneCardsiRASGRP1.
H-InvDBHIX0038076.
HGNCiHGNC:9878. RASGRP1.
HPAiCAB009204.
MIMi152700. phenotype.
603962. gene.
neXtProtiNX_O95267.
OpenTargetsiENSG00000172575.
PharmGKBiPA34240.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IQ6J. Eukaryota.
ENOG410ZKZ2. LUCA.
GeneTreeiENSGT00850000132267.
HOVERGENiHBG007513.
InParanoidiO95267.
KOiK04350.
PhylomeDBiO95267.
TreeFamiTF312918.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000172575-MONOMER.
ReactomeiR-HSA-114508. Effects of PIP2 hydrolysis.
R-HSA-1169092. Activation of RAS in B cells.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-354192. Integrin alphaIIb beta3 signaling.
R-HSA-392517. Rap1 signalling.
R-HSA-5673001. RAF/MAP kinase cascade.

Miscellaneous databases

GeneWikiiRASGRP1.
GenomeRNAii10125.
PROiO95267.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000172575.
ExpressionAtlasiO95267. baseline and differential.
GenevisibleiO95267. HS.

Family and domain databases

CDDicd00029. C1. 1 hit.
cd00155. RasGEF. 1 hit.
cd06224. REM. 1 hit.
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.
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...

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: November 30, 2016
This is version 140 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

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.