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Protein

RAS guanyl-releasing protein 2

Gene

Rasgrp2

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 DAG-regulated nucleotide exchange factor specifically activating Rap through the exchange of bound GDP for GTP. May also activates other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. Functions in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation. May function in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway.9 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi439 – 450121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi468 – 479122PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri498 – 54851Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. guanyl-nucleotide exchange factor activity Source: MGI

GO - Biological processi

  1. cellular response to calcium ion Source: MGI
  2. positive regulation of Rap GTPase activity Source: MGI
  3. small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_219232. Effects of PIP2 hydrolysis.
REACT_237855. Rap1 signalling.
REACT_246176. Integrin alphaIIb beta3 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
RAS guanyl-releasing protein 2
Alternative name(s):
Calcium and DAG-regulated guanine nucleotide exchange factor I
Short name:
CalDAG-GEFI
F25B3.3 kinase-like protein
Gene namesi
Name:Rasgrp2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:1333849. Rasgrp2.

Subcellular locationi

Cytoplasmcytosol By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity. Cell junctionsynapsesynaptosome By similarity. Cell projectionruffle membrane Curated; Peripheral membrane protein Curated
Note: Found both in the cytosol and associated with membranes. Enriched at juxtamembrane areas and membrane ruffles. Localizes to the cell bodies and axons of striatal neurons.By similarity

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cytosol Source: UniProtKB
  3. neuron projection Source: UniProtKB-SubCell
  4. plasma membrane Source: UniProtKB
  5. ruffle membrane Source: UniProtKB-SubCell
  6. synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Synapse, Synaptosome

Pathology & Biotechi

Disruption phenotypei

Mice have a combination of defects in leukocytes and platelet functions which are reminiscent of the human leukocyte adhesion deficiency type III syndrome (LAD3). They display bleeding diathesis due to a defect in platelet aggregation and are resistant to collagen-induced thrombosis. In parallel, they also display impaired response to acute inflammation associated with defects in beta-1 and beta-2 integrin-mediated adhesion of neutrophils.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 608608RAS guanyl-releasing protein 2PRO_0000315609Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei116 – 1161Phosphoserine1 Publication
Modified residuei117 – 1171Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9QUG9.
PaxDbiQ9QUG9.
PRIDEiQ9QUG9.

PTM databases

PhosphoSiteiQ9QUG9.

Expressioni

Tissue specificityi

Detected in megakaryocytes, platelet and neutrophils but not in lymphocytes (at protein level). Isoform 1 and isoform 3 are detected in brain basal glanglia, heart, lung, spleen, liver and kidney interstitial cells.3 Publications

Developmental stagei

Expressed in embryo with higher expression between E15 and E17.1 Publication

Gene expression databases

BgeeiQ9QUG9.
CleanExiMM_RASGRP2.
ExpressionAtlasiQ9QUG9. baseline and differential.
GenevestigatoriQ9QUG9.

Interactioni

Subunit structurei

Forms a signaling complex with RAP1 and BRAF. Interacts with F-actin (By similarity). Interacts with RAP1.By similarity1 Publication

Protein-protein interaction databases

IntActiQ9QUG9. 1 interaction.
MINTiMINT-4130449.

Structurei

3D structure databases

ProteinModelPortaliQ9QUG9.
SMRiQ9QUG9. Positions 7-550.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 126123N-terminal Ras-GEFPROSITE-ProRule annotationAdd
BLAST
Domaini154 – 387234Ras-GEFPROSITE-ProRule annotationAdd
BLAST
Domaini426 – 46136EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini455 – 49036EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Domaini

The N-terminal Ras-GEF domain mediates association with F-actin.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 fingeri498 – 54851Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG256085.
GeneTreeiENSGT00780000121847.
HOGENOMiHOG000293171.
HOVERGENiHBG007513.
InParanoidiQ9QUG9.
KOiK12361.
OMAiFPYLSAF.
OrthoDBiEOG72G16V.
PhylomeDBiQ9QUG9.
TreeFamiTF312918.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.840.10. 1 hit.
InterProiIPR011992. 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.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF13202. EF-hand_5. 2 hits.
PF00617. RasGEF. 1 hit.
PF00618. RasGEF_N. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 1 hit.
SM00054. EFh. 2 hits.
SM00147. RasGEF. 1 hit.
SM00229. RasGEFN. 1 hit.
[Graphical view]
SUPFAMiSSF48366. SSF48366. 1 hit.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9QUG9-1) [UniParc]FASTAAdd to basket

Also known as: CalDAG-GEF1a

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
MTSTLDLDKG CTVEELLRGC IEAFDDSGKV RDPQLVRMFL MMHPWYIPSS
60 70 80 90 100
QLASKLLHFY QQSRKDNSNS LQMKTCHLVR YWISAFPAEF DLNPELAEQI
110 120 130 140 150
KELKALLDQE GNRRHSSLID IESVPTYKWK RQVTQRNPVE QKKRKMSLLF
160 170 180 190 200
DHLEPMELAE HLTYLEYRSF CKILFQDYHS FVTHGCTVDN PVLERFISLF
210 220 230 240 250
NSVSQWVQLM ILSKPTATQR ALVITHFVHV AERLLQLQNF NTLMAVVGGL
260 270 280 290 300
SHSSISRLKE THSHVSPDTI KLWEGLTELV TATGNYSNYR RRLAACVGFR
310 320 330 340 350
FPILGVHLKD LVALQLALPD WLDPGRTRLN GAKMRQLFCI LEELAMVTSL
360 370 380 390 400
RPPVQANPDL LSLLTVSLDQ YQTEDELYQL SLQREPRSKS SPTSPTSCTP
410 420 430 440 450
PPRPPVLEEW TSVAKPKLDQ ALVAEHIEKM VESVFRNFDV DGDGHISQEE
460 470 480 490 500
FQIIRGNFPY LSAFGDLDQN QDGCISREEM ISYFLRSSSV LGGRMGFVHN
510 520 530 540 550
FQESNSLRPV ACRHCKALIL GIYKQGLKCR ACGVNCHKQC KERLSVECRR
560 570 580 590 600
RAQSVSLEGS APSPSPTHTH HRAFSFSLPR PGRRSSRPPE IREEEVQSVE

DGVFDIHL
Length:608
Mass (Da):69,446
Last modified:January 15, 2008 - v2
Checksum:i1E6F768EF00B0468
GO
Isoform 2 (identifier: Q9QUG9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     472-608: Missing.

Note: No experimental confirmation available.

Show »
Length:471
Mass (Da):54,054
Checksum:i3C2F75238F062E1A
GO
Isoform 3 (identifier: Q9QUG9-3) [UniParc]FASTAAdd to basket

Also known as: CalDAG-GEF1b

The sequence of this isoform differs from the canonical sequence as follows:
     125-141: PTYKWKRQVTQRNPVEQ → CVGAERKGHYACYTICA
     142-608: Missing.

Note: The corresponding protein is not undetectable.

Show »
Length:141
Mass (Da):16,187
Checksum:i242C314B00AD9191
GO

Sequence cautioni

The sequence BAC28797.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21T → A in AAC79697 (PubMed:9789079).Curated
Sequence conflicti2 – 21T → A in AAD12742 (PubMed:9789079).Curated
Sequence conflicti73 – 731M → V in AAC79697 (PubMed:9789079).Curated
Sequence conflicti73 – 731M → V in AAD12742 (PubMed:9789079).Curated
Sequence conflicti83 – 831I → V in AAC79697 (PubMed:9789079).Curated
Sequence conflicti83 – 831I → V in AAD12742 (PubMed:9789079).Curated
Sequence conflicti99 – 991Q → P in AAC79697 (PubMed:9789079).Curated
Sequence conflicti99 – 991Q → P in AAD12742 (PubMed:9789079).Curated
Sequence conflicti233 – 2331R → K in AAC79697 (PubMed:9789079).Curated
Sequence conflicti233 – 2331R → K in AAD12742 (PubMed:9789079).Curated
Sequence conflicti339 – 3391C → S in AAC79697 (PubMed:9789079).Curated
Sequence conflicti339 – 3391C → S in AAD12742 (PubMed:9789079).Curated
Sequence conflicti542 – 5421E → D in AAC79697 (PubMed:9789079).Curated
Sequence conflicti542 – 5421E → D in AAD12742 (PubMed:9789079).Curated
Sequence conflicti598 – 5981S → T in AAC79697 (PubMed:9789079).Curated
Sequence conflicti598 – 5981S → T in AAD12742 (PubMed:9789079).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei125 – 14117PTYKW…NPVEQ → CVGAERKGHYACYTICA in isoform 3. 1 PublicationVSP_030577Add
BLAST
Alternative sequencei142 – 608467Missing in isoform 3. 1 PublicationVSP_030578Add
BLAST
Alternative sequencei472 – 608137Missing in isoform 2. 1 PublicationVSP_030579Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF081193 mRNA. Translation: AAC79697.1.
U78171 mRNA. Translation: AAD12742.1.
BC051474 mRNA. Translation: AAH51474.1.
AK034683 mRNA. Translation: BAC28797.1. Different initiation.
Y12339 mRNA. Translation: CAA73008.1.
CCDSiCCDS37898.1. [Q9QUG9-1]
RefSeqiNP_035372.2. NM_011242.2. [Q9QUG9-1]
XP_006531748.1. XM_006531685.1. [Q9QUG9-1]
XP_006531749.1. XM_006531686.1. [Q9QUG9-1]
XP_006531750.1. XM_006531687.1. [Q9QUG9-1]
XP_006531751.1. XM_006531688.1. [Q9QUG9-1]
XP_006531752.1. XM_006531689.1. [Q9QUG9-1]
XP_006531753.1. XM_006531690.1. [Q9QUG9-1]
XP_006531754.1. XM_006531691.1. [Q9QUG9-1]
UniGeneiMm.77017.

Genome annotation databases

EnsembliENSMUST00000035716; ENSMUSP00000041135; ENSMUSG00000032946. [Q9QUG9-1]
ENSMUST00000113471; ENSMUSP00000109099; ENSMUSG00000032946. [Q9QUG9-3]
ENSMUST00000113472; ENSMUSP00000109100; ENSMUSG00000032946. [Q9QUG9-3]
ENSMUST00000113475; ENSMUSP00000109103; ENSMUSG00000032946. [Q9QUG9-3]
ENSMUST00000113476; ENSMUSP00000109104; ENSMUSG00000032946. [Q9QUG9-1]
ENSMUST00000167240; ENSMUSP00000129873; ENSMUSG00000032946. [Q9QUG9-1]
GeneIDi19395.
KEGGimmu:19395.
UCSCiuc008gip.1. mouse. [Q9QUG9-1]
uc008gir.1. mouse. [Q9QUG9-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF081193 mRNA. Translation: AAC79697.1.
U78171 mRNA. Translation: AAD12742.1.
BC051474 mRNA. Translation: AAH51474.1.
AK034683 mRNA. Translation: BAC28797.1. Different initiation.
Y12339 mRNA. Translation: CAA73008.1.
CCDSiCCDS37898.1. [Q9QUG9-1]
RefSeqiNP_035372.2. NM_011242.2. [Q9QUG9-1]
XP_006531748.1. XM_006531685.1. [Q9QUG9-1]
XP_006531749.1. XM_006531686.1. [Q9QUG9-1]
XP_006531750.1. XM_006531687.1. [Q9QUG9-1]
XP_006531751.1. XM_006531688.1. [Q9QUG9-1]
XP_006531752.1. XM_006531689.1. [Q9QUG9-1]
XP_006531753.1. XM_006531690.1. [Q9QUG9-1]
XP_006531754.1. XM_006531691.1. [Q9QUG9-1]
UniGeneiMm.77017.

3D structure databases

ProteinModelPortaliQ9QUG9.
SMRiQ9QUG9. Positions 7-550.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9QUG9. 1 interaction.
MINTiMINT-4130449.

PTM databases

PhosphoSiteiQ9QUG9.

Proteomic databases

MaxQBiQ9QUG9.
PaxDbiQ9QUG9.
PRIDEiQ9QUG9.

Protocols and materials databases

DNASUi19395.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035716; ENSMUSP00000041135; ENSMUSG00000032946. [Q9QUG9-1]
ENSMUST00000113471; ENSMUSP00000109099; ENSMUSG00000032946. [Q9QUG9-3]
ENSMUST00000113472; ENSMUSP00000109100; ENSMUSG00000032946. [Q9QUG9-3]
ENSMUST00000113475; ENSMUSP00000109103; ENSMUSG00000032946. [Q9QUG9-3]
ENSMUST00000113476; ENSMUSP00000109104; ENSMUSG00000032946. [Q9QUG9-1]
ENSMUST00000167240; ENSMUSP00000129873; ENSMUSG00000032946. [Q9QUG9-1]
GeneIDi19395.
KEGGimmu:19395.
UCSCiuc008gip.1. mouse. [Q9QUG9-1]
uc008gir.1. mouse. [Q9QUG9-2]

Organism-specific databases

CTDi10235.
MGIiMGI:1333849. Rasgrp2.

Phylogenomic databases

eggNOGiNOG256085.
GeneTreeiENSGT00780000121847.
HOGENOMiHOG000293171.
HOVERGENiHBG007513.
InParanoidiQ9QUG9.
KOiK12361.
OMAiFPYLSAF.
OrthoDBiEOG72G16V.
PhylomeDBiQ9QUG9.
TreeFamiTF312918.

Enzyme and pathway databases

ReactomeiREACT_219232. Effects of PIP2 hydrolysis.
REACT_237855. Rap1 signalling.
REACT_246176. Integrin alphaIIb beta3 signaling.

Miscellaneous databases

NextBioi296505.
PROiQ9QUG9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QUG9.
CleanExiMM_RASGRP2.
ExpressionAtlasiQ9QUG9. baseline and differential.
GenevestigatoriQ9QUG9.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.840.10. 1 hit.
InterProiIPR011992. 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.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF13202. EF-hand_5. 2 hits.
PF00617. RasGEF. 1 hit.
PF00618. RasGEF_N. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 1 hit.
SM00054. EFh. 2 hits.
SM00147. RasGEF. 1 hit.
SM00229. RasGEFN. 1 hit.
[Graphical view]
SUPFAMiSSF48366. SSF48366. 1 hit.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS A RAP ACTIVATOR.
  2. "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 3).
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  3. "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] OF 204-608 (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Embryo.
  4. "The germinal centre kinase gene and a novel CDC25-like gene are located in the vicinity of the PYGM gene on 11q13."
    Kedra D., Seroussi E., Fransson I., Trifunovic J., Clark M., Lagercrantz J., Blennow E., Mehlin H., Dumanski J.
    Hum. Genet. 100:611-619(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 349-608 (ISOFORM 1).
  5. Cited for: FUNCTION.
  6. Cited for: TISSUE SPECIFICITY.
  7. Cited for: FUNCTION AS RAP2 ACTIVATOR.
  8. "Requirement for C3G-dependent Rap1 activation for cell adhesion and embryogenesis."
    Ohba Y., Ikuta K., Ogura A., Matsuda J., Mochizuki N., Nagashima K., Kurokawa K., Mayer B.J., Maki K., Miyazaki J., Matsuda M.
    EMBO J. 20:3333-3341(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Activation of the Rap1 guanine nucleotide exchange gene, CalDAG-GEF I, in BXH-2 murine myeloid leukemia."
    Dupuy A.J., Morgan K., von Lintig F.C., Shen H., Acar H., Hasz D.E., Jenkins N.A., Copeland N.G., Boss G.R., Largaespada D.A.
    J. Biol. Chem. 276:11804-11811(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  10. "Megakaryocytes derived from embryonic stem cells implicate CalDAG-GEFI in integrin signaling."
    Eto K., Murphy R., Kerrigan S.W., Bertoni A., Stuhlmann H., Nakano T., Leavitt A.D., Shattil S.J.
    Proc. Natl. Acad. Sci. U.S.A. 99:12819-12824(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "CalDAG-GEFI integrates signaling for platelet aggregation and thrombus formation."
    Crittenden J.R., Bergmeier W., Zhang Y., Piffath C.L., Liang Y., Wagner D.D., Housman D.E., Graybiel A.M.
    Nat. Med. 10:982-986(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PLATELET AGGREGATION, DISRUPTION PHENOTYPE, INTERACTION WITH RAP1, TISSUE SPECIFICITY.
  12. "The small GTPase Rap1b regulates the cross talk between platelet integrin alpha2beta1 and integrin alphaIIbbeta3."
    Bernardi B., Guidetti G.F., Campus F., Crittenden J.R., Graybiel A.M., Balduini C., Torti M.
    Blood 107:2728-2735(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Mice lacking the signaling molecule CalDAG-GEFI represent a model for leukocyte adhesion deficiency type III."
    Bergmeier W., Goerge T., Wang H.-W., Crittenden J.R., Baldwin A.C.W., Cifuni S.M., Housman D.E., Graybiel A.M., Wagner D.D.
    J. Clin. Invest. 117:1699-1707(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiGRP2_MOUSE
AccessioniPrimary (citable) accession number: Q9QUG9
Secondary accession number(s): O09004, Q80WC0, Q8BSC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: February 4, 2015
This is version 116 of the entry and version 2 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

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 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.