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Protein

Rho guanine nucleotide exchange factor 1

Gene

Arhgef1

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

Functioni

Seems to play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13) subunits. Acts as GTPase-activating protein (GAP) for GNA12 and GNA13, and as guanine nucleotide exchange factor (GEF) for RhoA GTPase. Activated G alpha 13/GNA13 stimulates the RhoGEF activity through interaction with the RGS-like domain. This GEF activity is inhibited by binding to activated GNA12. Mediates angiotensin-2-induced RhoA activation. Isoform 3 and isoform 4 do not homooligomerize and show an enhanced RhoGEF activity.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation, Guanine-nucleotide releasing factor

Enzyme and pathway databases

ReactomeiR-MMU-193634. Axonal growth inhibition (RHOA activation).
R-MMU-416482. G alpha (12/13) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho guanine nucleotide exchange factor 1
Alternative name(s):
Lbc's second cousin
Lymphoid blast crisis-like 2
Gene namesi
Name:Arhgef1
Synonyms:Lbcl2, Lsc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1353510. Arhgef1.

Subcellular locationi

  • Cytoplasm By similarity
  • Membrane By similarity

  • Note: Translocated to the membrane by activated GNA13 or LPA stimulation.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice have reduced response to angiotensin-2 and lowered RhoA signaling pathway.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 920920Rho guanine nucleotide exchange factor 1PRO_0000080907Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei373 – 3731PhosphoserineBy similarity
Modified residuei408 – 4081PhosphoserineBy similarity
Modified residuei694 – 6941PhosphothreonineBy similarity
Modified residuei737 – 7371Phosphotyrosine; by JAK21 Publication
Modified residuei905 – 9051PhosphoserineCombined sources
Isoform 5 (identifier: Q61210-5)
Modified residuei386 – 3861PhosphoserineCombined sources
Modified residuei390 – 3901PhosphoserineCombined sources
Modified residuei412 – 4121PhosphoserineCombined sources
Modified residuei432 – 4321PhosphothreonineCombined sources

Post-translational modificationi

Phosphorylated by PKCA (By similarity). Angiotensin-2 induced Tyr-737 phosphorylation is mediated by JAK2. Isoform 5 is phosphorylated at 'Ser-390'.By similarity1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ61210.
MaxQBiQ61210.
PeptideAtlasiQ61210.
PRIDEiQ61210.

PTM databases

iPTMnetiQ61210.
SwissPalmiQ61210.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ61210.
CleanExiMM_ARHGEF1.
ExpressionAtlasiQ61210. baseline and differential.
GenevisibleiQ61210. MM.

Interactioni

Subunit structurei

Interacts with RHOA, GNA12 and GNA13 (By similarity). Homooligomerizes through the coiled coil region. Interacts with CTNNAL1 (By similarity). May interact with CCPG1.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
VclQ647273EBI-641821,EBI-432047

Protein-protein interaction databases

BioGridi201115. 4 interactions.
IntActiQ61210. 11 interactions.
MINTiMINT-1634426.

Structurei

3D structure databases

ProteinModelPortaliQ61210.
SMRiQ61210. Positions 42-231, 394-760.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 230192RGSLAdd
BLAST
Domaini415 – 604190DHPROSITE-ProRule annotationAdd
BLAST
Domaini646 – 759114PHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili865 – 89430Sequence analysisAdd
BLAST

Domaini

The RGSL domain, also known as rgRGS domain, is necessary but not sufficient for full GAP activity.By similarity
The DH domain is involved in interaction with CCPG1.

Sequence similaritiesi

Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 RGSL (RGS-like) domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00760000119193.
HOGENOMiHOG000034043.
HOVERGENiHBG050565.
InParanoidiQ61210.
KOiK12330.
OMAiFYHSFLD.
PhylomeDBiQ61210.
TreeFamiTF106495.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR000219. DH-domain.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR016137. RGS.
IPR015212. RGS-like_dom.
[Graphical view]
PfamiPF09128. RGS-like. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF48097. SSF48097. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q61210-1) [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
MGEVAGGAAP GPPRSGLVSI IIGAEDEDFE NELEANSEDQ NSQFQSLEQV
60 70 80 90 100
KRRPAHLMAL LQHVALQFEP GPLLCCLHAD MLSSLGPKEA KKAFLDFYHS
110 120 130 140 150
FLEKTAVLRV PVPPSVAFEL DRTRPDLISE DVQRRFIQEV VQSQQAAVSR
160 170 180 190 200
QLEDFRSKRL MGMTPWEQEL SLLEPWIGKD RGNYEARERH VAERLLSHLE
210 220 230 240 250
ETQHTISTDE EKSAAVVTAI SLYMRHLGVR TKSGDKKSGR NFFRKKVMGN
260 270 280 290 300
RRSDEPPKTK KGLSSILDPA RWNRGEPSAP DCRHLKVEAD AEKPGPADRK
310 320 330 340 350
GGLGMSSRDR TVGTPGQDNP GVSLHPLSTD SVDSREPGVD TPQEPGDTPP
360 370 380 390 400
QGPTSLEPLA PPESTEDNGE TESPEPGDDG EPGRSGLELE PEEPPGWREL
410 420 430 440 450
VPPDTLLSLP KSQVKRQEVI SELLVTEAAH VRMLRVLHDL FYQPMADGGF
460 470 480 490 500
FPLDELQNIF PSLDELIEVH SLFLDRLMKR RQESGYLIEE IGDVLLARFD
510 520 530 540 550
GAEGSWFQKI SSRFCSRQSF ALEQLKAKQR KEPRFCAFVQ EAESRPRCRR
560 570 580 590 600
LQLKDMIPTE MQRLTKYPLL LQSIGQNTEE STERGKVELA AECCREILHH
610 620 630 640 650
VNQAVRDMED LLRLKDYQRR LDLTHLRQSS DPMLSEFKNL DITKKKLVHE
660 670 680 690 700
GPLTWRVTKD KAIEVHVLLL DDLLLLLQRQ DERLLLKSHS RTLTPTPDGK
710 720 730 740 750
TMLRPVLRLT SAMTREVATD HKAFYVIFTW DQEAQIYELV AQTSSERKNW
760 770 780 790 800
CNLITETAGS LKVPAPASRL KPRPSPSSIR EPLLSSSENG TGGAEMAPAD
810 820 830 840 850
ARTERLLNDL LPFCRPGPEG QLAATALQKV LSLKQILLST EEDSGAGPPR
860 870 880 890 900
DGDGVPGGRA PGPVHTQEIE ENLLSLEVAI RQLEELEEEF CRLRPLLSQL
910 920
GGTLSPNLAA PERSAQTGLS
Length:920
Mass (Da):102,805
Last modified:August 29, 2003 - v2
Checksum:i913A819972CBACC8
GO
Isoform 2 (identifier: Q61210-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     291-291: Missing.

Show »
Length:919
Mass (Da):102,733
Checksum:i751EBF35E31F38BB
GO
Isoform 3 (identifier: Q61210-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     780-791: REPLLSSSENGT → SHPRGLEQREIG
     792-920: Missing.

Show »
Length:791
Mass (Da):89,294
Checksum:i07126CD40D75A2C1
GO
Isoform 4 (identifier: Q61210-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     830-856: VLSLKQILLSTEEDSGAGPPRDGDGVP → GVGRGILSPKTPPVPAWGDSVPQPGCT
     857-920: Missing.

Show »
Length:856
Mass (Da):95,823
Checksum:i99B42F760C3435C6
GO
Isoform 5 (identifier: Q61210-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     291-291: Missing.
     372-373: ES → ERRWKRLSGRLGRSESLRVSDRRRPSRGSLGAKGRGGGRSRSDVDMDPGSATAVLGPTRRAT

Show »
Length:979
Mass (Da):109,249
Checksum:iFEF62EF944FFABD6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti574 – 5741I → M in AAC36527 (PubMed:9798653).Curated
Sequence conflicti663 – 6631I → T in AAC36527 (PubMed:9798653).Curated
Sequence conflicti689 – 6891H → Y in AAO91659 (PubMed:12773540).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei291 – 2911Missing in isoform 2 and isoform 5. 3 PublicationsVSP_008126
Alternative sequencei372 – 3732ES → ERRWKRLSGRLGRSESLRVS DRRRPSRGSLGAKGRGGGRS RSDVDMDPGSATAVLGPTRR AT in isoform 5. 1 PublicationVSP_026131
Alternative sequencei780 – 79112REPLL…SENGT → SHPRGLEQREIG in isoform 3. 1 PublicationVSP_008127Add
BLAST
Alternative sequencei792 – 920129Missing in isoform 3. 1 PublicationVSP_008128Add
BLAST
Alternative sequencei830 – 85627VLSLK…GDGVP → GVGRGILSPKTPPVPAWGDS VPQPGCT in isoform 4. 1 PublicationVSP_008129Add
BLAST
Alternative sequencei857 – 92064Missing in isoform 4. 1 PublicationVSP_008130Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58203 mRNA. Translation: AAC52693.1.
AF314539 mRNA. Translation: AAG33860.1.
AK157056 mRNA. Translation: BAE33947.1.
AK172354 mRNA. Translation: BAE42963.1.
BC012488 mRNA. Translation: AAH12488.1.
U89421 mRNA. Translation: AAC36527.1.
AY246272 mRNA. Translation: AAO91658.1.
AY246273 mRNA. Translation: AAO91659.1.
CCDSiCCDS52141.1. [Q61210-1]
CCDS52142.1. [Q61210-5]
RefSeqiNP_001123622.1. NM_001130150.1. [Q61210-5]
NP_001123623.1. NM_001130151.1.
NP_001123624.1. NM_001130152.1. [Q61210-1]
NP_001123625.1. NM_001130153.1. [Q61210-1]
NP_032514.1. NM_008488.2. [Q61210-2]
UniGeneiMm.3181.

Genome annotation databases

EnsembliENSMUST00000047873; ENSMUSP00000046469; ENSMUSG00000040940. [Q61210-1]
ENSMUST00000098683; ENSMUSP00000096280; ENSMUSG00000040940. [Q61210-5]
ENSMUST00000117419; ENSMUSP00000113366; ENSMUSG00000040940. [Q61210-1]
ENSMUST00000206508; ENSMUSP00000146314; ENSMUSG00000040940. [Q61210-2]
GeneIDi16801.
KEGGimmu:16801.
UCSCiuc009fqv.2. mouse. [Q61210-2]
uc009fqw.2. mouse. [Q61210-5]
uc009fqy.2. mouse. [Q61210-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58203 mRNA. Translation: AAC52693.1.
AF314539 mRNA. Translation: AAG33860.1.
AK157056 mRNA. Translation: BAE33947.1.
AK172354 mRNA. Translation: BAE42963.1.
BC012488 mRNA. Translation: AAH12488.1.
U89421 mRNA. Translation: AAC36527.1.
AY246272 mRNA. Translation: AAO91658.1.
AY246273 mRNA. Translation: AAO91659.1.
CCDSiCCDS52141.1. [Q61210-1]
CCDS52142.1. [Q61210-5]
RefSeqiNP_001123622.1. NM_001130150.1. [Q61210-5]
NP_001123623.1. NM_001130151.1.
NP_001123624.1. NM_001130152.1. [Q61210-1]
NP_001123625.1. NM_001130153.1. [Q61210-1]
NP_032514.1. NM_008488.2. [Q61210-2]
UniGeneiMm.3181.

3D structure databases

ProteinModelPortaliQ61210.
SMRiQ61210. Positions 42-231, 394-760.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201115. 4 interactions.
IntActiQ61210. 11 interactions.
MINTiMINT-1634426.

PTM databases

iPTMnetiQ61210.
SwissPalmiQ61210.

Proteomic databases

EPDiQ61210.
MaxQBiQ61210.
PeptideAtlasiQ61210.
PRIDEiQ61210.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000047873; ENSMUSP00000046469; ENSMUSG00000040940. [Q61210-1]
ENSMUST00000098683; ENSMUSP00000096280; ENSMUSG00000040940. [Q61210-5]
ENSMUST00000117419; ENSMUSP00000113366; ENSMUSG00000040940. [Q61210-1]
ENSMUST00000206508; ENSMUSP00000146314; ENSMUSG00000040940. [Q61210-2]
GeneIDi16801.
KEGGimmu:16801.
UCSCiuc009fqv.2. mouse. [Q61210-2]
uc009fqw.2. mouse. [Q61210-5]
uc009fqy.2. mouse. [Q61210-1]

Organism-specific databases

CTDi9138.
MGIiMGI:1353510. Arhgef1.

Phylogenomic databases

GeneTreeiENSGT00760000119193.
HOGENOMiHOG000034043.
HOVERGENiHBG050565.
InParanoidiQ61210.
KOiK12330.
OMAiFYHSFLD.
PhylomeDBiQ61210.
TreeFamiTF106495.

Enzyme and pathway databases

ReactomeiR-MMU-193634. Axonal growth inhibition (RHOA activation).
R-MMU-416482. G alpha (12/13) signalling events.

Miscellaneous databases

PROiQ61210.
SOURCEiSearch...

Gene expression databases

BgeeiQ61210.
CleanExiMM_ARHGEF1.
ExpressionAtlasiQ61210. baseline and differential.
GenevisibleiQ61210. MM.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR000219. DH-domain.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR016137. RGS.
IPR015212. RGS-like_dom.
[Graphical view]
PfamiPF09128. RGS-like. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF48097. SSF48097. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expression cloning of lsc, a novel oncogene with structural similarities to the Dbl family of guanine nucleotide exchange factors."
    Whitehead I.P., Khosravi-Far R., Kirk H., Trigo-Gonzalez G., Der C.J., Kay R.
    J. Biol. Chem. 271:18643-18650(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
  2. Lanson N.A. Jr., Egeland D.B., Claycomb W.C.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  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] (ISOFORM 5).
    Strain: NOD.
    Tissue: Spleen.
  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: Mammary tumor.
  5. "Expressed genes in interleukin-4 treated B cells identified by cDNA representational difference analysis."
    Chu C.C., Paul W.E.
    Mol. Immunol. 35:487-502(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 557-720.
    Strain: BALB/cJ.
    Tissue: Spleen.
  6. "The Rho guanine excchange factors Lsc homo-oligomerizes and is negatively regulated through domains in its carboxyl-terminus that are absent in novel splenic isoforms."
    Eisenhaure T.M., Francis S.A., Willison L.D., Coughlin S.R., Lerner D.J.
    J. Biol. Chem. 278:30975-30984(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 670-920 (ISOFORMS 3 AND 4), FUNCTION (ISOFORMS 3 AND 4), SUBUNIT.
    Strain: C57BL/6J.
    Tissue: Spleen.
  7. "Lfc and Lsc oncoproteins represent two new guanine nucleotide exchange factors for the Rho GTP-binding protein."
    Glaven J.A., Whitehead I.P., Nomanbhoy T., Kay R., Cerione R.A.
    J. Biol. Chem. 271:27374-27381(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RHOA.
  8. "Ccpg1, a novel scaffold protein that regulates the activity of the Rho guanine nucleotide exchange factor Dbs."
    Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.
    Mol. Cell. Biol. 26:8964-8975(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INTERACTION WITH CCPG1.
  9. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-390; SER-412 AND THR-432 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-905, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND THR-432 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  11. "The Rho exchange factor Arhgef1 mediates the effects of angiotensin II on vascular tone and blood pressure."
    Guilluy C., Bregeon J., Toumaniantz G., Rolli-Derkinderen M., Retailleau K., Loufrani L., Henrion D., Scalbert E., Bril A., Torres R.M., Offermanns S., Pacaud P., Loirand G.
    Nat. Med. 16:183-190(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT TYR-737.

Entry informationi

Entry nameiARHG1_MOUSE
AccessioniPrimary (citable) accession number: Q61210
Secondary accession number(s): O89074
, Q3T9Q7, Q80YE8, Q80YE9, Q91VL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: August 29, 2003
Last modified: July 6, 2016
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Ref. 2 sequence was originally submitted as from rat origin.Curated

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.