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Protein

Rho guanine nucleotide exchange factor 1

Gene

ARHGEF1

Organism
Homo sapiens (Human)
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.4 Publications

GO - Molecular functioni

  • GTPase activator activity Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB
  • Rho guanyl-nucleotide exchange factor activity Source: ProtInc

GO - Biological processi

  • cell proliferation Source: ProtInc
  • negative regulation of axonogenesis Source: Reactome
  • neurotrophin TRK receptor signaling pathway Source: Reactome
  • positive regulation of GTPase activity Source: GOC
  • regulation of axonogenesis Source: Reactome
  • Rho protein signal transduction Source: ProtInc
  • termination of G-protein coupled receptor signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation, Guanine-nucleotide releasing factor

Enzyme and pathway databases

ReactomeiREACT_13815. Axonal growth inhibition (RHOA activation).
REACT_18407. G alpha (12/13) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho guanine nucleotide exchange factor 1
Alternative name(s):
115 kDa guanine nucleotide exchange factor
Short name:
p115-RhoGEF
Short name:
p115RhoGEF
Sub1.5
Gene namesi
Name:ARHGEF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:681. ARHGEF1.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Membrane 1 Publication

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi487 – 4871Y → F: No effect. 1 Publication
Mutagenesisi738 – 7381Y → F: Lowers the exchange activity. 1 Publication

Organism-specific databases

PharmGKBiPA24966.

Polymorphism and mutation databases

BioMutaiARHGEF1.
DMDMi34395524.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 912912Rho guanine nucleotide exchange factor 1PRO_0000080906Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei374 – 3741Phosphoserine1 Publication
Modified residuei738 – 7381Phosphotyrosine; by JAK21 Publication
Modified residuei863 – 8631Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated by PKCA. Angiotensin-2 induced Tyr-738 phosphorylation is mediated by JAK2.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ92888.
PaxDbiQ92888.
PRIDEiQ92888.

PTM databases

PhosphoSiteiQ92888.

Miscellaneous databases

PMAP-CutDBQ92888.

Expressioni

Tissue specificityi

Ubiquitously expressed.2 Publications

Gene expression databases

BgeeiQ92888.
CleanExiHS_ARHGEF1.
ExpressionAtlasiQ92888. baseline and differential.
GenevestigatoriQ92888.

Organism-specific databases

HPAiCAB009502.
HPA012924.
HPA060784.

Interactioni

Subunit structurei

Interacts with RHOA, GNA12 and GNA13. Homooligomerizes through the coiled coil region. May interact with CCPG1 (By similarity). Interacts with CTNNAL1.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GNA13Q143443EBI-465400,EBI-465387
TCF4P158843EBI-465400,EBI-533224
Z5115Q7DB747EBI-465400,EBI-7864788From a different organism.

Protein-protein interaction databases

BioGridi114585. 23 interactions.
IntActiQ92888. 13 interactions.
MINTiMINT-2813461.
STRINGi9606.ENSP00000337261.

Structurei

Secondary structure

1
912
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 203Combined sources
Turni26 – 338Combined sources
Helixi49 – 524Combined sources
Helixi56 – 6914Combined sources
Helixi73 – 8412Combined sources
Helixi89 – 10315Combined sources
Helixi116 – 1227Combined sources
Turni127 – 1293Combined sources
Helixi132 – 14413Combined sources
Helixi147 – 16216Combined sources
Helixi169 – 1768Combined sources
Helixi183 – 20321Combined sources
Helixi205 – 2073Combined sources
Helixi212 – 22817Combined sources
Turni399 – 4013Combined sources
Helixi404 – 4074Combined sources
Helixi413 – 44129Combined sources
Helixi443 – 4497Combined sources
Helixi454 – 4607Combined sources
Helixi464 – 48421Combined sources
Helixi493 – 5008Combined sources
Helixi502 – 51716Combined sources
Helixi519 – 53214Combined sources
Helixi534 – 54411Combined sources
Helixi547 – 5493Combined sources
Helixi554 – 5574Combined sources
Helixi560 – 57718Combined sources
Helixi582 – 62140Combined sources
Helixi625 – 6295Combined sources
Helixi633 – 6353Combined sources
Beta strandi636 – 6383Combined sources
Beta strandi644 – 6463Combined sources
Beta strandi648 – 66114Combined sources
Beta strandi663 – 68119Combined sources
Beta strandi684 – 6863Combined sources
Beta strandi694 – 6974Combined sources
Beta strandi706 – 7094Combined sources
Helixi710 – 7123Combined sources
Beta strandi713 – 7175Combined sources
Beta strandi719 – 7213Combined sources
Beta strandi724 – 7296Combined sources
Beta strandi737 – 7415Combined sources
Helixi745 – 76016Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IAPX-ray1.90A42-252[»]
1SHZX-ray2.85C/F7-239[»]
3AB3X-ray2.40B/D1-233[»]
3ODOX-ray2.90A/B395-766[»]
3ODWX-ray3.20A/B240-766[»]
3ODXX-ray3.20A/B353-766[»]
3P6AX-ray2.50A/B395-766[»]
ProteinModelPortaliQ92888.
SMRiQ92888. Positions 44-233, 395-761.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92888.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 232192RGSLAdd
BLAST
Domaini416 – 605190DHPROSITE-ProRule annotationAdd
BLAST
Domaini647 – 760114PHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili865 – 89632Sequence AnalysisAdd
BLAST

Domaini

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

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

eggNOGiCOG5422.
GeneTreeiENSGT00760000119193.
HOGENOMiHOG000034043.
HOVERGENiHBG050565.
InParanoidiQ92888.
KOiK12330.
OMAiFCRLRLL.
OrthoDBiEOG7GJ6CF.
PhylomeDBiQ92888.
TreeFamiTF106495.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR000219. DH-domain.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR016137. RGS.
IPR015212. RGS-like_dom.
IPR015721. RhoGEF-like.
[Graphical view]
PANTHERiPTHR22825. PTHR22825. 1 hit.
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.
PROSITEiPS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q92888-1) [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
MEDFARGAAS PGPSRPGLVP VSIIGAEDED FENELETNSE EQNSQFQSLE
60 70 80 90 100
QVKRRPAHLM ALLQHVALQF EPGPLLCCLH ADMLGSLGPK EAKKAFLDFY
110 120 130 140 150
HSFLEKTAVL RVPVPPNVAF ELDRTRADLI SEDVQRRFVQ EVVQSQQVAV
160 170 180 190 200
GRQLEDFRSK RLMGMTPWEQ ELAQLEAWVG RDRASYEARE RHVAERLLMH
210 220 230 240 250
LEEMQHTIST DEEKSAAVVN AIGLYMRHLG VRTKSGDKKS GRNFFRKKVM
260 270 280 290 300
GNRRSDEPAK TKKGLSSILD AARWNRGEPQ VPDFRHLKAE VDAEKPGATD
310 320 330 340 350
RKGGVGMPSR DRNIGAPGQD TPGVSLHPLS LDSPDREPGA DAPLELGDSS
360 370 380 390 400
PQGPMSLESL APPESTDEGA ETESPEPGDE GEPGRSGLEL EPEEPPGWRE
410 420 430 440 450
LVPPDTLHSL PKSQVKRQEV ISELLVTEAA HVRMLRVLHD LFFQPMAECL
460 470 480 490 500
FFPLEELQNI FPSLDELIEV HSLFLDRLMK RRQESGYLIE EIGDVLLARF
510 520 530 540 550
DGAEGSWFQK ISSRFCSRQS FALEQLKAKQ RKDPRFCAFV QEAESRPRCR
560 570 580 590 600
RLQLKDMIPT EMQRLTKYPL LLQSIGQNTE EPTEREKVEL AAECCREILH
610 620 630 640 650
HVNQAVRDME DLLRLKDYQR RLDLSHLRQS SDPMLSEFKN LDITKKKLVH
660 670 680 690 700
EGPLTWRVTK DKAVEVHVLL LDDLLLLLQR QDERLLLKSH SRTLTPTPDG
710 720 730 740 750
KTMLRPVLRL TSAMTREVAT DHKAFYVLFT WDQEAQIYEL VAQTVSERKN
760 770 780 790 800
WCALITETAG SLKVPAPASR PKPRPSPSST REPLLSSSEN GNGGRETSPA
810 820 830 840 850
DARTERILSD LLPFCRPGPE GQLAATALRK VLSLKQLLFP AEEDNGAGPP
860 870 880 890 900
RDGDGVPGGG PLSPARTQEI QENLLSLEET MKQLEELEEE FCRLRPLLSQ
910
LGGNSVPQPG CT
Length:912
Mass (Da):102,435
Last modified:August 29, 2003 - v2
Checksum:i1E773D041652190D
GO
Isoform 2 (identifier: Q92888-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     76-108: Missing.

Note: No experimental confirmation available.

Show »
Length:879
Mass (Da):98,768
Checksum:i1D0863A5D1A57C9B
GO
Isoform 3 (identifier: Q92888-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MASLSTWSSPAEPREM

Note: No experimental confirmation available.

Show »
Length:927
Mass (Da):104,066
Checksum:iB2E593D5B2DCE417
GO
Isoform 4 (identifier: Q92888-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MASLSTWSSPAEPREM
     76-108: Missing.
     831-912: VLSLKQLLFP...GNSVPQPGCT → GVGGGILPPE...PKCLRSVFIP

Note: No experimental confirmation available.

Show »
Length:948
Mass (Da):105,854
Checksum:iD4F76D1F6EADD661
GO

Sequence cautioni

The sequence CAA70356.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated
The sequence CAA70356.1 differs from that shown. Reason: Frameshift at position 904. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti257 – 2593EPA → DPP in AAB17896 (PubMed:8810315).Curated
Sequence conflicti305 – 3084VGMP → GGDA in CAA70356 (PubMed:9135076).Curated
Sequence conflicti339 – 3391Missing in CAA70356 (PubMed:9135076).Curated
Sequence conflicti346 – 3527LGDSSPQ → PGGLIPA in CAA70356 (PubMed:9135076).Curated
Sequence conflicti549 – 5491C → S in CAA70356 (PubMed:9135076).Curated
Sequence conflicti752 – 7521C → S in CAA70356 (PubMed:9135076).Curated
Sequence conflicti776 – 7761S → R in AAB17896 (PubMed:8810315).Curated
Sequence conflicti862 – 8621L → R in CAA70356 (PubMed:9135076).Curated
Sequence conflicti876 – 8761S → R in CAA70356 (PubMed:9135076).Curated
Sequence conflicti883 – 8831Q → T in CAA70356 (PubMed:9135076).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti165 – 1651M → V in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035969
Natural varianti375 – 3751P → L.
Corresponds to variant rs2303797 [ dbSNP | Ensembl ].
VAR_033521

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MASLSTWSSPAEPREM in isoform 3 and isoform 4. 1 PublicationVSP_037766
Alternative sequencei76 – 10833Missing in isoform 2 and isoform 4. 1 PublicationVSP_008125Add
BLAST
Alternative sequencei831 – 91282VLSLK…QPGCT → GVGGGILPPETPPVSAWGEL CPPAWLHLRFPPRKAFCKKE RNGGEDVRDHPHPHSCRSIS HPEGLRRGSCGPRLGGAQLG LLAPHEPRPSLPPALCLGDS GLHSGGHHGDPGHLSIACGG HPSTPTPKCLRSVFIP in isoform 4. 1 PublicationVSP_057289Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U64105 mRNA. Translation: AAB17896.1.
AC010616 Genomic DNA. No translation available.
AC243967 Genomic DNA. No translation available.
CH471126 Genomic DNA. Translation: EAW57084.1.
BC005155 mRNA. Translation: AAH05155.2.
BC011726 mRNA. Translation: AAH11726.1.
BC015652 mRNA. No translation available.
BC034013 mRNA. Translation: AAH34013.2.
BC067262 mRNA. Translation: AAH67262.1.
Y09160 mRNA. Translation: CAA70356.1. Sequence problems.
BT007421 mRNA. Translation: AAP36089.1.
CCDSiCCDS12590.1. [Q92888-3]
CCDS12591.1. [Q92888-1]
CCDS12592.1. [Q92888-2]
RefSeqiNP_004697.2. NM_004706.3. [Q92888-1]
NP_945328.1. NM_198977.1. [Q92888-2]
NP_945353.1. NM_199002.1. [Q92888-3]
UniGeneiHs.631550.

Genome annotation databases

EnsembliENST00000337665; ENSP00000337261; ENSG00000076928. [Q92888-3]
ENST00000347545; ENSP00000344429; ENSG00000076928. [Q92888-2]
ENST00000354532; ENSP00000346532; ENSG00000076928. [Q92888-1]
ENST00000378152; ENSP00000367394; ENSG00000076928. [Q92888-4]
GeneIDi9138.
KEGGihsa:9138.
UCSCiuc002orx.3. human. [Q92888-1]
uc002ory.3. human. [Q92888-2]
uc002osa.3. human. [Q92888-3]
uc002osb.3. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U64105 mRNA. Translation: AAB17896.1.
AC010616 Genomic DNA. No translation available.
AC243967 Genomic DNA. No translation available.
CH471126 Genomic DNA. Translation: EAW57084.1.
BC005155 mRNA. Translation: AAH05155.2.
BC011726 mRNA. Translation: AAH11726.1.
BC015652 mRNA. No translation available.
BC034013 mRNA. Translation: AAH34013.2.
BC067262 mRNA. Translation: AAH67262.1.
Y09160 mRNA. Translation: CAA70356.1. Sequence problems.
BT007421 mRNA. Translation: AAP36089.1.
CCDSiCCDS12590.1. [Q92888-3]
CCDS12591.1. [Q92888-1]
CCDS12592.1. [Q92888-2]
RefSeqiNP_004697.2. NM_004706.3. [Q92888-1]
NP_945328.1. NM_198977.1. [Q92888-2]
NP_945353.1. NM_199002.1. [Q92888-3]
UniGeneiHs.631550.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IAPX-ray1.90A42-252[»]
1SHZX-ray2.85C/F7-239[»]
3AB3X-ray2.40B/D1-233[»]
3ODOX-ray2.90A/B395-766[»]
3ODWX-ray3.20A/B240-766[»]
3ODXX-ray3.20A/B353-766[»]
3P6AX-ray2.50A/B395-766[»]
ProteinModelPortaliQ92888.
SMRiQ92888. Positions 44-233, 395-761.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114585. 23 interactions.
IntActiQ92888. 13 interactions.
MINTiMINT-2813461.
STRINGi9606.ENSP00000337261.

PTM databases

PhosphoSiteiQ92888.

Polymorphism and mutation databases

BioMutaiARHGEF1.
DMDMi34395524.

Proteomic databases

MaxQBiQ92888.
PaxDbiQ92888.
PRIDEiQ92888.

Protocols and materials databases

DNASUi9138.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337665; ENSP00000337261; ENSG00000076928. [Q92888-3]
ENST00000347545; ENSP00000344429; ENSG00000076928. [Q92888-2]
ENST00000354532; ENSP00000346532; ENSG00000076928. [Q92888-1]
ENST00000378152; ENSP00000367394; ENSG00000076928. [Q92888-4]
GeneIDi9138.
KEGGihsa:9138.
UCSCiuc002orx.3. human. [Q92888-1]
uc002ory.3. human. [Q92888-2]
uc002osa.3. human. [Q92888-3]
uc002osb.3. human.

Organism-specific databases

CTDi9138.
GeneCardsiGC19P042387.
HGNCiHGNC:681. ARHGEF1.
HPAiCAB009502.
HPA012924.
HPA060784.
MIMi601855. gene.
neXtProtiNX_Q92888.
PharmGKBiPA24966.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5422.
GeneTreeiENSGT00760000119193.
HOGENOMiHOG000034043.
HOVERGENiHBG050565.
InParanoidiQ92888.
KOiK12330.
OMAiFCRLRLL.
OrthoDBiEOG7GJ6CF.
PhylomeDBiQ92888.
TreeFamiTF106495.

Enzyme and pathway databases

ReactomeiREACT_13815. Axonal growth inhibition (RHOA activation).
REACT_18407. G alpha (12/13) signalling events.

Miscellaneous databases

ChiTaRSiARHGEF1. human.
EvolutionaryTraceiQ92888.
GeneWikiiARHGEF1.
GenomeRNAii9138.
NextBioi34263.
PMAP-CutDBQ92888.
PROiQ92888.
SOURCEiSearch...

Gene expression databases

BgeeiQ92888.
CleanExiHS_ARHGEF1.
ExpressionAtlasiQ92888. baseline and differential.
GenevestigatoriQ92888.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR000219. DH-domain.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR016137. RGS.
IPR015212. RGS-like_dom.
IPR015721. RhoGEF-like.
[Graphical view]
PANTHERiPTHR22825. PTHR22825. 1 hit.
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.
PROSITEiPS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel guanine nucleotide exchange factor for the rho GTPase."
    Hart M.J., Sharma S., el Masry N., Qiu R.-G., McCabe P., Polakis P., Bollag G.
    J. Biol. Chem. 271:25452-25458(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH RHOA, TISSUE SPECIFICITY.
  2. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORMS 1; 2; 3 AND 4).
    Tissue: B-cell, Muscle, Placenta and Uterus.
  5. "Characterization, expression and chromosomal localization of a human gene homologous to the mouse Lsc oncogene, with strongest expression in hematopoetic tissues."
    Aasheim H.-C., Pedeutour F., Smeland E.B.
    Oncogene 14:1747-1752(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-912 (ISOFORM 1), TISSUE SPECIFICITY.
  6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 60-912 (ISOFORM 1).
  7. "p115 RhoGEF, a GTPase activating protein for Galpha12 and Galpha13."
    Kozasa T., Jiang X., Hart M.J., Sternweis P.M., Singer W.D., Gilman A.G., Bollag G., Sternweis P.C.
    Science 280:2109-2111(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Direct stimulation of the guanine nucleotide exchange activity of p115 RhoGEF by Galpha13."
    Hart M.J., Jiang X., Kozasa T., Roscoe W., Singer W.D., Gilman A.G., Sternweis P.C., Bollag G.
    Science 280:2112-2114(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GNA13.
  9. "Galpha 13 requires palmitoylation for plasma membrane localization, Rho-dependent signaling, and promotion of p115-RhoGEF membrane binding."
    Bhattacharyya R., Wedegaertner P.B.
    J. Biol. Chem. 275:14992-14999(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "Association of Lbc Rho guanine nucleotide exchange factor with alpha-catenin-related protein, alpha-catulin/CTNNAL1, supports serum response factor activation."
    Park B., Nguyen N.T., Dutt P., Merdek K.D., Bashar M., Sterpetti P., Tosolini A., Testa J.R., Toksoz D.
    J. Biol. Chem. 277:45361-45370(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CTNNAL1.
  11. "PKCa-induced p115RhoGEF phosphorylation signals endothelial cytoskeletal rearrangement."
    Holinstat M., Mehta D., Kozasa T., Minshall R.D., Malik A.B.
    J. Biol. Chem. 278:28793-28798(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY PKCA.
  12. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "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, PHOSPHORYLATION AT TYR-738, MUTAGENESIS OF TYR-487 AND TYR-738.
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 42-252.
  20. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-165.

Entry informationi

Entry nameiARHG1_HUMAN
AccessioniPrimary (citable) accession number: Q92888
Secondary accession number(s): O00513
, Q6NX52, Q8N4J4, Q96BF4, Q96F17, Q9BSB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: August 29, 2003
Last modified: April 29, 2015
This is version 145 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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.