Q92888 (ARHG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

ARHGEF1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	912 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.5 Ref.6 Ref.13
Subunit structure	Interacts with RHOA, GNA12 and GNA13. Homooligomerizes through the coiled coil region. May interact with CCPG1 By similarity. Interacts with CTNNAL1. Ref.1 Ref.6 Ref.8
Subcellular location	Cytoplasm. Membrane. Note: Translocated to the membrane by activated GNA13 or LPA stimulation. Ref.7
Tissue specificity	Ubiquitously expressed. Ref.1 Ref.3
Domain	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.
Post-translational modification	Phosphorylated by PKCA. Angiotensin-2 induced Tyr-738 phosphorylation is mediated by JAK2. Ref.9 Ref.13
Sequence similarities	Contains 1 DH (DBL-homology) domain. Contains 1 PH domain. Contains 1 RGSL (RGS-like) domain.
Sequence caution	The sequence CAA70356.1 differs from that shown. Reason: Frameshift at position 904. The sequence CAA70356.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Molecular function	GTPase activation Guanine-nucleotide releasing factor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Rho protein signal transduction Traceable author statement Ref.7. Source: ProtInc cell proliferation Traceable author statement Ref.1. Source: ProtInc negative regulation of axonogenesis Traceable author statement. Source: Reactome nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome positive regulation of GTPase activity Inferred from electronic annotation. Source: GOC regulation of Rho protein signal transduction Inferred from electronic annotation. Source: InterPro termination of G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Traceable author statement. Source: Reactome plasma membrane Traceable author statement. Source: Reactome
Molecular_function	GTPase activator activity Inferred from electronic annotation. Source: UniProtKB-KW Rho guanyl-nucleotide exchange factor activity Traceable author statement Ref.1. Source: ProtInc phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GNA13	Q14344	2	EBI-465400,EBI-465387

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q92888-1)

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.

Isoform 2 (identifier: Q92888-2)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: Q92888-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 912

912

Rho guanine nucleotide exchange factor 1

PRO_0000080906

Regions

Domain

41 – 232

192

RGSL

Domain

416 – 605

190

DH

Domain

647 – 760

114

PH

Coiled coil

865 – 896

32

Potential

Amino acid modifications

Modified residue

738

1

Phosphotyrosine; by JAK2 Ref.13

Modified residue

863

1

Phosphoserine Ref.10 Ref.14

Natural variations

Alternative sequence

1

1

M → MASLSTWSSPAEPREM in isoform 3.

VSP_037766

Alternative sequence

76 – 108

33

Missing in isoform 2.

VSP_008125

Natural variant

165

1

M → V in a colorectal cancer sample; somatic mutation. Ref.17

VAR_035969

Natural variant

375

1

P → L.
Corresponds to variant rs2303797 [ dbSNP | Ensembl ].

VAR_033521

Experimental info

Mutagenesis

487

1

Y → F: No effect. Ref.13

Mutagenesis

738

1

Y → F: Lowers the exchange activity. Ref.13

Sequence conflict

257 – 259

3

EPA → DPP in AAB17896. Ref.1

Sequence conflict

305 – 308

4

VGMP → GGDA in CAA70356. Ref.3

Sequence conflict

339

1

Missing in CAA70356. Ref.3

Sequence conflict

346 – 352

7

LGDSSPQ → PGGLIPA in CAA70356. Ref.3

Sequence conflict

549

1

C → S in CAA70356. Ref.3

Sequence conflict

752

1

C → S in CAA70356. Ref.3

Sequence conflict

776

1

S → R in AAB17896. Ref.1

Sequence conflict

862

1

L → R in CAA70356. Ref.3

Sequence conflict

876

1

S → R in CAA70356. Ref.3

Sequence conflict

883

1

Q → T in CAA70356. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

912

Helix Strand Turn

Details...

Beta strand

18 – 20

3

Turn

26 – 33

8

Helix

49 – 52

4

Helix

56 – 69

14

Helix

73 – 84

12

Helix

89 – 103

15

Helix

116 – 122

7

Turn

127 – 129

3

Helix

132 – 144

13

Helix

147 – 162

16

Helix

169 – 176

8

Helix

183 – 203

21

Helix

205 – 207

3

Helix

212 – 228

17

Turn

399 – 401

3

Helix

404 – 407

4

Helix

413 – 441

29

Helix

443 – 449

7

Helix

454 – 460

7

Helix

464 – 484

21

Helix

493 – 500

8

Helix

502 – 517

16

Helix

519 – 532

14

Helix

534 – 544

11

Helix

547 – 549

3

Helix

554 – 557

4

Helix

560 – 577

18

Helix

582 – 621

40

Helix

625 – 629

5

Helix

633 – 635

3

Beta strand

636 – 638

3

Beta strand

644 – 646

3

Beta strand

648 – 661

14

Beta strand

663 – 681

19

Beta strand

684 – 686

3

Beta strand

694 – 697

4

Beta strand

706 – 709

4

Helix

710 – 712

3

Beta strand

713 – 717

5

Beta strand

719 – 721

3

Beta strand

724 – 729

6

Beta strand

737 – 741

5

Helix

745 – 760

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 29, 2003. Version 2. Checksum: 1E773D041652190D	FASTA	912	102,435
	10 20 30 40 50 60 MEDFARGAAS PGPSRPGLVP VSIIGAEDED FENELETNSE EQNSQFQSLE QVKRRPAHLM 70 80 90 100 110 120 ALLQHVALQF EPGPLLCCLH ADMLGSLGPK EAKKAFLDFY HSFLEKTAVL RVPVPPNVAF 130 140 150 160 170 180 ELDRTRADLI SEDVQRRFVQ EVVQSQQVAV GRQLEDFRSK RLMGMTPWEQ ELAQLEAWVG 190 200 210 220 230 240 RDRASYEARE RHVAERLLMH LEEMQHTIST DEEKSAAVVN AIGLYMRHLG VRTKSGDKKS 250 260 270 280 290 300 GRNFFRKKVM GNRRSDEPAK TKKGLSSILD AARWNRGEPQ VPDFRHLKAE VDAEKPGATD 310 320 330 340 350 360 RKGGVGMPSR DRNIGAPGQD TPGVSLHPLS LDSPDREPGA DAPLELGDSS PQGPMSLESL 370 380 390 400 410 420 APPESTDEGA ETESPEPGDE GEPGRSGLEL EPEEPPGWRE LVPPDTLHSL PKSQVKRQEV 430 440 450 460 470 480 ISELLVTEAA HVRMLRVLHD LFFQPMAECL FFPLEELQNI FPSLDELIEV HSLFLDRLMK 490 500 510 520 530 540 RRQESGYLIE EIGDVLLARF DGAEGSWFQK ISSRFCSRQS FALEQLKAKQ RKDPRFCAFV 550 560 570 580 590 600 QEAESRPRCR RLQLKDMIPT EMQRLTKYPL LLQSIGQNTE EPTEREKVEL AAECCREILH 610 620 630 640 650 660 HVNQAVRDME DLLRLKDYQR RLDLSHLRQS SDPMLSEFKN LDITKKKLVH EGPLTWRVTK 670 680 690 700 710 720 DKAVEVHVLL LDDLLLLLQR QDERLLLKSH SRTLTPTPDG KTMLRPVLRL TSAMTREVAT 730 740 750 760 770 780 DHKAFYVLFT WDQEAQIYEL VAQTVSERKN WCALITETAG SLKVPAPASR PKPRPSPSST 790 800 810 820 830 840 REPLLSSSEN GNGGRETSPA DARTERILSD LLPFCRPGPE GQLAATALRK VLSLKQLLFP 850 860 870 880 890 900 AEEDNGAGPP RDGDGVPGGG PLSPARTQEI QENLLSLEET MKQLEELEEE FCRLRPLLSQ 910 LGGNSVPQPG CT
	Isoform 2 [UniParc]. Checksum: 1D0863A5D1A57C9B	FASTA	879	98,768
	10 20 30 40 50 60 MEDFARGAAS PGPSRPGLVP VSIIGAEDED FENELETNSE EQNSQFQSLE QVKRRPAHLM 70 80 90 100 110 120 ALLQHVALQF EPGPLVLRVP VPPNVAFELD RTRADLISED VQRRFVQEVV QSQQVAVGRQ 130 140 150 160 170 180 LEDFRSKRLM GMTPWEQELA QLEAWVGRDR ASYEARERHV AERLLMHLEE MQHTISTDEE 190 200 210 220 230 240 KSAAVVNAIG LYMRHLGVRT KSGDKKSGRN FFRKKVMGNR RSDEPAKTKK GLSSILDAAR 250 260 270 280 290 300 WNRGEPQVPD FRHLKAEVDA EKPGATDRKG GVGMPSRDRN IGAPGQDTPG VSLHPLSLDS 310 320 330 340 350 360 PDREPGADAP LELGDSSPQG PMSLESLAPP ESTDEGAETE SPEPGDEGEP GRSGLELEPE 370 380 390 400 410 420 EPPGWRELVP PDTLHSLPKS QVKRQEVISE LLVTEAAHVR MLRVLHDLFF QPMAECLFFP 430 440 450 460 470 480 LEELQNIFPS LDELIEVHSL FLDRLMKRRQ ESGYLIEEIG DVLLARFDGA EGSWFQKISS 490 500 510 520 530 540 RFCSRQSFAL EQLKAKQRKD PRFCAFVQEA ESRPRCRRLQ LKDMIPTEMQ RLTKYPLLLQ 550 560 570 580 590 600 SIGQNTEEPT EREKVELAAE CCREILHHVN QAVRDMEDLL RLKDYQRRLD LSHLRQSSDP 610 620 630 640 650 660 MLSEFKNLDI TKKKLVHEGP LTWRVTKDKA VEVHVLLLDD LLLLLQRQDE RLLLKSHSRT 670 680 690 700 710 720 LTPTPDGKTM LRPVLRLTSA MTREVATDHK AFYVLFTWDQ EAQIYELVAQ TVSERKNWCA 730 740 750 760 770 780 LITETAGSLK VPAPASRPKP RPSPSSTREP LLSSSENGNG GRETSPADAR TERILSDLLP 790 800 810 820 830 840 FCRPGPEGQL AATALRKVLS LKQLLFPAEE DNGAGPPRDG DGVPGGGPLS PARTQEIQEN 850 860 870 LLSLEETMKQ LEELEEEFCR LRPLLSQLGG NSVPQPGCT
	Isoform 3 [UniParc]. Checksum: B2E593D5B2DCE417	FASTA	927	104,066
	10 20 30 40 50 60 MASLSTWSSP AEPREMEDFA RGAASPGPSR PGLVPVSIIG AEDEDFENEL ETNSEEQNSQ 70 80 90 100 110 120 FQSLEQVKRR PAHLMALLQH VALQFEPGPL LCCLHADMLG SLGPKEAKKA FLDFYHSFLE 130 140 150 160 170 180 KTAVLRVPVP PNVAFELDRT RADLISEDVQ RRFVQEVVQS QQVAVGRQLE DFRSKRLMGM 190 200 210 220 230 240 TPWEQELAQL EAWVGRDRAS YEARERHVAE RLLMHLEEMQ HTISTDEEKS AAVVNAIGLY 250 260 270 280 290 300 MRHLGVRTKS GDKKSGRNFF RKKVMGNRRS DEPAKTKKGL SSILDAARWN RGEPQVPDFR 310 320 330 340 350 360 HLKAEVDAEK PGATDRKGGV GMPSRDRNIG APGQDTPGVS LHPLSLDSPD REPGADAPLE 370 380 390 400 410 420 LGDSSPQGPM SLESLAPPES TDEGAETESP EPGDEGEPGR SGLELEPEEP PGWRELVPPD 430 440 450 460 470 480 TLHSLPKSQV KRQEVISELL VTEAAHVRML RVLHDLFFQP MAECLFFPLE ELQNIFPSLD 490 500 510 520 530 540 ELIEVHSLFL DRLMKRRQES GYLIEEIGDV LLARFDGAEG SWFQKISSRF CSRQSFALEQ 550 560 570 580 590 600 LKAKQRKDPR FCAFVQEAES RPRCRRLQLK DMIPTEMQRL TKYPLLLQSI GQNTEEPTER 610 620 630 640 650 660 EKVELAAECC REILHHVNQA VRDMEDLLRL KDYQRRLDLS HLRQSSDPML SEFKNLDITK 670 680 690 700 710 720 KKLVHEGPLT WRVTKDKAVE VHVLLLDDLL LLLQRQDERL LLKSHSRTLT PTPDGKTMLR 730 740 750 760 770 780 PVLRLTSAMT REVATDHKAF YVLFTWDQEA QIYELVAQTV SERKNWCALI TETAGSLKVP 790 800 810 820 830 840 APASRPKPRP SPSSTREPLL SSSENGNGGR ETSPADARTE RILSDLLPFC RPGPEGQLAA 850 860 870 880 890 900 TALRKVLSLK QLLFPAEEDN GAGPPRDGDG VPGGGPLSPA RTQEIQENLL SLEETMKQLE 910 920 ELEEEFCRLR PLLSQLGGNS VPQPGCT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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 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 AND 3). Tissue: B-cell, Muscle and Placenta.
[3]	"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.
[4]	"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).
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[12]	"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.
[13]	"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.
[14]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"Structure of the rgRGS domain of p115RhoGEF." Chen Z., Wells C.D., Sternweis P.C., Sprang S.R. Nat. Struct. Biol. 8:805-809(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 42-252.
[17]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-165.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U64105 mRNA. Translation: AAB17896.1.
BC005155 mRNA. Translation: AAH05155.2.
BC011726 mRNA. Translation: AAH11726.1.
BC015652 mRNA. No translation available.
BC034013 mRNA. Translation: AAH34013.2.
Y09160 mRNA. Translation: CAA70356.1. Sequence problems.
BT007421 mRNA. Translation: AAP36089.1.

IPI

IPI00339379.
IPI00395605.
IPI00647786.

RefSeq

NP_004697.2. NM_004706.3.
NP_945328.1. NM_198977.1.
NP_945353.1. NM_199002.1.

UniGene

Hs.631550.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IAP	X-ray	1.90	A	42-252	[»]
1SHZ	X-ray	2.85	C/F	7-239	[»]
3AB3	X-ray	2.40	B/D	1-233	[»]
3ODO	X-ray	2.90	A/B	395-766	[»]
3ODW	X-ray	3.20	A/B	240-766	[»]
3ODX	X-ray	3.20	A/B	353-766	[»]
3P6A	X-ray	2.50	A/B	395-766	[»]

ProteinModelPortal

Q92888.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q92888. 8 interactions.

STRING

9606.ENSP00000337261.

PTM databases

PhosphoSite

Q92888.

Polymorphism databases

DMDM

34395524.

Proteomic databases

PaxDb

Q92888.

PRIDE

Q92888.

Protocols and materials databases

DNASU

9138.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000337665; ENSP00000337261; ENSG00000076928.
ENST00000347545; ENSP00000344429; ENSG00000076928.
ENST00000354532; ENSP00000346532; ENSG00000076928.

GeneID

9138.

KEGG

hsa:9138.

UCSC

uc002orx.3. human.
uc002ory.3. human.
uc002osa.3. human.

Organism-specific databases

CTD

9138.

GeneCards

GC19P042387.

HGNC

HGNC:681. ARHGEF1.

HPA

CAB009502.
HPA012924.

MIM

601855. gene.

neXtProt

NX_Q92888.

PharmGKB

PA24966.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5422.

HOGENOM

HOG000034043.

HOVERGEN

HBG050565.

KO

K12330.

Enzyme and pathway databases

Pathway_Interaction_DB

lysophospholipid_pathway. LPA receptor mediated events.
txa2pathway. Thromboxane A2 receptor signaling.

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

Q92888.

Bgee

Q92888.

CleanEx

HS_ARHGEF1.

Genevestigator

Q92888.

GermOnline

ENSG00000076928. Homo sapiens.

Family and domain databases

Gene3D

1.20.900.10. 1 hit.
2.30.29.30. 1 hit.

InterPro

IPR000219. DH-domain.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR015212. Regulat_G_prot_signal-like.
IPR016137. Regulat_G_prot_signal_superfam.
IPR015721. RhoGEF-like.
[Graphical view]

PANTHER

PTHR22825. PTHR22825. 1 hit.

Pfam

PF09128. RGS-like. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]

SMART

SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]

SUPFAM

SSF48065. DH-domain. 1 hit.
SSF48097. Regulat_G_prot_signal_superfam. 1 hit.

PROSITE

PS00741. DH_1. False negative.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ARHGEF1. human.

EvolutionaryTrace

Q92888.

GenomeRNAi

9138.

NextBio

34263.

PMAP-CutDB

Q92888.

SOURCE

Search...

Entry information

Entry name

ARHG1_HUMAN

Accession

Primary (citable) accession number: Q92888
Secondary accession number(s): O00513 , Q8N4J4, Q96BF4, Q96F17, Q9BSB1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2003
Last sequence update:	August 29, 2003
Last modified:	May 1, 2013
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.