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Protein

Rho guanine nucleotide exchange factor 2

Gene

ARHGEF2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Activates Rho-GTPases by promoting the exchange of GDP for GTP. May be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. Binds Rac-GTPases, but does not seem to promote nucleotide exchange activity toward Rac-GTPases, which was uniquely reported in PubMed:9857026. May stimulate instead the cortical activity of Rac. Inactive toward CDC42, TC10, or Ras-GTPases. Forms an intracellular sensing system along with NOD1 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIP2 dependent NF-kappaB signaling pathways activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides through NOD1 that is independent of its GEF activity, but also in the activation of NF-kappaB by Shigella effector proteins (IpgB2 and OspB) which requires its GEF activity and the activation of RhoA. Involved in innate immune signaling transduction pathway promoting cytokine IL6/interleukin-6 and TNF-alpha secretion in macrophage upon stimulation by bacterial peptidoglycans; acts as a signaling intermediate between NOD2 receptor and RIPK2 kinase. Contributes to the tyrosine phosphorylation of RIPK2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2.3 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri39 – 86Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST48

GO - Molecular functioni

  • guanyl-nucleotide exchange factor activity Source: Reactome
  • microtubule binding Source: UniProtKB
  • Rac GTPase binding Source: UniProtKB
  • Rac guanyl-nucleotide exchange factor activity Source: UniProtKB
  • Rho GTPase binding Source: UniProtKB
  • Rho guanyl-nucleotide exchange factor activity Source: UniProtKB
  • transcription factor binding Source: BHF-UCL
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Biological processi

Cell cycle, Cell division, Immunity, Innate immunity, Mitosis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000116584-MONOMER.
ReactomeiR-HSA-193648. NRAGE signals death through JNK.
R-HSA-194840. Rho GTPase cycle.
R-HSA-416482. G alpha (12/13) signalling events.
SIGNORiQ92974.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho guanine nucleotide exchange factor 2
Alternative name(s):
Guanine nucleotide exchange factor H1
Short name:
GEF-H1
Microtubule-regulated Rho-GEF
Proliferating cell nucleolar antigen p40
Gene namesi
Name:ARHGEF2
Synonyms:KIAA0651, LFP40
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:682. ARHGEF2.

Subcellular locationi

GO - Cellular componenti

  • bicellular tight junction Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytoplasmic, membrane-bounded vesicle Source: UniProtKB-SubCell
  • cytoskeleton Source: UniProtKB
  • cytosol Source: Reactome
  • dendritic shaft Source: Ensembl
  • focal adhesion Source: UniProtKB
  • Golgi apparatus Source: UniProtKB-SubCell
  • microtubule Source: UniProtKB
  • neuronal cell body Source: Ensembl
  • postsynaptic density Source: Ensembl
  • protein complex Source: UniProtKB
  • ruffle membrane Source: UniProtKB
  • spindle Source: UniProtKB-SubCell
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Golgi apparatus, Membrane, Microtubule, Tight junction

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi53C → R: Abolishes microtubule binding, increased activity in vitro. 1 Publication1
Mutagenesisi143S → A: Abolishes phosphorylation by PAK4, self aggregation in the cytoplasm. Increases activity; when associated with A-896. 1 Publication1
Mutagenesisi394Y → A: Reduces phosphorylation level, normal microtubule localization and activity. 1 Publication1
Mutagenesisi679T → A: Reduces phosphorylation level. 1 Publication1
Mutagenesisi886S → A: Normal activity. 1
Mutagenesisi886S → D: Increases activity. Abolishes nucleotide exchange activity; when associated with D-960. 1
Mutagenesisi896S → A: Abolishes phosphorylation by PAK4, self aggregation in the cytoplasm. Increases activity; when associated with A-143. 1 Publication1
Mutagenesisi960S → A: Normal activity. 1
Mutagenesisi960S → D: Increases activity. Abolishes nucleotide exchange activity; when associated with D-886. 1

Organism-specific databases

DisGeNETi9181.
OpenTargetsiENSG00000116584.
PharmGKBiPA24972.

Polymorphism and mutation databases

BioMutaiARHGEF2.
DMDMi205830906.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000809091 – 986Rho guanine nucleotide exchange factor 2Add BLAST986

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei109PhosphoserineCombined sources1
Modified residuei122PhosphoserineCombined sources1
Modified residuei129PhosphoserineCombined sources1
Modified residuei133PhosphoserineCombined sources1
Modified residuei137PhosphoserineCombined sources1
Modified residuei143Phosphoserine; by PAK41 Publication1
Modified residuei151PhosphoserineCombined sources1
Modified residuei163PhosphoserineCombined sources1
Modified residuei172PhosphoserineCombined sources1
Modified residuei174PhosphoserineCombined sources1
Modified residuei177PhosphoserineCombined sources1
Modified residuei353N6-acetyllysineCombined sources1
Modified residuei645PhosphoserineCombined sources1
Modified residuei648PhosphoserineCombined sources1
Modified residuei679Phosphothreonine; by MAPK1 or MAPK3Combined sources1 Publication1
Modified residuei691PhosphoserineCombined sources1
Modified residuei696PhosphoserineCombined sources1
Modified residuei711PhosphoserineCombined sources1
Modified residuei782PhosphoserineBy similarity1
Modified residuei886Phosphoserine; by PAK1 and AURKACombined sources2 Publications1
Modified residuei894PhosphotyrosineCombined sources1
Modified residuei896Phosphoserine; by PAK41 Publication1
Modified residuei932PhosphoserineCombined sources1
Modified residuei940PhosphoserineCombined sources1
Modified residuei941PhosphoserineCombined sources1
Modified residuei945PhosphothreonineCombined sources1
Modified residuei947PhosphoserineCombined sources1
Modified residuei952PhosphoserineBy similarity1
Modified residuei953PhosphoserineCombined sources1
Modified residuei956PhosphoserineCombined sources1
Modified residuei960PhosphoserineCombined sources1 Publication1

Post-translational modificationi

Phosphorylation of Ser-886 by PAK1 induces binding to protein YWHAZ, promoting its relocation to microtubules and the inhibition of its activity. Phosphorylated by AURKA and CDK1 during mitosis, which negatively regulates its activity. Phosphorylation by MAPK1 or MAPK3 increases nucleotide exchange activity. Phosphorylation by PAK4 releases GEF-H1 from the microtubules. Phosphorylated on serine, threonine and tyrosine residues in a RIPK2-dependent manner.4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ92974.
MaxQBiQ92974.
PaxDbiQ92974.
PeptideAtlasiQ92974.
PRIDEiQ92974.
TopDownProteomicsiQ92974-2. [Q92974-2]

PTM databases

iPTMnetiQ92974.
PhosphoSitePlusiQ92974.

Expressioni

Inductioni

Up-regulated by bacterial peptidoglycans stimulation, such as muramyl dipeptide and in biopsies from inflamed mucosal areas of Crohn's disease patients.1 Publication

Gene expression databases

BgeeiENSG00000116584.
CleanExiHS_ARHGEF2.
ExpressionAtlasiQ92974. baseline and differential.
GenevisibleiQ92974. HS.

Organism-specific databases

HPAiHPA017046.
HPA043437.

Interactioni

Subunit structurei

Found in a complex composed at least of ARHGEF2, NOD2 and RIPK2. Interacts with RIPK2; the interaction mediates tyrosine phosphorylation of RIPK2 by Src kinase CSK. Interacts with RIPK1 and RIPK3. Interacts with YWHAZ/14-3-3 zeta; when phosphorylated at Ser-886. Interacts with the kinases PAK4, AURKA and MAPK1. Interacts with RHOA and RAC1. Interacts with NOD1. Interacts (via the N-terminal zinc finger) with CAPN6 (via domain II) (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
FOXO3O435242EBI-302405,EBI-1644164
RPP25LQ8N5L83EBI-302405,EBI-10189722
YWHAZP631042EBI-302405,EBI-347088

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • Rac GTPase binding Source: UniProtKB
  • Rho GTPase binding Source: UniProtKB
  • transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi114618. 54 interactors.
IntActiQ92974. 36 interactors.
MINTiMINT-1683482.
STRINGi9606.ENSP00000354837.

Structurei

Secondary structure

1986
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi440 – 447Combined sources8
Beta strandi454 – 457Combined sources4
Turni458 – 460Combined sources3
Beta strandi461 – 464Combined sources4
Helixi465 – 469Combined sources5
Beta strandi473 – 482Combined sources10
Beta strandi488 – 504Combined sources17
Beta strandi509 – 511Combined sources3
Beta strandi519 – 522Combined sources4
Beta strandi527 – 530Combined sources4
Beta strandi537 – 542Combined sources6
Turni543 – 546Combined sources4
Beta strandi547 – 552Combined sources6
Helixi556 – 571Combined sources16
Turni576 – 578Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5EFXX-ray2.45A439-582[»]
ProteinModelPortaliQ92974.
SMRiQ92974.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini235 – 432DHPROSITE-ProRule annotationAdd BLAST198
Domaini472 – 571PHPROSITE-ProRule annotationAdd BLAST100

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili587 – 611Sequence analysisAdd BLAST25
Coiled coili798 – 867Sequence analysisAdd BLAST70

Domaini

The DH (DBL-homology) domain interacts with and promotes loading of GTP on RhoA. Promotes tyrosine phosphorylation of RIPK2.
The PH (pleckstrin-homology) domain is involved in microtubule binding and targeting to tight junctions.

Sequence similaritiesi

Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri39 – 86Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST48

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IR0Y. Eukaryota.
ENOG410XT68. LUCA.
GeneTreeiENSGT00760000119193.
HOVERGENiHBG050566.
InParanoidiQ92974.
KOiK12791.
PhylomeDBiQ92974.
TreeFamiTF325887.

Family and domain databases

CDDicd00029. C1. 1 hit.
Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR000219. DH-domain.
IPR002219. PE/DAG-bd.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 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: Q92974-1) [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
MSRIESLTRA RIDRSRELAS KTREKEKMKE AKDARYTNGH LFTTISVSGM
60 70 80 90 100
TMCYACNKSI TAKEALICPT CNVTIHNRCK DTLANCTKVK QKQQKAALLK
110 120 130 140 150
NNTALQSVSL RSKTTIRERP SSAIYPSDSF RQSLLGSRRG RSSLSLAKSV
160 170 180 190 200
STTNIAGHFN DESPLGLRRI LSQSTDSLNM RNRTLSVESL IDEAEVIYSE
210 220 230 240 250
LMSDFEMDEK DFAADSWSLA VDSSFLQQHK KEVMKQQDVI YELIQTELHH
260 270 280 290 300
VRTLKIMTRL FRTGMLEELH LEPGVVQGLF PCVDELSDIH TRFLSQLLER
310 320 330 340 350
RRQALCPGST RNFVIHRLGD LLISQFSGPS AEQMCKTYSE FCSRHSKALK
360 370 380 390 400
LYKELYARDK RFQQFIRKVT RPAVLKRHGV QECILLVTQR ITKYPLLISR
410 420 430 440 450
ILQHSHGIEE ERQDLTTALG LVKELLSNVD EGIYQLEKGA RLQEIYNRMD
460 470 480 490 500
PRAQTPVPGK GPFGREELLR RKLIHDGCLL WKTATGRFKD VLVLLMTDVL
510 520 530 540 550
VFLQEKDQKY IFPTLDKPSV VSLQNLIVRD IANQEKGMFL ISAAPPEMYE
560 570 580 590 600
VHTASRDDRS TWIRVIQQSV RTCPSREDFP LIETEDEAYL RRIKMELQQK
610 620 630 640 650
DRALVELLRE KVGLFAEMTH FQAEEDGGSG MALPTLPRGL FRSESLESPR
660 670 680 690 700
GERLLQDAIR EVEGLKDLLV GPGVELLLTP REPALPLEPD SGGNTSPGVT
710 720 730 740 750
ANGEARTFNG SIELCRADSD SSQRDRNGNQ LRSPQEEALQ RLVNLYGLLH
760 770 780 790 800
GLQAAVAQQD TLMEARFPEG PERREKLCRA NSRDGEAGRA GAAPVAPEKQ
810 820 830 840 850
ATELALLQRQ HALLQEELRR CRRLGEERAT EAGSLEARLR ESEQARALLE
860 870 880 890 900
REAEEARRQL AALGQTEPLP AEAPWARRPV DPRRRSLPAG DALYLSFNPP
910 920 930 940 950
QPSRGTDRLD LPVTTRSVHR NFEDRERQEL GSPEERLQDS SDPDTGSEEE
960 970 980
GSSRLSPPHS PRDFTRMQDI PEETESRDGE AVASES
Length:986
Mass (Da):111,543
Last modified:July 22, 2008 - v4
Checksum:i8986AF0A1174EA71
GO
Isoform 2 (identifier: Q92974-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     194-194: Missing.

Show »
Length:985
Mass (Da):111,471
Checksum:i6CD4CC60C17E19B4
GO
Isoform 3 (identifier: Q92974-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: Missing.
     194-194: Missing.

Show »
Length:958
Mass (Da):108,242
Checksum:iE9A0C474243344D3
GO

Sequence cautioni

The sequence AAC97383 differs from that shown. Sequence differs at a large extent from the sequence shown in the paper.Curated
The sequence AAH20567 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA31626 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA33634 differs from that shown. Reason: Frameshift at positions 887 and 984.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1 – 20MSRIE…RELAS → IVGAAGHGRALSLCFDNGPL EQVPLALEETASIGMPRPQG GPLPADPRRTGHLSGTGHQG GYASRLDQDSCHPSAGPLDH SATGMLSKSVPVSGINCLLD RSDTDGNVSQSSAIDLRKRC SQLEGHSGTRVGSSLRQTFS FLSGMTGKA in BAA31626 (PubMed:9734811).CuratedAdd BLAST20
Sequence conflicti631M → L in CAA33634 (PubMed:2466560).Curated1
Sequence conflicti868P → Q in CAA33634 (PubMed:2466560).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0394571 – 27Missing in isoform 3. 2 PublicationsAdd BLAST27
Alternative sequenceiVSP_039458194Missing in isoform 2 and isoform 3. 3 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72206 mRNA. Translation: AAC97383.1. Sequence problems.
AF486838 mRNA. Translation: AAL96658.1.
AB014551 mRNA. Translation: BAA31626.3. Different initiation.
AL512715 mRNA. Translation: CAC21656.1.
AL355388 Genomic DNA. Translation: CAH72627.1.
AL355388 Genomic DNA. Translation: CAH72629.1.
AL355388 Genomic DNA. Translation: CAH72630.1.
CH471121 Genomic DNA. Translation: EAW53013.1.
CH471121 Genomic DNA. Translation: EAW53015.1.
CH471121 Genomic DNA. Translation: EAW53014.1.
BC020567 mRNA. Translation: AAH20567.1. Different initiation.
BT007407 mRNA. Translation: AAP36075.1.
X15610 mRNA. Translation: CAA33634.1. Frameshift.
CCDSiCCDS1125.1. [Q92974-3]
CCDS53375.1. [Q92974-2]
CCDS53376.1. [Q92974-1]
PIRiS28660.
RefSeqiNP_001155855.1. NM_001162383.1. [Q92974-1]
NP_001155856.1. NM_001162384.1. [Q92974-2]
NP_004714.2. NM_004723.3. [Q92974-3]
UniGeneiHs.743352.

Genome annotation databases

EnsembliENST00000313667; ENSP00000314787; ENSG00000116584. [Q92974-2]
ENST00000313695; ENSP00000315325; ENSG00000116584. [Q92974-3]
ENST00000361247; ENSP00000354837; ENSG00000116584. [Q92974-1]
GeneIDi9181.
KEGGihsa:9181.
UCSCiuc001fmr.3. human. [Q92974-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

ARHGEF2 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72206 mRNA. Translation: AAC97383.1. Sequence problems.
AF486838 mRNA. Translation: AAL96658.1.
AB014551 mRNA. Translation: BAA31626.3. Different initiation.
AL512715 mRNA. Translation: CAC21656.1.
AL355388 Genomic DNA. Translation: CAH72627.1.
AL355388 Genomic DNA. Translation: CAH72629.1.
AL355388 Genomic DNA. Translation: CAH72630.1.
CH471121 Genomic DNA. Translation: EAW53013.1.
CH471121 Genomic DNA. Translation: EAW53015.1.
CH471121 Genomic DNA. Translation: EAW53014.1.
BC020567 mRNA. Translation: AAH20567.1. Different initiation.
BT007407 mRNA. Translation: AAP36075.1.
X15610 mRNA. Translation: CAA33634.1. Frameshift.
CCDSiCCDS1125.1. [Q92974-3]
CCDS53375.1. [Q92974-2]
CCDS53376.1. [Q92974-1]
PIRiS28660.
RefSeqiNP_001155855.1. NM_001162383.1. [Q92974-1]
NP_001155856.1. NM_001162384.1. [Q92974-2]
NP_004714.2. NM_004723.3. [Q92974-3]
UniGeneiHs.743352.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5EFXX-ray2.45A439-582[»]
ProteinModelPortaliQ92974.
SMRiQ92974.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114618. 54 interactors.
IntActiQ92974. 36 interactors.
MINTiMINT-1683482.
STRINGi9606.ENSP00000354837.

PTM databases

iPTMnetiQ92974.
PhosphoSitePlusiQ92974.

Polymorphism and mutation databases

BioMutaiARHGEF2.
DMDMi205830906.

Proteomic databases

EPDiQ92974.
MaxQBiQ92974.
PaxDbiQ92974.
PeptideAtlasiQ92974.
PRIDEiQ92974.
TopDownProteomicsiQ92974-2. [Q92974-2]

Protocols and materials databases

DNASUi9181.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313667; ENSP00000314787; ENSG00000116584. [Q92974-2]
ENST00000313695; ENSP00000315325; ENSG00000116584. [Q92974-3]
ENST00000361247; ENSP00000354837; ENSG00000116584. [Q92974-1]
GeneIDi9181.
KEGGihsa:9181.
UCSCiuc001fmr.3. human. [Q92974-1]

Organism-specific databases

CTDi9181.
DisGeNETi9181.
GeneCardsiARHGEF2.
HGNCiHGNC:682. ARHGEF2.
HPAiHPA017046.
HPA043437.
MIMi607560. gene.
neXtProtiNX_Q92974.
OpenTargetsiENSG00000116584.
PharmGKBiPA24972.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IR0Y. Eukaryota.
ENOG410XT68. LUCA.
GeneTreeiENSGT00760000119193.
HOVERGENiHBG050566.
InParanoidiQ92974.
KOiK12791.
PhylomeDBiQ92974.
TreeFamiTF325887.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000116584-MONOMER.
ReactomeiR-HSA-193648. NRAGE signals death through JNK.
R-HSA-194840. Rho GTPase cycle.
R-HSA-416482. G alpha (12/13) signalling events.
SIGNORiQ92974.

Miscellaneous databases

ChiTaRSiARHGEF2. human.
GeneWikiiARHGEF2.
GenomeRNAii9181.
PROiQ92974.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000116584.
CleanExiHS_ARHGEF2.
ExpressionAtlasiQ92974. baseline and differential.
GenevisibleiQ92974. HS.

Family and domain databases

CDDicd00029. C1. 1 hit.
Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR000219. DH-domain.
IPR002219. PE/DAG-bd.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiARHG2_HUMAN
AccessioniPrimary (citable) accession number: Q92974
Secondary accession number(s): D3DVA6
, O75142, Q15079, Q5VY92, Q8TDA3, Q8WUG4, Q9H023
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 22, 2008
Last modified: November 30, 2016
This is version 171 of the entry and version 4 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 1
    Human chromosome 1: 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.