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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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri39 – 8648Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

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

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
  • neuronal 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi53 – 531C → R: Abolishes microtubule binding, increased activity in vitro. 1 Publication
Mutagenesisi143 – 1431S → A: Abolishes phosphorylation by PAK4, self aggregation in the cytoplasm. Increases activity; when associated with A-896. 1 Publication
Mutagenesisi394 – 3941Y → A: Reduces phosphorylation level, normal microtubule localization and activity. 1 Publication
Mutagenesisi679 – 6791T → A: Reduces phosphorylation level. 1 Publication
Mutagenesisi886 – 8861S → A: Normal activity.
Mutagenesisi886 – 8861S → D: Increases activity. Abolishes nucleotide exchange activity; when associated with D-960.
Mutagenesisi896 – 8961S → A: Abolishes phosphorylation by PAK4, self aggregation in the cytoplasm. Increases activity; when associated with A-143. 1 Publication
Mutagenesisi960 – 9601S → A: Normal activity.
Mutagenesisi960 – 9601S → D: Increases activity. Abolishes nucleotide exchange activity; when associated with D-886.

Organism-specific databases

PharmGKBiPA24972.

Polymorphism and mutation databases

BioMutaiARHGEF2.
DMDMi205830906.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 986986Rho guanine nucleotide exchange factor 2PRO_0000080909Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei109 – 1091PhosphoserineCombined sources
Modified residuei122 – 1221PhosphoserineCombined sources
Modified residuei129 – 1291PhosphoserineCombined sources
Modified residuei133 – 1331PhosphoserineCombined sources
Modified residuei137 – 1371PhosphoserineCombined sources
Modified residuei143 – 1431Phosphoserine; by PAK41 Publication
Modified residuei151 – 1511PhosphoserineCombined sources
Modified residuei163 – 1631PhosphoserineCombined sources
Modified residuei172 – 1721PhosphoserineCombined sources
Modified residuei174 – 1741PhosphoserineCombined sources
Modified residuei177 – 1771PhosphoserineCombined sources
Modified residuei353 – 3531N6-acetyllysineCombined sources
Modified residuei645 – 6451PhosphoserineCombined sources
Modified residuei648 – 6481PhosphoserineCombined sources
Modified residuei679 – 6791Phosphothreonine; by MAPK1 or MAPK3Combined sources1 Publication
Modified residuei691 – 6911PhosphoserineCombined sources
Modified residuei696 – 6961PhosphoserineCombined sources
Modified residuei711 – 7111PhosphoserineCombined sources
Modified residuei782 – 7821PhosphoserineBy similarity
Modified residuei886 – 8861Phosphoserine; by PAK1 and AURKACombined sources2 Publications
Modified residuei894 – 8941PhosphotyrosineCombined sources
Modified residuei896 – 8961Phosphoserine; by PAK41 Publication
Modified residuei932 – 9321PhosphoserineCombined sources
Modified residuei940 – 9401PhosphoserineCombined sources
Modified residuei941 – 9411PhosphoserineCombined sources
Modified residuei945 – 9451PhosphothreonineCombined sources
Modified residuei947 – 9471PhosphoserineCombined sources
Modified residuei952 – 9521PhosphoserineBy similarity
Modified residuei953 – 9531PhosphoserineCombined sources
Modified residuei956 – 9561PhosphoserineCombined sources
Modified residuei960 – 9601PhosphoserineCombined sources1 Publication

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.
PhosphoSiteiQ92974.

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

BgeeiQ92974.
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 interactions.
IntActiQ92974. 35 interactions.
MINTiMINT-1683482.
STRINGi9606.ENSP00000354837.

Structurei

3D structure databases

ProteinModelPortaliQ92974.
SMRiQ92974. Positions 210-572.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini235 – 432198DHPROSITE-ProRule annotationAdd
BLAST
Domaini472 – 571100PHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili587 – 61125Sequence analysisAdd
BLAST
Coiled coili798 – 86770Sequence analysisAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri39 – 8648Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IR0Y. Eukaryota.
ENOG410XT68. LUCA.
GeneTreeiENSGT00760000119193.
HOVERGENiHBG050566.
InParanoidiQ92974.
KOiK12791.
OrthoDBiEOG7Q8CMK.
PhylomeDBiQ92974.
TreeFamiTF325887.

Family and domain databases

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 AAC97383.1 differs from that shown.Sequence differs at a large extent from the sequence shown in the paper.Curated
The sequence AAH20567.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA31626.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA33634.1 differs from that shown. Reason: Frameshift at positions 887 and 984. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 2020MSRIE…RELAS → IVGAAGHGRALSLCFDNGPL EQVPLALEETASIGMPRPQG GPLPADPRRTGHLSGTGHQG GYASRLDQDSCHPSAGPLDH SATGMLSKSVPVSGINCLLD RSDTDGNVSQSSAIDLRKRC SQLEGHSGTRVGSSLRQTFS FLSGMTGKA in BAA31626 (PubMed:9734811).CuratedAdd
BLAST
Sequence conflicti631 – 6311M → L in CAA33634 (PubMed:2466560).Curated
Sequence conflicti868 – 8681P → Q in CAA33634 (PubMed:2466560).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2727Missing in isoform 3. 2 PublicationsVSP_039457Add
BLAST
Alternative sequencei194 – 1941Missing in isoform 2 and isoform 3. 3 PublicationsVSP_039458

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

ProteinModelPortaliQ92974.
SMRiQ92974. Positions 210-572.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114618. 54 interactions.
IntActiQ92974. 35 interactions.
MINTiMINT-1683482.
STRINGi9606.ENSP00000354837.

PTM databases

iPTMnetiQ92974.
PhosphoSiteiQ92974.

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

Phylogenomic databases

eggNOGiENOG410IR0Y. Eukaryota.
ENOG410XT68. LUCA.
GeneTreeiENSGT00760000119193.
HOVERGENiHBG050566.
InParanoidiQ92974.
KOiK12791.
OrthoDBiEOG7Q8CMK.
PhylomeDBiQ92974.
TreeFamiTF325887.

Enzyme and pathway databases

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

BgeeiQ92974.
CleanExiHS_ARHGEF2.
ExpressionAtlasiQ92974. baseline and differential.
GenevisibleiQ92974. HS.

Family and domain databases

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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases."
    Ren Y., Li R., Zheng Y., Busch H.
    J. Biol. Chem. 273:34954-34960(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH RHOA AND RAC1.
    Tissue: Cervix carcinoma.
  2. "Nucleotide exchange factor GEF-H1 mediates cross-talk between microtubules and the actin cytoskeleton."
    Krendel M., Zenke F.T., Bokoch G.M.
    Nat. Cell Biol. 4:294-301(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), MUTAGENESIS OF CYS-53 AND TYR-394.
  3. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  4. Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Brain.
  9. "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 28-986 (ISOFORMS 1/3).
  10. "Isolation and characterization of complementary DNA to proliferating cell nucleolar antigen P40."
    Reddy A.B., Chatterjee A., Rothblum L.I., Black A., Busch H.
    Cancer Res. 49:1763-1767(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 630-986 (ISOFORMS 1/2/3).
  11. "p21-activated kinase 1 phosphorylates and regulates 14-3-3 binding to GEF-H1, a microtubule-localized Rho exchange factor."
    Zenke F.T., Krendel M., DerMardirossian C., King C.C., Bohl B.P., Bokoch G.M.
    J. Biol. Chem. 279:18392-18400(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-886, INTERACTION WITH YWHAZ.
  12. "PAK4 mediates morphological changes through the regulation of GEF-H1."
    Callow M.G., Zozulya S., Gishizky M.L., Jallal B., Smeal T.
    J. Cell Sci. 118:1861-1872(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-143 AND SER-896, MUTAGENESIS OF SER-143 AND SER-896, SUBCELLULAR LOCATION, INTERACTION WITH PAK4.
  13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-932, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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-696, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "GEF-H1 modulates localized RhoA activation during cytokinesis under the control of mitotic kinases."
    Birkenfeld J., Nalbant P., Bohl B.P., Pertz O., Hahn K.M., Bokoch G.M.
    Dev. Cell 12:699-712(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-886 AND SER-960, INTERACTION WITH AURKA, SUBCELLULAR LOCATION.
  16. "ERK1/2 phosphorylate GEF-H1 to enhance its guanine nucleotide exchange activity toward RhoA."
    Fujishiro S.H., Tanimura S., Mure S., Kashimoto Y., Watanabe K., Kohno M.
    Biochem. Biophys. Res. Commun. 368:162-167(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-679, INTERACTION WITH MAPK1, MUTAGENESIS OF THR-679.
  17. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  19. "GEF-H1 mediated control of NOD1 dependent NF-kappaB activation by Shigella effectors."
    Fukazawa A., Alonso C., Kurachi K., Gupta S., Lesser C.F., McCormick B.A., Reinecker H.C.
    PLoS Pathog. 4:E1000228-E1000228(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NOD1.
  20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-645; SER-648; SER-696; SER-886; TYR-894; SER-940; SER-941; SER-956 AND SER-960, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. "Cellular functions of GEF-H1, a microtubule-regulated Rho-GEF: is altered GEF-H1 activity a crucial determinant of disease pathogenesis?"
    Birkenfeld J., Nalbant P., Yoon S.-H., Bokoch G.M.
    Trends Cell Biol. 18:210-219(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  22. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172; THR-679; SER-691; SER-696; SER-886; SER-941; THR-945; SER-947; SER-953; SER-956 AND SER-960, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  24. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-956 AND SER-960, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH NOD2 AND RIPK2, INTERACTION WITH RIPK1; RIPK2 AND RIPK3, SUBCELLULAR LOCATION, INDUCTION.
  29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-122; SER-129; SER-133; SER-137; SER-151; SER-163; SER-172; SER-174; SER-177; SER-645; SER-711; SER-886; SER-932; SER-956 AND SER-960, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  31. "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 THR-679 AND SER-956, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  32. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: July 6, 2016
This is version 167 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

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. 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.