Rho guanine nucleotide exchange factor 2

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Q5FVC2 (ARHG2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Rho guanine nucleotide exchange factor 2

Alternative name(s):
Guanine nucleotide exchange factor H1
Short name=GEF-H1

Gene names

Name:

Arhgef2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	985 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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, and cancer. Binds Rac-GTPases, but does not seem to promote nucleotide exchange activity toward Rac-GTPases. 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 By similarity.
Subunit structure	Interacts with 14-3-3 zeta; when phosphorylated at Ser-885. Interacts with the kinases PAK4, AURKA and MAPK1. Interacts with RHOA and RAC1. Interacts with NOD1 By similarity. Interacts (via the N- terminal zinc finger) with CAPN6 (via domain II) By similarity.
Subcellular location	Cytoplasm By similarity. Cell junction › tight junction By similarity. Golgi apparatus By similarity. Cytoplasm › cytoskeleton › spindle By similarity. Note: Localizes to the tips of cortical microtubules of the mitotic spindle during cell division, and is further released upon microtubule depolymerization By similarity.
Domain	The DH (DBL-homology) domain interacts with and promotes loading of GTP on RhoA. The PH (pleckstrin-homology) domain is involved in microtubule binding and targeting to tight junctions.
Post-translational modification	Phosphorylation of Ser-885 by PAK1 induces binding to protein 14-3-3 zeta, 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 By similarity.
Sequence similarities	Contains 1 DH (DBL-homology) domain. Contains 1 PH domain. Contains 1 phorbol-ester/DAG-type zinc finger.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cell junction Cytoplasm Cytoskeleton Golgi apparatus Microtubule Tight junction
Disease	Proto-oncogene
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Guanine-nucleotide releasing factor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin filament organization Inferred from sequence or structural similarity. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW cell morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB establishment of mitotic spindle orientation Inferred from electronic annotation. Source: Compara intracellular signal transduction Inferred from electronic annotation. Source: InterPro mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of microtubule depolymerization Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of neurogenesis Inferred from electronic annotation. Source: Compara positive regulation of NF-kappaB transcription factor activity Inferred from sequence or structural similarity. Source: UniProtKB regulation of Rho protein signal transduction Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell dendritic shaft Inferred from electronic annotation. Source: Compara microtubule Inferred from sequence or structural similarity. Source: UniProtKB neuronal cell body Inferred from electronic annotation. Source: Compara ruffle membrane Inferred from sequence or structural similarity. Source: UniProtKB spindle Inferred from electronic annotation. Source: UniProtKB-SubCell tight junction Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	Rac GTPase binding Inferred from sequence or structural similarity. Source: UniProtKB Rac guanyl-nucleotide exchange factor activity Inferred from sequence or structural similarity. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW microtubule binding Inferred from sequence or structural similarity. Source: UniProtKB phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 985

985

Rho guanine nucleotide exchange factor 2

PRO_0000345624

Regions

Domain

236 – 433

198

Domain

473 – 572

100

Zinc finger

39 – 86

Phorbol-ester/DAG-type

Coiled coil

591 – 615

Potential

Coiled coil

797 – 866

Potential

Compositional bias

493 – 496

Poly-Leu

Amino acid modifications

Modified residue

143

Phosphoserine; by PAK4 By similarity

Modified residue

163

Phosphoserine By similarity

Modified residue

172

Phosphoserine By similarity

Modified residue

354

N6-acetyllysine By similarity

Modified residue

646

Phosphoserine By similarity

Modified residue

649

Phosphoserine By similarity

Modified residue

680

Phosphothreonine; by MAPK1 or MAPK3 By similarity

Modified residue

692

Phosphoserine By similarity

Modified residue

781

Phosphoserine By similarity

Modified residue

795

Phosphothreonine By similarity

Modified residue

885

Phosphoserine; by PAK1 and AURKA By similarity

Modified residue

893

Phosphotyrosine By similarity

Modified residue

895

Phosphoserine; by PAK4 By similarity

Modified residue

931

Phosphoserine By similarity

Modified residue

939

Phosphoserine By similarity

Modified residue

940

Phosphoserine By similarity

Modified residue

944

Phosphothreonine By similarity

Modified residue

946

Phosphoserine By similarity

Modified residue

952

Phosphoserine By similarity

Modified residue

955

Phosphoserine By similarity

Modified residue

959

Phosphoserine; by CDK1 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q5FVC2 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 73684403A04B9242
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FASTA

985

111,909

        10         20         30         40         50         60 
MSRIESLTRA RIDRSKEQAT KTREKEKMKE AKDARYTNGH LFTTISVSGM TMCYACNKSI 

        70         80         90        100        110        120 
TAKEALICPT CNVTIHNRCK DTLANCTKVK QKQQKAALLR NNTALQSVSL RSKTTTRERP 

       130        140        150        160        170        180 
TSAIYPSDSF RQSLLGSRRG LSSLSLAKSV STTNIAGHFN DESPLGLRQI LSQSTDSLNM 

       190        200        210        220        230        240 
RNRTLSVESL IDEGVEVFYN ELMSDFEMDE KDFEADSWSL AVDSSFLQQH KKEVMKKQDV 

       250        260        270        280        290        300 
IYELIQTELH HVRTLKIMTR LFRTGMLEEL QMEPEVVQGL FPCVDELSDI HTRFLSQLLE 

       310        320        330        340        350        360 
RRRQALCPGS TRNFVIHRLG DLLISQFSGS NAEQMRKTYS EFCSRHTKAL KLYKELYARD 

       370        380        390        400        410        420 
KRFQQFIRKM TRSAVLKRHG VQECILLVTQ RITKYPVLIN RILQNSHGIE EEYQDLAAAL 

       430        440        450        460        470        480 
GLVKELLSNV DQDVHELEKE ARLQEIYNRM DPRAQTPVPG KGPFGRDELL RRKLIHDGCL 

       490        500        510        520        530        540 
LWKTATGRFK DVLLLLMTDV LVFLQEKDQK YIFTSLDKPS VVSLQNLIVR DIANQAKGMF 

       550        560        570        580        590        600 
LISSGPPEMY EVHAASRDDR TTWIRVIQQS VRLCPSREDF PLIETEDKAY LRRIKTKLQQ 

       610        620        630        640        650        660 
KNQALVELLQ MNVELFAEMV HFQALKAGFI GMPPPTLPRG LFRLESFESL RGERLLKDAL 

       670        680        690        700        710        720 
REVEGLKDLL LGPCVDLPLT AREPALPVEA DSGSCPGVTA NGEARTFNGS IELCRADSDS 

       730        740        750        760        770        780 
SQKDRNGNQL RSPQEEALQP LVNLYGLLQG LQAVVVQQER LMEALFPEGP ERWEKLSRAN 

       790        800        810        820        830        840 
SRDGEAGRAA VASVTPEKQA TELALLQRQH SLLQEELRRC QRLGEERATE AGSLEARLRE 

       850        860        870        880        890        900 
SEQARALLER EAEEIRRQLA ALGQNEPLPA EAPWARRPLD PRRRSLPAGD ALYLSFNPPQ 

       910        920        930        940        950        960 
PSRGHDRLDL PVTVRSLHRP FDDREAQELG SPEDRLQDSS DPDTCSEEEV SSRLSPPHSP 

       970        980 
RDFTRMQDIP EETESRDGEP TASES

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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]. Tissue: Lung.
[2]	"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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC090078 mRNA. Translation: AAH90078.1.
IPI	IPI00368617.
RefSeq	NP_001012079.1. NM_001012079.1.
UniGene	Rn.12255.
3D structure databases
HSSP	HSSP built from PDB template 1XCG based on UniProtKB O15085.
ProteinModelPortal	Q5FVC2.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48721N.
STRING	10116.ENSRNOP00000027182.
PTM databases
PhosphoSite	Q5FVC2.
Proteomic databases
PaxDb	Q5FVC2.
PRIDE	Q5FVC2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000027182; ENSRNOP00000027182; ENSRNOG00000020027.
GeneID	310635.
KEGG	rno:310635.
Organism-specific databases
CTD	9181.
RGD	1304659. Arhgef2.
Phylogenomic databases
eggNOG	COG5422.
GeneTree	ENSGT00660000095401.
HOGENOM	HOG000236361.
HOVERGEN	HBG050566.
InParanoid	Q5FVC2.
KO	K12791.
OMA	EPDSGGN.
OrthoDB	EOG43FGW6.
Gene expression databases
ArrayExpress	Q5FVC2.
Genevestigator	Q5FVC2.
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. IPR002219. Prot_Kinase_C-like_PE/DAG-bd. IPR015721. RhoGEF-like. [Graphical view]
PANTHER	PTHR22825. PTHR22825. 1 hit.
Pfam	PF00169. PH. 1 hit. PF00621. RhoGEF. 1 hit. [Graphical view]
SMART	SM00109. C1. 1 hit. SM00233. PH. 1 hit. SM00325. RhoGEF. 1 hit. [Graphical view]
SUPFAM	SSF48065. DH-domain. 1 hit.
PROSITE	PS00741. DH_1. False negative. PS50010. 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]
ProtoNet	Search...
Other
NextBio	662276.

Entry information

Entry name

ARHG2_RAT

Accession

Primary (citable) accession number: Q5FVC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 22, 2008
Last sequence update:	March 1, 2005
Last modified:	April 3, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents