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Reviewed, UniProtKB/Swiss-Prot O15085 (ARHGB_HUMAN)

Last modified December 16, 2008. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Rho guanine nucleotide exchange factor 11
Alternative name(s):
    PDZ-RhoGEF
Gene names
Name: ARHGEF11
Synonyms: KIAA0380
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1522 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13.

Subunit structure

Interacts with GNA12 and GNA13 through the RGS domain. Interacts with RHOA, PLXNB1 and PLXNB2. Interacts with SLC1A6 By similarity.

Subcellular location

Cytoplasm. Membrane. Note= Translocated to the membrane upon stimulation. Ref.7

Tissue specificity

Ubiquitously expressed. Ref.4

Domain

The poly-Pro region is essential for plasma membrane localization upon stimulation.

Sequence similarities

Contains 1 DH (DBL-homology) domain.

Contains 1 PDZ (DHR) domain.

Contains 1 PH domain.

Contains 1 RGSL (RGS-like) domain.

Ontologies

Keywords

   Cellular componentCytoplasm
Membrane
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   Molecular functionGTPase activation
Guanine-nucleotide releasing factor
   PTMPhosphoprotein
   Technical term3D-structure

Gene Ontology (GO)

   Biological processG-protein coupled receptor protein signaling pathway Ref.4

Traceable author statement. Source: UniProtKB

actin cytoskeleton organization Ref.4

Non-traceable author statement. Source: UniProtKB

cell motion Ref.4

Non-traceable author statement. Source: UniProtKB

cytokinesis Ref.4

Non-traceable author statement. Source: UniProtKB

establishment of cell polarity Ref.4

Non-traceable author statement. Source: UniProtKB

positive regulation of transcription, DNA-dependent Ref.4

Inferred from direct assay. Source: UniProtKB

regulation of Rho protein signal transduction

Inferred from electronic annotation. Source: InterPro

regulation of cell growth Ref.4

Non-traceable author statement. Source: UniProtKB

striated muscle contraction Ref.4

Non-traceable author statement. Source: UniProtKB

   Cellular componentcytoplasm

Inferred from direct assay. Source: MGI

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionG-protein-coupled receptor binding

Inferred from direct assay. Source: MGI

GTPase activator activity

Inferred from electronic annotation. Source: UniProtKB-KW

Rho guanyl-nucleotide exchange factor activity Ref.4

Traceable author statement. Source: UniProtKB

signal transducer activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15221522Rho guanine nucleotide exchange factor 11
PRO_0000080928

Regions

Domain47 – 12680PDZ
Domain306 – 486181RGSL
Domain734 – 923190DH
Domain965 – 1079115PH
Coiled coil444 – 47027 Potential
Compositional bias1094 – 10996Poly-Pro

Amino acid modifications

Modified residue2451Phosphoserine Ref.10
Modified residue2511Phosphoserine Ref.10
Modified residue2541Phosphothreonine Ref.10
Modified residue2551Phosphoserine Ref.10
Modified residue6631Phosphoserine Ref.8 Ref.9
Modified residue6681Phosphothreonine Ref.10 Ref.8 Ref.9
Modified residue6721Phosphothreonine Ref.10 Ref.9
Modified residue11551Phosphoserine Ref.10 Ref.8
Modified residue12951Phosphoserine Ref.10
Modified residue13001Phosphoserine Ref.10
Modified residue14571Phosphoserine Ref.10
Modified residue14581Phosphoserine Ref.10
Modified residue14621Phosphothreonine Ref.10
Modified residue14751Phosphothreonine Ref.10
Modified residue14801Phosphoserine Ref.10
Modified residue14891Phosphoserine Ref.10
Modified residue14911Phosphoserine Ref.10

Natural variations

Natural variant14271H → R: dbSNP rs945508.
VAR_024285

Secondary structure

................................................................................................. 1522
Helix Strand Turn

Details...

Sequences

Sequence LengthMass