ID:ROCK2_HUMAN DESCRIPTION: RecName: Full=Rho-associated protein kinase 2; EC=2.7.11.1; AltName: Full=Rho kinase 2; AltName: Full=Rho-associated, coiled-coil-containing protein kinase 2; AltName: Full=Rho-associated, coiled-coil-containing protein kinase II; Short=ROCK-II; AltName: Full=p164 ROCK-2; FUNCTION: Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of ADD1, BRCA2, CNN1, EZR, DPYSL2, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM. Phosphorylates SORL1 and IRF4. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Positively regulates the activation of p42/MAPK1-p44/MAPK3 and of p90RSK/RPS6KA1 during myogenic differentiation. Plays an important role in the timely initiation of centrosome duplication. Inhibits keratinocyte terminal differentiation. May regulate closure of the eyelids and ventral body wall through organization of actomyosin bundles. Plays a critical role in the regulation of spine and synaptic properties in the hippocampus. CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. COFACTOR: Magnesium (By similarity). ENZYME REGULATION: Activated by RHOA binding. Inhibited by Y-27632 (By similarity). SUBUNIT: Homodimer. Interacts with IRS1, RHOB and RHOC (By similarity). Interacts with RHOA (activated by GTP), PPP1R12A, CHORDC1, SORL1, EP300 and BRCA2. Interacts with NPM1 and this interaction enhances its activity. Interacts with RAF1 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein (By similarity). Nucleus. Cytoplasm, cytoskeleton, centrosome. Note=Cytoplasmic, and associated with actin microfilaments and the plasma membrane (By similarity). DOMAIN: An interaction between Thr-414 and Asp-48 is essential for kinase activity and dimerization (By similarity). PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. Phosphorylation at Tyr-722 reduces its binding to RHOA and is crucial for focal adhesion dynamics. Dephosphorylation by PTPN11 stimulates its RHOA binding activity. PTM: Cleaved by granzyme B during apoptosis. This leads to constitutive activation of the kinase and membrane blebbing. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. SIMILARITY: Contains 1 AGC-kinase C-terminal domain. SIMILARITY: Contains 1 PH domain. SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger. SIMILARITY: Contains 1 protein kinase domain. SIMILARITY: Contains 1 REM (Hr1) repeat. SEQUENCE CAUTION: Sequence=AAX93049.1; Type=Erroneous gene model prediction; Sequence=BAA31594.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on O75116
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.