Rock2
entrez
25537
canonical
uniprot
Q62868
canonical
ensembl
ENSRNOG00000004496
resolver
ensp
ENSRNOP00000073496
resolver
enst
ENSRNOT00000090816
resolver
genesymbol
Rock2
resolver
uniprot
A0A0G2K5N6
resolver
uniprot_entry
A0A0G2K5N6_RAT
resolver
uniprot_entry
ROCK2_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Activated by RHOA binding. Inhibited by Y-27632.
uniprot
proteins
amino_acid_sequence
MSRPPPTGKMPGAPEAAAGDGAGAGRQRKLEALIRDPRSPINVESLLDGLNSLVLDLDFPALRKNKNIDNFLNRYEKIVKKIRGLQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKHGHLKLADFGTCMKMDETGMVHCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSLCFPEDTEISKHAKNLICAFLTDREVRLGRNGVEEIKSASFFKNDQWNWDNIRETAAPVVPELSSDIDSSNFDDIEDDKGDVETFPIPKAFVGNQLPFIGFTYFRENLLLSDSPPCRENDAIQTRKSEESQEIQKKLYALEEHLSSEVQAKEELEQKCKSINTRLEKTAKELEEEITFRKNVESTLRQLEREKALLQHKNAEYQRKADHEADKKRNLENDVNSLKDQLEDLKKRNQSSQISTEKVNQLQKQLDEANALLRTESDTAARLRKTQAESSKQIQQLESNNRDLQDKNCLLETAKLKLEKEFINLQSALESERRDRTHGSEIINDLQGRISGLEEDLKTGKTLLAKVELEKRQLQEKLTDLEKEKSNMEIDMTYQLKVIQQSLEQEEAEHKTTKARLADKNKIYESIEEAKSEAMKEMEKKLLEERSLKQKVENLLLEAEKRCSILDCDLKQSQQKLNELLKQKDVLNEDVRNLTLKIEQETQKRCLMQNDLKMQTQQVNTLKMSEKQIKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEENEEKTKLCKELQQKKQDLQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDTQEQLSKLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGSDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQALHIGMDSSSIGSGPGDAEPDDGFPESRLEGWLSLPVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQSNPYMVLDIDKLFHVRPVTQTDVYRADAKEIPRIFQILYANEGESKKEPEFPVEPVGEKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECSRCHIKCHKDHMDKKEEIIAPCKVYYDISSAKNLLLLANSTEEQQKWVSRLVKKIPKKPPAPDPFARSSPRTSMKIQQNQSIRRPSRQLAPNKPS
uniprot
proteins
disease_involvement
DISEASE: Note=May play a role in hypertension. ROCK-inhibitors lower the blood pressure in spontaneous hypertensive, renal hypertensive and deoxycorticosterone acetate-induced hypertensive rats, but not in normal rats.
uniprot
proteins
ec_number
2.7.11.39
uniprot
proteins
function
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. Plays a role in placental homeostasis during the perinatal period. Plays an important role in generating the circadian rhythm of the aortic myofilament Ca(2+) sensitivity and vascular contractility by modulating the myosin light chain phosphorylation. {ECO:0000269|PubMed:19131646, ECO:0000269|PubMed:21457715, ECO:0000269|PubMed:7493923, ECO:0000269|PubMed:8816443, ECO:0000269|PubMed:9353125}.
uniprot
proteins
mass_dalton
160387
uniprot
proteins
mutagenesis
MUTAGEN 48; /note="D->A: Loss of kinase activity; autophosphorylation and dimerization."; /evidence="ECO:0000269|PubMed:19099536"; MUTAGEN 121; /note="K->A: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:19099536, ECO:0000269|PubMed:8816443"; MUTAGEN 121; /note="K->M: Loss of autophosphorylation."; /evidence="ECO:0000269|PubMed:19099536, ECO:0000269|PubMed:8816443"; MUTAGEN 414; /note="T->A: Loss of kinase activity; autophosphorylation and dimerization."; /evidence="ECO:0000269|PubMed:19099536"; MUTAGEN 1170; /note="W->A: Increased activity and autophosphorylation."; /evidence="ECO:0000269|PubMed:19099536
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated. Phosphorylation at Tyr-722 reduces its binding to RHOA and is crucial for focal adhesion dynamics. Dephosphorylation by PTPN11 stimulates its RHOA binding activity (By similarity). {ECO:0000250}.; PTM: Cleaved by granzyme B during apoptosis. This leads to constitutive activation of the kinase and membrane blebbing.
uniprot
proteins
protein_family
AGC Ser/Thr protein kinase family
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
11739394
uniprot
proteins
pubmed
15699075
uniprot
proteins
pubmed
15753127
uniprot
proteins
pubmed
19099536
uniprot
proteins
pubmed
19131646
uniprot
proteins
pubmed
21457715
uniprot
proteins
pubmed
7493923
uniprot
proteins
pubmed
8816443
uniprot
proteins
pubmed
9353125
uniprot
proteins
sequence_length
1388
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Cytoplasmic, and associated with actin microfilaments and the plasma membrane.
uniprot
proteins