ROCK1
entrez
6093
canonical
uniprot
Q13464
canonical
ensembl
ENSG00000067900
resolver
ensp
ENSP00000382697
resolver
enst
ENST00000399799
resolver
genesymbol
ROCK1
resolver
hgnc
HGNC:10251
resolver
uniprot
B0YJ91
resolver
uniprot
Q2KHM4
resolver
uniprot
Q59GZ4
resolver
uniprot_entry
ROCK1_HUMAN
resolver
uniprot_sec
B0YJ91
resolver
uniprot_sec
Q2KHM4
resolver
uniprot_sec
Q59GZ4
resolver
activity_regulation
ACTIVITY REGULATION: Activated by RHOA binding. Inhibited by Y-27632.
uniprot
proteins
amino_acid_sequence
MSTGDSFETRFEKMDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNFLSRYKDTINKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDLEEDKGEEETFPIPKAFVGNQLPFVGFTYYSNRRYLSSANPNDNRTSSNADKSLQESLQKTIYKLEEQLHNEMQLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLLQHRINEYQRKAEQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKLSQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLESLNRELQERNRILENSKSQTDKDYYQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLNHSEKEKNNLEIDLNYKLKSLQQRLEQEVNEHKVTKARLTDKHQSIEEAKSVAMCEMEKKLKEEREAREKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEVKNLTLQLEQESNKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMRELQDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLKKIQELQNEKETLATQLDLAETKAESEQLARGLLEEQYFELTQESKKAASRNRQEITDKDHTVSRLEEANSMLTKDIEILRRENEELTEKMKKAEEEYKLEKEEEISNLKAAFEKNINTERTLKTQAVNKLAEIMNRKDFKIDRKKANTQDLRKKEKENRKLQLELNQEREKFNQMVVKHQKELNDMQAQLVEECAHRNELQMQLASKESDIEQLRAKLLDLSDSTSVASFPSADETDGNLPESRIEGWLSVPNRGNIKRYGWKKQYVVVSSKKILFYNDEQDKEQSNPSMVLDIDKLFHVRPVTQGDVYRAETEEIPKIFQILYANEGECRKDVEMEPVQQAEKTNFQNHKGHEFIPTLYHFPANCDACAKPLWHVFKPPPALECRRCHVKCHRDHLDKKEDLICPCKVSYDVTSARDMLLLACSQDEQKKWVTHLVKKIPKNPPSGFVRASPRTLSTRSTANQSFRKVVKNTSGKTS
uniprot
proteins
ec_number
2.7.11.39
uniprot
proteins
function
FUNCTION: Protein kinase which is a key regulator of the actin cytoskeleton and cell polarity (PubMed:10436159, PubMed:10652353, PubMed:11018042, PubMed:11283607, PubMed:17158456, PubMed:18573880, PubMed:19131646, PubMed:8617235, PubMed:9722579). 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 DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, TPPP, PFN1 and PPP1R12A (PubMed:10436159, PubMed:10652353, PubMed:11018042, PubMed:11283607, PubMed:17158456, PubMed:18573880, PubMed:19131646, PubMed:23093407, PubMed:23355470, PubMed:8617235, PubMed:9722579). Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing (PubMed:18694941). Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress (PubMed:19036714). Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability (By similarity). Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation (PubMed:19181962). Required for centrosome positioning and centrosome-dependent exit from mitosis (By similarity). Plays a role in terminal erythroid differentiation (PubMed:21072057). Inhibits podocyte motility via regulation of actin cytoskeletal dynamics and phosphorylation of CFL1 (By similarity). Promotes keratinocyte terminal differentiation (PubMed:19997641). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (By similarity). May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles (By similarity). {ECO:0000250|UniProtKB:P70335, ECO:0000250|UniProtKB:Q8MIT6, ECO:0000269|PubMed:10436159, ECO:0000269|PubMed:10652353, ECO:0000269|PubMed:11018042, ECO:0000269|PubMed:11283607, ECO:0000269|PubMed:17158456, ECO:0000269|PubMed:18573880, ECO:0000269|PubMed:18694941, ECO:0000269|PubMed:19036714, ECO:0000269|PubMed:19131646, ECO:0000269|PubMed:19181962, ECO:0000269|PubMed:19997641, ECO:0000269|PubMed:21072057, ECO:0000269|PubMed:23093407, ECO:0000269|PubMed:23355470, ECO:0000269|PubMed:8617235, ECO:0000269|PubMed:9722579}.
uniprot
proteins
mass_dalton
158175
uniprot
proteins
mutagenesis
MUTAGEN 1113; /note="D->A: Abolishes cleavage by caspase-3."; /evidence="ECO:0000269|PubMed:11283607
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated on serine and threonine residues. {ECO:0000269|PubMed:8617235}.; PTM: Cleaved by caspase-3 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
10436159
uniprot
proteins
pubmed
10508479
uniprot
proteins
pubmed
10652353
uniprot
proteins
pubmed
11018042
uniprot
proteins
pubmed
11283607
uniprot
proteins
pubmed
11956230
uniprot
proteins
pubmed
12773565
uniprot
proteins
pubmed
12778124
uniprot
proteins
pubmed
14660612
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16249185
uniprot
proteins
pubmed
17158456
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17853893
uniprot
proteins
pubmed
18573880
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18694941
uniprot
proteins
pubmed
19036714
uniprot
proteins
pubmed
19131646
uniprot
proteins
pubmed
19181962
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19997641
uniprot
proteins
pubmed
20230755
uniprot
proteins
pubmed
20803696
uniprot
proteins
pubmed
21072057
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22493320
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23093407
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23355470
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
27399334
uniprot
proteins
pubmed
8617235
uniprot
proteins
pubmed
9722579
uniprot
proteins
sequence_length
1354
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8617235}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:P70335}. Golgi apparatus membrane {ECO:0000269|PubMed:12773565}; Peripheral membrane protein {ECO:0000269|PubMed:12773565}. Cell projection, bleb {ECO:0000269|PubMed:18694941}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P70335}. Cell membrane {ECO:0000250|UniProtKB:P70335}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P70335}. Cell projection, ruffle {ECO:0000250|UniProtKB:P70335}. Note=A small proportion is associated with Golgi membranes (PubMed:12773565). Associated with the mother centriole and an intercentriolar linker (By similarity). Colocalizes with ITGB1BP1 and ITGB1 at the cell membrane predominantly in lamellipodia and membrane ruffles, but also in retraction fibers (By similarity). Localizes at the cell membrane in an ITGB1BP1-dependent manner (By similarity). {ECO:0000250|UniProtKB:P70335, ECO:0000269|PubMed:12773565}.
uniprot
proteins