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Details on Person UniProt:Q13464 ROCK1

Class:IdReferenceGeneProduct:153167
_chainChangeLoginitiator methionine:1 added on Fri February 6 2015;chain:2-1354 added on Fri February 6 2015;initiator methionine:1 for 153167 removed on Fri Nov 03 2023;initiator methionine: for 153167 added on Fri Nov 03 2023;initiator methionine: for 153167 removed on Fri Aug 15 2025;initiator methionine:1 for 153167 added on Fri Aug 15 2025
_displayNameUniProt:Q13464 ROCK1
_timestamp2026-02-20 21:53:25
chaininitiator methionine:1
chain:2-1354
checksum93078CBB009A6F27
commentFUNCTION 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).CATALYTIC ACTIVITY L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)CATALYTIC ACTIVITY L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)COFACTOR Activated by RHOA binding. Inhibited by Y-27632.SUBUNIT Homodimer. Interacts with RHOB, RHOC, MYLC2B and PTEN. Interacts with ITGB1BP1 (via N-terminus and PTB domain) (By similarity). Interacts with RHOA (activated by GTP), CHORDC1, DAPK3, GEM, JIP3, RHOE, PPP1R12A, PFN1, LIMK1, LIMK2 and TSG101. Interacts with FHOD1 in a Src-dependent manner. Interacts with SHROOM3 (PubMed:22493320).INTERACTION 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).TISSUE SPECIFICITY Detected in blood platelets.DOMAIN The C-terminal auto-inhibitory domain interferes with kinase activity. RHOA binding leads to a conformation change and activation of the kinase. Truncated ROCK1 is constitutively activated.PTM Autophosphorylated on serine and threonine residues.PTM Cleaved by caspase-3 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.
created[InstanceEdit:143527] Schmidt, EE, 2004-11-12 07:45:10
descriptionrecommendedName: Rho-associated protein kinase 1 ecNumber evidence="12 13 14 32 33"2.7.11.39 alternativeName: Renal carcinoma antigen NY-REN-35 alternativeName: Rho-associated, coiled-coil-containing protein kinase 1 alternativeName: Rho-associated, coiled-coil-containing protein kinase I shortName: ROCK-I alternativeName: p160 ROCK-1 shortName: p160ROCK
geneNameROCK1
identifierQ13464
isSequenceChangedFALSE
keyword3D-structure
Acetylation
Apoptosis
ATP-binding
Cell membrane
Cell projection
Coiled coil
Cytoplasm
Cytoskeleton
Direct protein sequencing
Golgi apparatus
Kinase
Magnesium
Membrane
Metal-binding
Nucleotide-binding
Phosphoprotein
Proteomics identification
Reference proteome
Serine/threonine-protein kinase
Transferase
Zinc
Zinc-finger
modified[InstanceEdit:9836292] Weiser, Joel, 2023-05-25
[InstanceEdit:9852000] Weiser, Joel, 2023-11-03
[InstanceEdit:9917590] Weiser, Joel, 2024-08-09
[InstanceEdit:9926675] Weiser, Joel, 2024-11-03
[InstanceEdit:9939033] Weiser, Joel, 2025-02-21
[InstanceEdit:9963647] Weiser, Joel, 2025-08-15
[InstanceEdit:9983091] Weiser, Joel, 2026-02-20
nameROCK1
referenceDatabase[ReferenceDatabase:2] UniProt
referenceGene[ReferenceDNASequence:8962125] ENSEMBL:ENSG00000067900 ROCK1 [Homo sapiens]
secondaryIdentifierROCK1_HUMAN
B0YJ91
Q2KHM4
Q59GZ4
sequenceLength1354
species[Species:48887] Homo sapiens
(referenceEntity)[EntityWithAccessionedSequence:212509] ROCK1 [cytosol] [Homo sapiens]
[EntityWithAccessionedSequence:212523] ROCK1(1-1113) [cytosol] [Homo sapiens]
[EntityWithAccessionedSequence:212524] ROCK1(1114-1354) [cytosol] [Homo sapiens]
[EntityWithAccessionedSequence:4687777] Activated ROCK1 [cytosol] [Homo sapiens]
[EntityWithAccessionedSequence:6804967] ROCK1 [secretory granule lumen] [Homo sapiens]
[EntityWithAccessionedSequence:6804988] ROCK1 [extracellular exosome] [Homo sapiens]
[EntityWithAccessionedSequence:6806527] ROCK1 [extracellular region] [Homo sapiens]
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No pathways have been reviewed or authored by UniProt:Q13464 ROCK1 (153167)