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Protein Page:
ROCK1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
ROCK1 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 DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, PFN1 and PPP1R12A. Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing. Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress. Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Required for centrosome positioning and centrosome-dependent exit from mitosis. Plays a role in terminal erythroid differentiation. May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles. Promotes keratinocyte terminal differentiation. Homodimer. Interacts with RHOB, RHOC, MYLC2B snd PTEN. 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. Detected in blood platelets. Activated by RHOA binding. Inhibited by Y- 27632. Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. Note: This description may include information from UniProtKB.
Protein type: Protein kinase, Ser/Thr (non-receptor); Protein kinase, AGC; Kinase, protein; EC 2.7.11.1; AGC group; DMPK family; ROCK subfamily
Cellular Component: Golgi membrane; centriole; ruffle; cytoskeleton; lamellipodium; plasma membrane; cytosol
Molecular Function: protein serine/threonine kinase activity; protein binding; Rho GTPase binding; metal ion binding; ATP binding; protein kinase activity
Biological Process: regulation of cell adhesion; axon guidance; apoptosis; bleb formation; signal transduction; protein amino acid phosphorylation; Rho protein signal transduction; leukocyte adhesion; negative regulation of angiogenesis; smooth muscle contraction; positive regulation of focal adhesion formation; regulation of stress fiber formation; regulation of actin cytoskeleton organization and biogenesis; myoblast migration; regulation of focal adhesion formation; membrane to membrane docking; negative regulation of neuron apoptosis; actin cytoskeleton organization and biogenesis; leukocyte tethering or rolling; regulation of keratinocyte differentiation; leukocyte migration; cell structure disassembly during apoptosis
Reference #:  Q13464 (UniProtKB)
Alt. Names/Synonyms: MGC131603; MGC43611; p160 ROCK-1; p160-ROCK; p160ROCK; PRO0435; Renal carcinoma antigen NY-REN-35; Rho kinase; Rho-associated protein kinase 1; Rho-associated, coiled-coil containing protein kinase 1; Rho-associated, coiled-coil-containing protein kinase 1; ROCK1
Gene Symbols: ROCK1
Molecular weight: 158,175 Da
Basal Isoelectric point: 5.67  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics  |  Adherens Junction Dynamics  |  Apoptosis Regulation  |  Death Receptor Signaling  |  Microtubule Dynamics  |  TGF-├č Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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ROCK1

Protein Structure Not Found.

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Sites Implicated In
enzymatic activity, induced: S1333‑p

Modification Sites and Domains Show Modification Legend
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Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 Y255-p SQGGDGYyGRECDWW
0 22 S282-p DTPFYADsLVGTYSK
0 2 Y405-p TYYSNRRyLsSANPN
0 1 S407-p YSNRRyLsSANPNDN
0 1 T455-p EMEQKCRtsNIKLDK
0 1 S456-p MEQKCRtsNIKLDKI
0 1 K462 tsNIKLDKIMKELDE
0 1 K647-a HLKHNLEkVEGERKE
0 1 S679-p DLNYKLKsLQQRLEQ
0 114 Y913-p RGLLEEQyFELTQES
1 0 T1024-p IDRKKANtQDLRKKE
0 1 K1093 DIEQLRAKLLDLSDs
0 3 S1100-p KLLDLSDstsVAsFP
0 2 T1101-p LLDLSDstsVAsFPs
0 8 S1102-p LDLSDstsVAsFPsA
0 19 S1105-p SDstsVAsFPsADET
0 2 S1108-p tsVAsFPsADETDGN
0 1 T1112 sFPsADETDGNLPES
0 2 Y1153-p SSKKILFyNDEQDKE
0 2 T1180-p LFHVRPVtQGDVYRA
0 4 T1189-p GDVYRAEtEEIPKIF
0 7 Y1287-p ICPCKVSyDVTSARD
0 3 S1328-p PSGFVRAsPRtLstR
0 2 T1331-p FVRAsPRtLstRstA
2 10 S1333-p RAsPRtLstRstANQ
1 5 T1334-p AsPRtLstRstANQs
0 11 S1336-p PRtLstRstANQsFR
1 3 T1337-p RtLstRstANQsFRK
1 35 S1341-p tRstANQsFRKVVKN
  mouse

 
Y255 SQGGDGYYGRECDWW
S282-p DTPFYADsLVGTYSK
Y405 TYYSNRRYLPSANAS
P407 YSNRRYLPSANASEN
T455 EMEQKCRTSNLKLDK
S456 MEQKCRTSNLKLDKI
K462 TSNLKLDKIMKELDE
R647 HLKHNLERVEGERKE
S679 DLNYKLKSIQQRLEQ
Y913 RGILEEQYFELTQES
T1024 IDRKKANTQDLRKKE
K1093-u DIEQLRAkLLDLSDs
S1100-p kLLDLSDstsVAsFP
T1101-p LLDLSDstsVAsFPs
S1102-p LDLSDstsVAsFPsA
S1105-p SDstsVAsFPsADEt
S1108-p tsVAsFPsADEtDGN
T1112-p sFPsADEtDGNLPES
Y1153 SSKKILFYNDEQDKE
T1180 LFHVRPVTQGDVYRA
T1189-p GDVYRAEtEEIPKIF
Y1287 ISPCKVSYDVTSARD
S1328-p PSGFVRAsPRTLSTR
T1331 FVRAsPRTLSTRStA
S1333 RAsPRTLSTRStANQ
T1334 AsPRTLSTRStANQs
S1336 PRTLSTRStANQsFR
T1337-p RTLSTRStANQsFRK
S1341-p TRStANQsFRKVVKN
  rat

 
Y255 SQGGDGYYGRECDWW
S282 DTPFYADSLVGTYSK
Y405 TYYSNRRYLPSANPS
P407 YSNRRYLPSANPSEN
T455 EMEQKCRTSNIKLDk
S456 MEQKCRTSNIKLDkI
K462-m1 TSNIKLDkIMKELDE
R647 HLKHNLERVEGERKE
S679 DLNYKLKSIQQRLEQ
Y913 RGILEEQYFELTQES
T1024 IDRKKANTQDLRKKE
K1093 DIEQLRAKLLDLSDS
S1100 KLLDLSDSTSVASFP
T1101 LLDLSDSTSVASFPS
S1102 LDLSDSTSVASFPSA
S1105 SDSTSVASFPSADET
S1108 TSVASFPSADETDGN
T1112 SFPSADETDGNLPVG
Y1168 SSKKMLFYNDEQDKE
T1195 LFHVRPVTQGDVYRA
T1204 GDVYRAETEEIPKIF
Y1302 IPPCKVSYDVTSARD
S1343 PSGFVRASPRTLSTR
T1346 FVRASPRTLSTRSTA
S1348 RASPRTLSTRSTANQ
T1349 ASPRTLSTRSTANQS
S1351 PRTLSTRSTANQSFR
T1352 RTLSTRSTANQSFRK
S1356 TRSTANQSFRKVVKN
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