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Protein Page:
ROCK2 (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
ROCK2 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. Homodimer. Interacts with IRS1, RHOB and RHOC. Interacts with RHOA (activated by GTP), PPP1R12A, CHORDC1, SORL1, EP300 and BRCA2. Interacts with NPM1 and this interaction enhances its activity. Interacts with RAF1. 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, AGC; Protein kinase, Ser/Thr (non-receptor); EC 2.7.11.1; Kinase, protein; AGC group; DMPK family; ROCK subfamily
Cellular Component: centrosome; plasma membrane; spindle pole centrosome; cytosol; nucleus
Molecular Function: protein serine/threonine kinase activity; protein binding; Rho GTPase binding; metal ion binding; structural molecule activity; ATP binding
Biological Process: regulation of cell adhesion; axon guidance; negative regulation of angiogenesis; smooth muscle contraction; induction of apoptosis via death domain receptors; regulation of actin cytoskeleton organization and biogenesis; regulation of stress fiber formation; regulation of focal adhesion formation; neural tube closure; cytokinesis; actin cytoskeleton organization and biogenesis; regulation of keratinocyte differentiation; protein amino acid phosphorylation; centrosome duplication
Reference #:  O75116 (UniProtKB)
Alt. Names/Synonyms: KIAA0619; p164 ROCK-2; Rho kinase 2; Rho-associated protein kinase 2; Rho-associated, coiled-coil containing protein kinase 2; Rho-associated, coiled-coil-containing protein kinase 2; ROCK2
Gene Symbols: ROCK2
Molecular weight: 160,900 Da
Basal Isoelectric point: 5.75  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics  |  Adherens Junction Dynamics  |  Apoptosis Regulation  |  Microtubule Dynamics  |  TGF-├č Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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ROCK2

Protein Structure Not Found.

Substrate Sequence Logo
Sequence Logo

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Sites Implicated In
cell adhesion, altered: Y722‑p
enzymatic activity, induced: S1366‑p
enzymatic activity, inhibited: Y722‑p
molecular association, regulation: Y722‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

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 1 S2 ______MSRPPPTGK
0 1 T7 _MSRPPPTGKMPGAP
0 1 K121-u SQKVYAMkLLSKFEM
0 2 T253 HCDTAVGTPDYISPE
1 0 Y256 TAVGTPDYISPEVLK
0 22 S298-p DTPFYADsLVGTYSK
1 0 T414 QLPFIGFTYYRENLL
0 4 S425-p ENLLLSDsPSCRETD
0 1 T567-p LQRQLDEtNALLRTE
0 2 T577-p LLRTESDtAARLRKT
2 79 Y722-p LADKNKIyEsIEEAK
0 3 S724-p DKNKIyEsIEEAKSE
0 6 Y936-p RSIAEEQySDLEKEK
1 1 T967 ELTEKDATIASLEET
0 1 K989-u VANLANEkEELNNkL
0 1 K995-u EkEELNNkLKDVQEQ
0 1 K1022 AIKAQFEKQLLTERT
0 1 N1052 KEPVKRGNDTDVRRK
0 2 K1071-u RKLHMELkSEREKLt
0 1 T1078-p kSEREKLtQQMIKYQ
1 1 S1099 QAQIAEESQIRIELQ
0 1 S1132-p ALHIGLDsssIGsGP
1 2 S1133-p LHIGLDsssIGsGPG
0 5 S1134-p HIGLDsssIGsGPGD
0 10 S1137-p LDsssIGsGPGDAEA
0 1 T1212-p LFHVRPVtQTDVYRA
0 17 Y1319-p IAPCKVYyDISTAKN
0 1 S1362-p PDPFARSsPRTsMkI
2 0 S1366-p ARSsPRTsMkIQQNQ
0 1 K1368-m1 SsPRTsMkIQQNQsI
2 8 S1374-p MkIQQNQsIRRPsRQ
2 16 S1379-p NQsIRRPsRQLAPNK
  mouse

 
S2-p ______MsRPPPtGK
T7-p _MsRPPPtGKMPGAP
K121 SQKVYAMKLLSKFEM
T253-p HCDTAVGtPDYISPE
Y256 TAVGtPDYISPEVLK
S298-p DTPFYADsLVGTYSK
T414 QLPFIGFTYFRENLL
S425-p ENLLLSDsPPCREND
A567 LQKQLDEANALLRTE
T577 LLRTESDTAARLRKT
Y722-p LADKNKIyEsIEEAK
S724-p DKNKIyEsIEEAKSE
Y936 RSIAEEQYSDLEKEK
T967 ELTEKDTTIASLEET
K989 VANLANEKEELNNKL
K995 EKEELNNKLKDSQEQ
K1022-u AIKAQFEkQLLNERT
S1052-p KEPVKRGsDTDVRRK
K1071 RKLHMELKSEREKLT
T1078 KSEREKLTQQMIKYQ
S1099 QAQIAEESQIRIELQ
S1132 ALHIGMDSSsIGsGP
S1133 LHIGMDSSsIGsGPG
S1134-p HIGMDSSsIGsGPGD
S1137-p MDSSsIGsGPGDAEP
T1212 LFHVRPVTQTDVYRA
Y1319 IAPCKVYYDISSAKN
S1362 PDPFARSSPRTSMKI
S1366 ARSSPRTSMKIQQNQ
K1368 SSPRTSMKIQQNQsI
S1374-p MKIQQNQsIRRPsRQ
S1379-p NQsIRRPsRQLAPNK
  rat

 
- gap
- gap
K121 SQKVYAMKLLSKFEM
T253 HCDTAVGTPDyISPE
Y256-p TAVGTPDyISPEVLK
S298 DTPFYADSLVGTYSK
T414-p QLPFIGFtYFRENLL
S425 ENLLLSDSPPCREND
A567 LQKQLDEANALLRTE
T577 LLRTESDTAARLRKT
Y722 LADKNKIYESIEEAK
S724 DKNKIYESIEEAKSE
Y936 RSIAEEQYSDLEKEK
T967 ELTEKDATIASLEET
K989 VANLANEKEELNNKL
K995 EKEELNNKLKDTQEQ
K1022 AIKAQFEKQLLTERT
S1052 KEPVKRGSDTDVRRK
K1071 RKLHMELKSEREKLT
T1078 KSEREKLTQQMIKYQ
S1099 QAQIAEESQIRIELQ
S1132 ALHIGMDSSSIGSGP
S1133 LHIGMDSSSIGSGPG
S1134 HIGMDSSSIGSGPGD
S1137 MDSSSIGSGPGDAEP
T1212 LFHVRPVTQTDVYRA
Y1319 IAPCKVYYDISSAKN
S1362 PDPFARSSPRTSMKI
S1366 ARSSPRTSMKIQQNQ
K1368 SSPRTSMKIQQNQSI
S1374 MKIQQNQSIRRPsRQ
S1379-p NQSIRRPsRQLAPNK
  cow

 
S2 ______MSRPPPTGK
T7 _MSRPPPTGKMPGAP
K121 SQKVYAMKLLSKFEM
T253 HCDTAVGTPDYISPE
Y256 TAVGTPDYISPEVLK
S298 DTPFYADSLVGTYSK
T414 QLPFIGFTYYRENLL
S425 ENLLLSDSPSCKEND
T567 LQRQLDETNALLRTE
T577 LLRTESDTAARLRKT
Y722 LADKNKIYESIEEAK
S724 DKNKIYESIEEAKSE
Y936 RSIAEEQYSDLEKEK
T967-p ELTEKDAtIASLEET
K989 VANLANEKEELNNKL
K995 EKEELNNKLKEAQEQ
K1022 AIKAQFEKQLLTERT
N1052 KEPVKRGNDTDVRRK
K1071 RKLHMELKSEREKLT
T1078 KSEREKLTQQMIKYQ
S1099-p QAQIAEEsQIRIELQ
S1132 ALHIGLDSsSIGSGP
S1133-p LHIGLDSsSIGSGPG
S1134 HIGLDSsSIGSGPGD
S1137 LDSsSIGSGPGDTEA
T1212 LFHVRPVTQTDVYRA
Y1319 IAPCKVYYDISSAKN
S1362 PDPFARSSPRTSMKI
S1366 ARSSPRTSMKIQQNQ
K1368 SSPRTSMKIQQNQsI
S1374-p MKIQQNQsIRRPSRQ
S1379 NQsIRRPSRQLAPNK
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