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Protein

Rho-associated protein kinase 2

Gene

ROCK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 an important role in generating the circadian rhythm of the aortic myofilament Ca2+ sensitivity and vascular contractility by modulating the myosin light chain phosphorylation.8 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Enzyme regulationi

Activated by RHOA binding. Inhibited by Y-27632 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei121 – 1211ATPPROSITE-ProRule annotation
Active sitei214 – 2141Proton acceptorPROSITE-ProRule annotation
Sitei1131 – 11322Cleavage; by granzyme B

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi98 – 1069ATPPROSITE-ProRule annotation
Zinc fingeri1260 – 131556Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB
  • structural molecule activity Source: ProtInc

GO - Biological processi

  • actin cytoskeleton organization Source: Ensembl
  • axon guidance Source: Reactome
  • centrosome duplication Source: UniProtKB
  • cytokinesis Source: ProtInc
  • dendrite morphogenesis Source: Ensembl
  • ephrin receptor signaling pathway Source: Reactome
  • extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
  • negative regulation of angiogenesis Source: UniProtKB
  • neural tube closure Source: Ensembl
  • positive regulation of centrosome duplication Source: Ensembl
  • protein phosphorylation Source: UniProtKB
  • regulation of actin cytoskeleton organization Source: UniProtKB
  • regulation of cell adhesion Source: UniProtKB
  • regulation of cell motility Source: UniProtKB
  • regulation of circadian rhythm Source: UniProtKB
  • regulation of establishment of cell polarity Source: UniProtKB
  • regulation of focal adhesion assembly Source: UniProtKB
  • regulation of keratinocyte differentiation Source: UniProtKB
  • regulation of stress fiber assembly Source: UniProtKB
  • Rho protein signal transduction Source: InterPro
  • rhythmic process Source: UniProtKB-KW
  • small GTPase mediated signal transduction Source: Reactome
  • smooth muscle contraction Source: UniProtKB
  • vascular endothelial growth factor receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Biological rhythms

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_18407. G alpha (12/13) signalling events.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.
REACT_263952. EPHB-mediated forward signaling.
REACT_264464. VEGFA-VEGFR2 Pathway.
REACT_264548. EPHA-mediated growth cone collapse.
REACT_355192. RHO GTPases Activate ROCKs.
SignaLinkiO75116.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho-associated protein kinase 2 (EC:2.7.11.1)
Alternative name(s):
Rho kinase 2
Rho-associated, coiled-coil-containing protein kinase 2
Rho-associated, coiled-coil-containing protein kinase II
Short name:
ROCK-II
p164 ROCK-2
Gene namesi
Name:ROCK2
Synonyms:KIAA0619
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:10252. ROCK2.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  • cytosol Source: Reactome
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB-SubCell
  • spindle pole centrosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1131 – 11311D → A: Abolishes cleavage by granzyme B. 1 Publication

Organism-specific databases

PharmGKBiPA34624.

Polymorphism and mutation databases

BioMutaiROCK2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13881388Rho-associated protein kinase 2PRO_0000086625Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei414 – 4141Phosphothreonine; by ROCK2By similarity
Modified residuei722 – 7221Phosphotyrosine; by SRC2 Publications
Modified residuei1137 – 11371Phosphoserine5 Publications

Post-translational modificationi

Phosphorylation at Tyr-722 reduces its binding to RHOA and is crucial for focal adhesion dynamics. Dephosphorylation by PTPN11 stimulates its RHOA binding activity.2 Publications
Cleaved by granzyme B during apoptosis. This leads to constitutive activation of the kinase and membrane blebbing.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO75116.
PaxDbiO75116.
PRIDEiO75116.

PTM databases

PhosphoSiteiO75116.

Expressioni

Gene expression databases

BgeeiO75116.
CleanExiHS_ROCK2.
ExpressionAtlasiO75116. baseline and differential.
GenevisibleiO75116. HS.

Organism-specific databases

HPAiCAB008666.
HPA007459.
HPA044109.

Interactioni

Subunit structurei

Homodimer. Interacts with IRS1, RHOB and RHOC (By similarity). Interacts with RHOA (activated by GTP), PPP1R12A, CHORDC1, SORL1, EP300 and BRCA2. Interacts with NPM1 and this interaction enhances its activity. Interacts with RAF1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi114860. 14 interactions.
IntActiO75116. 8 interactions.
MINTiMINT-4299744.
STRINGi9606.ENSP00000317985.

Structurei

Secondary structure

1
1388
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 357Combined sources
Helixi43 – 5715Combined sources
Helixi60 – 634Combined sources
Helixi66 – 8520Combined sources
Helixi89 – 913Combined sources
Beta strandi92 – 1009Combined sources
Beta strandi102 – 11110Combined sources
Turni112 – 1143Combined sources
Beta strandi117 – 1248Combined sources
Helixi125 – 1306Combined sources
Helixi138 – 1469Combined sources
Beta strandi155 – 1606Combined sources
Beta strandi162 – 1698Combined sources
Helixi177 – 1837Combined sources
Helixi188 – 20720Combined sources
Helixi217 – 2193Combined sources
Beta strandi220 – 2223Combined sources
Beta strandi228 – 2303Combined sources
Beta strandi241 – 2466Combined sources
Helixi254 – 2563Combined sources
Helixi259 – 2646Combined sources
Beta strandi270 – 2723Combined sources
Helixi274 – 28916Combined sources
Helixi299 – 3079Combined sources
Helixi309 – 3124Combined sources
Helixi323 – 33210Combined sources
Helixi336 – 3383Combined sources
Turni340 – 3434Combined sources
Helixi346 – 3494Combined sources
Helixi352 – 3543Combined sources
Turni361 – 3633Combined sources
Helixi364 – 3663Combined sources
Helixi408 – 4103Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4L6QX-ray2.79A/B19-417[»]
4WOTX-ray2.93A/B/C/D22-417[»]
ProteinModelPortaliO75116.
SMRiO75116. Positions 27-417, 559-709, 857-926, 979-1045, 1151-1351.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini92 – 354263Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini357 – 42569AGC-kinase C-terminalAdd
BLAST
Repeati475 – 55985REMAdd
BLAST
Domaini1150 – 1349200PHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni363 – 784422Interaction with PPP1R12AAdd
BLAST
Regioni373 – 42048Interaction with NPM1Add
BLAST
Regioni979 – 104769RHOA bindingBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili429 – 1024596Sequence AnalysisAdd
BLAST
Coiled coili1053 – 113179Sequence AnalysisAdd
BLAST

Domaini

An interaction between Thr-414 and Asp-48 is essential for kinase activity and dimerization.By similarity

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 REM (Hr1) repeat.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1260 – 131556Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118994.
HOGENOMiHOG000017259.
HOVERGENiHBG053111.
InParanoidiO75116.
KOiK17388.
OMAiNQSIRRP.
OrthoDBiEOG7DZ8J4.
PhylomeDBiO75116.
TreeFamiTF313551.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR000961. AGC-kinase_C.
IPR011072. HR1_rho-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR011993. PH-like_dom.
IPR001849. PH_domain.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015008. Rho-bd_dom.
IPR020684. ROCK1/ROCK2.
IPR029878. ROCK2.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR22988:SF24. PTHR22988:SF24. 1 hit.
PfamiPF02185. HR1. 1 hit.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF08912. Rho_Binding. 1 hit.
[Graphical view]
PIRSFiPIRSF037568. Rho_kinase. 1 hit.
SMARTiSM00109. C1. 1 hit.
SM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O75116-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRPPPTGKM PGAPETAPGD GAGASRQRKL EALIRDPRSP INVESLLDGL
60 70 80 90 100
NSLVLDLDFP ALRKNKNIDN FLNRYEKIVK KIRGLQMKAE DYDVVKVIGR
110 120 130 140 150
GAFGEVQLVR HKASQKVYAM KLLSKFEMIK RSDSAFFWEE RDIMAFANSP
160 170 180 190 200
WVVQLFYAFQ DDRYLYMVME YMPGGDLVNL MSNYDVPEKW AKFYTAEVVL
210 220 230 240 250
ALDAIHSMGL IHRDVKPDNM LLDKHGHLKL ADFGTCMKMD ETGMVHCDTA
260 270 280 290 300
VGTPDYISPE VLKSQGGDGF YGRECDWWSV GVFLYEMLVG DTPFYADSLV
310 320 330 340 350
GTYSKIMDHK NSLCFPEDAE ISKHAKNLIC AFLTDREVRL GRNGVEEIRQ
360 370 380 390 400
HPFFKNDQWH WDNIRETAAP VVPELSSDID SSNFDDIEDD KGDVETFPIP
410 420 430 440 450
KAFVGNQLPF IGFTYYRENL LLSDSPSCRE TDSIQSRKNE ESQEIQKKLY
460 470 480 490 500
TLEEHLSNEM QAKEELEQKC KSVNTRLEKT AKELEEEITL RKSVESALRQ
510 520 530 540 550
LEREKALLQH KNAEYQRKAD HEADKKRNLE NDVNSLKDQL EDLKKRNQNS
560 570 580 590 600
QISTEKVNQL QRQLDETNAL LRTESDTAAR LRKTQAESSK QIQQLESNNR
610 620 630 640 650
DLQDKNCLLE TAKLKLEKEF INLQSALESE RRDRTHGSEI INDLQGRICG
660 670 680 690 700
LEEDLKNGKI LLAKVELEKR QLQERFTDLE KEKSNMEIDM TYQLKVIQQS
710 720 730 740 750
LEQEEAEHKA TKARLADKNK IYESIEEAKS EAMKEMEKKL LEERTLKQKV
760 770 780 790 800
ENLLLEAEKR CSLLDCDLKQ SQQKINELLK QKDVLNEDVR NLTLKIEQET
810 820 830 840 850
QKRCLTQNDL KMQTQQVNTL KMSEKQLKQE NNHLMEMKMN LEKQNAELRK
860 870 880 890 900
ERQDADGQMK ELQDQLEAEQ YFSTLYKTQV RELKEECEEK TKLGKELQQK
910 920 930 940 950
KQELQDERDS LAAQLEITLT KADSEQLARS IAEEQYSDLE KEKIMKELEI
960 970 980 990 1000
KEMMARHKQE LTEKDATIAS LEETNRTLTS DVANLANEKE ELNNKLKDVQ
1010 1020 1030 1040 1050
EQLSRLKDEE ISAAAIKAQF EKQLLTERTL KTQAVNKLAE IMNRKEPVKR
1060 1070 1080 1090 1100
GNDTDVRRKE KENRKLHMEL KSEREKLTQQ MIKYQKELNE MQAQIAEESQ
1110 1120 1130 1140 1150
IRIELQMTLD SKDSDIEQLR SQLQALHIGL DSSSIGSGPG DAEADDGFPE
1160 1170 1180 1190 1200
SRLEGWLSLP VRNNTKKFGW VKKYVIVSSK KILFYDSEQD KEQSNPYMVL
1210 1220 1230 1240 1250
DIDKLFHVRP VTQTDVYRAD AKEIPRIFQI LYANEGESKK EQEFPVEPVG
1260 1270 1280 1290 1300
EKSNYICHKG HEFIPTLYHF PTNCEACMKP LWHMFKPPPA LECRRCHIKC
1310 1320 1330 1340 1350
HKDHMDKKEE IIAPCKVYYD ISTAKNLLLL ANSTEEQQKW VSRLVKKIPK
1360 1370 1380
KPPAPDPFAR SSPRTSMKIQ QNQSIRRPSR QLAPNKPS
Length:1,388
Mass (Da):160,900
Last modified:November 24, 2009 - v4
Checksum:i876240F410C2487E
GO

Sequence cautioni

The sequence AAX93049.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAA31594.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831R → K in BAA75636 (PubMed:9933571).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti431 – 4311T → N.3 Publications
Corresponds to variant rs2230774 [ dbSNP | Ensembl ].
VAR_041062
Natural varianti601 – 6011D → V.1 Publication
Corresponds to variant rs35768389 [ dbSNP | Ensembl ].
VAR_041063
Natural varianti1083 – 10831K → M.
Corresponds to variant rs34945852 [ dbSNP | Ensembl ].
VAR_057110
Natural varianti1194 – 11941S → P in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_041064

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87931 mRNA. Translation: BAA75636.1.
AB014519 mRNA. Translation: BAA31594.2. Different initiation.
AC018463 Genomic DNA. Translation: AAX93049.1. Sequence problems.
AC099344 Genomic DNA. Translation: AAY14825.1.
CCDSiCCDS42654.1.
RefSeqiNP_004841.2. NM_004850.3.
UniGeneiHs.681743.

Genome annotation databases

EnsembliENST00000315872; ENSP00000317985; ENSG00000134318.
GeneIDi9475.
KEGGihsa:9475.
UCSCiuc002rbd.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87931 mRNA. Translation: BAA75636.1.
AB014519 mRNA. Translation: BAA31594.2. Different initiation.
AC018463 Genomic DNA. Translation: AAX93049.1. Sequence problems.
AC099344 Genomic DNA. Translation: AAY14825.1.
CCDSiCCDS42654.1.
RefSeqiNP_004841.2. NM_004850.3.
UniGeneiHs.681743.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4L6QX-ray2.79A/B19-417[»]
4WOTX-ray2.93A/B/C/D22-417[»]
ProteinModelPortaliO75116.
SMRiO75116. Positions 27-417, 559-709, 857-926, 979-1045, 1151-1351.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114860. 14 interactions.
IntActiO75116. 8 interactions.
MINTiMINT-4299744.
STRINGi9606.ENSP00000317985.

Chemistry

BindingDBiO75116.
ChEMBLiCHEMBL2111459.
GuidetoPHARMACOLOGYi1504.

PTM databases

PhosphoSiteiO75116.

Polymorphism and mutation databases

BioMutaiROCK2.

Proteomic databases

MaxQBiO75116.
PaxDbiO75116.
PRIDEiO75116.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000315872; ENSP00000317985; ENSG00000134318.
GeneIDi9475.
KEGGihsa:9475.
UCSCiuc002rbd.1. human.

Organism-specific databases

CTDi9475.
GeneCardsiGC02M011319.
H-InvDBHIX0001828.
HGNCiHGNC:10252. ROCK2.
HPAiCAB008666.
HPA007459.
HPA044109.
MIMi604002. gene.
neXtProtiNX_O75116.
PharmGKBiPA34624.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118994.
HOGENOMiHOG000017259.
HOVERGENiHBG053111.
InParanoidiO75116.
KOiK17388.
OMAiNQSIRRP.
OrthoDBiEOG7DZ8J4.
PhylomeDBiO75116.
TreeFamiTF313551.

Enzyme and pathway databases

ReactomeiREACT_18407. G alpha (12/13) signalling events.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.
REACT_263952. EPHB-mediated forward signaling.
REACT_264464. VEGFA-VEGFR2 Pathway.
REACT_264548. EPHA-mediated growth cone collapse.
REACT_355192. RHO GTPases Activate ROCKs.
SignaLinkiO75116.

Miscellaneous databases

ChiTaRSiROCK2. human.
GenomeRNAii9475.
NextBioi35508.
PROiO75116.
SOURCEiSearch...

Gene expression databases

BgeeiO75116.
CleanExiHS_ROCK2.
ExpressionAtlasiO75116. baseline and differential.
GenevisibleiO75116. HS.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR000961. AGC-kinase_C.
IPR011072. HR1_rho-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR011993. PH-like_dom.
IPR001849. PH_domain.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015008. Rho-bd_dom.
IPR020684. ROCK1/ROCK2.
IPR029878. ROCK2.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR22988:SF24. PTHR22988:SF24. 1 hit.
PfamiPF02185. HR1. 1 hit.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF08912. Rho_Binding. 1 hit.
[Graphical view]
PIRSFiPIRSF037568. Rho_kinase. 1 hit.
SMARTiSM00109. C1. 1 hit.
SM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Localization of the gene coding for ROCK II/Rho kinase on human chromosome 2p24."
    Takahashi N., Tuiki H., Saya H., Kaibuchi K.
    Genomics 55:235-237(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASN-431.
    Tissue: Brain.
  2. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-431.
    Tissue: Brain.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Phosphorylation of myosin-binding subunit (MBS) of myosin phosphatase by Rho-kinase in vivo."
    Kawano Y., Fukata Y., Oshiro N., Amano M., Nakamura T., Ito M., Matsumura F., Inagaki M., Kaibuchi K.
    J. Cell Biol. 147:1023-1038(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PPP1R12A.
  5. "Direct cleavage of ROCK II by granzyme B induces target cell membrane blebbing in a caspase-independent manner."
    Sebbagh M., Hamelin J., Bertoglio J., Solary E., Breard J.
    J. Exp. Med. 201:465-471(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY GRANZYME B, MUTAGENESIS OF ASP-1131, FUNCTION.
  6. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EP300.
  7. "Interaction between ROCK II and nucleophosmin/B23 in the regulation of centrosome duplication."
    Ma Z., Kanai M., Kawamura K., Kaibuchi K., Ye K., Fukasawa K.
    Mol. Cell. Biol. 26:9016-9034(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NPM1.
  8. "Regulation of RhoA-dependent ROCKII activation by Shp2."
    Lee H.H., Chang Z.F.
    J. Cell Biol. 181:999-1012(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-722, DEPHOSPHORYLATION.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "ROCK isoform regulation of myosin phosphatase and contractility in vascular smooth muscle cells."
    Wang Y., Zheng X.R., Riddick N., Bryden M., Baur W., Zhang X., Surks H.K.
    Circ. Res. 104:531-540(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PPP1R12A.
  12. "Distinct roles for ROCK1 and ROCK2 in the regulation of keratinocyte differentiation."
    Lock F.E., Hotchin N.A.
    PLoS ONE 4:E8190-E8190(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. Cited for: INTERACTION WITH CHORDC1.
  15. "Src-dependent phosphorylation of ROCK participates in regulation of focal adhesion dynamics."
    Lee H.H., Tien S.C., Jou T.S., Chang Y.C., Jhong J.G., Chang Z.F.
    J. Cell Sci. 123:3368-3377(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-722.
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "BRCA2 and nucleophosmin coregulate centrosome amplification and form a complex with the Rho effector kinase ROCK2."
    Wang H.F., Takenaka K., Nakanishi A., Miki Y.
    Cancer Res. 71:68-77(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BRCA2.
  19. "Rho kinase II phosphorylation of the lipoprotein receptor LR11/SORLA alters amyloid-beta production."
    Herskowitz J.H., Seyfried N.T., Gearing M., Kahn R.A., Peng J., Levey A.I., Lah J.J.
    J. Biol. Chem. 286:6117-6127(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SORL1.
  20. "Rocks: multifunctional kinases in cell behaviour."
    Riento K., Ridley A.J.
    Nat. Rev. Mol. Cell Biol. 4:446-456(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  21. "Rho-kinase/ROCK: A key regulator of the cytoskeleton and cell polarity."
    Amano M., Nakayama M., Kaibuchi K.
    Cytoskeleton 67:545-554(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  24. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASN-431; VAL-601 AND PRO-1194.

Entry informationi

Entry nameiROCK2_HUMAN
AccessioniPrimary (citable) accession number: O75116
Secondary accession number(s): Q53QZ0, Q53SJ7, Q9UQN5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: November 24, 2009
Last modified: July 22, 2015
This is version 158 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.