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Protein

Rho-associated protein kinase 1

Gene

ROCK1

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 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. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization.14 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Enzyme regulationi

Activated by RHOA binding. Inhibited by Y-27632.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei105 – 1051ATPPROSITE-ProRule annotation
Active sitei198 – 1981Proton acceptorPROSITE-ProRule annotation
Sitei1113 – 11142Cleavage; by caspase-3

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi82 – 909ATPPROSITE-ProRule annotation
Zinc fingeri1228 – 128154Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • protein kinase activity Source: ProtInc
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton organization Source: ProtInc
  • apical constriction Source: Ensembl
  • apoptotic process Source: Reactome
  • axon guidance Source: Reactome
  • bleb assembly Source: Ensembl
  • cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  • ephrin receptor signaling pathway Source: Reactome
  • leukocyte cell-cell adhesion Source: BHF-UCL
  • leukocyte migration Source: BHF-UCL
  • leukocyte tethering or rolling Source: BHF-UCL
  • membrane to membrane docking Source: BHF-UCL
  • myoblast migration Source: UniProtKB
  • negative regulation of angiogenesis Source: UniProtKB
  • negative regulation of neuron apoptotic process Source: Ensembl
  • negative regulation of protein binding Source: UniProtKB
  • positive regulation of focal adhesion assembly Source: UniProtKB
  • programmed cell death Source: Reactome
  • protein phosphorylation Source: ProtInc
  • regulation of actin cytoskeleton organization Source: UniProtKB
  • regulation of cell adhesion Source: UniProtKB
  • regulation of cell motility 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: ProtInc
  • signal transduction Source: ProtInc
  • 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

Apoptosis

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
REACT_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.
SignaLinkiQ13464.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho-associated protein kinase 1 (EC:2.7.11.1)
Alternative name(s):
Renal carcinoma antigen NY-REN-35
Rho-associated, coiled-coil-containing protein kinase 1
Rho-associated, coiled-coil-containing protein kinase I
Short name:
ROCK-I
p160 ROCK-1
Short name:
p160ROCK
Gene namesi
Name:ROCK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:10251. ROCK1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1113 – 11131D → A: Abolishes cleavage by caspase-3. 1 Publication

Organism-specific databases

PharmGKBiPA34623.

Polymorphism and mutation databases

BioMutaiROCK1.
DMDMi47605999.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 13541353Rho-associated protein kinase 1PRO_0000086619Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei647 – 6471N6-acetyllysine1 Publication
Modified residuei1105 – 11051Phosphoserine2 Publications

Post-translational modificationi

Autophosphorylated on serine and threonine residues.1 Publication
Cleaved by caspase-3 during apoptosis. This leads to constitutive activation of the kinase and membrane blebbing.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13464.
PaxDbiQ13464.
PRIDEiQ13464.

PTM databases

PhosphoSiteiQ13464.

Miscellaneous databases

PMAP-CutDBB0YJ91.

Expressioni

Tissue specificityi

Detected in blood platelets.1 Publication

Gene expression databases

BgeeiQ13464.
CleanExiHS_ROCK1.
ExpressionAtlasiQ13464. baseline and differential.
GenevestigatoriQ13464.

Organism-specific databases

HPAiCAB004562.
HPA007567.
HPA045639.

Interactioni

Subunit structurei

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.By similarity16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
C6orf165Q8IYR03EBI-876651,EBI-749051
FAM124AQ86V423EBI-876651,EBI-744506
LMO2P257913EBI-876651,EBI-739696
MAGEB4O154813EBI-876651,EBI-751857
MYBPHQ132032EBI-876651,EBI-5655165
POLR3CQ9BUI43EBI-876651,EBI-5452779
RHOAP615864EBI-876651,EBI-446668
TSG101Q998164EBI-876651,EBI-346882

Protein-protein interaction databases

BioGridi112020. 29 interactions.
IntActiQ13464. 15 interactions.
MINTiMINT-1195170.
STRINGi9606.ENSP00000382697.

Structurei

Secondary structure

1
1354
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 1911Combined sources
Helixi27 – 4115Combined sources
Helixi44 – 474Combined sources
Helixi50 – 6920Combined sources
Helixi73 – 753Combined sources
Beta strandi76 – 849Combined sources
Beta strandi86 – 9510Combined sources
Turni96 – 983Combined sources
Beta strandi101 – 1088Combined sources
Helixi109 – 1146Combined sources
Helixi121 – 13010Combined sources
Beta strandi139 – 1446Combined sources
Beta strandi146 – 1538Combined sources
Beta strandi157 – 1604Combined sources
Helixi161 – 1677Combined sources
Helixi172 – 19120Combined sources
Helixi201 – 2033Combined sources
Beta strandi204 – 2063Combined sources
Beta strandi212 – 2143Combined sources
Beta strandi227 – 2304Combined sources
Helixi238 – 2403Combined sources
Helixi243 – 2475Combined sources
Turni248 – 2525Combined sources
Beta strandi254 – 2563Combined sources
Helixi258 – 27316Combined sources
Helixi283 – 2919Combined sources
Helixi293 – 2964Combined sources
Helixi307 – 31610Combined sources
Helixi320 – 3223Combined sources
Turni324 – 3274Combined sources
Helixi329 – 3335Combined sources
Helixi336 – 3383Combined sources
Turni345 – 3473Combined sources
Helixi348 – 3503Combined sources
Helixi365 – 3673Combined sources
Helixi392 – 3943Combined sources
Beta strandi399 – 4024Combined sources
Helixi544 – 691148Combined sources
Helixi840 – 90263Combined sources
Helixi947 – 98236Combined sources
Helixi984 – 101128Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S1CX-ray2.60X/Y947-1015[»]
2ESMX-ray3.20A/B6-415[»]
2ETKX-ray2.96A/B6-415[»]
2ETRX-ray2.60A/B6-415[»]
2V55X-ray3.70A/C1-406[»]
3D9VX-ray3.30A/B6-415[»]
3NCZX-ray3.00A/B/C/D6-415[»]
3NDMX-ray3.30A/B/C/D6-415[»]
3O0ZX-ray2.33A/B/C/D535-700[»]
3TV7X-ray2.75A/B/C/D6-415[»]
3TWJX-ray2.90A/B/C/D6-415[»]
3V8SX-ray2.29A/B/C/D6-415[»]
4L2WX-ray2.49A/B/C/D834-914[»]
4W7PX-ray2.80A/B/C/D2-410[»]
ProteinModelPortaliQ13464.
SMRiQ13464. Positions 6-402, 535-693, 835-902, 946-1014, 1119-1288.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13464.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini76 – 338263Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini341 – 40969AGC-kinase C-terminalAdd
BLAST
Repeati458 – 54285REMAdd
BLAST
Domaini1118 – 1317200PHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni368 – 727360Interaction with FHOD1Add
BLAST
Regioni998 – 101013RHOA bindingAdd
BLAST
Regioni1115 – 1354240Auto-inhibitoryAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili422 – 612191Sequence AnalysisAdd
BLAST
Coiled coili1011 – 110292Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi636 – 980345Glu-richAdd
BLAST

Domaini

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.

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 fingeri1228 – 128154Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118994.
HOGENOMiHOG000017259.
HOVERGENiHBG053111.
InParanoidiQ13464.
KOiK04514.
OMAiQIEKQCS.
OrthoDBiEOG7DZ8J4.
PhylomeDBiQ13464.
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.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015008. Rho-bd_dom.
IPR029876. ROCK1.
IPR020684. ROCK1/ROCK2.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR22988:SF28. PTHR22988:SF28. 1 hit.
PfamiPF02185. HR1. 1 hit.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q13464-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTGDSFETR FEKMDNLLRD PKSEVNSDCL LDGLDALVYD LDFPALRKNK
60 70 80 90 100
NIDNFLSRYK DTINKIRDLR MKAEDYEVVK VIGRGAFGEV QLVRHKSTRK
110 120 130 140 150
VYAMKLLSKF EMIKRSDSAF FWEERDIMAF ANSPWVVQLF YAFQDDRYLY
160 170 180 190 200
MVMEYMPGGD LVNLMSNYDV PEKWARFYTA EVVLALDAIH SMGFIHRDVK
210 220 230 240 250
PDNMLLDKSG HLKLADFGTC MKMNKEGMVR CDTAVGTPDY ISPEVLKSQG
260 270 280 290 300
GDGYYGRECD WWSVGVFLYE MLVGDTPFYA DSLVGTYSKI MNHKNSLTFP
310 320 330 340 350
DDNDISKEAK NLICAFLTDR EVRLGRNGVE EIKRHLFFKN DQWAWETLRD
360 370 380 390 400
TVAPVVPDLS SDIDTSNFDD LEEDKGEEET FPIPKAFVGN QLPFVGFTYY
410 420 430 440 450
SNRRYLSSAN PNDNRTSSNA DKSLQESLQK TIYKLEEQLH NEMQLKDEME
460 470 480 490 500
QKCRTSNIKL DKIMKELDEE GNQRRNLEST VSQIEKEKML LQHRINEYQR
510 520 530 540 550
KAEQENEKRR NVENEVSTLK DQLEDLKKVS QNSQLANEKL SQLQKQLEEA
560 570 580 590 600
NDLLRTESDT AVRLRKSHTE MSKSISQLES LNRELQERNR ILENSKSQTD
610 620 630 640 650
KDYYQLQAIL EAERRDRGHD SEMIGDLQAR ITSLQEEVKH LKHNLEKVEG
660 670 680 690 700
ERKEAQDMLN HSEKEKNNLE IDLNYKLKSL QQRLEQEVNE HKVTKARLTD
710 720 730 740 750
KHQSIEEAKS VAMCEMEKKL KEEREAREKA ENRVVQIEKQ CSMLDVDLKQ
760 770 780 790 800
SQQKLEHLTG NKERMEDEVK NLTLQLEQES NKRLLLQNEL KTQAFEADNL
810 820 830 840 850
KGLEKQMKQE INTLLEAKRL LEFELAQLTK QYRGNEGQMR ELQDQLEAEQ
860 870 880 890 900
YFSTLYKTQV KELKEEIEEK NRENLKKIQE LQNEKETLAT QLDLAETKAE
910 920 930 940 950
SEQLARGLLE EQYFELTQES KKAASRNRQE ITDKDHTVSR LEEANSMLTK
960 970 980 990 1000
DIEILRRENE ELTEKMKKAE EEYKLEKEEE ISNLKAAFEK NINTERTLKT
1010 1020 1030 1040 1050
QAVNKLAEIM NRKDFKIDRK KANTQDLRKK EKENRKLQLE LNQEREKFNQ
1060 1070 1080 1090 1100
MVVKHQKELN DMQAQLVEEC AHRNELQMQL ASKESDIEQL RAKLLDLSDS
1110 1120 1130 1140 1150
TSVASFPSAD ETDGNLPESR IEGWLSVPNR GNIKRYGWKK QYVVVSSKKI
1160 1170 1180 1190 1200
LFYNDEQDKE QSNPSMVLDI DKLFHVRPVT QGDVYRAETE EIPKIFQILY
1210 1220 1230 1240 1250
ANEGECRKDV EMEPVQQAEK TNFQNHKGHE FIPTLYHFPA NCDACAKPLW
1260 1270 1280 1290 1300
HVFKPPPALE CRRCHVKCHR DHLDKKEDLI CPCKVSYDVT SARDMLLLAC
1310 1320 1330 1340 1350
SQDEQKKWVT HLVKKIPKNP PSGFVRASPR TLSTRSTANQ SFRKVVKNTS

GKTS
Length:1,354
Mass (Da):158,175
Last modified:November 1, 1996 - v1
Checksum:i93078CBB009A6F27
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti170 – 1701V → A in AAI13115 (PubMed:15489334).Curated
Sequence conflicti197 – 1971R → G in AAI13115 (PubMed:15489334).Curated
Sequence conflicti220 – 2201C → R in AAI13115 (PubMed:15489334).Curated
Sequence conflicti323 – 3253RLG → GTR in BAD92202 (Ref. 5) Curated
Sequence conflicti521 – 5211D → N in AAI13115 (PubMed:15489334).Curated
Sequence conflicti965 – 9651K → R in AAI13115 (PubMed:15489334).Curated
Sequence conflicti1354 – 13541S → R in ACA06069 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti108 – 1081S → N.1 Publication
Corresponds to variant rs55811609 [ dbSNP | Ensembl ].
VAR_041055
Natural varianti773 – 7731T → S.1 Publication
Corresponds to variant rs45562542 [ dbSNP | Ensembl ].
VAR_041056
Natural varianti1112 – 11121T → P.1 Publication
Corresponds to variant rs35881519 [ dbSNP | Ensembl ].
VAR_041057
Natural varianti1193 – 11931P → S in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
VAR_041058
Natural varianti1217 – 12171Q → E.1 Publication
Corresponds to variant rs2847092 [ dbSNP | Ensembl ].
VAR_041059
Natural varianti1262 – 12621R → Q.1 Publication
Corresponds to variant rs1045142 [ dbSNP | Ensembl ].
VAR_041060
Natural varianti1264 – 12641C → R.1 Publication
Corresponds to variant rs2663698 [ dbSNP | Ensembl ].
VAR_041061

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43195 mRNA. Translation: AAB02814.1.
EF445027 Genomic DNA. Translation: ACA06069.1.
BC113114 mRNA. Translation: AAI13115.1.
AB208965 mRNA. Translation: BAD92202.1.
CCDSiCCDS11870.2.
PIRiS69211.
RefSeqiNP_005397.1. NM_005406.2.
UniGeneiHs.306307.

Genome annotation databases

EnsembliENST00000399799; ENSP00000382697; ENSG00000067900.
GeneIDi6093.
KEGGihsa:6093.
UCSCiuc002kte.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43195 mRNA. Translation: AAB02814.1.
EF445027 Genomic DNA. Translation: ACA06069.1.
BC113114 mRNA. Translation: AAI13115.1.
AB208965 mRNA. Translation: BAD92202.1.
CCDSiCCDS11870.2.
PIRiS69211.
RefSeqiNP_005397.1. NM_005406.2.
UniGeneiHs.306307.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S1CX-ray2.60X/Y947-1015[»]
2ESMX-ray3.20A/B6-415[»]
2ETKX-ray2.96A/B6-415[»]
2ETRX-ray2.60A/B6-415[»]
2V55X-ray3.70A/C1-406[»]
3D9VX-ray3.30A/B6-415[»]
3NCZX-ray3.00A/B/C/D6-415[»]
3NDMX-ray3.30A/B/C/D6-415[»]
3O0ZX-ray2.33A/B/C/D535-700[»]
3TV7X-ray2.75A/B/C/D6-415[»]
3TWJX-ray2.90A/B/C/D6-415[»]
3V8SX-ray2.29A/B/C/D6-415[»]
4L2WX-ray2.49A/B/C/D834-914[»]
4W7PX-ray2.80A/B/C/D2-410[»]
ProteinModelPortaliQ13464.
SMRiQ13464. Positions 6-402, 535-693, 835-902, 946-1014, 1119-1288.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112020. 29 interactions.
IntActiQ13464. 15 interactions.
MINTiMINT-1195170.
STRINGi9606.ENSP00000382697.

Chemistry

BindingDBiQ13464.
ChEMBLiCHEMBL2111459.
GuidetoPHARMACOLOGYi1503.

PTM databases

PhosphoSiteiQ13464.

Polymorphism and mutation databases

BioMutaiROCK1.
DMDMi47605999.

Proteomic databases

MaxQBiQ13464.
PaxDbiQ13464.
PRIDEiQ13464.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000399799; ENSP00000382697; ENSG00000067900.
GeneIDi6093.
KEGGihsa:6093.
UCSCiuc002kte.3. human.

Organism-specific databases

CTDi6093.
GeneCardsiGC18M018529.
HGNCiHGNC:10251. ROCK1.
HPAiCAB004562.
HPA007567.
HPA045639.
MIMi601702. gene.
neXtProtiNX_Q13464.
PharmGKBiPA34623.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118994.
HOGENOMiHOG000017259.
HOVERGENiHBG053111.
InParanoidiQ13464.
KOiK04514.
OMAiQIEKQCS.
OrthoDBiEOG7DZ8J4.
PhylomeDBiQ13464.
TreeFamiTF313551.

Enzyme and pathway databases

ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
REACT_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.
SignaLinkiQ13464.

Miscellaneous databases

EvolutionaryTraceiQ13464.
GeneWikiiROCK1.
GenomeRNAii6093.
NextBioi23695.
PMAP-CutDBB0YJ91.
PROiQ13464.
SOURCEiSearch...

Gene expression databases

BgeeiQ13464.
CleanExiHS_ROCK1.
ExpressionAtlasiQ13464. baseline and differential.
GenevestigatoriQ13464.

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.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015008. Rho-bd_dom.
IPR029876. ROCK1.
IPR020684. ROCK1/ROCK2.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR22988:SF28. PTHR22988:SF28. 1 hit.
PfamiPF02185. HR1. 1 hit.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 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. "The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase."
    Ishizaki T., Maekawa M., Fujisawa K., Okawa K., Iwamatsu A., Fujita A., Watanabe N., Saito Y., Kakizuka A., Morii N., Narumiya S.
    EMBO J. 15:1885-1893(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 187-195; 281-288; 465-473; 818-828; 885-893 AND 934-945, FUNCTION, PHOSPHORYLATION, INTERACTION WITH RHOA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Leukemia.
  2. NHLBI resequencing and genotyping service (RS&G)
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Bienvenut W.V., Ramsay A., Leung H.Y.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13; 85-94; 327-334; 405-415 AND 546-563, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 323-1027.
    Tissue: Brain.
  6. "Different molecular mechanisms for Rho family GTPase-dependent, Ca2+-independent contraction of smooth muscle."
    Van Eyk J.E., Arrell D.K., Foster D.B., Strauss J.D., Heinonen T.Y., Furmaniak-Kazmierczak E., Cote G.P., Mak A.S.
    J. Biol. Chem. 273:23433-23439(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN SMOOTH MUSCLE CONTRACTION.
  7. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    Tissue: Renal cell carcinoma.
  8. "Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase."
    Maekawa M., Ishizaki T., Boku S., Watanabe N., Fujita A., Iwamatsu A., Obinata T., Ohashi K., Mizuno K., Narumiya S.
    Science 285:895-898(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LIMK1 AND LIMK2, INHIBITION BY Y-27632.
  9. "Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop."
    Ohashi K., Nagata K., Maekawa M., Ishizaki T., Narumiya S., Mizuno K.
    J. Biol. Chem. 275:3577-3582(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LIMK1.
  10. "Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase."
    Sumi T., Matsumoto K., Nakamura T.
    J. Biol. Chem. 276:670-676(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LIMK2.
  11. "Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing."
    Sebbagh M., Renvoize C., Hamelin J., Riche N., Bertoglio J., Breard J.
    Nat. Cell Biol. 3:346-352(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY CASPASE-3, MUTAGENESIS OF ASP-1113, INTERACTION WITH PPP1R12A, FUNCTION.
  12. "The GTP binding proteins Gem and Rad are negative regulators of the Rho-Rho kinase pathway."
    Ward Y., Yap S.-F., Ravichandran V., Matsumura F., Ito M., Spinelli B., Kelly K.
    J. Cell Biol. 157:291-302(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GEM.
  13. "RhoE binds to ROCK I and inhibits downstream signaling."
    Riento K., Guasch R.M., Garg R., Jin B., Ridley A.J.
    Mol. Cell. Biol. 23:4219-4229(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RHOE AND PPP1R12A, SUBCELLULAR LOCATION.
  14. "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.
  15. "Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis."
    Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K., Sundquist W.I.
    EMBO J. 26:4215-4227(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TSG101.
  16. Cited for: FUNCTION, INTERACTION WITH DAPK3.
  17. "The diaphanous-related formin FHOD1 associates with ROCK1 and promotes Src-dependent plasma membrane blebbing."
    Hannemann S., Madrid R., Stastna J., Kitzing T., Gasteier J., Schoenichen A., Bouchet J., Jimenez A., Geyer M., Grosse R., Benichou S., Fackler O.T.
    J. Biol. Chem. 283:27891-27903(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FHOD1, SUBCELLULAR LOCATION.
  18. "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-1105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "Phosphorylation of profilin by ROCK1 regulates polyglutamine aggregation."
    Shao J., Welch W.J., Diprospero N.A., Diamond M.I.
    Mol. Cell. Biol. 28:5196-5208(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PFN1.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. "Identification of ROCK1 as an upstream activator of the JIP-3 to JNK signaling axis in response to UVB damage."
    Ongusaha P.P., Qi H.H., Raj L., Kim Y.B., Aaronson S.A., Davis R.J., Shi Y., Liao J.K., Lee S.W.
    Sci. Signal. 1:RA14-RA14(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH JIP3.
  22. "Inhibition of Rho-dependent kinases ROCK I/II activates VEGF-driven retinal neovascularization and sprouting angiogenesis."
    Kroll J., Epting D., Kern K., Dietz C.T., Feng Y., Hammes H.P., Wieland T., Augustin H.G.
    Am. J. Physiol. 296:H893-H899(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "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.
  24. "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.
  25. "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-1105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  26. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-647, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. Cited for: INTERACTION WITH CHORDC1.
  28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "Caspase-activated ROCK-1 allows erythroblast terminal maturation independently of cytokine-induced Rho signaling."
    Gabet A.S., Coulon S., Fricot A., Vandekerckhove J., Chang Y., Ribeil J.A., Lordier L., Zermati Y., Asnafi V., Belaid Z., Debili N., Vainchenker W., Varet B., Hermine O., Courtois G.
    Cell Death Differ. 18:678-689(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CLEAVAGE BY CASPASE-3.
  30. "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.
  31. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  33. "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.
  34. "Structural insights into the interaction of ROCKI with the switch regions of RhoA."
    Dvorsky R., Blumenstein L., Vetter I.R., Ahmadian M.R.
    J. Biol. Chem. 279:7098-7104(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 947-1015 IN COMPLEX WITH RHOA.
  35. "The structure of dimeric ROCK I reveals the mechanism for ligand selectivity."
    Jacobs M., Hayakawa K., Swenson L., Bellon S., Fleming M., Taslimi P., Doran J.
    J. Biol. Chem. 281:260-268(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 6-415, SUBUNIT.
  36. "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-108; SER-773; PRO-1112; SER-1193; GLU-1217; GLN-1262 AND ARG-1264.

Entry informationi

Entry nameiROCK1_HUMAN
AccessioniPrimary (citable) accession number: Q13464
Secondary accession number(s): B0YJ91, Q2KHM4, Q59GZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: November 1, 1996
Last modified: May 27, 2015
This is version 161 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: 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.