SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q13464

- ROCK1_HUMAN

UniProt

Q13464 - ROCK1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Rho-associated protein kinase 1

Gene
ROCK1
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Magnesium.

Enzyme regulationi

Activated by RHOA binding. Inhibited by Y-27632.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei105 – 1051ATP By similarity
Active sitei198 – 1981Proton acceptor By similarity
Sitei1113 – 11142Cleavage; by caspase-3

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi82 – 909ATP By similarity
Zinc fingeri1228 – 128154Phorbol-ester/DAG-typeAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: UniProtKB
  4. protein kinase activity Source: ProtInc
  5. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. actin cytoskeleton organization Source: ProtInc
  2. apical constriction Source: Ensembl
  3. apoptotic process Source: Reactome
  4. axon guidance Source: Reactome
  5. bleb assembly Source: Ensembl
  6. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  7. leukocyte cell-cell adhesion Source: BHF-UCL
  8. leukocyte migration Source: BHF-UCL
  9. leukocyte tethering or rolling Source: BHF-UCL
  10. membrane to membrane docking Source: BHF-UCL
  11. myoblast migration Source: UniProtKB
  12. negative regulation of angiogenesis Source: UniProtKB
  13. negative regulation of neuron apoptotic process Source: Ensembl
  14. positive regulation of focal adhesion assembly Source: UniProtKB
  15. protein phosphorylation Source: ProtInc
  16. regulation of actin cytoskeleton organization Source: UniProtKB
  17. regulation of cell adhesion Source: UniProtKB
  18. regulation of cell motility Source: UniProtKB
  19. regulation of establishment of cell polarity Source: UniProtKB
  20. regulation of focal adhesion assembly Source: UniProtKB
  21. regulation of keratinocyte differentiation Source: UniProtKB
  22. regulation of stress fiber assembly Source: UniProtKB
  23. Rho protein signal transduction Source: ProtInc
  24. signal transduction Source: ProtInc
  25. smooth muscle contraction Source: UniProtKB
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.
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: Chromosome 18

Organism-specific databases

HGNCiHGNC:10251. ROCK1.

Subcellular locationi

Cytoplasm. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole By similarity. Golgi apparatus membrane; Peripheral membrane protein. Cell projectionbleb. Cytoplasmcytoskeleton By similarity. Cell membrane By similarity. Cell projectionlamellipodium By similarity. Cell projectionruffle By similarity
Note: Associated with the mother centriole and an intercentriolar linker. Colocalizes with ITGB1BP1 and ITGB1 at the cell membrane predominantly in lamellipodia and membrane ruffles, but also in retraction fibers. Localizes at the cell membrane in an ITGB1BP1-dependent manner By similarity. A small proportion is associated with Golgi membranes.3 Publications

GO - Cellular componenti

  1. bleb Source: UniProtKB-SubCell
  2. centriole Source: UniProtKB-SubCell
  3. cytoskeleton Source: UniProtKB
  4. cytosol Source: Reactome
  5. Golgi membrane Source: UniProtKB-SubCell
  6. lamellipodium Source: UniProtKB
  7. plasma membrane Source: UniProtKB
  8. ruffle Source: UniProtKB
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
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

ArrayExpressiQ13464.
BgeeiQ13464.
CleanExiHS_ROCK1.
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.15 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MYBPHQ132032EBI-876651,EBI-5655165
RHOAP615864EBI-876651,EBI-446668
TSG101Q998164EBI-876651,EBI-346882

Protein-protein interaction databases

BioGridi112020. 23 interactions.
IntActiQ13464. 10 interactions.
MINTiMINT-1195170.
STRINGi9606.ENSP00000382697.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortaliQ13464.
SMRiQ13464. Positions 6-402, 535-693, 946-1014, 1119-1288.

Miscellaneous databases

EvolutionaryTraceiQ13464.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini76 – 338263Protein kinaseAdd
BLAST
Domaini341 – 40969AGC-kinase C-terminalAdd
BLAST
Repeati458 – 54285REMAdd
BLAST
Domaini1118 – 1317200PHAdd
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 – 612191 Reviewed predictionAdd
BLAST
Coiled coili1011 – 110292 Reviewed predictionAdd
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 PH domain.
Contains 1 REM (Hr1) repeat.

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
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.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR017892. Pkinase_C.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR020684. Rho-assoc_coiled-coil_kin.
IPR015008. Rho-bd_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
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

MSTGDSFETR FEKMDNLLRD PKSEVNSDCL LDGLDALVYD LDFPALRKNK     50
NIDNFLSRYK DTINKIRDLR MKAEDYEVVK VIGRGAFGEV QLVRHKSTRK 100
VYAMKLLSKF EMIKRSDSAF FWEERDIMAF ANSPWVVQLF YAFQDDRYLY 150
MVMEYMPGGD LVNLMSNYDV PEKWARFYTA EVVLALDAIH SMGFIHRDVK 200
PDNMLLDKSG HLKLADFGTC MKMNKEGMVR CDTAVGTPDY ISPEVLKSQG 250
GDGYYGRECD WWSVGVFLYE MLVGDTPFYA DSLVGTYSKI MNHKNSLTFP 300
DDNDISKEAK NLICAFLTDR EVRLGRNGVE EIKRHLFFKN DQWAWETLRD 350
TVAPVVPDLS SDIDTSNFDD LEEDKGEEET FPIPKAFVGN QLPFVGFTYY 400
SNRRYLSSAN PNDNRTSSNA DKSLQESLQK TIYKLEEQLH NEMQLKDEME 450
QKCRTSNIKL DKIMKELDEE GNQRRNLEST VSQIEKEKML LQHRINEYQR 500
KAEQENEKRR NVENEVSTLK DQLEDLKKVS QNSQLANEKL SQLQKQLEEA 550
NDLLRTESDT AVRLRKSHTE MSKSISQLES LNRELQERNR ILENSKSQTD 600
KDYYQLQAIL EAERRDRGHD SEMIGDLQAR ITSLQEEVKH LKHNLEKVEG 650
ERKEAQDMLN HSEKEKNNLE IDLNYKLKSL QQRLEQEVNE HKVTKARLTD 700
KHQSIEEAKS VAMCEMEKKL KEEREAREKA ENRVVQIEKQ CSMLDVDLKQ 750
SQQKLEHLTG NKERMEDEVK NLTLQLEQES NKRLLLQNEL KTQAFEADNL 800
KGLEKQMKQE INTLLEAKRL LEFELAQLTK QYRGNEGQMR ELQDQLEAEQ 850
YFSTLYKTQV KELKEEIEEK NRENLKKIQE LQNEKETLAT QLDLAETKAE 900
SEQLARGLLE EQYFELTQES KKAASRNRQE ITDKDHTVSR LEEANSMLTK 950
DIEILRRENE ELTEKMKKAE EEYKLEKEEE ISNLKAAFEK NINTERTLKT 1000
QAVNKLAEIM NRKDFKIDRK KANTQDLRKK EKENRKLQLE LNQEREKFNQ 1050
MVVKHQKELN DMQAQLVEEC AHRNELQMQL ASKESDIEQL RAKLLDLSDS 1100
TSVASFPSAD ETDGNLPESR IEGWLSVPNR GNIKRYGWKK QYVVVSSKKI 1150
LFYNDEQDKE QSNPSMVLDI DKLFHVRPVT QGDVYRAETE EIPKIFQILY 1200
ANEGECRKDV EMEPVQQAEK TNFQNHKGHE FIPTLYHFPA NCDACAKPLW 1250
HVFKPPPALE CRRCHVKCHR DHLDKKEDLI CPCKVSYDVT SARDMLLLAC 1300
SQDEQKKWVT HLVKKIPKNP PSGFVRASPR TLSTRSTANQ SFRKVVKNTS 1350
GKTS 1354
Length:1,354
Mass (Da):158,175
Last modified:November 1, 1996 - v1
Checksum:i93078CBB009A6F27
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti170 – 1701V → A in AAI13115. 1 Publication
Sequence conflicti197 – 1971R → G in AAI13115. 1 Publication
Sequence conflicti220 – 2201C → R in AAI13115. 1 Publication
Sequence conflicti323 – 3253RLG → GTR in BAD92202. 1 Publication
Sequence conflicti521 – 5211D → N in AAI13115. 1 Publication
Sequence conflicti965 – 9651K → R in AAI13115. 1 Publication
Sequence conflicti1354 – 13541S → R in ACA06069. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi47605999.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U43195 mRNA. Translation: AAB02814.1 .
EF445027 Genomic DNA. Translation: ACA06069.1 .
BC113114 mRNA. Translation: AAI13115.1 .
AB208965 mRNA. Translation: BAD92202.1 .
CCDSi CCDS11870.2.
PIRi S69211.
RefSeqi NP_005397.1. NM_005406.2.
UniGenei Hs.306307.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1S1C X-ray 2.60 X/Y 947-1015 [» ]
2ESM X-ray 3.20 A/B 6-415 [» ]
2ETK X-ray 2.96 A/B 6-415 [» ]
2ETR X-ray 2.60 A/B 6-415 [» ]
2V55 X-ray 3.70 A/C 1-406 [» ]
3D9V X-ray 3.30 A/B 6-415 [» ]
3NCZ X-ray 3.00 A/B/C/D 6-415 [» ]
3NDM X-ray 3.30 A/B/C/D 6-415 [» ]
3O0Z X-ray 2.33 A/B/C/D 535-700 [» ]
3TV7 X-ray 2.75 A/B/C/D 6-415 [» ]
3TWJ X-ray 2.90 A/B/C/D 6-415 [» ]
3V8S X-ray 2.29 A/B/C/D 6-415 [» ]
4L2W X-ray 2.49 A/B/C/D 834-914 [» ]
ProteinModelPortali Q13464.
SMRi Q13464. Positions 6-402, 535-693, 946-1014, 1119-1288.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112020. 23 interactions.
IntActi Q13464. 10 interactions.
MINTi MINT-1195170.
STRINGi 9606.ENSP00000382697.

Chemistry

BindingDBi Q13464.
ChEMBLi CHEMBL3231.
GuidetoPHARMACOLOGYi 1503.

PTM databases

PhosphoSitei Q13464.

Polymorphism databases

DMDMi 47605999.

Proteomic databases

MaxQBi Q13464.
PaxDbi Q13464.
PRIDEi Q13464.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000399799 ; ENSP00000382697 ; ENSG00000067900 .
GeneIDi 6093.
KEGGi hsa:6093.
UCSCi uc002kte.3. human.

Organism-specific databases

CTDi 6093.
GeneCardsi GC18M018529.
HGNCi HGNC:10251. ROCK1.
HPAi CAB004562.
HPA007567.
HPA045639.
MIMi 601702. gene.
neXtProti NX_Q13464.
PharmGKBi PA34623.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000017259.
HOVERGENi HBG053111.
InParanoidi Q13464.
KOi K04514.
OMAi QIEKQCS.
OrthoDBi EOG7DZ8J4.
PhylomeDBi Q13464.
TreeFami TF313551.

Enzyme and pathway databases

Reactomei REACT_107. Apoptotic cleavage of cellular proteins.
REACT_18407. G alpha (12/13) signalling events.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.
SignaLinki Q13464.

Miscellaneous databases

EvolutionaryTracei Q13464.
GeneWikii ROCK1.
GenomeRNAii 6093.
NextBioi 23695.
PMAP-CutDB B0YJ91.
PROi Q13464.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13464.
Bgeei Q13464.
CleanExi HS_ROCK1.
Genevestigatori Q13464.

Family and domain databases

Gene3Di 2.30.29.30. 2 hits.
InterProi IPR000961. AGC-kinase_C.
IPR011072. HR1_rho-bd.
IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR017892. Pkinase_C.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR020684. Rho-assoc_coiled-coil_kin.
IPR015008. Rho-bd_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF02185. HR1. 1 hit.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
PF08912. Rho_Binding. 1 hit.
[Graphical view ]
PIRSFi PIRSF037568. Rho_kinase. 1 hit.
SMARTi SM00109. C1. 1 hit.
SM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS51285. 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 ]
ProtoNeti Search...

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].
  33. "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.
  34. "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.
  35. "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: September 3, 2014
This is version 152 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