Rho-associated protein kinase 1

Details

Name
Rho-associated protein kinase 1
Synonyms
  • 2.7.11.1
  • p160 ROCK-1
  • p160ROCK
  • Renal carcinoma antigen NY-REN-35
  • Rho-associated, coiled-coil-containing protein kinase 1
  • Rho-associated, coiled-coil-containing protein kinase I
  • ROCK-I
Gene Name
ROCK1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0019048|Rho-associated protein kinase 1
MSTGDSFETRFEKMDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNFLSRYK
DTINKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAF
FWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTA
EVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDY
ISPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFP
DDNDISKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLS
SDIDTSNFDDLEEDKGEEETFPIPKAFVGNQLPFVGFTYYSNRRYLSSANPNDNRTSSNA
DKSLQESLQKTIYKLEEQLHNEMQLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLEST
VSQIEKEKMLLQHRINEYQRKAEQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKL
SQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLESLNRELQERNRILENSKSQTD
KDYYQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLN
HSEKEKNNLEIDLNYKLKSLQQRLEQEVNEHKVTKARLTDKHQSIEEAKSVAMCEMEKKL
KEEREAREKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEVKNLTLQLEQES
NKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMR
ELQDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLKKIQELQNEKETLATQLDLAETKAE
SEQLARGLLEEQYFELTQESKKAASRNRQEITDKDHTVSRLEEANSMLTKDIEILRRENE
ELTEKMKKAEEEYKLEKEEEISNLKAAFEKNINTERTLKTQAVNKLAEIMNRKDFKIDRK
KANTQDLRKKEKENRKLQLELNQEREKFNQMVVKHQKELNDMQAQLVEECAHRNELQMQL
ASKESDIEQLRAKLLDLSDSTSVASFPSADETDGNLPESRIEGWLSVPNRGNIKRYGWKK
QYVVVSSKKILFYNDEQDKEQSNPSMVLDIDKLFHVRPVTQGDVYRAETEEIPKIFQILY
ANEGECRKDVEMEPVQQAEKTNFQNHKGHEFIPTLYHFPANCDACAKPLWHVFKPPPALE
CRRCHVKCHRDHLDKKEDLICPCKVSYDVTSARDMLLLACSQDEQKKWVTHLVKKIPKNP
PSGFVRASPRTLSTRSTANQSFRKVVKNTSGKTS
Number of residues
1354
Molecular Weight
158173.545
Theoretical pI
5.67
GO Classification
Functions
ATP binding / metal ion binding / protein kinase activity / protein serine/threonine kinase activity
Processes
actin cytoskeleton organization / apical constriction / apoptotic process / axon guidance / bleb assembly / cellular component disassembly involved in execution phase of apoptosis / cortical actin cytoskeleton organization / ephrin receptor signaling pathway / establishment of protein localization to plasma membrane / I-kappaB kinase/NF-kappaB signaling / leukocyte cell-cell adhesion / leukocyte migration / leukocyte tethering or rolling / membrane to membrane docking / myoblast migration / negative regulation of angiogenesis / negative regulation of bicellular tight junction assembly / negative regulation of myosin-light-chain-phosphatase activity / negative regulation of neuron apoptotic process / negative regulation of protein binding / positive regulation of focal adhesion assembly / programmed cell death / protein phosphorylation / regulation of actin cytoskeleton organization / regulation of cell adhesion / regulation of cell motility / regulation of establishment of cell polarity / regulation of establishment of endothelial barrier / regulation of focal adhesion assembly / regulation of keratinocyte differentiation / regulation of stress fiber assembly / Rho protein signal transduction / signal transduction / small GTPase mediated signal transduction / smooth muscle contraction / vascular endothelial growth factor receptor signaling pathway
Components
bleb / centriole / cytoskeleton / cytosol / Golgi membrane / lamellipodium / plasma membrane / ruffle
General Function
Protein serine/threonine kinase activity
Specific Function
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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0019049|Rho-associated protein kinase 1 (ROCK1)
ATGTCGACTGGGGACAGTTTTGAGACTCGATTTGAAAAAATGGACAACCTGCTGCGGGAT
CCCAAATCGGAAGTGAATTCGGATTGTTTGCTGGATGGATTGGATGCTTTGGTATATGAT
TTGGATTTTCCTGCCTTAAGAAAAAACAAAAATATTGACAACTTTTTAAGCAGATATAAA
GACACAATAAATAAAATCAGAGATTTACGAATGAAAGCTGAAGATTATGAAGTAGTGAAG
GTGATTGGTAGAGGTGCATTTGGAGAAGTTCAATTGGTAAGGCATAAATCCACCAGGAAG
GTATATGCTATGAAGCTTCTCAGCAAATTTGAAATGATAAAGAGATCTGATTCTGCTTTT
TTCTGGGAAGAAAGGGACATCATGGCTTTTGCCAACAGTCCTTGGGTTGTTCAGCTTTTT
TATGCATTCCAAGATGATCGTTATCTCTACATGGTGATGGAATACATGCCTGGTGGAGAT
CTTGTAAACTTAATGAGCAACTATGATGTGCCTGAAAAATGGGCACGATTCTATACTGCA
GAAGTAGTTCTTGCATTGGATGCAATCCATTCCATGGGTTTTATTCACAGAGATGTGAAG
CCTGATAACATGCTGCTGGATAAATCTGGACATTTGAAGTTAGCAGATTTTGGTACTTGT
ATGAAGATGAATAAGGAAGGCATGGTACGATGTGATACAGCGGTTGGAACACCTGATTAT
ATTTCCCCTGAAGTATTAAAATCCCAAGGTGGTGATGGTTATTATGGAAGAGAATGTGAC
TGGTGGTCGGTTGGGGTATTTTTATACGAAATGCTTGTAGGTGATACACCTTTTTATGCA
GATTCTTTGGTTGGAACTTACAGTAAAATTATGAACCATAAAAATTCACTTACCTTTCCT
GATGATAATGACATATCAAAAGAAGCAAAAAACCTTATTTGTGCCTTCCTTACTGACAGG
GAAGTGAGGTTAGGGCGAAATGGTGTAGAAGAAATCAAACGACATCTCTTCTTCAAAAAT
GACCAGTGGGCTTGGGAAACGCTCCGAGACACTGTAGCACCAGTTGTACCCGATTTAAGT
AGTGACATTGATACTAGTAATTTTGATGACTTGGAAGAAGATAAAGGAGAGGAAGAAACA
TTCCCTATTCCTAAAGCTTTCGTTGGCAATCAACTACCTTTTGTAGGATTTACATATTAT
AGCAATCGTAGATACTTATCTTCAGCAAATCCTAATGATAACAGAACTAGCTCCAATGCA
GATAAAAGCTTGCAGGAAAGTTTGCAAAAAACAATCTATAAGCTGGAAGAACAGCTGCAT
AATGAAATGCAGTTAAAAGATGAAATGGAGCAGAAGTGCAGAACCTCAAACATAAAACTA
GACAAGATAATGAAAGAATTGGATGAAGAGGGAAATCAAAGAAGAAATCTAGAATCTACA
GTGTCTCAGATTGAGAAGGAGAAAATGTTGCTACAGCATAGAATTAATGAGTACCAAAGA
AAAGCTGAACAGGAAAATGAGAAGAGAAGAAATGTAGAAAATGAAGTTTCTACATTAAAG
GATCAGTTGGAAGACTTAAAGAAAGTCAGTCAGAATTCACAGCTTGCTAATGAGAAGCTG
TCCCAGTTACAAAAGCAGCTAGAAGAAGCCAATGACTTACTTAGGACAGAATCGGACACA
GCTGTAAGATTGAGGAAGAGTCACACAGAGATGAGCAAGTCAATTAGTCAGTTAGAGTCC
CTGAACAGAGAGTTGCAAGAGAGAAATCGAATTTTAGAGAATTCTAAGTCACAAACAGAC
AAAGATTATTACCAGCTGCAAGCTATATTAGAAGCTGAACGAAGAGACAGAGGTCATGAT
TCTGAGATGATTGGAGACCTTCAAGCTCGAATTACATCTTTACAAGAGGAGGTGAAGCAT
CTCAAACATAATCTCGAAAAAGTGGAAGGAGAAAGAAAAGAGGCTCAAGACATGCTTAAT
CACTCAGAAAAGGAAAAGAATAATTTAGAGATAGATTTAAACTACAAACTTAAATCATTA
CAACAACGGTTAGAACAAGAGGTAAATGAACACAAAGTAACCAAAGCTCGTTTAACTGAC
AAACATCAATCTATTGAAGAGGCAAAGTCTGTGGCAATGTGTGAGATGGAAAAAAAGCTG
AAAGAAGAAAGAGAAGCTCGAGAGAAGGCTGAAAATCGGGTTGTTCAGATTGAGAAACAG
TGTTCCATGCTAGACGTTGATCTGAAGCAATCTCAGCAGAAACTAGAACATTTGACTGGA
AATAAAGAAAGGATGGAGGATGAAGTTAAGAATCTAACCCTGCAACTGGAGCAGGAATCA
AATAAGCGGCTGTTGTTACAAAATGAATTGAAGACTCAAGCATTTGAGGCAGACAATTTA
AAAGGTTTAGAAAAGCAGATGAAACAGGAAATAAATACTTTATTGGAAGCAAAGAGATTA
TTAGAATTTGAGTTAGCTCAGCTTACGAAACAGTATAGAGGAAATGAAGGACAGATGCGG
GAGCTACAAGATCAGCTTGAAGCTGAGCAATATTTCTCGACACTTTATAAAACCCAGGTA
AAGGAACTTAAAGAAGAAATTGAAGAAAAAAACAGAGAAAATTTAAAGAAAATACAGGAA
CTACAAAATGAAAAAGAAACTCTTGCTACTCAGTTGGATCTAGCAGAAACAAAAGCTGAG
TCTGAGCAGTTGGCGCGAGGCCTTCTGGAAGAACAGTATTTTGAATTGACGCAAGAAAGC
AAGAAAGCTGCTTCAAGAAATAGACAAGAGATTACAGATAAAGATCACACTGTTAGTCGG
CTTGAAGAAGCAAACAGCATGCTAACCAAAGATATTGAAATATTAAGAAGAGAGAATGAA
GAGCTAACAGAGAAAATGAAGAAGGCAGAGGAAGAATATAAACTGGAGAAGGAGGAGGAG
ATCAGTAATCTTAAGGCTGCCTTTGAAAAGAATATCAACACTGAACGAACCCTTAAAACA
CAGGCTGTTAACAAATTGGCAGAAATAATGAATCGAAAAGATTTTAAAATTGATAGAAAG
AAAGCTAATACACAAGATTTGAGAAAGAAAGAAAAGGAAAATCGAAAGCTGCAACTGGAA
CTCAACCAAGAAAGAGAGAAATTCAACCAGATGGTAGTGAAACATCAGAAGGAACTGAAT
GACATGCAAGCGCAATTGGTAGAAGAATGTGCACATAGGAATGAGCTTCAGATGCAGTTG
GCCAGCAAAGAGAGTGATATTGAGCAATTGCGTGCTAAACTTTTGGACCTCTCGGATTCT
ACAAGTGTTGCTAGTTTTCCTAGTGCTGATGAAACTGATGGTAACCTCCCAGAGTCAAGA
ATTGAAGGTTGGCTTTCAGTACCAAATAGAGGAAATATCAAACGATATGGCTGGAAGAAA
CAGTATGTTGTGGTAAGCAGCAAAAAAATTTTGTTCTATAATGACGAACAAGATAAGGAG
CAATCCAATCCATCTATGGTATTGGACATAGATAAACTGTTTCACGTTAGACCTGTAACC
CAAGGAGATGTGTATAGAGCTGAAACTGAAGAAATTCCTAAAATATTCCAGATACTATAT
GCAAATGAAGGTGAATGTAGAAAAGATGTAGAGATGGAACCAGTACAACAAGCTGAAAAA
ACTAATTTCCAAAATCACAAAGGCCATGAGTTTATTCCTACACTCTACCACTTTCCTGCC
AATTGTGATGCCTGTGCCAAACCTCTCTGGCATGTTTTTAAGCCACCCCCTGCCCTAGAG
TGTCGAAGATGCCATGTTAAGTGCCACAGAGATCACTTAGATAAGAAAGAGGACTTAATT
TGTCCATGTAAAGTAAGTTATGATGTAACATCAGCAAGAGATATGCTGCTGTTAGCATGT
TCTCAGGATGAACAAAAAAAATGGGTAACTCATTTAGTAAAGAAAATCCCTAAGAATCCA
CCATCTGGTTTTGTTCGTGCTTCCCCTCGAACGCTTTCTACAAGATCCACTGCAAATCAG
TCTTTCCGGAAAGTGGTCAAAAATACATCTGGAAAAACTAGTTAA
Chromosome Location
18
Locus
18q11.1
External Identifiers
ResourceLink
UniProtKB IDQ13464
UniProtKB Entry NameROCK1_HUMAN
GenBank Protein ID1276901
GenBank Gene IDU43195
GenAtlas IDROCK1
HGNC IDHGNC:10251
General References
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04707HydroxyfasudilexperimentalunknowninhibitorDetails
DB07876(S)-2-METHYL-1-[(4-METHYL-5-ISOQUINOLINE)SULFONYL]-HOMOPIPERAZINEexperimentalunknownDetails
DB08162FasudilinvestigationalunknownDetails
DB08756(R)-TRANS-4-(1-AMINOETHYL)-N-(4-PYRIDYL) CYCLOHEXANECARBOXAMIDEexperimentalunknownDetails
DB13165RipasudilexperimentalunknowninhibitorDetails
DB13931NetarsudilapprovedyesinhibitorDetails