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Protein

Rho-associated protein kinase 1

Gene

Rock1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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 (By similarity).By similarity2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Activity regulationi

Activated by RHOA binding. Inhibited by Y-27632.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei105ATPPROSITE-ProRule annotation1
Active sitei198Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi82 – 90ATPPROSITE-ProRule annotation9
Zinc fingeri1243 – 1298Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST56

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processApoptosis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

SABIO-RKiQ63644

Names & Taxonomyi

Protein namesi
Recommended name:
Rho-associated protein kinase 1 (EC:2.7.11.1)
Alternative name(s):
Liver regeneration-related protein LRRG199
Rho-associated, coiled-coil-containing protein kinase 1
Rho-associated, coiled-coil-containing protein kinase I
Short name:
ROCK-I
p150 RhoA-binding kinase ROK beta
p160 ROCK-1
Short name:
p160ROCK
Gene namesi
Name:Rock1
ORF Names:Ac2-154
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620424 Rock1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

May play a role in hypertension. Rock1-inhibitors lower the blood pressure in spontaneous hypertensive, renal hypertensive and deoxycorticosterone acetate-induced hypertensive rats, but not in normal rats.

Chemistry databases

ChEMBLiCHEMBL5509

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000866232 – 1369Rho-associated protein kinase 1Add BLAST1368

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei1105PhosphoserineBy similarity1
Modified residuei1108PhosphoserineBy similarity1
Modified residuei1343PhosphoserineBy similarity1

Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1113 – 1114Cleavage; by caspase-3By similarity2

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ63644
PeptideAtlasiQ63644
PRIDEiQ63644

PTM databases

iPTMnetiQ63644
PhosphoSitePlusiQ63644

Expressioni

Tissue specificityi

Highly expressed in brain, spleen, lung, liver, skeletal muscle, kidney and testis.1 Publication

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with GEM, MYLC2B, RHOE, LIMK1, LIMK2, TSG101, CHORDC1, DAPK3, PFN1, PTEN and JIP3 (By similarity). Interacts with FHOD1 in a Src-dependent manner (By similarity). Interacts with ITGB1BP1 (via N-terminus and PTB domain) (By similarity). Interacts with RHOA (activated by GTP), RHOB, RHOC and PPP1R12A.By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

CORUMiQ63644
IntActiQ63644, 1 interactor
STRINGi10116.ENSRNOP00000047378

Chemistry databases

BindingDBiQ63644

Structurei

3D structure databases

ProteinModelPortaliQ63644
SMRiQ63644
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini76 – 338Protein kinasePROSITE-ProRule annotationAdd BLAST263
Domaini341 – 409AGC-kinase C-terminalAdd BLAST69
Domaini479 – 556REM-1PROSITE-ProRule annotationAdd BLAST78
Domaini949 – 1015RhoBDPROSITE-ProRule annotationAdd BLAST67
Domaini1133 – 1332PHPROSITE-ProRule annotationAdd BLAST200

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni368 – 727Interaction with FHOD1By similarityAdd BLAST360
Regioni998 – 1010RHOA bindingBy similarityAdd BLAST13
Regioni1115 – 1369Auto-inhibitoryBy similarityAdd BLAST255

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili422 – 692Sequence analysisAdd BLAST271
Coiled coili1011 – 1102Sequence analysisAdd BLAST92

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi636 – 980Glu-richAdd BLAST345

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1243 – 1298Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST56

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG0612 Eukaryota
ENOG410XR1Q LUCA
HOGENOMiHOG000017259
HOVERGENiHBG053111
InParanoidiQ63644
KOiK04514
PhylomeDBiQ63644

Family and domain databases

CDDicd00029 C1, 1 hit
cd11639 HR1_ROCK1, 1 hit
Gene3Di2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR000961 AGC-kinase_C
IPR011009 Kinase-like_dom_sf
IPR002219 PE/DAG-bd
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR015008 Rho-bd_dom
IPR029876 ROCK1
IPR020684 ROCK1/ROCK2
IPR037310 ROCK1_HR1
IPR008271 Ser/Thr_kinase_AS
PANTHERiPTHR22988:SF33 PTHR22988:SF33, 1 hit
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
PF08912 Rho_Binding, 1 hit
PIRSFiPIRSF037568 Rho_kinase, 1 hit
SMARTiView protein in SMART
SM00109 C1, 1 hit
SM00233 PH, 1 hit
SM00133 S_TK_X, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
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
PS51860 REM_1, 1 hit
PS51859 RHO_BD, 1 hit
PS50081 ZF_DAG_PE_2, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.iShow all

Isoform 1 (identifier: Q63644-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MSTGDSFETR FEKIDNLLRD 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 LEEDKGDEET FPIPKAFVGN QLPFVGFTYY
410 420 430 440 450
SNRRYLPSAN PSENRSSSNV DKNVQESLQK TIYKLEEQLH NEMQLKDEME
460 470 480 490 500
QKCRTSNIKL DKIMKELDEE GNQRRNLESA VSQIEKEKML LQHRINEYQR
510 520 530 540 550
KVEQENEKRR NVENEVSTLK DQLEDLRKAS QSSQLANEKL TQLQKQLEEA
560 570 580 590 600
NDLLRTESDT AVRLRKSHTE MSKSVSQLES LNRELQERNR MLENSKSQAD
610 620 630 640 650
KDYYQLQAVL EAERRDRGHD SEMIGDLQAR ITSLQEEVKH LKHNLERVEG
660 670 680 690 700
ERKEAQDMLN HSEKEKNNLE IDLNYKLKSI QQRLEQEVNE HKVTKARLTD
710 720 730 740 750
KHQSIEEAKS VAMCEMEKKL KEEREAREKA ENRVVETEKQ CSMLDVDLKQ
760 770 780 790 800
SQQKLEHLTE NKERLEDAVK SLTLQLEQES NKRILLQSEL KTQAFEADNL
810 820 830 840 850
KGLEKQMKQE INTLLEAKRL LEFELAQLTK QYRGNEGQMR ELQDQLEAEQ
860 870 880 890 900
YFSTLYKTQV KELKEEIEEK NRENLRKIQE LQSEKETLST QLDLAETKAE
910 920 930 940 950
SEQLARGILE EQYFELTQES KKAASRNRQE ITDKDHTVSR LEEANNALTK
960 970 980 990 1000
DIELLRKENE ELNERMRTAE EEYKLKKEEE ISNLKAAFEK NISTERTLKT
1010 1020 1030 1040 1050
QAVNKLAEIM NRKDFKIDRK KANTQDLRKK EKENRKLQLE LNQEREKFNQ
1060 1070 1080 1090 1100
MVVKHQKELN DMQAQLVEEC THRNELQMQL ASKESDIEQL RAKLLDLSDS
1110 1120 1130 1140 1150
TSVASFPSAD ETDGNLPVGS ACIPYLFIFY SSSSRIEGWL SVPNRGNIKR
1160 1170 1180 1190 1200
YGWKKQYVVV SSKKMLFYND EQDKEQSSPS MVLDIDKLFH VRPVTQGDVY
1210 1220 1230 1240 1250
RAETEEIPKI FQILYANEGE CRKDIEVEPV QQGEKTNFQN HKGHEFIPTL
1260 1270 1280 1290 1300
YHFPANCEAC AKPLWHVFKP PPALECRRCH VKSHRDHLDK KEDLIPPCKV
1310 1320 1330 1340 1350
SYDVTSARDM LLLACPQDEQ KKWVTHLVKK IPKKAPSGFV RASPRTLSTR
1360
STANQSFRKV VKNTSGKTS
Length:1,369
Mass (Da):159,626
Last modified:November 1, 1996 - v1
Checksum:iE29B9456D348C9D0
GO
Isoform 2 (identifier: Q63644-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-488: Missing.
     1369-1369: S → RLMPSSPCRV...QFMHQVLVDR

Note: No experimental confirmation available.
Show »
Length:980
Mass (Da):114,243
Checksum:i1465C2DFEC01255D
GO

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D4A5S0D4A5S0_RAT
Rho-associated protein kinase
Rock1
1,369Annotation score:
D3ZN37D3ZN37_RAT
Rho-associated protein kinase
Rock1
1,354Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1118 – 1133VGSAC…FYSSS → E in AAP92621 (Ref. 2) CuratedAdd BLAST16
Sequence conflicti1283S → C in AAP92621 (Ref. 2) Curated1
Sequence conflicti1296P → S in AAP92621 (Ref. 2) Curated1
Sequence conflicti1316P → S in AAP92621 (Ref. 2) Curated1
Sequence conflicti1334 – 1335KA → NP in AAP92621 (Ref. 2) Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0104491 – 488Missing in isoform 2. 1 PublicationAdd BLAST488
Alternative sequenceiVSP_0104501369S → RLMPSSPCRVGVGIDKWRSH RDRKREGLLTEDVPGSRLEK KLGRIGRAARRNKDGADIQP CLDINDLLCMCRLVPLLGLP LVVTSGTAHVQFMHQVLVDR in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U61266 mRNA Translation: AAB37571.1
AY325220 mRNA Translation: AAP92621.1
RefSeqiNP_112360.1, NM_031098.1 [Q63644-1]
UniGeneiRn.89756

Genome annotation databases

GeneIDi81762
KEGGirno:81762
UCSCiRGD:620424 rat [Q63644-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiROCK1_RAT
AccessioniPrimary (citable) accession number: Q63644
Secondary accession number(s): Q7TP31
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: November 1, 1996
Last modified: September 12, 2018
This is version 171 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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