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Protein

Rho-associated protein kinase 1

Gene

Rock1

Organism
Rattus norvegicus (Rat)
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 (By similarity).By similarity2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi82 – 909ATPPROSITE-ProRule annotation
Zinc fingeri1243 – 129856Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

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

  • actin cytoskeleton organization Source: InterPro
  • apoptotic process Source: UniProtKB-KW
  • cytoskeleton organization Source: RGD
  • myoblast migration Source: UniProtKB
  • positive regulation of focal adhesion assembly Source: UniProtKB
  • regulation of establishment of cell polarity Source: InterPro
  • regulation of stress fiber assembly Source: InterPro
  • Rho protein signal transduction Source: MGI
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

SABIO-RKQ63644.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620424. Rock1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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

ChEMBLiCHEMBL5509.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 13691368Rho-associated protein kinase 1PRO_0000086623Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei1105 – 11051PhosphoserineBy similarity
Modified residuei1108 – 11081PhosphoserineBy similarity
Modified residuei1343 – 13431PhosphoserineBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Sitei1113 – 11142Cleavage; by caspase-3By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ63644.
PeptideAtlasiQ63644.
PRIDEiQ63644.

PTM databases

iPTMnetiQ63644.
PhosphoSiteiQ63644.

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

  • GTP-Rho binding Source: RGD

Protein-protein interaction databases

IntActiQ63644. 1 interaction.
STRINGi10116.ENSRNOP00000047378.

Chemistry

BindingDBiQ63644.

Structurei

3D structure databases

ProteinModelPortaliQ63644.
SMRiQ63644. Positions 6-405, 946-1013, 1134-1303.
ModBaseiSearch...
MobiDBiSearch...

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
Domaini1133 – 1332200PHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni368 – 727360Interaction with FHOD1By similarityAdd
BLAST
Regioni998 – 101013RHOA bindingBy similarityAdd
BLAST
Regioni1115 – 1369255Auto-inhibitoryBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili422 – 613192Sequence 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 fingeri1243 – 129856Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG0612. Eukaryota.
ENOG410XR1Q. LUCA.
HOGENOMiHOG000017259.
HOVERGENiHBG053111.
InParanoidiQ63644.
KOiK04514.
PhylomeDBiQ63644.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015008. Rho-bd_dom.
IPR029876. ROCK1.
IPR020684. ROCK1/ROCK2.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR22988:SF33. PTHR22988:SF33. 1 hit.
PfamiPF00069. 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]
SUPFAMiSSF50729. SSF50729. 2 hits.
SSF56112. 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]

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

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1118 – 113316VGSAC…FYSSS → E in AAP92621 (Ref. 2) CuratedAdd
BLAST
Sequence conflicti1283 – 12831S → C in AAP92621 (Ref. 2) Curated
Sequence conflicti1296 – 12961P → S in AAP92621 (Ref. 2) Curated
Sequence conflicti1316 – 13161P → S in AAP92621 (Ref. 2) Curated
Sequence conflicti1334 – 13352KA → NP in AAP92621 (Ref. 2) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 488488Missing in isoform 2. 1 PublicationVSP_010449Add
BLAST
Alternative sequencei1369 – 13691S → RLMPSSPCRVGVGIDKWRSH RDRKREGLLTEDVPGSRLEK KLGRIGRAARRNKDGADIQP CLDINDLLCMCRLVPLLGLP LVVTSGTAHVQFMHQVLVDR in isoform 2. 1 PublicationVSP_010450

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

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ63644.
SMRiQ63644. Positions 6-405, 946-1013, 1134-1303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ63644. 1 interaction.
STRINGi10116.ENSRNOP00000047378.

Chemistry

BindingDBiQ63644.
ChEMBLiCHEMBL5509.

PTM databases

iPTMnetiQ63644.
PhosphoSiteiQ63644.

Proteomic databases

PaxDbiQ63644.
PeptideAtlasiQ63644.
PRIDEiQ63644.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6093.
RGDi620424. Rock1.

Phylogenomic databases

eggNOGiKOG0612. Eukaryota.
ENOG410XR1Q. LUCA.
HOGENOMiHOG000017259.
HOVERGENiHBG053111.
InParanoidiQ63644.
KOiK04514.
PhylomeDBiQ63644.

Enzyme and pathway databases

SABIO-RKQ63644.

Miscellaneous databases

PROiQ63644.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015008. Rho-bd_dom.
IPR029876. ROCK1.
IPR020684. ROCK1/ROCK2.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR22988:SF33. PTHR22988:SF33. 1 hit.
PfamiPF00069. 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]
SUPFAMiSSF50729. SSF50729. 2 hits.
SSF56112. 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...

Entry informationi

Entry nameiROCK1_RAT
AccessioniPrimary (citable) accession number: Q63644
Secondary accession number(s): Q7TP31
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.