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Reviewed, UniProtKB/Swiss-Prot Q63644 (ROCK1_RAT)

Last modified January 19, 2010. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Rho-associated protein kinase 1
    EC=2.7.11.1
Alternative name(s):
    Rho-associated, coiled-coil-containing protein kinase 1
    p160 ROCK-1
      Short name=p160ROCK
    p150 RhoA-binding kinase ROK beta
    Liver regeneration-related protein LRRG199
Gene names
Name: Rock1
ORF Names: Ac2-154
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length1369 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Phosphorylates and activates DAPK3, which then regulates myosin light chain phosphatase through phosphorylation of MYPT1 thereby regulating the assembly of the actin cytoskeleton, cell migration, invasiveness of tumor cells, smooth muscle contraction and neurite outgrowth. Required for centromere positioning and centromere-dependent exit from mitosis. Necessary for apoptotic membrane blebbing By similarity. Ref.3

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by RHOA binding.

Subunit structure

Binds RHOA that has been activated by GTP binding. Binds ADD1, GEM, RHOB, RHOC, RHOE, VIM, LIMK1 and LIMK2, myosin light chain and PPP1R12A (MYPT1/MBS). Interacts with DAPK3 By similarity. Ref.1 Ref.4

Subcellular location

Cytoplasm. Cytoplasm › cytoskeleton › centrosome › centriole. Golgi apparatus membrane; Peripheral membrane protein By similarity. Note: Associated with the mother centriole and an intercentriolar linker. A small proportion is associated with Golgi membranes By similarity.

Tissue specificity

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

Domain

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.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR By similarity.

Involvement in disease

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

Miscellaneous

Inhibited by Y-27632.

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 PH domain.

Contains 1 phorbol-ester/DAG-type zinc finger.

Contains 1 protein kinase domain.

Contains 1 REM (Hr1) repeat.

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q63644-1)

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.
Isoform 2 (identifier: Q63644-2)

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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 13691368Rho-associated protein kinase 1
PRO_0000086623

Regions

Domain76 – 338263Protein kinase
Domain341 – 40969AGC-kinase C-terminal
Repeat458 – 54285REM
Domain1133 – 1332200PH
Nucleotide binding82 – 909ATP By similarity
Zinc finger1243 – 129856Phorbol-ester/DAG-type
Region998 – 101013RHOA binding By similarity
Region1115 – 1369255Auto-inhibitory By similarity
Coiled coil422 – 613192 Potential
Coiled coil1011 – 110292 Potential
Compositional bias636 – 980345Glu-rich

Sites

Active site1981Proton acceptor By similarity
Binding site1051ATP By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue4551Phosphothreonine By similarity
Modified residue4561Phosphoserine By similarity
Modified residue11051Phosphoserine By similarity
Modified residue11951Phosphothreonine By similarity

Natural variations

Alternative sequence1 – 488488Missing in isoform 2.
VSP_010449
Alternative sequence13691S → RLMPSSPCRVGVGIDKWRSH RDRKREGLLTEDVPGSRLEK KLGRIGRAARRNKDGADIQP CLDINDLLCMCRLVPLLGLP LVVTSGTAHVQFMHQVLVDR in isoform 2.
VSP_010450

Experimental info

Sequence conflict1118 – 113316VGSAC…FYSSS → E in AAP92621. Ref.2
Sequence conflict12831S → C in AAP92621. Ref.2
Sequence conflict12961P → S in AAP92621. Ref.2
Sequence conflict13161P → S in AAP92621. Ref.2
Sequence conflict1334 – 13352KA → NP in AAP92621. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E29B9456D348C9D0

FASTA1,369159,626
        10         20         30         40         50         60 
MSTGDSFETR FEKIDNLLRD PKSEVNSDCL LDGLDALVYD LDFPALRKNK NIDNFLSRYK 

        70         80         90        100        110        120 
DTINKIRDLR MKAEDYEVVK VIGRGAFGEV QLVRHKSTRK VYAMKLLSKF EMIKRSDSAF 

       130        140        150        160        170        180 
FWEERDIMAF ANSPWVVQLF YAFQDDRYLY MVMEYMPGGD LVNLMSNYDV PEKWARFYTA 

       190        200        210        220        230        240 
EVVLALDAIH SMGFIHRDVK PDNMLLDKSG HLKLADFGTC MKMNKEGMVR CDTAVGTPDY 

       250        260        270        280        290        300 
ISPEVLKSQG GDGYYGRECD WWSVGVFLYE MLVGDTPFYA DSLVGTYSKI MNHKNSLTFP 

       310        320        330        340        350        360 
DDNDISKEAK NLICAFLTDR EVRLGRNGVE EIKRHLFFKN DQWAWETLRD TVAPVVPDLS 

       370        380        390        400        410        420 
SDIDTSNFDD LEEDKGDEET FPIPKAFVGN QLPFVGFTYY SNRRYLPSAN PSENRSSSNV 

       430        440        450        460        470        480 
DKNVQESLQK TIYKLEEQLH NEMQLKDEME QKCRTSNIKL DKIMKELDEE GNQRRNLESA 

       490        500        510        520        530        540 
VSQIEKEKML LQHRINEYQR KVEQENEKRR NVENEVSTLK DQLEDLRKAS QSSQLANEKL 

       550        560        570        580        590        600 
TQLQKQLEEA NDLLRTESDT AVRLRKSHTE MSKSVSQLES LNRELQERNR MLENSKSQAD 

       610        620        630        640        650        660 
KDYYQLQAVL EAERRDRGHD SEMIGDLQAR ITSLQEEVKH LKHNLERVEG ERKEAQDMLN 

       670        680        690        700        710        720 
HSEKEKNNLE IDLNYKLKSI QQRLEQEVNE HKVTKARLTD KHQSIEEAKS VAMCEMEKKL 

       730        740        750        760        770        780 
KEEREAREKA ENRVVETEKQ CSMLDVDLKQ SQQKLEHLTE NKERLEDAVK SLTLQLEQES 

       790        800        810        820        830        840 
NKRILLQSEL KTQAFEADNL KGLEKQMKQE INTLLEAKRL LEFELAQLTK QYRGNEGQMR 

       850        860        870        880        890        900 
ELQDQLEAEQ YFSTLYKTQV KELKEEIEEK NRENLRKIQE LQSEKETLST QLDLAETKAE 

       910        920        930        940        950        960 
SEQLARGILE EQYFELTQES KKAASRNRQE ITDKDHTVSR LEEANNALTK DIELLRKENE 

       970        980        990       1000       1010       1020 
ELNERMRTAE EEYKLKKEEE ISNLKAAFEK NISTERTLKT QAVNKLAEIM NRKDFKIDRK 

      1030       1040       1050       1060       1070       1080 
KANTQDLRKK EKENRKLQLE LNQEREKFNQ MVVKHQKELN DMQAQLVEEC THRNELQMQL 

      1090       1100       1110       1120       1130       1140 
ASKESDIEQL RAKLLDLSDS TSVASFPSAD ETDGNLPVGS ACIPYLFIFY SSSSRIEGWL 

      1150       1160       1170       1180       1190       1200 
SVPNRGNIKR YGWKKQYVVV SSKKMLFYND EQDKEQSSPS MVLDIDKLFH VRPVTQGDVY 

      1210       1220       1230       1240       1250       1260 
RAETEEIPKI FQILYANEGE CRKDIEVEPV QQGEKTNFQN HKGHEFIPTL YHFPANCEAC 

      1270       1280       1290       1300       1310       1320 
AKPLWHVFKP PPALECRRCH VKSHRDHLDK KEDLIPPCKV SYDVTSARDM LLLACPQDEQ 

      1330       1340       1350       1360 
KKWVTHLVKK IPKKAPSGFV RASPRTLSTR STANQSFRKV VKNTSGKTS

« Hide

Isoform 2.

Checksum: 1465C2DFEC01255D
Show »

FASTA980114,243

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References

« Hide 'large scale' references
[1]"The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton."
Leung T., Chen X.-Q., Manser E., Lim L.
Mol. Cell. Biol. 16:5313-5327(1996) [PubMed: 8816443] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RHOA; RHOB AND RHOC, TISSUE SPECIFICITY.
Tissue: Brain and Liver.
[2]"Liver regeneration after PH."
Xu C.S., Li W.Q., Li Y.C., Yang K.J., Yan H.M., Chang C.F., Zhao L.F., Ma H., Wang L., Wang S.F., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y., Shi J.B., Rahman S., Wang Q.N., Zhang J.B.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Liver.
[3]"Calcium sensitization of smooth muscle mediated by a Rho-associated protein kinase in hypertension."
Uehata M., Ishizaki T., Satoh H., Ono T., Kawahara T., Morishita T., Tamakawa H., Yamagami K., Inui J., Maekawa M., Narumiya S.
Nature 389:990-994(1997) [PubMed: 9353125] [Abstract]
Cited for: FUNCTION, ROLE IN SMOOTH MUSCLE CONTRACTION AND HYPERTENSION, INHIBITION BY Y-27632.
[4]"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: 11956230] [Abstract]
Cited for: INTERACTION WITH GEM.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U61266 mRNA. Translation: AAB37571.1.
AY325220 mRNA. Translation: AAP92621.1.
IPIIPI00211045.
IPI00951118.
RefSeqNP_112360.1.
UniGeneRn.89756

3D structure databases

SMRQ63644. Positions 6-405, 946-1013, 1134-1219, 1220-1303.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ63644.

PTM databases

PhosphoSiteQ63644.

Genome annotation databases

EnsemblENSRNOT00000040922; ENSRNOP00000049511; ENSRNOG00000031092; Rattus norvegicus. [Genome view]
GeneID81762.
KEGGrno:81762.

Organism-specific databases

CTD81762.
RGD620424. Rock1.

Phylogenomic databases

eggNOGroNOG04526.
HOVERGENQ63644.
InParanoidQ63644.
PhylomeDBQ63644.

Enzyme and pathway databases

BRENDA2.7.11.1. 248.

Gene expression databases

ArrayExpressQ63644.
GenevestigatorQ63644.
GermOnlineENSRNOG00000031092. Rattus norvegicus.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR000861. HR1-like_rho-bd.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR001849. Pleckstrin_homology.
IPR002219. Prot_Kinase_C-like_PE/DAG_bd.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR020684. Rho-assoc_coiled-coil_kin-like.
IPR015751. Rho-assoc_coiled-coil_kinase.
IPR015008. Rho_bd.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]
Gene3DG3DSA:1.20.5.730. Rho_bd. 1 hit.
PANTHERPTHR22988:SF3. Rho_kinase. 1 hit.
PfamPF02185. HR1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
PF08912. Rho_Binding. 1 hit.
[Graphical view]
PIRSFPIRSF037568. Rho_kinase. 1 hit.
SMARTSM00109. C1. 1 hit.
SM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS51285. 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.
PS00479. ZF_DAG_PE_1. False negative.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio615550.

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Entry information

Entry nameROCK1_RAT
AccessionPrimary (citable) accession number: Q63644
Secondary accession number(s): Q7TP31
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: November 1, 1996
Last modified: January 19, 2010
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents