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P70335

- ROCK1_MOUSE

UniProt

P70335 - ROCK1_MOUSE

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Protein

Rho-associated protein kinase 1

Gene

Rock1

Organism
Mus musculus (Mouse)
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. Required for centrosome positioning and centrosome-dependent exit from mitosis. Plays a role in terminal erythroid differentiation. Promotes keratinocyte terminal differentiation (By similarity). 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. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles.By similarity5 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.By similarity

Enzyme regulationi

Activated by RHOA binding. Inhibited by Y-27632 (By similarity).By similarity

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi82 – 909ATPPROSITE-ProRule annotation
Zinc fingeri1228 – 128356Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. actin cytoskeleton organization Source: MGI
  2. apical constriction Source: MGI
  3. apoptotic process Source: UniProtKB-KW
  4. bleb assembly Source: MGI
  5. leukocyte tethering or rolling Source: Ensembl
  6. membrane to membrane docking Source: Ensembl
  7. myoblast migration Source: UniProtKB
  8. negative regulation of angiogenesis Source: Ensembl
  9. negative regulation of neuron apoptotic process Source: MGI
  10. positive regulation of focal adhesion assembly Source: UniProtKB
  11. regulation of actin filament-based process Source: MGI
  12. regulation of keratinocyte differentiation Source: Ensembl
  13. 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

ReactomeiREACT_204733. G alpha (12/13) signalling events.
REACT_224460. Apoptotic cleavage of cellular proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho-associated protein kinase 1 (EC:2.7.11.1)
Alternative name(s):
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:107927. Rock1.

Subcellular locationi

Cytoplasm 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole 1 Publication. Golgi apparatus membrane By similarity; Peripheral membrane protein By similarity. Cell projectionbleb By similarity. Cytoplasmcytoskeleton 1 Publication. Cell membrane 1 Publication. Cell projectionlamellipodium 1 Publication. Cell projectionruffle 1 Publication
Note: Associated with the mother centriole and an intercentriolar linker. A small proportion is associated with Golgi membranes (By similarity). 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

GO - Cellular componenti

  1. cytoskeleton Source: UniProtKB
  2. Golgi apparatus Source: UniProtKB-KW
  3. lamellipodium Source: UniProtKB
  4. plasma membrane Source: UniProtKB
  5. ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Disruption phenotypei

Mice exhibit both EOB (eyes open at birth) and omphalocele phenotypes as a result of disorganization of actomyosin cables in the eyelid epithelium and defective actin assembly in the umbilical ring.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 13541353Rho-associated protein kinase 1PRO_0000086620Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP70335.
PaxDbiP70335.
PRIDEiP70335.

PTM databases

PhosphoSiteiP70335.

Expressioni

Tissue specificityi

Highly expressed in brain, heart, lung, liver, stomach, spleen, kidney, testis, muscle, embryo and placenta.1 Publication

Gene expression databases

BgeeiP70335.
GenevestigatoriP70335.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with RHOA (activated by GTP), RHOB, RHOC, GEM, MYLC2B, RHOE, PPP1R12A, LIMK1, LIMK2, TSG101, CHORDC1, DAPK3, PFN1 and JIP3 (By similarity). Interacts with FHOD1 in a Src-dependent manner (By similarity). Interacts with PTEN. Interacts with ITGB1BP1 (via N-terminus and PTB domain).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Rnd3P615887EBI-989293,EBI-6930266

Protein-protein interaction databases

BioGridi202950. 5 interactions.
IntActiP70335. 4 interactions.
MINTiMINT-4132852.

Structurei

3D structure databases

ProteinModelPortaliP70335.
SMRiP70335. Positions 6-402, 542-693, 835-902, 946-1014, 1119-1288.
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
Domaini1118 – 1317200PHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni368 – 727360Interaction with FHOD1By similarityAdd
BLAST
Regioni998 – 101013RHOA bindingBy similarityAdd
BLAST
Regioni1115 – 1354240Auto-inhibitoryBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili422 – 612191Sequence 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 fingeri1228 – 128356Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118994.
HOGENOMiHOG000017259.
HOVERGENiHBG053111.
InParanoidiP70335.
KOiK04514.
OMAiQIEKQCS.
OrthoDBiEOG7DZ8J4.
PhylomeDBiP70335.
TreeFamiTF313551.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR000961. AGC-kinase_C.
IPR011072. HR1_rho-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015008. Rho-bd_dom.
IPR020684. ROCK1/ROCK2.
IPR002290. Ser/Thr_dual-sp_kinase.
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]

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. Align

Isoform 1 (identifier: P70335-1) [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 ASENRSSSNV DKSLQESLQK TIYKLEEQLH NEMQLKDEME
460 470 480 490 500
QKCRTSNLKL DKIMKELDEE GNQRRNLESA VSQIEKEKML LQHRINEYQR
510 520 530 540 550
KVEQENEKRR NIENEVSTLK DQLEDLRKAS QTSQLANEKL TQLQKQLEEA
560 570 580 590 600
NDLLRTESDT AVRLRKSHTE MSKSISQLES LNRELQERNR ILENSKSQAD
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 NKERMEDEVK NLALQLEQES NKRLLLQNEL 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 LEETNSVLTK
960 970 980 990 1000
DIEMLRKENE ELNERMRTAE EEYKLKKEEE INNLKAAFEK 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 ETDGNLPESR IEGWLSVPNR GNIKRYGWKK QYVVVSSKKI
1160 1170 1180 1190 1200
LFYNDEQDKE QSSPSMVLDI DKLFHVRPVT QGDVYRAETE EIPKIFQILY
1210 1220 1230 1240 1250
ANEGECRKDI EVEPVQQGEK TNFQNHKGHE FIPTLYHFPA NCEACAKPLW
1260 1270 1280 1290 1300
HVFKPPPALE CRRCHVKCHR DHLDKKEDLI SPCKVSYDVT SARDMLLLAC
1310 1320 1330 1340 1350
SQDEQKKWVT HLVKKIPKNP PSGFVRASPR TLSTRSTANQ SFRKVVKNTS

GKTS
Length:1,354
Mass (Da):158,171
Last modified:February 1, 1997 - v1
Checksum:iA1CBD543B831CF96
GO
Isoform 2 (identifier: P70335-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     425-425: Missing.

Note: May be due to a competing donor splice site. No experimental confirmation available.

Show »
Length:1,353
Mass (Da):158,042
Checksum:i209CACFD07E756CF
GO

Sequence cautioni

The sequence AAH57154.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence BAC34154.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei425 – 4251Missing in isoform 2. 1 PublicationVSP_010448

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U58512 mRNA. Translation: AAC53132.1.
AK050269 mRNA. Translation: BAC34154.1. Different initiation.
AK085974 mRNA. Translation: BAC39581.1.
BC057154 mRNA. Translation: AAH57154.1. Sequence problems.
CCDSiCCDS29053.2. [P70335-1]
PIRiS74244.
RefSeqiNP_033097.1. NM_009071.2. [P70335-1]
XP_006525788.1. XM_006525725.1. [P70335-2]
UniGeneiMm.6710.

Genome annotation databases

EnsembliENSMUST00000067947; ENSMUSP00000069549; ENSMUSG00000024290. [P70335-1]
GeneIDi19877.
KEGGimmu:19877.
UCSCiuc008eaq.1. mouse. [P70335-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U58512 mRNA. Translation: AAC53132.1 .
AK050269 mRNA. Translation: BAC34154.1 . Different initiation.
AK085974 mRNA. Translation: BAC39581.1 .
BC057154 mRNA. Translation: AAH57154.1 . Sequence problems.
CCDSi CCDS29053.2. [P70335-1 ]
PIRi S74244.
RefSeqi NP_033097.1. NM_009071.2. [P70335-1 ]
XP_006525788.1. XM_006525725.1. [P70335-2 ]
UniGenei Mm.6710.

3D structure databases

ProteinModelPortali P70335.
SMRi P70335. Positions 6-402, 542-693, 835-902, 946-1014, 1119-1288.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202950. 5 interactions.
IntActi P70335. 4 interactions.
MINTi MINT-4132852.

PTM databases

PhosphoSitei P70335.

Proteomic databases

MaxQBi P70335.
PaxDbi P70335.
PRIDEi P70335.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000067947 ; ENSMUSP00000069549 ; ENSMUSG00000024290 . [P70335-1 ]
GeneIDi 19877.
KEGGi mmu:19877.
UCSCi uc008eaq.1. mouse. [P70335-1 ]

Organism-specific databases

CTDi 6093.
MGIi MGI:107927. Rock1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118994.
HOGENOMi HOG000017259.
HOVERGENi HBG053111.
InParanoidi P70335.
KOi K04514.
OMAi QIEKQCS.
OrthoDBi EOG7DZ8J4.
PhylomeDBi P70335.
TreeFami TF313551.

Enzyme and pathway databases

Reactomei REACT_204733. G alpha (12/13) signalling events.
REACT_224460. Apoptotic cleavage of cellular proteins.

Miscellaneous databases

ChiTaRSi ROCK1. mouse.
NextBioi 297366.
PROi P70335.
SOURCEi Search...

Gene expression databases

Bgeei P70335.
Genevestigatori P70335.

Family and domain databases

Gene3Di 2.30.29.30. 2 hits.
InterProi IPR000961. AGC-kinase_C.
IPR011072. HR1_rho-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015008. Rho-bd_dom.
IPR020684. ROCK1/ROCK2.
IPR002290. Ser/Thr_dual-sp_kinase.
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. "ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil forming protein serine/threonine kinase in mice."
    Nakagawa O., Fujisawa K., Ishizaki T., Saito Y., Nakao K., Narumiya S.
    FEBS Lett. 392:189-193(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Embryo and Heart.
  2. "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] OF 1-506 (ISOFORM 2).
    Strain: FVB/N.
    Tissue: Mammary gland.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 472-1354.
    Strain: C57BL/6J.
    Tissue: Heart and Liver.
  4. "ROCK-I regulates closure of the eyelids and ventral body wall by inducing assembly of actomyosin bundles."
    Shimizu Y., Thumkeo D., Keel J., Ishizaki T., Oshima H., Oshima M., Noda Y., Matsumura F., Taketo M.M., Narumiya S.
    J. Cell Biol. 168:941-953(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  5. "Integrin cytoplasmic domain-associated protein-1 (ICAP-1) interacts with the ROCK-I kinase at the plasma membrane."
    Stroeken P.J., Alvarez B., Van Rheenen J., Wijnands Y.M., Geerts D., Jalink K., Roos E.
    J. Cell. Physiol. 208:620-628(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ITGB1BP1, SUBCELLULAR LOCATION.
  6. "Integrin Cytoplasmic domain-Associated Protein-1 (ICAP-1) promotes migration of myoblasts and affects focal adhesions."
    Alvarez B., Stroeken P.J., Edel M.J., Roos E.
    J. Cell. Physiol. 214:474-482(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ITGB1BP1.
  7. "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.
  8. "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.
  9. "ROCK1 functions as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability."
    Vemula S., Shi J., Hanneman P., Wei L., Kapur R.
    Blood 115:1785-1796(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PTEN.
  10. "Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent fibronectin deposition."
    Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A., Mosher D., Block M.R., Albiges-Rizo C., Bouvard D.
    J. Cell Biol. 194:307-322(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiROCK1_MOUSE
AccessioniPrimary (citable) accession number: P70335
Secondary accession number(s): Q8C3G4, Q8C7H0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: February 1, 1997
Last modified: October 29, 2014
This is version 147 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3