Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P70335 (ROCK1_MOUSE)

Last modified January 19, 2010. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

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
Gene names
Name: Rock1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Hide | Top

Protein attributes

Sequence length1354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

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.

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, MYLC2B and PPP1R12A. Interacts with TSG101. Interacts with DAPK3 By similarity.

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, heart, lung, liver, stomach, spleen, kidney, testis, muscle, embryo and placenta. 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.

Miscellaneous

Inhibited by Y-27632 By similarity.

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.

Sequence caution

The sequence AAH57154.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

Hide | Top

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARHGAP24Q8N2641EBI-989293,EBI-988764From a different organism.

Hide | Top

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P70335-1)

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: P70335-2)

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.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 13541353Rho-associated protein kinase 1
PRO_0000086620

Regions

Domain76 – 338263Protein kinase
Domain341 – 40969AGC-kinase C-terminal
Repeat458 – 54285REM
Domain1118 – 1317200PH
Nucleotide binding82 – 909ATP By similarity
Zinc finger1228 – 128356Phorbol-ester/DAG-type
Region998 – 101013RHOA binding By similarity
Region1115 – 1354240Auto-inhibitory By similarity
Coiled coil422 – 612191 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 residue11801Phosphothreonine By similarity

Natural variations

Alternative sequence4251Missing in isoform 2.
VSP_010448

Hide | Top

Sequences

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

Last modified February 1, 1997. Version 1.
Checksum: A1CBD543B831CF96

FASTA1,354158,171
        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 ASENRSSSNV 

       430        440        450        460        470        480 
DKSLQESLQK TIYKLEEQLH NEMQLKDEME QKCRTSNLKL DKIMKELDEE GNQRRNLESA 

       490        500        510        520        530        540 
VSQIEKEKML LQHRINEYQR KVEQENEKRR NIENEVSTLK DQLEDLRKAS QTSQLANEKL 

       550        560        570        580        590        600 
TQLQKQLEEA NDLLRTESDT AVRLRKSHTE MSKSISQLES LNRELQERNR ILENSKSQAD 

       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 NKERMEDEVK NLALQLEQES 

       790        800        810        820        830        840 
NKRLLLQNEL 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 LEETNSVLTK DIEMLRKENE 

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

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

      1090       1100       1110       1120       1130       1140 
ASKESDIEQL RAKLLDLSDS TSVASFPSAD ETDGNLPESR IEGWLSVPNR GNIKRYGWKK 

      1150       1160       1170       1180       1190       1200 
QYVVVSSKKI LFYNDEQDKE QSSPSMVLDI DKLFHVRPVT QGDVYRAETE EIPKIFQILY 

      1210       1220       1230       1240       1250       1260 
ANEGECRKDI EVEPVQQGEK TNFQNHKGHE FIPTLYHFPA NCEACAKPLW HVFKPPPALE 

      1270       1280       1290       1300       1310       1320 
CRRCHVKCHR DHLDKKEDLI SPCKVSYDVT SARDMLLLAC SQDEQKKWVT HLVKKIPKNP 

      1330       1340       1350 
PSGFVRASPR TLSTRSTANQ SFRKVVKNTS GKTS

« Hide

Isoform 2.

Checksum: 209CACFD07E756CF
Show »

FASTA1,353158,042

Hide | Top

References

« Hide 'large scale' references
[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: 8772201] [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: 15489334] [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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 472-1354.
Strain: C57BL/6J.
Tissue: Heart and Liver.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U58512 mRNA. Translation: AAC53132.1.
AK050269 mRNA. Translation: BAC34154.1. Different initiation.
AK085974 mRNA. Translation: BAC39581.1.
BC057154 mRNA. Translation: AAH57154.1. Sequence problems.
IPIIPI00108147.
IPI00406463.
PIRS74244.
RefSeqNP_033097.1.
UniGeneMm.6710

3D structure databases

SMRP70335. Positions 6-405, 945-1013, 1119-1204, 1205-1288.
ModBaseSearch...

Protein-protein interaction databases

IntActP70335. 1 interaction.
STRINGP70335.

PTM databases

PhosphoSiteP70335.

Proteomic databases

PRIDEP70335.

Genome annotation databases

EnsemblENSMUST00000067947; ENSMUSP00000069549; ENSMUSG00000024290; Mus musculus. [Genome view]
GeneID19877.
KEGGmmu:19877.
UCSCuc008eaq.1. mouse.

Organism-specific databases

CTD19877.
MGIMGI:107927. Rock1.

Phylogenomic databases

eggNOGroNOG04526.
HOGENOMHBG445047.
HOVERGENP70335.
InParanoidP70335.
PhylomeDBP70335.

Enzyme and pathway databases

BRENDA2.7.11.1. 244.

Gene expression databases

ArrayExpressP70335.
BgeeP70335.
GenevestigatorP70335.
GermOnlineENSMUSG00000024290. Mus musculus.

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.
PF00169. PH. 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

NextBio297366.
SOURCESearch...

Hide | Top

Entry information

Entry nameROCK1_MOUSE
AccessionPrimary (citable) accession number: P70335
Secondary accession number(s): Q8C3G4, Q8C7H0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: February 1, 1997
Last modified: January 19, 2010
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

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