P70335 (ROCK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

Rock1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1354 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles. Ref.4 Ref.5 Ref.6 Ref.7
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Enzyme regulation	Activated by RHOA binding. Inhibited by Y-27632 By similarity.
Subunit structure	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. Ref.7
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton › centrosome › centriole. Golgi apparatus membrane; Peripheral membrane protein By similarity. Cell projection › bleb 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	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.
Disruption phenotype	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. Ref.4
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: Contaminating sequence. Potential poly-A sequence. The sequence BAC34154.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cell projection Cytoplasm Cytoskeleton Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Zinc-finger
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Rho protein signal transduction Inferred from sequence orthology PubMed 18332105. Source: MGI actin cytoskeleton organization Inferred from genetic interaction PubMed 16249236. Source: MGI apical constriction Inferred from genetic interaction PubMed 21685893. Source: MGI apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW bleb assembly Inferred from mutant phenotype PubMed 17135244. Source: MGI leukocyte tethering or rolling Inferred from electronic annotation. Source: Compara membrane to membrane docking Inferred from electronic annotation. Source: Compara negative regulation of angiogenesis Inferred from electronic annotation. Source: Compara negative regulation of neuron apoptotic process Inferred from mutant phenotype PubMed 15071095. Source: MGI regulation of actin filament-based process Inferred from genetic interaction PubMed 21685893. Source: MGI regulation of keratinocyte differentiation Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell bleb Inferred from electronic annotation. Source: UniProtKB-SubCell centriole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipid binding Inferred from electronic annotation. Source: InterPro protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 1354	1353	Rho-associated protein kinase 1		PRO_0000086620
Regions
	Domain	76 – 338	263	Protein kinase
	Domain	341 – 409	69	AGC-kinase C-terminal
	Repeat	458 – 542	85	REM
	Domain	1118 – 1317	200	PH
	Nucleotide binding	82 – 90	9	ATP By similarity
	Zinc finger	1228 – 1283	56	Phorbol-ester/DAG-type
	Region	368 – 727	360	Interaction with FHOD1 By similarity
	Region	998 – 1010	13	RHOA binding By similarity
	Region	1115 – 1354	240	Auto-inhibitory By similarity
	Coiled coil	422 – 612	191	Potential
	Coiled coil	1011 – 1102	92	Potential
	Compositional bias	636 – 980	345	Glu-rich
Sites
	Active site	198	1	Proton acceptor By similarity
	Binding site	105	1	ATP By similarity
	Site	1113 – 1114	2	Cleavage; by caspase-3 By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
	Modified residue	1105	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	425	1	Missing in isoform 2.		VSP_010448

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: A1CBD543B831CF96	FASTA	1,354	158,171
	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
	Isoform 2 [UniParc]. Checksum: 209CACFD07E756CF	FASTA	1,353	158,042
	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 DKSLESLQKT IYKLEEQLHN EMQLKDEMEQ KCRTSNLKLD KIMKELDEEG NQRRNLESAV 490 500 510 520 530 540 SQIEKEKMLL QHRINEYQRK VEQENEKRRN IENEVSTLKD QLEDLRKASQ TSQLANEKLT 550 560 570 580 590 600 QLQKQLEEAN DLLRTESDTA VRLRKSHTEM SKSISQLESL NRELQERNRI LENSKSQADK 610 620 630 640 650 660 DYYQLQAVLE AERRDRGHDS EMIGDLQARI TSLQEEVKHL KHNLERVEGE RKEAQDMLNH 670 680 690 700 710 720 SEKEKNNLEI DLNYKLKSIQ QRLEQEVNEH KVTKARLTDK HQSIEEAKSV AMCEMEKKLK 730 740 750 760 770 780 EEREAREKAE NRVVETEKQC SMLDVDLKQS QQKLEHLTEN KERMEDEVKN LALQLEQESN 790 800 810 820 830 840 KRLLLQNELK TQAFEADNLK GLEKQMKQEI NTLLEAKRLL EFELAQLTKQ YRGNEGQMRE 850 860 870 880 890 900 LQDQLEAEQY FSTLYKTQVK ELKEEIEEKN RENLRKIQEL QSEKETLSTQ LDLAETKAES 910 920 930 940 950 960 EQLARGILEE QYFELTQESK KAASRNRQEI TDKDHTVSRL EETNSVLTKD IEMLRKENEE 970 980 990 1000 1010 1020 LNERMRTAEE EYKLKKEEEI NNLKAAFEKN ISTERTLKTQ AVNKLAEIMN RKDFKIDRKK 1030 1040 1050 1060 1070 1080 ANTQDLRKKE KENRKLQLEL NQEREKFNQM VVKHQKELND MQAQLVEECT HRNELQMQLA 1090 1100 1110 1120 1130 1140 SKESDIEQLR AKLLDLSDST SVASFPSADE TDGNLPESRI EGWLSVPNRG NIKRYGWKKQ 1150 1160 1170 1180 1190 1200 YVVVSSKKIL FYNDEQDKEQ SSPSMVLDID KLFHVRPVTQ GDVYRAETEE IPKIFQILYA 1210 1220 1230 1240 1250 1260 NEGECRKDIE VEPVQQGEKT NFQNHKGHEF IPTLYHFPAN CEACAKPLWH VFKPPPALEC 1270 1280 1290 1300 1310 1320 RRCHVKCHRD HLDKKEDLIS PCKVSYDVTS ARDMLLLACS QDEQKKWVTH LVKKIPKNPP 1330 1340 1350 SGFVRASPRT LSTRSTANQS FRKVVKNTSG KTS

References

	« Hide 'large scale' referencesShow '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] [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]	"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.
[6]	"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.
[7]	"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.
+	Additional computationally mapped references.

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.
IPI	IPI00108147. IPI00406463.
PIR	S74244.
RefSeq	NP_033097.1. NM_009071.2.
UniGene	Mm.6710.
3D structure databases
ProteinModelPortal	P70335.
SMR	P70335. Positions 6-402, 542-693, 946-1014, 1119-1288.
ModBase	Search...
Protein-protein interaction databases
IntAct	P70335. 2 interactions.
PTM databases
PhosphoSite	P70335.
Proteomic databases
PaxDb	P70335.
PRIDE	P70335.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000067947; ENSMUSP00000069549; ENSMUSG00000024290.
GeneID	19877.
KEGG	mmu:19877.
UCSC	uc008eaq.1. mouse.
Organism-specific databases
CTD	6093.
MGI	MGI:107927. Rock1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00700000104041.
HOGENOM	HOG000017259.
HOVERGEN	HBG053111.
InParanoid	P70335.
KO	K04514.
OMA	QIEKQCS.
OrthoDB	EOG4C2H8P.
Gene expression databases
Bgee	P70335.
Genevestigator	P70335.
GermOnline	ENSMUSG00000024290. Mus musculus.
Family and domain databases
Gene3D	2.30.29.30. 2 hits.
InterPro	IPR000961. AGC-kinase_C. IPR011072. HR1_rho-bd. IPR011009. Kinase-like_dom. IPR011993. PH_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. IPR015008. Rho-bd_dom. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
PANTHER	PTHR22988:SF3. PTHR22988:SF3. 1 hit.
Pfam	PF02185. HR1. 1 hit. PF00169. PH. 1 hit. PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. PF08912. Rho_Binding. 1 hit. [Graphical view]
PIRSF	PIRSF037568. Rho_kinase. 1 hit.
SMART	SM00109. C1. 1 hit. SM00233. PH. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
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. PS00479. ZF_DAG_PE_1. False negative. PS50081. ZF_DAG_PE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ROCK1. mouse.
NextBio	297366.
SOURCE	Search...

Entry information

Entry name

ROCK1_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program