P70336 (ROCK2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rho-associated protein kinase 2
EC=2.7.11.1

Alternative name(s):
Rho-associated, coiled-coil-containing protein kinase 2
Rho-associated, coiled-coil-containing protein kinase II
Short name=ROCK-II
p164 ROCK-2

Gene names

Name:

Rock2

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	1388 AA.
Sequence status	Complete.
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 ADD1, BRCA2, CNN1, EZR, DPYSL2, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM. Phosphorylates SORL1 and IRF4. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Positively regulates the activation of p42/MAPK1-p44/MAPK3 and of p90RSK/RPS6KA1 during myogenic differentiation. Plays an important role in the timely initiation of centrosome duplication. Inhibits keratinocyte terminal differentiation. May regulate closure of the eyelids and ventral body wall through organization of actomyosin bundles. Plays a critical role in the regulation of spine and synaptic properties in the hippocampus. Plays a role in placental homeostasis during the perinatal period. Ref.4 Ref.7 Ref.8 Ref.9
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), CHORDC1, IRS1, RHOB, RHOC, PPP1R12A, SORL1, EP300 and BRCA2 By similarity. Interacts with NPM1 and this interaction enhances its activity By similarity. Interacts with RAF1 By similarity.
Subcellular location	Isoform 1: Cytoplasm. Cell membrane; Peripheral membrane protein Ref.2. Nucleus By similarity. Cytoplasm › cytoskeleton › centrosome By similarity. Note: Cytoplasmic, and associated with actin microfilaments and the plasma membrane By similarity. Ref.2 Isoform 2: Cytoplasm. Cell membrane; Peripheral membrane protein Ref.2.
Tissue specificity	Highly expressed in brain, heart, lung, liver, stomach, spleen, kidney, testis, muscle, embryo and placenta. Isoform 2 is expressed predominantly in the skeletal muscle. Ref.1 Ref.2
Domain	An interaction between Thr-414 and Asp-48 is essential for kinase activity and dimerization By similarity.
Post-translational modification	Autophosphorylated. Phosphorylation at Tyr-722 reduces its binding to RHOA and is crucial for focal adhesion dynamics. Dephosphorylation by PTPN11 stimulates its RHOA binding activity By similarity. Ref.2 Cleaved by granzyme B during apoptosis. This leads to constitutive activation of the kinase and membrane blebbing.
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. Mice are impaired in both basal synaptic transmission and hippocampal long-term potentiation (LTP). Embryos manifest extensive thrombus formation in the placenta, resulting in placental dysfunction, intrauterine growth retardation, and fetal death. Ref.4 Ref.5 Ref.8
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.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane Nucleus
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	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 neural tube closure Inferred from genetic interaction PubMed 17229766. Source: MGI positive regulation of centrosome duplication Inferred from mutant phenotype PubMed 17015463. Source: MGI
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell spindle pole centrosome Inferred from direct assay PubMed 17015463. Source: MGI
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: P70336-1)

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: P70336-2)

Also known as: ROCK2m;

The sequence of this isoform differs from the canonical sequence as follows:
     1149-1149: P → PVHITQSHTMESMSFTYQRSSTSLSIATKPSSSHTLLDFDSEEDSLPYLPSSSEPIST
     1388-1388: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1388	1388	Rho-associated protein kinase 2		PRO_0000086626
Regions
	Domain	92 – 354	263	Protein kinase
	Domain	357 – 425	69	AGC-kinase C-terminal
	Repeat	475 – 559	85	REM
	Domain	1150 – 1349	200	PH
	Nucleotide binding	98 – 106	9	ATP By similarity
	Zinc finger	1260 – 1315	56	Phorbol-ester/DAG-type
	Region	363 – 784	422	Interaction with PPP1R12A By similarity
	Region	373 – 420	48	Interaction with NPM1 By similarity
	Region	979 – 1047	69	RHOA binding By similarity
	Coiled coil	439 – 1131	693	Potential
Sites
	Active site	214	1	Proton acceptor By similarity
	Binding site	121	1	ATP By similarity
	Site	1131 – 1132	2	Cleavage; by granzyme B
Amino acid modifications
	Modified residue	414	1	Phosphothreonine; by ROCK2 By similarity
	Modified residue	722	1	Phosphotyrosine; by SRC By similarity
	Modified residue	1137	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1149	1	P → PVHITQSHTMESMSFTYQRS STSLSIATKPSSSHTLLDFD SEEDSLPYLPSSSEPIST in isoform 2.		VSP_041818
	Alternative sequence	1388	1	Missing in isoform 2.		VSP_041819

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 7A4F331165038161	FASTA	1,388	160,586
	10 20 30 40 50 60 MSRPPPTGKM PGAPEAAPGD GAGAGRQRKL EALIRDPRSP INVESLLDGL NSLVLDLDFP 70 80 90 100 110 120 ALRKNKNIDN FLNRYEKIVK KIRGLQMKAE DYDVVKVIGR GAFGEVQLVR HKASQKVYAM 130 140 150 160 170 180 KLLSKFEMIK RSDSAFFWEE RDIMAFANSP WVVQLFCAFQ DDRYLYMVME YMPGGDLVNL 190 200 210 220 230 240 MSNYDVPEKW AKFYTAEVVL ALDAIHSMGL IHRDVKPDNM LLDKHGHLKL ADFGTCMKMD 250 260 270 280 290 300 ETGMVHCDTA VGTPDYISPE VLKSQGGDGY YGRECDWWSV GVFLFEMLVG DTPFYADSLV 310 320 330 340 350 360 GTYSKIMDHK NSLCFPEDTE ISKHAKNLIC AFLTDREVRL GRNGVEEIKQ HPFFKNDQWN 370 380 390 400 410 420 WDNIRETAAP VVPELSSDID SSNFDDIEDD KGDVETFPIP KAFVGNQLPF IGFTYFRENL 430 440 450 460 470 480 LLSDSPPCRE NDAIQTRKSE ESQEIQKKLY ALEEHLSSEV QAKEELEQKC KSINTRLEKT 490 500 510 520 530 540 AKELEEEITL RKSVESTLRQ LEREKALLQH KNAEYQRKAD HEADKKRNLE NDVNSLKDQL 550 560 570 580 590 600 EDLKKRNQSS QISTEKVNQL QKQLDEANAL LRTESDTAAR LRKTQAESSK QIQQLESNNR 610 620 630 640 650 660 DLQDKNCLLE TAKLKLEKEF INLQSALESE RRDRTHGSEI INDLQGRISG LEEDLKTGKA 670 680 690 700 710 720 LLAKVELEKR QLQEKLTDLE KEKSNMEIDM TYQLKVIQQS LEQEEAEHKT TKARLADKNK 730 740 750 760 770 780 IYESIEEAKS EAMKEMEKKL LEERSLKQKV ENLLLEAEKR CSILDCDLKQ SQQKLNELLK 790 800 810 820 830 840 QKDVLNEDVR NLTLKIEQET QKRCLMQNDL KMQTQQVNTL KMSEKQIKQE NNHLMEMKMN 850 860 870 880 890 900 LEKQNTELRK ERQDADGQMK ELQDQLEAEQ YFSTLYKTQV RELKEENEEK TKLCKELQQK 910 920 930 940 950 960 KQDLQDERDS LAAQLEITLT KADSEQLARS IAEEQYSDLE KEKIMKELEI KEMMARHKQE 970 980 990 1000 1010 1020 LTEKDTTIAS LEETNRTLTS DVANLANEKE ELNNKLKDSQ EQLSKLKDEE MSAAAIKAQF 1030 1040 1050 1060 1070 1080 EKQLLNERTL KTQAVNKLAE IMNRKEPVKR GSDTDVRRKE KENRKLHMEL KSEREKLTQQ 1090 1100 1110 1120 1130 1140 MIKYQKELNE MQAQIAEESQ IRIELQMTLD SKDSDIEQLR SQLQALHIGM DSSSIGSGPG 1150 1160 1170 1180 1190 1200 DAEPDDGFPE SRLEGWLSLP VRNNTKKFGW VKKYVIVSSK KILFYDSEQD KEQSNPYMVL 1210 1220 1230 1240 1250 1260 DIDKLFHVRP VTQTDVYRAD AKEIPRIFQI LYANEGESKK EPEFPVEPVG EKSNYICHKG 1270 1280 1290 1300 1310 1320 HEFIPTLYHF PTNCEACMKP LWHMFKPPPA LECRRCHIKC HKDHMDKKEE IIAPCKVYYD 1330 1340 1350 1360 1370 1380 ISSAKNLLLL ANSTEEQQKW VSRLVKKIPK KPPAPDPFAR SSPRTSMKIQ QNQSIRRPSR QLAPNKPS
	Isoform 2 (ROCK2m) [UniParc]. Checksum: 42E61D28C806D715	FASTA	1,444	166,760
	10 20 30 40 50 60 MSRPPPTGKM PGAPEAAPGD GAGAGRQRKL EALIRDPRSP INVESLLDGL NSLVLDLDFP 70 80 90 100 110 120 ALRKNKNIDN FLNRYEKIVK KIRGLQMKAE DYDVVKVIGR GAFGEVQLVR HKASQKVYAM 130 140 150 160 170 180 KLLSKFEMIK RSDSAFFWEE RDIMAFANSP WVVQLFCAFQ DDRYLYMVME YMPGGDLVNL 190 200 210 220 230 240 MSNYDVPEKW AKFYTAEVVL ALDAIHSMGL IHRDVKPDNM LLDKHGHLKL ADFGTCMKMD 250 260 270 280 290 300 ETGMVHCDTA VGTPDYISPE VLKSQGGDGY YGRECDWWSV GVFLFEMLVG DTPFYADSLV 310 320 330 340 350 360 GTYSKIMDHK NSLCFPEDTE ISKHAKNLIC AFLTDREVRL GRNGVEEIKQ HPFFKNDQWN 370 380 390 400 410 420 WDNIRETAAP VVPELSSDID SSNFDDIEDD KGDVETFPIP KAFVGNQLPF IGFTYFRENL 430 440 450 460 470 480 LLSDSPPCRE NDAIQTRKSE ESQEIQKKLY ALEEHLSSEV QAKEELEQKC KSINTRLEKT 490 500 510 520 530 540 AKELEEEITL RKSVESTLRQ LEREKALLQH KNAEYQRKAD HEADKKRNLE NDVNSLKDQL 550 560 570 580 590 600 EDLKKRNQSS QISTEKVNQL QKQLDEANAL LRTESDTAAR LRKTQAESSK QIQQLESNNR 610 620 630 640 650 660 DLQDKNCLLE TAKLKLEKEF INLQSALESE RRDRTHGSEI INDLQGRISG LEEDLKTGKA 670 680 690 700 710 720 LLAKVELEKR QLQEKLTDLE KEKSNMEIDM TYQLKVIQQS LEQEEAEHKT TKARLADKNK 730 740 750 760 770 780 IYESIEEAKS EAMKEMEKKL LEERSLKQKV ENLLLEAEKR CSILDCDLKQ SQQKLNELLK 790 800 810 820 830 840 QKDVLNEDVR NLTLKIEQET QKRCLMQNDL KMQTQQVNTL KMSEKQIKQE NNHLMEMKMN 850 860 870 880 890 900 LEKQNTELRK ERQDADGQMK ELQDQLEAEQ YFSTLYKTQV RELKEENEEK TKLCKELQQK 910 920 930 940 950 960 KQDLQDERDS LAAQLEITLT KADSEQLARS IAEEQYSDLE KEKIMKELEI KEMMARHKQE 970 980 990 1000 1010 1020 LTEKDTTIAS LEETNRTLTS DVANLANEKE ELNNKLKDSQ EQLSKLKDEE MSAAAIKAQF 1030 1040 1050 1060 1070 1080 EKQLLNERTL KTQAVNKLAE IMNRKEPVKR GSDTDVRRKE KENRKLHMEL KSEREKLTQQ 1090 1100 1110 1120 1130 1140 MIKYQKELNE MQAQIAEESQ IRIELQMTLD SKDSDIEQLR SQLQALHIGM DSSSIGSGPG 1150 1160 1170 1180 1190 1200 DAEPDDGFPV HITQSHTMES MSFTYQRSST SLSIATKPSS SHTLLDFDSE EDSLPYLPSS 1210 1220 1230 1240 1250 1260 SEPISTESRL EGWLSLPVRN NTKKFGWVKK YVIVSSKKIL FYDSEQDKEQ SNPYMVLDID 1270 1280 1290 1300 1310 1320 KLFHVRPVTQ TDVYRADAKE IPRIFQILYA NEGESKKEPE FPVEPVGEKS NYICHKGHEF 1330 1340 1350 1360 1370 1380 IPTLYHFPTN CEACMKPLWH MFKPPPALEC RRCHIKCHKD HMDKKEEIIA PCKVYYDISS 1390 1400 1410 1420 1430 1440 AKNLLLLANS TEEQQKWVSR LVKKIPKKPP APDPFARSSP RTSMKIQQNQ SIRRPSRQLA PNKP

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.
[2]	"ROCK2 and its alternatively spliced isoform ROCK2m positively control the maturation of the myogenic program." Pelosi M., Marampon F., Zani B.M., Prudente S., Perlas E., Caputo V., Cianetti L., Berno V., Narumiya S., Kang S.W., Musaro A., Rosenthal N. Mol. Cell. Biol. 27:6163-6176(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1144 (ISOFORM 2), PHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Strain: C57BL/6J.
[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 633-1388 AND 677-1388. Strain: C57BL/6J. Tissue: Brain and Urinary bladder.
[4]	"Targeted disruption of the mouse rho-associated kinase 2 gene results in intrauterine growth retardation and fetal death." Thumkeo D., Keel J., Ishizaki T., Hirose M., Nonomura K., Oshima H., Oshima M., Taketo M.M., Narumiya S. Mol. Cell. Biol. 23:5043-5055(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[5]	"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: DISRUPTION PHENOTYPE.
[6]	"Direct cleavage of ROCK II by granzyme B induces target cell membrane blebbing in a caspase-independent manner." Sebbagh M., Hamelin J., Bertoglio J., Solary E., Breard J. J. Exp. Med. 201:465-471(2005) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE BY GRANZYME B.
[7]	"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.
[8]	"A critical role of Rho-kinase ROCK2 in the regulation of spine and synaptic function." Zhou Z., Meng Y., Asrar S., Todorovski Z., Jia Z. Neuropharmacology 56:81-89(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[9]	"Phosphorylation of IRF4 by ROCK2 regulates IL-17 and IL-21 production and the development of autoimmunity in mice." Biswas P.S., Gupta S., Chang E., Song L., Stirzaker R.A., Liao J.K., Bhagat G., Pernis A.B. J. Clin. Invest. 120:3280-3295(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U58513 mRNA. Translation: AAC53133.1. DQ864977 mRNA. Translation: ABI75318.1. AK045517 mRNA. Translation: BAC32403.1. AK035509 mRNA. Translation: BAC29084.1.
IPI	IPI00853802. IPI01027776.
PIR	S74245.
RefSeq	NP_033098.2. NM_009072.2.
UniGene	Mm.276024.
3D structure databases
ProteinModelPortal	P70336.
SMR	P70336. Positions 27-417, 559-709, 979-1045, 1151-1351.
ModBase	Search...
Protein-protein interaction databases
IntAct	P70336. 3 interactions.
MINT	MINT-4132887.
PTM databases
PhosphoSite	P70336.
Proteomic databases
PaxDb	P70336.
PRIDE	P70336.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	19878.
KEGG	mmu:19878.
Organism-specific databases
CTD	9475.
MGI	MGI:107926. Rock2.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000017259.
HOVERGEN	HBG053111.
InParanoid	P70336.
KO	K04514.
OrthoDB	EOG4PZJ5T.
Gene expression databases
Genevestigator	P70336.
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
NextBio	297370.
SOURCE	Search...

Entry information

Entry name

ROCK2_MOUSE

Accession

Primary (citable) accession number: P70336
Secondary accession number(s): A5XDA7, Q8BR64, Q8CBR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	February 1, 1997
Last modified:	May 29, 2013
This is version 127 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program