O75116 (ROCK2_HUMAN) 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 kinase 2
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
Synonyms:	KIAA0619

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.11 Ref.12 Ref.18 Ref.19
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. Interacts with IRS1, RHOB and RHOC By similarity. Interacts with RHOA (activated by GTP), PPP1R12A, CHORDC1, SORL1, EP300 and BRCA2. Interacts with NPM1 and this interaction enhances its activity. Interacts with RAF1 By similarity. Ref.4 Ref.6 Ref.7 Ref.11 Ref.14 Ref.18 Ref.19
Subcellular location	Cytoplasm. Cell membrane; Peripheral membrane protein By similarity. Nucleus. Cytoplasm › cytoskeleton › centrosome. Note: Cytoplasmic, and associated with actin microfilaments and the plasma membrane By similarity. Ref.6 Ref.7
Domain	An interaction between Thr-414 and Asp-48 is essential for kinase activity and dimerization By similarity.
Post-translational modification	Phosphorylation at Tyr-722 reduces its binding to RHOA and is crucial for focal adhesion dynamics. Dephosphorylation by PTPN11 stimulates its RHOA binding activity. Cleaved by granzyme B during apoptosis. This leads to constitutive activation of the kinase and membrane blebbing.
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 AAX93049.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAA31594.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane Nucleus
Coding sequence diversity	Polymorphism
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	actin cytoskeleton organization Inferred from electronic annotation. Source: Compara axon guidance Traceable author statement. Source: Reactome centrosome duplication Inferred from mutant phenotype Ref.7. Source: UniProtKB cytokinesis Non-traceable author statement Ref.1. Source: ProtInc intracellular signal transduction Inferred from electronic annotation. Source: InterPro negative regulation of angiogenesis Inferred from mutant phenotype PubMed 19181962. Source: UniProtKB neural tube closure Inferred from electronic annotation. Source: Compara positive regulation of centrosome duplication Inferred from electronic annotation. Source: Compara regulation of cell motility Traceable author statement Ref.20. Source: UniProtKB regulation of establishment of cell polarity Traceable author statement Ref.21. Source: UniProtKB regulation of focal adhesion assembly Traceable author statement Ref.20. Source: UniProtKB regulation of keratinocyte differentiation Inferred from mutant phenotype Ref.12. Source: UniProtKB regulation of stress fiber assembly Traceable author statement Ref.20. Source: UniProtKB smooth muscle contraction Traceable author statement Ref.20. Source: UniProtKB
Cellular_component	centrosome Inferred from direct assay Ref.7. Source: UniProtKB cytosol Traceable author statement. Source: Reactome nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell spindle pole centrosome Inferred from electronic annotation. Source: Compara
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 direct assay Ref.6Ref.19. Source: UniProtKB structural molecule activity Non-traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

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_0000086625
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
	Region	373 – 420	48	Interaction with NPM1
	Region	979 – 1047	69	RHOA binding By similarity
	Coiled coil	429 – 1024	596	Potential
	Coiled coil	1053 – 1131	79	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 Ref.8 Ref.15
	Modified residue	1137	1	Phosphoserine Ref.9 Ref.10 Ref.13 Ref.16 Ref.22
Natural variations
	Natural variant	431	1	T → N. Ref.1 Ref.2 Ref.23 Corresponds to variant rs2230774 [ dbSNP | Ensembl ].		VAR_041062
	Natural variant	601	1	D → V. Ref.23 Corresponds to variant rs35768389 [ dbSNP | Ensembl ].		VAR_041063
	Natural variant	1083	1	K → M. Corresponds to variant rs34945852 [ dbSNP | Ensembl ].		VAR_057110
	Natural variant	1194	1	S → P in a metastatic melanoma sample; somatic mutation. Ref.23		VAR_041064
Experimental info
	Mutagenesis	1131	1	D → A: Abolishes cleavage by granzyme B. Ref.5
	Sequence conflict	83	1	R → K in BAA75636. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O75116 [UniParc]. Last modified November 24, 2009. Version 4. Checksum: 876240F410C2487E	FASTA	1,388	160,900
	10 20 30 40 50 60 MSRPPPTGKM PGAPETAPGD GAGASRQRKL EALIRDPRSP INVESLLDGL NSLVLDLDFP 70 80 90 100 110 120 ALRKNKNIDN FLNRYEKIVK KIRGLQMKAE DYDVVKVIGR GAFGEVQLVR HKASQKVYAM 130 140 150 160 170 180 KLLSKFEMIK RSDSAFFWEE RDIMAFANSP WVVQLFYAFQ DDRYLYMVME YMPGGDLVNL 190 200 210 220 230 240 MSNYDVPEKW AKFYTAEVVL ALDAIHSMGL IHRDVKPDNM LLDKHGHLKL ADFGTCMKMD 250 260 270 280 290 300 ETGMVHCDTA VGTPDYISPE VLKSQGGDGF YGRECDWWSV GVFLYEMLVG DTPFYADSLV 310 320 330 340 350 360 GTYSKIMDHK NSLCFPEDAE ISKHAKNLIC AFLTDREVRL GRNGVEEIRQ HPFFKNDQWH 370 380 390 400 410 420 WDNIRETAAP VVPELSSDID SSNFDDIEDD KGDVETFPIP KAFVGNQLPF IGFTYYRENL 430 440 450 460 470 480 LLSDSPSCRE TDSIQSRKNE ESQEIQKKLY TLEEHLSNEM QAKEELEQKC KSVNTRLEKT 490 500 510 520 530 540 AKELEEEITL RKSVESALRQ LEREKALLQH KNAEYQRKAD HEADKKRNLE NDVNSLKDQL 550 560 570 580 590 600 EDLKKRNQNS QISTEKVNQL QRQLDETNAL LRTESDTAAR LRKTQAESSK QIQQLESNNR 610 620 630 640 650 660 DLQDKNCLLE TAKLKLEKEF INLQSALESE RRDRTHGSEI INDLQGRICG LEEDLKNGKI 670 680 690 700 710 720 LLAKVELEKR QLQERFTDLE KEKSNMEIDM TYQLKVIQQS LEQEEAEHKA TKARLADKNK 730 740 750 760 770 780 IYESIEEAKS EAMKEMEKKL LEERTLKQKV ENLLLEAEKR CSLLDCDLKQ SQQKINELLK 790 800 810 820 830 840 QKDVLNEDVR NLTLKIEQET QKRCLTQNDL KMQTQQVNTL KMSEKQLKQE NNHLMEMKMN 850 860 870 880 890 900 LEKQNAELRK ERQDADGQMK ELQDQLEAEQ YFSTLYKTQV RELKEECEEK TKLGKELQQK 910 920 930 940 950 960 KQELQDERDS LAAQLEITLT KADSEQLARS IAEEQYSDLE KEKIMKELEI KEMMARHKQE 970 980 990 1000 1010 1020 LTEKDATIAS LEETNRTLTS DVANLANEKE ELNNKLKDVQ EQLSRLKDEE ISAAAIKAQF 1030 1040 1050 1060 1070 1080 EKQLLTERTL KTQAVNKLAE IMNRKEPVKR GNDTDVRRKE KENRKLHMEL KSEREKLTQQ 1090 1100 1110 1120 1130 1140 MIKYQKELNE MQAQIAEESQ IRIELQMTLD SKDSDIEQLR SQLQALHIGL DSSSIGSGPG 1150 1160 1170 1180 1190 1200 DAEADDGFPE SRLEGWLSLP VRNNTKKFGW VKKYVIVSSK KILFYDSEQD KEQSNPYMVL 1210 1220 1230 1240 1250 1260 DIDKLFHVRP VTQTDVYRAD AKEIPRIFQI LYANEGESKK EQEFPVEPVG EKSNYICHKG 1270 1280 1290 1300 1310 1320 HEFIPTLYHF PTNCEACMKP LWHMFKPPPA LECRRCHIKC HKDHMDKKEE IIAPCKVYYD 1330 1340 1350 1360 1370 1380 ISTAKNLLLL ANSTEEQQKW VSRLVKKIPK KPPAPDPFAR SSPRTSMKIQ QNQSIRRPSR QLAPNKPS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Localization of the gene coding for ROCK II/Rho kinase on human chromosome 2p24." Takahashi N., Tuiki H., Saya H., Kaibuchi K. Genomics 55:235-237(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASN-431. Tissue: Brain.
[2]	"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-431. Tissue: Brain.
[3]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Phosphorylation of myosin-binding subunit (MBS) of myosin phosphatase by Rho-kinase in vivo." Kawano Y., Fukata Y., Oshiro N., Amano M., Nakamura T., Ito M., Matsumura F., Inagaki M., Kaibuchi K. J. Cell Biol. 147:1023-1038(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PPP1R12A.
[5]	"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, MUTAGENESIS OF ASP-1131, FUNCTION.
[6]	"Nuclear Rho kinase, ROCK2, targets p300 acetyltransferase." Tanaka T., Nishimura D., Wu R.C., Amano M., Iso T., Kedes L., Nishida H., Kaibuchi K., Hamamori Y. J. Biol. Chem. 281:15320-15329(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EP300.
[7]	"Interaction between ROCK II and nucleophosmin/B23 in the regulation of centrosome duplication." Ma Z., Kanai M., Kawamura K., Kaibuchi K., Ye K., Fukasawa K. Mol. Cell. Biol. 26:9016-9034(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NPM1.
[8]	"Regulation of RhoA-dependent ROCKII activation by Shp2." Lee H.H., Chang Z.F. J. Cell Biol. 181:999-1012(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-722, DEPHOSPHORYLATION.
[9]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1137, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1137, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"ROCK isoform regulation of myosin phosphatase and contractility in vascular smooth muscle cells." Wang Y., Zheng X.R., Riddick N., Bryden M., Baur W., Zhang X., Surks H.K. Circ. Res. 104:531-540(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PPP1R12A.
[12]	"Distinct roles for ROCK1 and ROCK2 in the regulation of keratinocyte differentiation." Lock F.E., Hotchin N.A. PLoS ONE 4:E8190-E8190(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1137, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"Morgana/chp-1, a ROCK inhibitor involved in centrosome duplication and tumorigenesis." Ferretti R., Palumbo V., Di Savino A., Velasco S., Sbroggio M., Sportoletti P., Micale L., Turco E., Silengo L., Palumbo G., Hirsch E., Teruya-Feldstein J., Bonaccorsi S., Pandolfi P.P., Gatti M., Tarone G., Brancaccio M. Dev. Cell 18:486-495(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CHORDC1.
[15]	"Src-dependent phosphorylation of ROCK participates in regulation of focal adhesion dynamics." Lee H.H., Tien S.C., Jou T.S., Chang Y.C., Jhong J.G., Chang Z.F. J. Cell Sci. 123:3368-3377(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-722.
[16]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1137, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"BRCA2 and nucleophosmin coregulate centrosome amplification and form a complex with the Rho effector kinase ROCK2." Wang H.F., Takenaka K., Nakanishi A., Miki Y. Cancer Res. 71:68-77(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH BRCA2.
[19]	"Rho kinase II phosphorylation of the lipoprotein receptor LR11/SORLA alters amyloid-beta production." Herskowitz J.H., Seyfried N.T., Gearing M., Kahn R.A., Peng J., Levey A.I., Lah J.J. J. Biol. Chem. 286:6117-6127(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SORL1.
[20]	"Rocks: multifunctional kinases in cell behaviour." Riento K., Ridley A.J. Nat. Rev. Mol. Cell Biol. 4:446-456(2003) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[21]	"Rho-kinase/ROCK: A key regulator of the cytoskeleton and cell polarity." Amano M., Nakayama M., Kaibuchi K. Cytoskeleton 67:545-554(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[22]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1137, MASS SPECTROMETRY.
[23]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASN-431; VAL-601 AND PRO-1194.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D87931 mRNA. Translation: BAA75636.1. AB014519 mRNA. Translation: BAA31594.2. Different initiation. AC018463 Genomic DNA. Translation: AAX93049.1. Sequence problems. AC099344 Genomic DNA. Translation: AAY14825.1.
IPI	IPI00307155.
RefSeq	NP_004841.2. NM_004850.3.
UniGene	Hs.681743.
3D structure databases
ProteinModelPortal	O75116.
SMR	O75116. Positions 27-417, 559-709, 979-1045, 1151-1351.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75116. 4 interactions.
MINT	MINT-4299744.
STRING	9606.ENSP00000317985.
PTM databases
PhosphoSite	O75116.
Proteomic databases
PaxDb	O75116.
PRIDE	O75116.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000315872; ENSP00000317985; ENSG00000134318.
GeneID	9475.
KEGG	hsa:9475.
UCSC	uc002rbd.1. human.
Organism-specific databases
CTD	9475.
GeneCards	GC02M011272.
H-InvDB	HIX0001828.
HGNC	HGNC:10252. ROCK2.
HPA	CAB008666. HPA007459.
MIM	604002. gene.
neXtProt	NX_O75116.
PharmGKB	PA34624.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000017259.
HOVERGEN	HBG053111.
KO	K04514.
OMA	PRTSMKV.
OrthoDB	EOG4PZJ5T.
Enzyme and pathway databases
Pathway_Interaction_DB	avb3_opn_pathway. Osteopontin-mediated events. er_nongenomic_pathway. Plasma membrane estrogen receptor signaling.
Reactome	REACT_111045. Developmental Biology. REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	O75116.
Bgee	O75116.
CleanEx	HS_ROCK2.
Genevestigator	O75116.
GermOnline	ENSG00000134318. Homo sapiens.
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
ChEMBL	CHEMBL2973.
GenomeRNAi	9475.
NextBio	35508.
SOURCE	Search...

Entry information

Entry name

ROCK2_HUMAN

Accession

Primary (citable) accession number: O75116
Secondary accession number(s): Q53QZ0, Q53SJ7, Q9UQN5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	November 24, 2009
Last modified:	May 1, 2013
This is version 134 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.