Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O75116 (ROCK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1388 AA.
Sequence statusComplete.
Protein existenceEvidence 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 an important role in generating the circadian rhythm of the aortic myofilament Ca2+ sensitivity and vascular contractility by modulating the myosin light chain phosphorylation. 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. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. 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
   Biological processBiological rhythms
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   Coding sequence diversityPolymorphism
   DomainCoiled coil
Zinc-finger
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

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

extrinsic apoptotic signaling pathway via death domain receptors

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

positive regulation of centrosome duplication

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay Ref.8. Source: UniProtKB

regulation of actin cytoskeleton organization

Traceable author statement Ref.20. Source: UniProtKB

regulation of cell adhesion

Traceable author statement Ref.20. Source: UniProtKB

regulation of cell motility

Traceable author statement Ref.20. Source: UniProtKB

regulation of circadian rhythm

Inferred from sequence or structural similarity. 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_componentcentrosome

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: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.7Ref.14. Source: UniProtKB

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13881388Rho-associated protein kinase 2
PRO_0000086625

Regions

Domain92 – 354263Protein kinase
Domain357 – 42569AGC-kinase C-terminal
Repeat475 – 55985REM
Domain1150 – 1349200PH
Nucleotide binding98 – 1069ATP By similarity
Zinc finger1260 – 131556Phorbol-ester/DAG-type
Region363 – 784422Interaction with PPP1R12A
Region373 – 42048Interaction with NPM1
Region979 – 104769RHOA binding By similarity
Coiled coil429 – 1024596 Potential
Coiled coil1053 – 113179 Potential

Sites

Active site2141Proton acceptor By similarity
Binding site1211ATP By similarity
Site1131 – 11322Cleavage; by granzyme B

Amino acid modifications

Modified residue4141Phosphothreonine; by ROCK2 By similarity
Modified residue7221Phosphotyrosine; by SRC Ref.8 Ref.15
Modified residue11371Phosphoserine Ref.9 Ref.10 Ref.13 Ref.16 Ref.22

Natural variations

Natural variant4311T → N. Ref.1 Ref.2 Ref.23
Corresponds to variant rs2230774 [ dbSNP | Ensembl ].
VAR_041062
Natural variant6011D → V. Ref.23
Corresponds to variant rs35768389 [ dbSNP | Ensembl ].
VAR_041063
Natural variant10831K → M.
Corresponds to variant rs34945852 [ dbSNP | Ensembl ].
VAR_057110
Natural variant11941S → P in a metastatic melanoma sample; somatic mutation. Ref.23
VAR_041064

Experimental info

Mutagenesis11311D → A: Abolishes cleavage by granzyme B. Ref.5
Sequence conflict831R → K in BAA75636. Ref.1

Secondary structure

.............................................................. 1388
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75116 [UniParc].

Last modified November 24, 2009. Version 4.
Checksum: 876240F410C2487E

FASTA1,388160,900
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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. expand/collapse author list , 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.
CCDSCCDS42654.1.
RefSeqNP_004841.2. NM_004850.3.
UniGeneHs.681743.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4L6QX-ray2.79A/B19-417[»]
ProteinModelPortalO75116.
SMRO75116. Positions 27-417, 559-709, 979-1045, 1151-1351.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114860. 15 interactions.
IntActO75116. 8 interactions.
MINTMINT-4299744.
STRING9606.ENSP00000317985.

Chemistry

ChEMBLCHEMBL2111459.
GuidetoPHARMACOLOGY1504.

PTM databases

PhosphoSiteO75116.

Proteomic databases

MaxQBO75116.
PaxDbO75116.
PRIDEO75116.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000315872; ENSP00000317985; ENSG00000134318.
GeneID9475.
KEGGhsa:9475.
UCSCuc002rbd.1. human.

Organism-specific databases

CTD9475.
GeneCardsGC02M011272.
H-InvDBHIX0001828.
HGNCHGNC:10252. ROCK2.
HPACAB008666.
HPA007459.
HPA044109.
MIM604002. gene.
neXtProtNX_O75116.
PharmGKBPA34624.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000017259.
HOVERGENHBG053111.
KOK17388.
OMANQSIRRP.
OrthoDBEOG7DZ8J4.
PhylomeDBO75116.
TreeFamTF313551.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
SignaLinkO75116.

Gene expression databases

ArrayExpressO75116.
BgeeO75116.
CleanExHS_ROCK2.
GenevestigatorO75116.

Family and domain databases

Gene3D2.30.29.30. 2 hits.
InterProIPR000961. AGC-kinase_C.
IPR011072. HR1_rho-bd.
IPR011009. Kinase-like_dom.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_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]
PfamPF02185. HR1. 1 hit.
PF00169. PH. 1 hit.
PF00069. Pkinase. 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]
SUPFAMSSF56112. SSF56112. 1 hit.
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.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi9475.
NextBio35508.
PROO75116.
SOURCESearch...

Entry information

Entry nameROCK2_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 147 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM