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O75116

- ROCK2_HUMAN

UniProt

O75116 - ROCK2_HUMAN

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Protein
Rho-associated protein kinase 2
Gene
ROCK2, KIAA0619
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.8 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium By similarity.

Enzyme regulationi

Activated by RHOA binding. Inhibited by Y-27632 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei121 – 1211ATP By similarity
Active sitei214 – 2141Proton acceptor By similarity
Sitei1131 – 11322Cleavage; by granzyme B

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi98 – 1069ATP By similarity
Zinc fingeri1260 – 131556Phorbol-ester/DAG-type
Add
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: UniProtKB
  5. protein serine/threonine kinase activity Source: UniProtKB
  6. structural molecule activity Source: ProtInc

GO - Biological processi

  1. actin cytoskeleton organization Source: Ensembl
  2. axon guidance Source: Reactome
  3. centrosome duplication Source: UniProtKB
  4. cytokinesis Source: ProtInc
  5. extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
  6. intracellular signal transduction Source: InterPro
  7. negative regulation of angiogenesis Source: UniProtKB
  8. neural tube closure Source: Ensembl
  9. positive regulation of centrosome duplication Source: Ensembl
  10. protein phosphorylation Source: UniProtKB
  11. regulation of actin cytoskeleton organization Source: UniProtKB
  12. regulation of cell adhesion Source: UniProtKB
  13. regulation of cell motility Source: UniProtKB
  14. regulation of circadian rhythm Source: UniProtKB
  15. regulation of establishment of cell polarity Source: UniProtKB
  16. regulation of focal adhesion assembly Source: UniProtKB
  17. regulation of keratinocyte differentiation Source: UniProtKB
  18. regulation of stress fiber assembly Source: UniProtKB
  19. smooth muscle contraction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Biological rhythms

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_18407. G alpha (12/13) signalling events.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.
SignaLinkiO75116.

Names & Taxonomyi

Protein namesi
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 namesi
Name:ROCK2
Synonyms:KIAA0619
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:10252. ROCK2.

Subcellular locationi

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.2 Publications

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytosol Source: Reactome
  3. nucleus Source: UniProtKB-SubCell
  4. plasma membrane Source: UniProtKB-SubCell
  5. spindle pole centrosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1131 – 11311D → A: Abolishes cleavage by granzyme B. 1 Publication

Organism-specific databases

PharmGKBiPA34624.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13881388Rho-associated protein kinase 2
PRO_0000086625Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei414 – 4141Phosphothreonine; by ROCK2 By similarity
Modified residuei722 – 7221Phosphotyrosine; by SRC2 Publications
Modified residuei1137 – 11371Phosphoserine5 Publications

Post-translational modificationi

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.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO75116.
PaxDbiO75116.
PRIDEiO75116.

PTM databases

PhosphoSiteiO75116.

Expressioni

Gene expression databases

ArrayExpressiO75116.
BgeeiO75116.
CleanExiHS_ROCK2.
GenevestigatoriO75116.

Organism-specific databases

HPAiCAB008666.
HPA007459.
HPA044109.

Interactioni

Subunit structurei

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.7 Publications

Protein-protein interaction databases

BioGridi114860. 15 interactions.
IntActiO75116. 8 interactions.
MINTiMINT-4299744.
STRINGi9606.ENSP00000317985.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 357
Helixi43 – 5715
Helixi60 – 634
Helixi66 – 8520
Helixi89 – 913
Beta strandi92 – 1009
Beta strandi102 – 11110
Turni112 – 1143
Beta strandi117 – 1248
Helixi125 – 1306
Helixi138 – 1469
Beta strandi155 – 1606
Beta strandi162 – 1698
Helixi177 – 1837
Helixi188 – 20720
Helixi217 – 2193
Beta strandi220 – 2223
Beta strandi228 – 2303
Beta strandi241 – 2466
Helixi254 – 2563
Helixi259 – 2646
Beta strandi270 – 2723
Helixi274 – 28916
Helixi299 – 3079
Helixi309 – 3124
Helixi323 – 33210
Helixi336 – 3383
Turni340 – 3434
Helixi346 – 3494
Helixi352 – 3543
Turni361 – 3633
Helixi364 – 3663
Helixi408 – 4103

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4L6QX-ray2.79A/B19-417[»]
ProteinModelPortaliO75116.
SMRiO75116. Positions 27-417, 559-709, 979-1045, 1151-1351.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini92 – 354263Protein kinase
Add
BLAST
Domaini357 – 42569AGC-kinase C-terminal
Add
BLAST
Repeati475 – 55985REM
Add
BLAST
Domaini1150 – 1349200PH
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni363 – 784422Interaction with PPP1R12A
Add
BLAST
Regioni373 – 42048Interaction with NPM1
Add
BLAST
Regioni979 – 104769RHOA binding By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili429 – 1024596 Reviewed prediction
Add
BLAST
Coiled coili1053 – 113179 Reviewed prediction
Add
BLAST

Domaini

An interaction between Thr-414 and Asp-48 is essential for kinase activity and dimerization By similarity.

Sequence similaritiesi

Contains 1 PH domain.
Contains 1 REM (Hr1) repeat.

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000017259.
HOVERGENiHBG053111.
KOiK17388.
OMAiNQSIRRP.
OrthoDBiEOG7DZ8J4.
PhylomeDBiO75116.
TreeFamiTF313551.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR000961. AGC-kinase_C.
IPR011072. HR1_rho-bd.
IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
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]
PfamiPF02185. HR1. 1 hit.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF08912. Rho_Binding. 1 hit.
[Graphical view]
PIRSFiPIRSF037568. Rho_kinase. 1 hit.
SMARTiSM00109. C1. 1 hit.
SM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. 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]

Sequencei

Sequence statusi: Complete.

O75116-1 [UniParc]FASTAAdd to Basket

« Hide

MSRPPPTGKM PGAPETAPGD GAGASRQRKL EALIRDPRSP INVESLLDGL     50
NSLVLDLDFP ALRKNKNIDN FLNRYEKIVK KIRGLQMKAE DYDVVKVIGR 100
GAFGEVQLVR HKASQKVYAM KLLSKFEMIK RSDSAFFWEE RDIMAFANSP 150
WVVQLFYAFQ DDRYLYMVME YMPGGDLVNL MSNYDVPEKW AKFYTAEVVL 200
ALDAIHSMGL IHRDVKPDNM LLDKHGHLKL ADFGTCMKMD ETGMVHCDTA 250
VGTPDYISPE VLKSQGGDGF YGRECDWWSV GVFLYEMLVG DTPFYADSLV 300
GTYSKIMDHK NSLCFPEDAE ISKHAKNLIC AFLTDREVRL GRNGVEEIRQ 350
HPFFKNDQWH WDNIRETAAP VVPELSSDID SSNFDDIEDD KGDVETFPIP 400
KAFVGNQLPF IGFTYYRENL LLSDSPSCRE TDSIQSRKNE ESQEIQKKLY 450
TLEEHLSNEM QAKEELEQKC KSVNTRLEKT AKELEEEITL RKSVESALRQ 500
LEREKALLQH KNAEYQRKAD HEADKKRNLE NDVNSLKDQL EDLKKRNQNS 550
QISTEKVNQL QRQLDETNAL LRTESDTAAR LRKTQAESSK QIQQLESNNR 600
DLQDKNCLLE TAKLKLEKEF INLQSALESE RRDRTHGSEI INDLQGRICG 650
LEEDLKNGKI LLAKVELEKR QLQERFTDLE KEKSNMEIDM TYQLKVIQQS 700
LEQEEAEHKA TKARLADKNK IYESIEEAKS EAMKEMEKKL LEERTLKQKV 750
ENLLLEAEKR CSLLDCDLKQ SQQKINELLK QKDVLNEDVR NLTLKIEQET 800
QKRCLTQNDL KMQTQQVNTL KMSEKQLKQE NNHLMEMKMN LEKQNAELRK 850
ERQDADGQMK ELQDQLEAEQ YFSTLYKTQV RELKEECEEK TKLGKELQQK 900
KQELQDERDS LAAQLEITLT KADSEQLARS IAEEQYSDLE KEKIMKELEI 950
KEMMARHKQE LTEKDATIAS LEETNRTLTS DVANLANEKE ELNNKLKDVQ 1000
EQLSRLKDEE ISAAAIKAQF EKQLLTERTL KTQAVNKLAE IMNRKEPVKR 1050
GNDTDVRRKE KENRKLHMEL KSEREKLTQQ MIKYQKELNE MQAQIAEESQ 1100
IRIELQMTLD SKDSDIEQLR SQLQALHIGL DSSSIGSGPG DAEADDGFPE 1150
SRLEGWLSLP VRNNTKKFGW VKKYVIVSSK KILFYDSEQD KEQSNPYMVL 1200
DIDKLFHVRP VTQTDVYRAD AKEIPRIFQI LYANEGESKK EQEFPVEPVG 1250
EKSNYICHKG HEFIPTLYHF PTNCEACMKP LWHMFKPPPA LECRRCHIKC 1300
HKDHMDKKEE IIAPCKVYYD ISTAKNLLLL ANSTEEQQKW VSRLVKKIPK 1350
KPPAPDPFAR SSPRTSMKIQ QNQSIRRPSR QLAPNKPS 1388
Length:1,388
Mass (Da):160,900
Last modified:November 24, 2009 - v4
Checksum:i876240F410C2487E
GO

Sequence cautioni

The sequence BAA31594.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAX93049.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti431 – 4311T → N.3 Publications
Corresponds to variant rs2230774 [ dbSNP | Ensembl ].
VAR_041062
Natural varianti601 – 6011D → V.1 Publication
Corresponds to variant rs35768389 [ dbSNP | Ensembl ].
VAR_041063
Natural varianti1083 – 10831K → M.
Corresponds to variant rs34945852 [ dbSNP | Ensembl ].
VAR_057110
Natural varianti1194 – 11941S → P in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_041064

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831R → K in BAA75636. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS42654.1.
RefSeqiNP_004841.2. NM_004850.3.
UniGeneiHs.681743.

Genome annotation databases

EnsembliENST00000315872; ENSP00000317985; ENSG00000134318.
GeneIDi9475.
KEGGihsa:9475.
UCSCiuc002rbd.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS42654.1.
RefSeqi NP_004841.2. NM_004850.3.
UniGenei Hs.681743.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4L6Q X-ray 2.79 A/B 19-417 [» ]
ProteinModelPortali O75116.
SMRi O75116. Positions 27-417, 559-709, 979-1045, 1151-1351.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114860. 15 interactions.
IntActi O75116. 8 interactions.
MINTi MINT-4299744.
STRINGi 9606.ENSP00000317985.

Chemistry

ChEMBLi CHEMBL2111459.
GuidetoPHARMACOLOGYi 1504.

PTM databases

PhosphoSitei O75116.

Proteomic databases

MaxQBi O75116.
PaxDbi O75116.
PRIDEi O75116.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000315872 ; ENSP00000317985 ; ENSG00000134318 .
GeneIDi 9475.
KEGGi hsa:9475.
UCSCi uc002rbd.1. human.

Organism-specific databases

CTDi 9475.
GeneCardsi GC02M011272.
H-InvDB HIX0001828.
HGNCi HGNC:10252. ROCK2.
HPAi CAB008666.
HPA007459.
HPA044109.
MIMi 604002. gene.
neXtProti NX_O75116.
PharmGKBi PA34624.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000017259.
HOVERGENi HBG053111.
KOi K17388.
OMAi NQSIRRP.
OrthoDBi EOG7DZ8J4.
PhylomeDBi O75116.
TreeFami TF313551.

Enzyme and pathway databases

Reactomei REACT_18407. G alpha (12/13) signalling events.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.
SignaLinki O75116.

Miscellaneous databases

GenomeRNAii 9475.
NextBioi 35508.
PROi O75116.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75116.
Bgeei O75116.
CleanExi HS_ROCK2.
Genevestigatori O75116.

Family and domain databases

Gene3Di 2.30.29.30. 2 hits.
InterProi IPR000961. AGC-kinase_C.
IPR011072. HR1_rho-bd.
IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
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 ]
Pfami PF02185. HR1. 1 hit.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF08912. Rho_Binding. 1 hit.
[Graphical view ]
PIRSFi PIRSF037568. Rho_kinase. 1 hit.
SMARTi SM00109. C1. 1 hit.
SM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi 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.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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.
    , 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.

Entry informationi

Entry nameiROCK2_HUMAN
AccessioniPrimary (citable) accession number: O75116
Secondary accession number(s): Q53QZ0, Q53SJ7, Q9UQN5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: November 24, 2009
Last modified: September 3, 2014
This is version 148 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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