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Reviewed, UniProtKB/Swiss-Prot Q62868 (ROCK2_RAT)

Last modified October 13, 2009. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Rho-associated protein kinase 2
    EC=2.7.11.1
Alternative name(s):
    Rho-associated, coiled-coil-containing protein kinase 2
    p164 ROCK-2
    RhoA-binding kinase 2
    p150 ROK-alpha
      Short name=ROKalpha
Gene names
Name: Rock2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1379 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Protein kinase that phosphorylates a large number of important signaling proteins, and thereby regulates the assembly of the actin cytoskeleton. Promotes formation of stress fibers and of focal adhesion complexes. Plays a role in smooth muscle contraction. Ref.1 Ref.2 Ref.3

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Activated by RHOA binding.

Subunit structure

Homodimer By similarity. Binds RHOA that has been activated by GTP binding. Binds IRS1, RHOB and RHOC.

Subcellular location

Cytoplasm. Cell membrane; Peripheral membrane protein. Note: Cytoplasmic, and associated with actin microfilaments and the plasma membrane. Ref.1

Tissue specificity

Highly expressed in brain, lung, liver, skeletal muscle, kidney and testis. Ref.2

Post-translational modification

Autophosphorylated. Phosphorylated upon DNA damage, probably by ATM or ATR By similarity.

Involvement in disease

May play a role in hypertension. ROCK-inhibitors lower the blood pressure in spontaneous hypertensive, renal hypertensive and deoxcorticosterone acetate-induced hypertensive rats, but not in normal rats.

Miscellaneous

Inhibited by Y-27632.

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13791379Rho-associated protein kinase 2
PRO_0000086627

Regions

Domain83 – 345263Protein kinase
Domain348 – 41669AGC-kinase C-terminal
Repeat466 – 55085REM
Domain1141 – 1340200PH
Nucleotide binding89 – 979ATP By similarity
Zinc finger1251 – 130656Phorbol-ester/DAG-type
Region970 – 103869RHOA binding By similarity
Coiled coil430 – 1015586 Potential
Coiled coil1043 – 112280 Potential

Sites

Active site2051Proton acceptor By similarity
Binding site1121ATP By similarity

Amino acid modifications

Modified residue4161Phosphoserine By similarity
Modified residue10691Phosphothreonine By similarity
Modified residue11241Phosphoserine By similarity
Modified residue11251Phosphoserine By similarity
Modified residue11281Phosphoserine By similarity
Modified residue13531Phosphoserine By similarity
Modified residue13651Phosphoserine By similarity

Experimental info

Mutagenesis1121K → A: Loss of kinase activity. Ref.2

Secondary structure

.............................. 1379
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q62868-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 7FDBA284838506C1

FASTA1,379159,435
        10         20         30         40         50         60 
MPGAPEAAAG DGAGAGRQRK LEALIRDPRS PINVESLLDG LNSLVLDLDF PALRKNKNID 

        70         80         90        100        110        120 
NFLNRYEKIV KKIRGLQMKA EDYDVVKVIG RGAFGEVQLV RHKASQKVYA MKLLSKFEMI 

       130        140        150        160        170        180 
KRSDSAFFWE ERDIMAFANS PWVVQLFCAF QDDRYLYMVM EYMPGGDLVN LMSNYDVPEK 

       190        200        210        220        230        240 
WAKFYTAEVV LALDAIHSMG LIHRDVKPDN MLLDKHGHLK LADFGTCMKM DETGMVHCDT 

       250        260        270        280        290        300 
AVGTPDYISP EVLKSQGGDG YYGRECDWWS VGVFLFEMLV GDTPFYADSL VGTYSKIMDH 

       310        320        330        340        350        360 
KNSLCFPEDT EISKHAKNLI CAFLTDREVR LGRNGVEEIK SASFFKNDQW NWDNIRETAA 

       370        380        390        400        410        420 
PVVPELSSDI DSSNFDDIED DKGDVETFPI PKAFVGNQLP FIGFTYFREN LLLSDSPPCR 

       430        440        450        460        470        480 
ENDAIQTRKS EESQEIQKKL YALEEHLSSE VQAKEELEQK CKSINTRLEK TAKELEEEIT 

       490        500        510        520        530        540 
FRKNVESTLR QLEREKALLQ HKNAEYQRKA DHEADKKRNL ENDVNSLKDQ LEDLKKRNQS 

       550        560        570        580        590        600 
SQISTEKVNQ LQKQLDEANA LLRTESDTAA RLRKTQAESS KQIQQLESNN RDLQDKNCLL 

       610        620        630        640        650        660 
ETAKLKLEKE FINLQSALES ERRDRTHGSE IINDLQGRIS GLEEDLKTGK TLLAKVELEK 

       670        680        690        700        710        720 
RQLQEKLTDL EKEKSNMEID MTYQLKVIQQ SLEQEEAEHK TTKARLADKN KIYESIEEAK 

       730        740        750        760        770        780 
SEAMKEMEKK LLEERSLKQK VENLLLEAEK RCSILDCDLK QSQQKLNELL KQKDVLNEDV 

       790        800        810        820        830        840 
RNLTLKIEQE TQKRCLMQND LKMQTQQVNT LKMSEKQIKQ ENNHLMEMKM NLEKQNAELR 

       850        860        870        880        890        900 
KERQDADGQM KELQDQLEAE QYFSTLYKTQ VRELKEENEE KTKLCKELQQ KKQDLQDERD 

       910        920        930        940        950        960 
SLAAQLEITL TKADSEQLAR SIAEEQYSDL EKEKIMKELE IKEMMARHKQ ELTEKDATIA 

       970        980        990       1000       1010       1020 
SLEETNRTLT SDVANLANEK EELNNKLKDT QEQLSKLKDE EISAAAIKAQ FEKQLLTERT 

      1030       1040       1050       1060       1070       1080 
LKTQAVNKLA EIMNRKEPVK RGSDTDVRRK EKENRKLHME LKSEREKLTQ QMIKYQKELN 

      1090       1100       1110       1120       1130       1140 
EMQAQIAEES QIRIELQMTL DSKDSDIEQL RSQLQALHIG MDSSSIGSGP GDAEPDDGFP 

      1150       1160       1170       1180       1190       1200 
ESRLEGWLSL PVRNNTKKFG WVKKYVIVSS KKILFYDSEQ DKEQSNPYMV LDIDKLFHVR 

      1210       1220       1230       1240       1250       1260 
PVTQTDVYRA DAKEIPRIFQ ILYANEGESK KEPEFPVEPV GEKSNYICHK GHEFIPTLYH 

      1270       1280       1290       1300       1310       1320 
FPTNCEACMK PLWHMFKPPP ALECSRCHIK CHKDHMDKKE EIIAPCKVYY DISSAKNLLL 

      1330       1340       1350       1360       1370 
LANSTEEQQK WVSRLVKKIP KKPPAPDPFA RSSPRTSMKI QQNQSIRRPS RQLAPNKPS 

« Hide

References

[1]"A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes."
Leung T., Manser E., Tan L., Lim L.
J. Biol. Chem. 270:29051-29054(1995) [PubMed: 7493923] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AUTOPHOSPHORYLATION, INTERACTION WITH RHOA, SUBCELLULAR LOCATION.
Tissue: Brain.
[2]"The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton."
Leung T., Chen X.-Q., Manser E., Lim L.
Mol. Cell. Biol. 16:5313-5327(1996) [PubMed: 8816443] [Abstract]
Cited for: FUNCTION, AUTOPHOSPHORYLATION, INTERACTION WITH RHOA; RHOB AND RHOC, MUTAGENESIS OF LYS-112, TISSUE SPECIFICITY.
[3]"Calcium sensitization of smooth muscle mediated by a Rho-associated protein kinase in hypertension."
Uehata M., Ishizaki T., Satoh H., Ono T., Kawahara T., Morishita T., Tamakawa H., Yamagami K., Inui J., Maekawa M., Narumiya S.
Nature 389:990-994(1997) [PubMed: 9353125] [Abstract]
Cited for: FUNCTION, ROLE IN HYPERTENSION, INHIBITION BY Y-27632.
[4]"Active Rho kinase (ROK-alpha) associates with insulin receptor substrate-1 and inhibits insulin signaling in vascular smooth muscle cells."
Begum N., Sandu O.A., Ito M., Lohmann S.M., Smolenski A.
J. Biol. Chem. 277:6214-6222(2002) [PubMed: 11739394] [Abstract]
Cited for: INTERACTION WITH IRS1.
+Additional computationally mapped references.

Cross-references

Sequence databases

U38481 mRNA. Translation: AAB37540.1.
IPIIPI00565862.
RefSeqNP_037154.1.
UniGeneRn.88642

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2ROVNMR-A1142-1342[»]
2ROWNMR-A1228-1311[»]
SMRQ62868. Positions 18-408, 970-1036.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ62868.

PTM databases

PhosphoSiteQ62868.

Genome annotation databases

EnsemblENSRNOT00000006403; ENSRNOP00000006403; ENSRNOG00000004496; Rattus norvegicus. [Genome view]
GeneID25537.
KEGGrno:25537.
UCSCNM_013022. rat.

Organism-specific databases

CTD25537.
RGD3590. Rock2.

Phylogenomic databases

HOVERGENQ62868.

Enzyme and pathway databases

BRENDA2.7.11.1. 248.

Gene expression databases

ArrayExpressQ62868.
GenevestigatorQ62868.
GermOnlineENSRNOG00000004496. Rattus norvegicus.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR000861. HR1-like_rho-bd.
IPR017892. Pkinase_C.
IPR001849. Pleckstrin_homology.
IPR002219. Prot_Kinase_C-like_PE/DAG_bd.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR015751. Rho-assoc_coiled-coil_kinase.
IPR015008. Rho_bd.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]
Gene3DG3DSA:1.20.5.730. Rho_bd. 1 hit.
PANTHERPTHR22988:SF3. Rho_kinase. 1 hit.
PfamPF00130. C1_1. 1 hit.
PF02185. HR1. 1 hit.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
PF08912. Rho_Binding. 1 hit.
[Graphical view]
PIRSFPIRSF037568. Rho_kinase. 1 hit.
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00109. C1. 1 hit.
SM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
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.
PS00479. ZF_DAG_PE_1. False negative.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio607045.

Entry information

Entry nameROCK2_RAT
AccessionPrimary (citable) accession number: Q62868
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: November 1, 1996
Last modified: October 13, 2009
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents