Rho-associated protein kinase 2 - Rattus norvegicus (Rat)

Contribute

Send feedback

Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot Q62868 (ROCK2_RAT)

Last modified October 13, 2009. Version 89. 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

Hide | Top

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
    p164 ROCK-2
    RhoA-binding kinase 2
    p150 ROK-alpha
      Short name=ROKalpha

Gene names

Name:

Rock2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Hide | Top

Protein attributes

Sequence length	1379 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

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.

Hide | Top

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Domain	Coiled coil Phorbol-ester binding Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	chromosome condensation Traceable author statement. Source: RGD cytokinesis Inferred from electronic annotation. Source: InterPro intracellular signaling cascade Inferred from electronic annotation. Source: InterPro protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW diacylglycerol binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1379

1379

Rho-associated protein kinase 2

PRO_0000086627

Regions

Domain

83 – 345

263

Protein kinase

Domain

348 – 416

AGC-kinase C-terminal

Repeat

466 – 550

REM

Domain

1141 – 1340

200

Nucleotide binding

89 – 97

ATP By similarity

Zinc finger

1251 – 1306

Phorbol-ester/DAG-type

Region

970 – 1038

RHOA binding By similarity

Coiled coil

430 – 1015

586

Potential

Coiled coil

1043 – 1122

Potential

Sites

Active site

205

Proton acceptor By similarity

Binding site

112

ATP By similarity

Amino acid modifications

Modified residue

416

Phosphoserine By similarity

Modified residue

1069

Phosphothreonine By similarity

Modified residue

1124

Phosphoserine By similarity

Modified residue

1125

Phosphoserine By similarity

Modified residue

1128

Phosphoserine By similarity

Modified residue

1353

Phosphoserine By similarity

Modified residue

1365

Phosphoserine By similarity

Experimental info

Mutagenesis

112

K → A: Loss of kinase activity. Ref.2

Secondary structure

1379

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q62868-1 [UniParc].

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

FASTA

1,379

159,435

        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

Hide | Top

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.

Hide | Top

Cross-references

Sequence databases

U38481 mRNA. Translation: AAB37540.1.

IPI

IPI00565862.

RefSeq

NP_037154.1.

UniGene

Rn.88642

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ROV	NMR	-	A	1142-1342	[»]
2ROW	NMR	-	A	1228-1311	[»]

SMR

Q62868. Positions 18-408, 970-1036.

ModBase

Search...

Protein-protein interaction databases

STRING

Q62868.

PTM databases

PhosphoSite

Q62868.

Genome annotation databases

Ensembl

ENSRNOT00000006403; ENSRNOP00000006403; ENSRNOG00000004496; Rattus norvegicus. [Genome view]

GeneID

25537.

KEGG

rno:25537.

UCSC

NM_013022. rat.

Organism-specific databases

CTD

25537.

RGD

3590. Rock2.

Phylogenomic databases

HOVERGEN

Q62868.

Enzyme and pathway databases

BRENDA

2.7.11.1. 248.

Gene expression databases

ArrayExpress

Q62868.

Genevestigator

Q62868.

GermOnline

ENSRNOG00000004496. Rattus norvegicus.

Family and domain databases

InterPro

IPR000961. 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]

Gene3D

G3DSA:1.20.5.730. Rho_bd. 1 hit.

PANTHER

PTHR22988:SF3. Rho_kinase. 1 hit.

Pfam

PF00130. 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]

PIRSF

PIRSF037568. Rho_kinase. 1 hit.

ProDom

PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00109. C1. 1 hit.
SM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

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 Resources

NextBio

607045.

Hide | Top

Entry information

Entry name

ROCK2_RAT

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families