Rho-associated protein kinase 2 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot O75116 (ROCK2_HUMAN)

Last modified November 25, 2008. Version 85. History...

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

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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
    Rho kinase 2

Gene names

Name:	ROCK2
Synonyms:	KIAA0619

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	1388 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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 By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated by RHOA binding.
Subunit structure	Homodimer. Binds RHOA that has been activated by GTP binding. Binds IRS1, RHOB and RHOC By similarity.
Subcellular location	CytoplasmBy similarity. Cell membrane; Peripheral membrane proteinBy similarity. Note= Cytoplasmic, and associated with actin microfilaments and the plasma membrane By similarity.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR.
Miscellaneous	Inhibited by Y-27632 By similarity.
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.

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Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Polymorphism
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
Gene Ontology (GO)
Biological process	cytokinesis Ref.1 Non-traceable author statement. Source: ProtInc intracellular signaling cascade Inferred from electronic annotation. Source: InterPro protein amino acid phosphorylation Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro diacylglycerol binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Ref.1 Traceable author statement. Source: ProtInc structural molecule activity Ref.1 Non-traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
IKBKE	Q14164	1	EBI-366288,EBI-307369
STK16	O75716	1	EBI-366288,EBI-1046308

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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

AGC-kinase C-terminal

Repeat

475 – 559

REM

Domain

1150 – 1349

200

Nucleotide binding

98 – 106

ATP By similarity

Zinc finger

1260 – 1315

Phorbol-ester/DAG-type

Region

979 – 1047

RHOA binding By similarity

Coiled coil

429 – 1024

596

Potential

Coiled coil

1053 – 1131

Potential

Sites

Active site

214

Proton acceptor By similarity

Binding site

121

ATP By similarity

Amino acid modifications

Modified residue

1078

Phosphothreonine

Modified residue

1134

Phosphoserine

Modified residue

1137

Phosphoserine

Modified residue

1362

Phosphoserine

Modified residue

1374

Phosphoserine

Natural variations

Natural variant

431

N → T

VAR_041062

Natural variant

601

D → V

VAR_041063

Natural variant

1194

S → P in a metastatic melanoma sample; somatic mutation.

VAR_041064

Experimental info

Sequence conflict

R → K in BAA75636. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

O75116-1 [UniParc].

Last modified May 24, 2004. Version 3.
Checksum: 7763190F0A817D59
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FASTA

1,388

160,913

        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 NDSIQSRKNE 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

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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: 9933571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 9734811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1134 AND SER-1137, MASS SPECTROMETRY. Tissue: Epithelium.
[4]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1362, MASS SPECTROMETRY. Tissue: Epithelium.
[5]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1374, MASS SPECTROMETRY. Tissue: Epithelium.
[6]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1078, MASS SPECTROMETRY.
[7]	"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. Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-431; VAL-601 AND PRO-1194.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	D87931 mRNA. Translation: BAA75636.1. AB014519 mRNA. Translation: BAA31594.2. Different initiation.
RefSeq	NP_004841.2.
UniGene	Hs.591600
3D structure databases
HSSP	HSSP built from PDB template 1GZK based on UniProtKB P31751.
SMR	O75116. Positions 27-417, 979-1045.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75116.
PTM databases
PhosphoSite	O75116.
Genome annotation databases
Ensembl	ENSG00000134318. Homo sapiens. [Contig view]
GeneID	9475.
KEGG	hsa:9475.
Organism-specific databases
H-InvDB	HIX0001828.
HGNC	HGNC:10252. ROCK2.
HPA	CAB008666. HPA007459.
MIM	604002. gene.
PharmGKB	PA34624.
HUGE	Search...
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	O75116.
HOVERGEN	O75116.
Gene expression databases
ArrayExpress	O75116.
CleanEx	HS_ROCK2.
GermOnline	ENSG00000134318. Homo sapiens.
Family and domain databases
InterPro	IPR002219. DAG_PE_bd. IPR000861. HR1-like_rho-bd. IPR001849. PH. IPR000961. Pkinase_C. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_bd_CS. IPR015008. Rho_bd. IPR015751. Rho_kinase. 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	35508.
SOURCE	Search...

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Entry information

Entry name

ROCK2_HUMAN

Accession

Primary (citable) accession number: O75116
Secondary accession number(s): Q9UQN5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	May 24, 2004
Last modified:	November 25, 2008
This is version 85 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 2

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents