CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001111
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Rho-associated protein kinase 2 
Protein Synonyms/Alias
 Rho kinase 2; Rho-associated, coiled-coil-containing protein kinase 2; Rho-associated, coiled-coil-containing protein kinase II; ROCK-II; p164 ROCK-2 
Gene Name
 ROCK2 
Gene Synonyms/Alias
 KIAA0619 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
121SQKVYAMKLLSKFEMubiquitination[1]
216GLIHRDVKPDNMLLDubiquitination[1]
989VANLANEKEELNNKLubiquitination[1]
995EKEELNNKLKDVQEQubiquitination[1]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 92 354 Protein kinase.
 DOMAIN 357 425 AGC-kinase C-terminal.
 REPEAT 475 559 REM.
 DOMAIN 1150 1349 PH.
 NP_BIND 98 106 ATP (By similarity).
 ZN_FING 1260 1315 Phorbol-ester/DAG-type.
 REGION 363 784 Interaction with PPP1R12A.
 REGION 373 420 Interaction with NPM1.
 REGION 979 1047 RHOA binding (By similarity).
 ACT_SITE 214 214 Proton acceptor (By similarity).
 BINDING 121 121 ATP (By similarity).
 MOD_RES 414 414 Phosphothreonine; by ROCK2 (By
 MOD_RES 722 722 Phosphotyrosine; by SRC.
 MOD_RES 1137 1137 Phosphoserine.  
Keyword
 ATP-binding; Cell membrane; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1388 AA 
Protein Sequence
MSRPPPTGKM PGAPETAPGD GAGASRQRKL EALIRDPRSP INVESLLDGL NSLVLDLDFP 60
ALRKNKNIDN FLNRYEKIVK KIRGLQMKAE DYDVVKVIGR GAFGEVQLVR HKASQKVYAM 120
KLLSKFEMIK RSDSAFFWEE RDIMAFANSP WVVQLFYAFQ DDRYLYMVME YMPGGDLVNL 180
MSNYDVPEKW AKFYTAEVVL ALDAIHSMGL IHRDVKPDNM LLDKHGHLKL ADFGTCMKMD 240
ETGMVHCDTA VGTPDYISPE VLKSQGGDGF YGRECDWWSV GVFLYEMLVG DTPFYADSLV 300
GTYSKIMDHK NSLCFPEDAE ISKHAKNLIC AFLTDREVRL GRNGVEEIRQ HPFFKNDQWH 360
WDNIRETAAP VVPELSSDID SSNFDDIEDD KGDVETFPIP KAFVGNQLPF IGFTYYRENL 420
LLSDSPSCRE TDSIQSRKNE ESQEIQKKLY TLEEHLSNEM QAKEELEQKC KSVNTRLEKT 480
AKELEEEITL RKSVESALRQ LEREKALLQH KNAEYQRKAD HEADKKRNLE NDVNSLKDQL 540
EDLKKRNQNS QISTEKVNQL QRQLDETNAL LRTESDTAAR LRKTQAESSK QIQQLESNNR 600
DLQDKNCLLE TAKLKLEKEF INLQSALESE RRDRTHGSEI INDLQGRICG LEEDLKNGKI 660
LLAKVELEKR QLQERFTDLE KEKSNMEIDM TYQLKVIQQS LEQEEAEHKA TKARLADKNK 720
IYESIEEAKS EAMKEMEKKL LEERTLKQKV ENLLLEAEKR CSLLDCDLKQ SQQKINELLK 780
QKDVLNEDVR NLTLKIEQET QKRCLTQNDL KMQTQQVNTL KMSEKQLKQE NNHLMEMKMN 840
LEKQNAELRK ERQDADGQMK ELQDQLEAEQ YFSTLYKTQV RELKEECEEK TKLGKELQQK 900
KQELQDERDS LAAQLEITLT KADSEQLARS IAEEQYSDLE KEKIMKELEI KEMMARHKQE 960
LTEKDATIAS LEETNRTLTS DVANLANEKE ELNNKLKDVQ EQLSRLKDEE ISAAAIKAQF 1020
EKQLLTERTL KTQAVNKLAE IMNRKEPVKR GNDTDVRRKE KENRKLHMEL KSEREKLTQQ 1080
MIKYQKELNE MQAQIAEESQ IRIELQMTLD SKDSDIEQLR SQLQALHIGL DSSSIGSGPG 1140
DAEADDGFPE SRLEGWLSLP VRNNTKKFGW VKKYVIVSSK KILFYDSEQD KEQSNPYMVL 1200
DIDKLFHVRP VTQTDVYRAD AKEIPRIFQI LYANEGESKK EQEFPVEPVG EKSNYICHKG 1260
HEFIPTLYHF PTNCEACMKP LWHMFKPPPA LECRRCHIKC HKDHMDKKEE IIAPCKVYYD 1320
ISTAKNLLLL ANSTEEQQKW VSRLVKKIPK KPPAPDPFAR SSPRTSMKIQ QNQSIRRPSR 1380
QLAPNKPS 1388 
Gene Ontology
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0031616; C:spindle pole centrosome; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
 GO:0005198; F:structural molecule activity; NAS:ProtInc.
 GO:0030036; P:actin cytoskeleton organization; IEA:Compara.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0051298; P:centrosome duplication; IMP:UniProtKB.
 GO:0000910; P:cytokinesis; NAS:ProtInc.
 GO:0035556; P:intracellular signal transduction; IEA:InterPro.
 GO:0016525; P:negative regulation of angiogenesis; IMP:UniProtKB.
 GO:0001843; P:neural tube closure; IEA:Compara.
 GO:0010825; P:positive regulation of centrosome duplication; IEA:Compara.
 GO:2000145; P:regulation of cell motility; TAS:UniProtKB.
 GO:2000114; P:regulation of establishment of cell polarity; TAS:UniProtKB.
 GO:0051893; P:regulation of focal adhesion assembly; TAS:UniProtKB.
 GO:0045616; P:regulation of keratinocyte differentiation; IMP:UniProtKB.
 GO:0051492; P:regulation of stress fiber assembly; TAS:UniProtKB.
 GO:0006939; P:smooth muscle contraction; TAS:UniProtKB. 
Interpro
 IPR000961; AGC-kinase_C.
 IPR011072; HR1_rho-bd.
 IPR011009; Kinase-like_dom.
 IPR011993; PH_like_dom.
 IPR017892; Pkinase_C.
 IPR001849; Pleckstrin_homology.
 IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
 IPR000719; Prot_kinase_cat_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. 
Pfam
 PF02185; HR1
 PF00169; PH
 PF00069; Pkinase
 PF00433; Pkinase_C
 PF08912; Rho_Binding 
SMART
 SM00109; C1
 SM00233; PH
 SM00133; S_TK_X
 SM00220; S_TKc 
PROSITE
 PS51285; AGC_KINASE_CTER
 PS50003; PH_DOMAIN
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST
 PS00479; ZF_DAG_PE_1
 PS50081; ZF_DAG_PE_2 
PRINTS