CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012111
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Rho-associated protein kinase 1 
Protein Synonyms/Alias
 Renal carcinoma antigen NY-REN-35; Rho-associated, coiled-coil-containing protein kinase 1; Rho-associated, coiled-coil-containing protein kinase I; ROCK-I; p160 ROCK-1; p160ROCK 
Gene Name
 ROCK1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
200GFIHRDVKPDNMLLDubiquitination[1]
225GTCMKMNKEGMVRCDubiquitination[2]
647HLKHNLEKVEGERKEacetylation[3, 4, 5]
718VAMCEMEKKLKEEREacetylation[3, 5]
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]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
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 DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, PFN1 and PPP1R12A. Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing. Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress. Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Required for centrosome positioning and centrosome-dependent exit from mitosis. Plays a role in terminal erythroid differentiation. May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles. Promotes keratinocyte terminal differentiation. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. 
Sequence Annotation
 DOMAIN 76 338 Protein kinase.
 DOMAIN 341 409 AGC-kinase C-terminal.
 REPEAT 458 542 REM.
 DOMAIN 1118 1317 PH.
 NP_BIND 82 90 ATP (By similarity).
 ZN_FING 1228 1281 Phorbol-ester/DAG-type.
 REGION 368 727 Interaction with FHOD1.
 REGION 998 1010 RHOA binding.
 REGION 1115 1354 Auto-inhibitory.
 ACT_SITE 198 198 Proton acceptor (By similarity).
 BINDING 105 105 ATP (By similarity).
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 647 647 N6-acetyllysine.
 MOD_RES 1105 1105 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Apoptosis; ATP-binding; Cell membrane; Cell projection; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Golgi apparatus; Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1354 AA 
Protein Sequence
MSTGDSFETR FEKMDNLLRD PKSEVNSDCL LDGLDALVYD LDFPALRKNK NIDNFLSRYK 60
DTINKIRDLR MKAEDYEVVK VIGRGAFGEV QLVRHKSTRK VYAMKLLSKF EMIKRSDSAF 120
FWEERDIMAF ANSPWVVQLF YAFQDDRYLY MVMEYMPGGD LVNLMSNYDV PEKWARFYTA 180
EVVLALDAIH SMGFIHRDVK PDNMLLDKSG HLKLADFGTC MKMNKEGMVR CDTAVGTPDY 240
ISPEVLKSQG GDGYYGRECD WWSVGVFLYE MLVGDTPFYA DSLVGTYSKI MNHKNSLTFP 300
DDNDISKEAK NLICAFLTDR EVRLGRNGVE EIKRHLFFKN DQWAWETLRD TVAPVVPDLS 360
SDIDTSNFDD LEEDKGEEET FPIPKAFVGN QLPFVGFTYY SNRRYLSSAN PNDNRTSSNA 420
DKSLQESLQK TIYKLEEQLH NEMQLKDEME QKCRTSNIKL DKIMKELDEE GNQRRNLEST 480
VSQIEKEKML LQHRINEYQR KAEQENEKRR NVENEVSTLK DQLEDLKKVS QNSQLANEKL 540
SQLQKQLEEA NDLLRTESDT AVRLRKSHTE MSKSISQLES LNRELQERNR ILENSKSQTD 600
KDYYQLQAIL EAERRDRGHD SEMIGDLQAR ITSLQEEVKH LKHNLEKVEG ERKEAQDMLN 660
HSEKEKNNLE IDLNYKLKSL QQRLEQEVNE HKVTKARLTD KHQSIEEAKS VAMCEMEKKL 720
KEEREAREKA ENRVVQIEKQ CSMLDVDLKQ SQQKLEHLTG NKERMEDEVK NLTLQLEQES 780
NKRLLLQNEL KTQAFEADNL KGLEKQMKQE INTLLEAKRL LEFELAQLTK QYRGNEGQMR 840
ELQDQLEAEQ YFSTLYKTQV KELKEEIEEK NRENLKKIQE LQNEKETLAT QLDLAETKAE 900
SEQLARGLLE EQYFELTQES KKAASRNRQE ITDKDHTVSR LEEANSMLTK DIEILRRENE 960
ELTEKMKKAE EEYKLEKEEE ISNLKAAFEK NINTERTLKT QAVNKLAEIM NRKDFKIDRK 1020
KANTQDLRKK EKENRKLQLE LNQEREKFNQ MVVKHQKELN DMQAQLVEEC AHRNELQMQL 1080
ASKESDIEQL RAKLLDLSDS TSVASFPSAD ETDGNLPESR IEGWLSVPNR GNIKRYGWKK 1140
QYVVVSSKKI LFYNDEQDKE QSNPSMVLDI DKLFHVRPVT QGDVYRAETE EIPKIFQILY 1200
ANEGECRKDV EMEPVQQAEK TNFQNHKGHE FIPTLYHFPA NCDACAKPLW HVFKPPPALE 1260
CRRCHVKCHR DHLDKKEDLI CPCKVSYDVT SARDMLLLAC SQDEQKKWVT HLVKKIPKNP 1320
PSGFVRASPR TLSTRSTANQ SFRKVVKNTS GKTS 1354 
Gene Ontology
 GO:0032059; C:bleb; IEA:UniProtKB-SubCell.
 GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
 GO:0005856; C:cytoskeleton; ISS:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0030027; C:lamellipodium; ISS:UniProtKB.
 GO:0005886; C:plasma membrane; ISS:UniProtKB.
 GO:0001726; C:ruffle; ISS:UniProtKB.
 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:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
 GO:0003383; P:apical constriction; IEA:Compara.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0032060; P:bleb assembly; IEA:Compara.
 GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome.
 GO:0050901; P:leukocyte tethering or rolling; IDA:BHF-UCL.
 GO:0022614; P:membrane to membrane docking; IDA:BHF-UCL.
 GO:0016525; P:negative regulation of angiogenesis; IMP:UniProtKB.
 GO:0043524; P:negative regulation of neuron apoptotic process; 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:0007266; P:Rho protein signal transduction; TAS:ProtInc.
 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