CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-037417
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Rho-associated protein kinase 2 
Protein Synonyms/Alias
  
Gene Name
 ROCK2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
347KTQAESSKQIQQLESubiquitination[1]
703LEKEKIMKELEIKEMacetylation[2]
746VANLANEKEELNNKLubiquitination[3]
752EKEELNNKLKDVQEQubiquitination[3]
Reference
 [1] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [2] 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]
 [3] 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
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Kinase; Metal-binding; Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1145 AA 
Protein Sequence
MVHCDTAVGT PDYISPEVLK SQGGDGFYGR ECDWWSVGVF LYEMLVGDTP FYADSLVGTY 60
SKIMDHKNSL CFPEDAEISK HAKNLICAFL TDREVRLGRN GVEEIRQHPF FKNDQWHWDN 120
IRETAAPVVP ELSSDIDSSN FDDIEDDKGD VETFPIPKAF VGNQLPFIGF TYYRENLLLS 180
DSPSCRETDS IQSRKNEESQ EIQKKLYTLE EHLSNEMQAK EELEQKCKSV NTRLEKTAKE 240
LEEEITLRKS VESALRQLER EKALLQHKNA EYQRKADHEA DKKRNLENDV NSLKDQLEDL 300
KKRNQNSQIS TEKVNQLQRQ LDETNALLRT ESDTAARLRK TQAESSKQIQ QLESNNRDLQ 360
DKNCLLETAK LKLEKEFINL QSALESERRD RTHGSEIIND LQGRICGLEE DLKNGKILLA 420
KVELEKRQLQ ERFTDLEKEK SNMEIDMTYQ LKVIQQSLEQ EEAEHKATKA RLADKNKIYE 480
SIEEAKSEAM KEMEKKLLEE RTLKQKVENL LLEAEKRCSL LDCDLKQSQQ KINELLKQKD 540
VLNEDVRNLT LKIEQETQKR CLTQNDLKMQ TQQVNTLKMS EKQLKQENNH LMEMKMNLEK 600
QNAELRKERQ DADGQMKELQ DQLEAEQYFS TLYKTQVREL KEECEEKTKL GKELQQKKQE 660
LQDERDSLAA QLEITLTKAD SEQLARSIAE EQYSDLEKEK IMKELEIKEM MARHKQELTE 720
KDATIASLEE TNRTLTSDVA NLANEKEELN NKLKDVQEQL SRLKDEEISA AAIKAQFEKQ 780
LLTERTLKTQ AVNKLAEIMN RKEPVKRGND TDVRRKEKEN RKLHMELKSE REKLTQQMIK 840
YQKELNEMQA QIAEESQIRI ELQMTLDSKD SDIEQLRSQL QALHIGLDSS SIGSGPGDAE 900
ADDGFPESRL EGWLSLPVRN NTKKFGWVKK YVIVSSKKIL FYDSEQDKEQ SNPYMVLDID 960
KLFHVRPVTQ TDVYRADAKE IPRIFQILYA NEGESKKEQE FPVEPVGEKS NYICHKGHEF 1020
IPTLYHFPTN CEACMKPLWH MFKPPPALEC RRCHIKCHKD HMDKKEEIIA PCKVYYDIST 1080
AKNLLLLANS TEEQQKWVSR LVKKIPKKPP APDPFARSSP RTSMKIQQNQ SIRRPSRQLA 1140
PNKPS 1145 
Gene Ontology
 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; IEA:UniProtKB-KW.
 GO:0030036; P:actin cytoskeleton organization; IEA:Compara.
 GO:0035556; P:intracellular signal transduction; IEA:InterPro.
 GO:0001843; P:neural tube closure; IEA:Compara.
 GO:0010825; P:positive regulation of centrosome duplication; IEA:Compara. 
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.
 IPR020684; Rho-assoc_coiled-coil_kin.
 IPR015008; Rho-bd_dom. 
Pfam
 PF02185; HR1
 PF00169; PH
 PF00069; Pkinase
 PF00433; Pkinase_C
 PF08912; Rho_Binding 
SMART
 SM00109; C1
 SM00233; PH
 SM00133; S_TK_X 
PROSITE
 PS51285; AGC_KINASE_CTER
 PS50003; PH_DOMAIN
 PS50011; PROTEIN_KINASE_DOM
 PS50081; ZF_DAG_PE_2 
PRINTS