CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-038988
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
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
820LKEENEEKTKLCKELacetylation[1]
1001RKLHMELKSEREKLTacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
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
 1318 AA 
Protein Sequence
FLNRNEKIVK KIRGLQMKAE DYDVVKVIGR GAFGEVQLVR HKASQKVYAM KLLSKFEMIK 60
RSDSAFFWEE RDIMAFANSP WVVQLFCAFQ DDRYLYMVME YMPGGDLVNL MSNYDVPEKW 120
AKFYTAEVVL ALDAIHSMGL IHRDVKPDNM LLDKHGHLKL ADFGTCMKMD ETGMVHCDTA 180
VGTPDYISPE VLKSQGGDGY YGRECDWWSV GVFLFEMLVG DTPFYADSLV GTYSKIMDHK 240
NSLCFPEDTE ISKHAKNLIC AFLTDREVRL GRNGVEEIKQ HPFFKNDQWN WDNIRETAAP 300
VVPELSSDID SSNFDDIEDD KGDVETFPIP KAFVGNQLPF IGFTYFRENL LLSDSPPCRE 360
NDAIQTRKSE KGGQIQKKLY ALEEHLSSEV QAKEELEQKC KSINTRLEKT AKELEEEITF 420
RKNVESTLRQ LEREKALLQH KNAEYQRKAD HEADKKRNLE NDVNSLKDQL EDLKKRNQSS 480
QISTEKVNQL QKQLDEANAL LRTESDTAAR LRKTQAESSK QIQQLESNNR DLQDKNCLLE 540
TAKLKLEKEF INLQSALESE RRDRTHGSEI INDLQGRISG LEEDLKTGKT LLAKVELEKR 600
QLQEKLTDLE KEKSNMEIDM TYQLKVIQQS LEQEEAEHKT TKARLADKNK IYESIEEAKS 660
EAMKEMEKKL LEERSLKQKV ENLLLEAEKR CSILDCDLKQ SQQKLNELLK QKDVLNEDVR 720
NLTLKIEQET QKRCLMQNDL KMQTQQVNTL KMSEKQIKQE NNHLMEMKMN LEKQNAELRK 780
ERQDADGQMK ELQDQLEAEQ YFSTLYKTQV RELKEENEEK TKLCKELQQK KQDLQDERDS 840
LAAQLEITLT KADSEQLARS IAEEQYSDLE KEKIMKELEI KEMMARHKQE LTEKDATIAS 900
LEETNRTLTS DVANLANEKE ELNNKLKDTQ EQLSKLKDEE ISAAAIKAQF EKQLLTERTL 960
KTQAVNKLAE IMNRKEPVKR GSDTDVRRKE KENRKLHMEL KSEREKLTQQ MIKYQKELNE 1020
MQAQIAEESQ IRIELQMTLD SKDSDIEQLR SQLQALHIGM DSSSIGSGPG DAEPDDGFPE 1080
SRLEGWLSLP VRNNTKKFGW VKKYVIVSSK KILFYDSEQD KEQSNPYMVL DIDKLFHVRP 1140
VTQTDVYRAD AKEIPRIFQI LYANEGESKK EPEFPVEPVG EKSNYICHKG HEFIPTLYHF 1200
PTNCEACMKP LWHMFKPPPA LECRRCHIKC HKDHMDKKEE IIAPCKVYYD ISSAKNLLLL 1260
ANSTEEQQKW VSRLVKKIPK KPPAPDPFAR SSPRTSMKIQ QNQSIRRPSR QLAPNKPS 1318 
Gene Ontology
 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:0035556; P:intracellular signal transduction; IEA:InterPro. 
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
 PS50081; ZF_DAG_PE_2 
PRINTS