CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-040545
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
1022AIKAQFEKQLLNERTubiquitination[1]
1037LKTQAVNKLAEIMNRubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
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
 1388 AA 
Protein Sequence
MSRPPPTGKM PGAPETAPGD GAGAGRQRKL EALIRDPRSP INVESLLDGL NSLVLDLDFP 60
ALRKNKNIDN FLNRYEKIVK KIRGLQMKAE DYDVVKVIGR GAFGEVQLVR HKASQKVYAM 120
KLLSKFEMIK RSDSAFFWEE RDIMAFANSP WVVQLFCAFQ DDRYLYMVME YMPGGDLVNL 180
MSNYDVPEKW AKFYTAEVVL ALDAIHSMGL IHRDVKPDNM LLDKHGHLKL ADFGTCMKMD 240
ETGMVHCDTA VGTPDYISPE VLKSQGGDGY YGRECDWWSV GVFLFEMLVG DTPFYADSLV 300
GTYSKIMDHK NSLCFPEDTE ISKHAKNLIC AFLTDREVRL GRNGVEEIKQ HPFFKNDQWN 360
WDNIRETAAP VVPELSSDID SSNFDDIEDD KGDVETFPIP KAFVGNQLPF IGFTYFRENL 420
LLSDSPPCRE NDAIQTRKSE ESQEIQKKLY ALEEHLSSEV QAKEELEQKC KSINTRLEKT 480
AKELEEEITL RKSVESTLRQ LEREKALLQH KNAEYQRKAD HEADKKRNLE NDVNSLKDQL 540
EDLKKRNQSS QISTEKVNQL QKQLDEANAL LRTESDTAAR LRKTQAESSK QIQQLESNNR 600
DLQDKNCLLE TAKLKLEKEF INLQSALESE RRDRTHGSEI INDLQGRISG LEEDLKTGKA 660
LLAKVELEKR QLQEKLTDLE KEKSNMEIDM TYQLKVIQQS LEQEEAEHKT TKARLADKNK 720
IYESIEEAKS EAMKEMEKKL LEERSLKQKV ENLLLEAEKR CSILDCDLKQ SQQKLNELLK 780
QKDVLNEDVR NLTLKIEQET QKRCLMQNDL KMQTQQVNTL KMSEKQIKQE NNHLMEMKMN 840
LEKQNTELRK ERQDADGQMK ELQDQLEAEQ YFSTLYKTQV RELKEENEEK TKLCKELQQK 900
KQDLQDERDS LAAQLEITLT KADSEQLARS IAEEQYSDLE KEKIMKELEI KEMMARHKQE 960
LTEKDTTIAS LEETNRTLTS DVANLANEKE ELNNKLKDSQ EQLSKLKDEE MSAAAIKAQF 1020
EKQLLNERTL KTQAVNKLAE IMNRKEPVKR GSDTDVRRKE KENRKLHMEL KSEREKLTQQ 1080
MIKYQKELNE MQAQIAEESQ IRIELQMTLD SKDSDIEQLR SQLQALHIGM DSSSIGSGPG 1140
DAEPDDGFPE SRLEGWLSLP VRNNTKKFGW VKKYVIVSSK KILFYDSEQD KEQSNPYMVL 1200
DIDKLFHVRP VTQTDVYRAD AKEIPRIFQI LYANEGESKK EPEFPVEPVG EKSNYICHKG 1260
HEFIPTLYHF PTNCEACMKP LWHMFKPPPA LECRRCHIKC HKDHMDKKEE IIAPCKVYYD 1320
ISSAKNLLLL ANSTEEQQKW VSRLVKKIPK KPPAPDPFAR SSPRTSMKIQ QNQSIRRPSR 1380
QLAPNKPS 1388 
Gene Ontology
 GO:0031616; C:spindle pole centrosome; IDA:MGI.
 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; IGI:MGI.
 GO:0051298; P:centrosome duplication; IEA:Compara.
 GO:0016525; P:negative regulation of angiogenesis; IEA:Compara.
 GO:0001843; P:neural tube closure; IGI:MGI.
 GO:0010825; P:positive regulation of centrosome duplication; IMP:MGI.
 GO:0045616; P:regulation of keratinocyte differentiation; IEA:Compara.
 GO:0007266; P:Rho protein signal transduction; ISO:MGI. 
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