Tag | Content |
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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 |
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820 | LKEENEEKTKLCKEL | acetylation | [1] | 1001 | RKLHMELKSEREKLT | acetylation | [1] |
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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 | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |