| Tag | Content |
|---|
| CPLM ID | CPLM-016013 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Protein phosphatase 1E |
Protein Synonyms/Alias | Ca(2+)/calmodulin-dependent protein kinase phosphatase N; CaMKP-N; CaMKP-nucleus; CaMKN; Partner of PIX 1; Partner of PIX-alpha; Partner of PIXA |
Gene Name | Ppm1e |
Gene Synonyms/Alias | Camkn; Kiaa1072 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 197 | TVEIETVKLARSVFS | ubiquitination | [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 | Protein phosphatase that inactivates multifunctional CaM kinases such as CAMK4 and CAMK2. Dephosphorylates and inactivates PAK. May play a role in the inhibition of actin fiber stress breakdown and in morphological changes driven by TNK2/CDC42 (By similarity). |
Sequence Annotation | REPEAT 31 32 1.
REPEAT 33 34 2.
REPEAT 35 36 3.
REPEAT 37 38 4; approximate.
REPEAT 39 40 5.
REPEAT 41 42 6.
REPEAT 43 44 7.
DOMAIN 243 485 PP2C-like.
REGION 31 44 7 X 2 AA tandem repeats of P-E.
METAL 270 270 Manganese 1 (By similarity).
METAL 270 270 Manganese 2 (By similarity).
METAL 271 271 Manganese 1; via carbonyl oxygen (By
METAL 432 432 Manganese 2 (By similarity).
METAL 476 476 Manganese 2 (By similarity). |
Keyword | Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Magnesium; Manganese; Metal-binding; Nucleus; Protein phosphatase; Reference proteome; Repeat. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 749 AA |
Protein Sequence | MAGCIPEEKT YRRFLELFLG EFRGPCGGGE PEPEPESEPE PEPEAELVAA EAAEASGEEP 60
GEDAATVEAT EEGEQDQDPE PEDEAVEEET ATEGEEEEEE EAAAPGHSAV PPPPQPQLPP 120
LPPLPRPLSE RITREEVEGE SLDLCLQQLY KYNCPSFLAA ALARATSDEV LQSDLSAHCI 180
PKETDGTEGT VEIETVKLAR SVFSKLHEIC CSWVKDFPLR RRPQIYYETS IHAIKNMRRK 240
MEDKHVCIPD FNMLFNLEDQ EEQAYFAVFD GHGGVDAAIY ASVHLHVNLV RQEMFPHDPA 300
EALCRAFRVT DERFVQKAAR ESLRCGTTGV VTFIRGNMLH VAWVGDSQVM LVRKGQAVEL 360
MKPHKPDRED EKQRIEALGG CVVWFGAWRV NGSLSVSRAI GDAEHKPYIC GDADSASTVL 420
DGTEDYLILA CDGFYDTVNP DEAVKVVSDH LKENNGDSSM VAHKLVASAR DAGSSDNITV 480
IVVFLRDMNK AVNVSEESEW TENSFQGGQE DGGDDKETHG ECKRPWPQHQ CSAPADLGYE 540
GRVDSFTDRT SLSPGPQINV LEDPDYLDLT QIEASKPHST QFLPPVEMIG PGAPKKDLNE 600
LIMEERSVKS SLPERSGAGE PRVSFNLGST GQQICRMENL SPVSSGLENE QFKSRGKTAS 660
RLYHLRHHYS KRQRGFRFNP KFYSFLSARE PSHKIGISLS SLTRSGKRNK MLRSSLPWRE 720
NSWEGYSGNV KIRKRNDIPC PDFPWSYKI 749 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005730; C:nucleolus; IEA:Compara. GO:0043234; C:protein complex; IEA:Compara. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0004722; F:protein serine/threonine phosphatase activity; IEA:Compara. GO:0035690; P:cellular response to drug; IEA:Compara. GO:0006469; P:negative regulation of protein kinase activity; IEA:Compara. GO:0035970; P:peptidyl-threonine dephosphorylation; IEA:Compara. GO:0051496; P:positive regulation of stress fiber assembly; IEA:Compara. GO:0006470; P:protein dephosphorylation; IMP:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |