CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016838
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein phosphatase 1F 
Protein Synonyms/Alias
 Ca(2+)/calmodulin-dependent protein kinase phosphatase; CaM-kinase phosphatase; CaMKPase 
Gene Name
 Ppm1f 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
331AIGDVFQKPYVSGEAubiquitination[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
 Dephosphorylates and concomitantly deactivates CaM- kinase II activated upon autophosphorylation, and CaM-kinases IV and I activated upon phosphorylation by CaM-kinase kinase. Promotes apoptosis (By similarity). 
Sequence Annotation
 METAL 195 195 Manganese 1 (By similarity).
 METAL 195 195 Manganese 2 (By similarity).
 METAL 196 196 Manganese 1; via carbonyl oxygen (By
 METAL 357 357 Manganese 2 (By similarity).
 METAL 401 401 Manganese 2 (By similarity).  
Keyword
 Apoptosis; Complete proteome; Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 452 AA 
Protein Sequence
MASGAAQNSS QMACDSEIPG FLDAFLQDFP APLSLESPLP WKVPGTVLSQ EEVEAELIEL 60
ALGFLGSRNA PPSFAVAVTH EAISQLLQTD LSEFKRLPEQ EEEEEEEEEE KALVTLLDAK 120
GLARSFFNCL WKVCSQWQKQ VPLTAQAPQW QWLVSIHAIR NTRRKMEDRH VSLPAFNHLF 180
GLSDSVHRAY FAVFDGHGGV DAARYASVHV HTNASHQPEL RTNPAAALKE AFRLTDEMFL 240
QKAKRERLQS GTTGVCALIA GAALHVAWLG DSQVILVQQG RVVKLMEPHK PERQDEKARI 300
EALGGFVSLM DCWRVNGTLA VSRAIGDVFQ KPYVSGEADA ASRELTGSED YLLLACDGFF 360
DVVPHHEVTG LVHGHLLRHK GNGMRIAEEL VAVARDRGSH DNITVMVVFL REPLELLEGG 420
VQGTGDAQAD VGSQDLSTGL SELEISNTSQ RS 452 
Gene Ontology
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0043234; C:protein complex; ISS:UniProtKB.
 GO:0033192; F:calmodulin-dependent protein phosphatase activity; ISS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0035690; P:cellular response to drug; ISS:UniProtKB.
 GO:0097193; P:intrinsic apoptotic signaling pathway; ISS:UniProtKB.
 GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
 GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; ISS:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; ISS:UniProtKB.
 GO:0035970; P:peptidyl-threonine dephosphorylation; ISS:UniProtKB.
 GO:0050921; P:positive regulation of chemotaxis; ISS:UniProtKB.
 GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
 GO:0010634; P:positive regulation of epithelial cell migration; ISS:UniProtKB.
 GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
 GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
 GO:0045927; P:positive regulation of growth; ISS:UniProtKB.
 GO:0051496; P:positive regulation of stress fiber assembly; IEA:Compara. 
Interpro
 IPR001932; PP2C-like.
 IPR000222; PP2C_Mn2_Asp60_BS.
 IPR015655; Protein_Pase_2C. 
Pfam
 PF00481; PP2C 
SMART
 SM00331; PP2C_SIG
 SM00332; PP2Cc 
PROSITE
 PS01032; PP2C 
PRINTS