Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00519
Entry Name
UniProt Accession
Theoretical PI
5.04
Molecular Weight
42794.97
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Protein phosphatase 1B
Protein Synonyms/Alias
3.1.3.16; Protein phosphatase 2C isoform beta; PP2C-beta;
Gene Name
Ppm1b
Gene Synonyms/Alias
Pp2c2; Pppm1b;
Created Date
01-JUN-1994
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGAFLDKPK
[1]
N-Myristoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Chida T, Ando M, Matsuki T, Masu Y, Nagaura Y, Takano-Yamamoto T, Tamura S,Kobayashi T. N-Myristoylation is essential for protein phosphatases PPM1A andPPM1B to dephosphorylate their physiological substrates in cells. Biochem J. 2013Feb 1;449(3):741-9. doi: 10.1042/BJ20121201.[PMID:23088624]
Functional Description
Enzyme with a broad specificity. Dephosphorylates PRKAA1 and PRKAA2. Inhibits TBK1-mediated antiviral signaling by dephosphorylating it at 'Ser-172'. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB.
Sequence Annotation
Metal binding site: 60 60 Manganese 1.
Metal binding site: 60 60 Manganese 2.
Metal binding site: 61 61 Manganese 1; via carbonyl oxygen.
Metal binding site: 243 243 Manganese 2.
Metal binding site: 286 286 Manganese 2.
Protein Length
390 AA.
Protein Sequence
(Canonical)
MGAFLDKPKT EKHNAHGAGN GLRYGLSSMQ GWRVEMEDAH TAVVGIPHGL DNWSFFAVYD  60
GHAGSRVANY CSTHLLEHIT TNEDFRAADK SGSALEPSVE SVKTGIRTGF LKIDEYMRNF  120
SDLRNGMDRS GSTAVGVMVS PTHMYFINCG DSRAVLCRNG QVCFSTQDHK PCNPVEKERI  180
QNAGGSVMIQ RVNGSLAVSR ALGDYDYKCV DGKGPTEQLV SPEPEVYEIV RAEEDEFVVL  240
ACDGIWDVMS NEELCEFVKS RLEVSDDLEN VCNWVVDTCL HKGSRDNMSV VLVCFSNAPK  300
VSEEAVKRDS ELDKHLESRV EEIMQKSGEE GMPDLAHVMR ILSAENIPNL PPGGGLAGKR  360
HVIEAVYSRL NPHKDNDGGA GDLEDSLVAL                                   390
FASTA
(Canonical)
>LipidDB-10090-00519|P36993
MGAFLDKPKTEKHNAHGAGNGLRYGLSSMQGWRVEMEDAHTAVVGIPHGLDNWSFFAVYD
GHAGSRVANYCSTHLLEHITTNEDFRAADKSGSALEPSVESVKTGIRTGFLKIDEYMRNF
SDLRNGMDRSGSTAVGVMVSPTHMYFINCGDSRAVLCRNGQVCFSTQDHKPCNPVEKERI
QNAGGSVMIQRVNGSLAVSRALGDYDYKCVDGKGPTEQLVSPEPEVYEIVRAEEDEFVVL
ACDGIWDVMSNEELCEFVKSRLEVSDDLENVCNWVVDTCLHKGSRDNMSVVLVCFSNAPK
VSEEAVKRDSELDKHLESRVEEIMQKSGEEGMPDLAHVMRILSAENIPNLPPGGGLAGKR
HVIEAVYSRLNPHKDNDGGAGDLEDSLVAL
Gene Ontology
GO:0005829; C:cytosol; IDA:UniProtKB
GO:0016020; C:membrane; IDA:UniProtKB
GO:0000287; F:magnesium ion binding; IEA:InterPro
GO:0030145; F:manganese ion binding; IEA:InterPro
GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro
GO:0006499; P:N-terminal protein myristoylation; IDA:UniProtKB
GO:0050687; P:negative regulation of defense response to virus; ISS:UniProtKB
GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB
GO:0032688; P:negative regulation of interferon-beta production; ISS:UniProtKB
GO:0042347; P:negative regulation of NF-kappaB import into nucleus; ISS:UniProtKB
GO:0006470; P:protein dephosphorylation; IMP:UniProtKB
Interpro
InterPro; IPR001932; PP2C-like_dom
InterPro; IPR012911; PP2C_C
InterPro; IPR000222; PP2C_Mn2_Asp60_BS
InterPro; IPR015655; Protein_Pase_2C
Pfam
Pfam; PF00481; PP2C;
Pfam; PF07830; PP2C_C;
SMART
SMART; SM00331; PP2C_SIG;
SMART; SM00332; PP2Cc;
PROSITE
PROSITE; PS01032; PP2C;
PRINTS