Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01251
Entry Name
UniProt Accession
Theoretical PI
4.95
Molecular Weight
52642.59
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
PP2CB;
Created Date
01-DEC-2000
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGAFLDKPK
[1]
N-Myristoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
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 CDK2 and CDK6 in vitro. 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
479 AA.
Protein Sequence
(Canonical)
MGAFLDKPKT EKHNAHGAGN GLRYGLSSMQ GWRVEMEDAH TAVVGIPHGL EDWSFFAVYD  60
GHAGSRVANY CSTHLLEHIT TNEDFRAAGK SGSALELSVE NVKNGIRTGF LKIDEYMRNF  120
SDLRNGMDRS GSTAVGVMIS PKHIYFINCG DSRAVLYRNG QVCFSTQDHK PCNPREKERI  180
QNAGGSVMIQ RVNGSLAVSR ALGDYDYKCV DGKGPTEQLV SPEPEVYEIL RAEEDEFIIL  240
ACDGIWDVMS NEELCEYVKS RLEVSDDLEN VCNWVVDTCL HKGSRDNMSI VLVCFSNAPK  300
VSDEAVKKDS ELDKHLESRV EEIMEKSGEE GMPDLAHVMR ILSAENIPNL PPGGGLAGKR  360
NVIEAVYSRL NPHRESDGAS DEAEESGSQG KLVEALRQMR INHRGNYRQL LEEMLTSYRL  420
AKVEGEESPA EPAATATSSN SDAGNPVTMQ ESHTESESGL AELDSSNEDA GTKMSGEKI   479
FASTA
(Canonical)
>LipidDB-9606-01251|O75688
MGAFLDKPKTEKHNAHGAGNGLRYGLSSMQGWRVEMEDAHTAVVGIPHGLEDWSFFAVYD
GHAGSRVANYCSTHLLEHITTNEDFRAAGKSGSALELSVENVKNGIRTGFLKIDEYMRNF
SDLRNGMDRSGSTAVGVMISPKHIYFINCGDSRAVLYRNGQVCFSTQDHKPCNPREKERI
QNAGGSVMIQRVNGSLAVSRALGDYDYKCVDGKGPTEQLVSPEPEVYEILRAEEDEFIIL
ACDGIWDVMSNEELCEYVKSRLEVSDDLENVCNWVVDTCLHKGSRDNMSIVLVCFSNAPK
VSDEAVKKDSELDKHLESRVEEIMEKSGEEGMPDLAHVMRILSAENIPNLPPGGGLAGKR
NVIEAVYSRLNPHRESDGASDEAEESGSQGKLVEALRQMRINHRGNYRQLLEEMLTSYRL
AKVEGEESPAEPAATATSSNSDAGNPVTMQESHTESESGLAELDSSNEDAGTKMSGEKI
Gene Ontology
GO:0005829; C:cytosol; ISS:UniProtKB
GO:0016020; C:membrane; ISS: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; IDA:UniProtKB
GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome
GO:0006499; P:N-terminal protein myristoylation; ISS:UniProtKB
GO:0050687; P:negative regulation of defense response to virus; IMP:UniProtKB
GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB
GO:0032688; P:negative regulation of interferon-beta production; IMP:UniProtKB
GO:0042347; P:negative regulation of NF-kappaB import into nucleus; IMP:UniProtKB
GO:0035970; P:peptidyl-threonine dephosphorylation; IDA: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