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Protein

Protein phosphatase 1A

Gene

PPM1A

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Enzyme with a broad specificity. Negatively regulates TGF-beta signaling through dephosphorylating SMAD2 and SMAD3, resulting in their dissociation from SMAD4, nuclear export of the SMADs and termination of the TGF-beta-mediated signaling (By similarity). Dephosphorylates PRKAA1 and PRKAA2. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB (By similarity).By similarity

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactori

Mg2+, Mn2+Note: Binds 2 magnesium or manganese ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi60 – 601Manganese 1By similarity
Metal bindingi60 – 601Manganese 2By similarity
Metal bindingi61 – 611Manganese 1; via carbonyl oxygenBy similarity
Metal bindingi239 – 2391Manganese 2By similarity
Metal bindingi282 – 2821Manganese 2By similarity

GO - Molecular functioni

  1. calmodulin-dependent protein phosphatase activity Source: Ensembl
  2. magnesium ion binding Source: InterPro
  3. manganese ion binding Source: InterPro
  4. phosphoprotein phosphatase activity Source: AgBase
  5. R-SMAD binding Source: UniProtKB
  6. signal transducer activity Source: AgBase

GO - Biological processi

  1. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  2. negative regulation of NF-kappaB import into nucleus Source: UniProtKB
  3. negative regulation of SMAD protein complex assembly Source: Ensembl
  4. negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
  5. N-terminal protein myristoylation Source: UniProtKB
  6. peptidyl-threonine dephosphorylation Source: Ensembl
  7. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: AgBase
  8. positive regulation of transcription, DNA-templated Source: Ensembl
  9. positive regulation of Wnt signaling pathway Source: Ensembl
  10. protein dephosphorylation Source: UniProtKB
  11. Wnt signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase 1A (EC:3.1.3.16)
Alternative name(s):
Protein phosphatase 2C isoform alpha
Short name:
PP2C-alpha
Protein phosphatase IA
Gene namesi
Name:PPM1A
Synonyms:PPPM1A
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

Nucleus By similarity. Cytoplasmcytosol By similarity. Membrane By similarity
Note: Weakly associates at the membrane and N-myristoylation mediates the membrane localization.By similarity

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. membrane Source: UniProtKB
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 382381Protein phosphatase 1APRO_0000057743Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Modified residuei375 – 3751PhosphoserineBy similarity

Post-translational modificationi

N-myristoylation is essential for the recognition of its substrates for dephosphorylation.By similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Interactioni

Subunit structurei

Monomer (By similarity). Interacts with SMAD2; the interaction dephosphorylates SMAD2 in its C-terminal SXS motif resulting in disruption of the SMAD2/SMAD4 complex, SMAD2 nuclear export and termination of the TGF-beta-mediated signaling. Interacts with SMAD2; the interaction dephosphorylates SMAD2 in its C-terminal SXS motif resulting in disruption of the SMAD2/SMAD4 complex, SMAD2 nuclear export and termination of the TGF-beta-mediated signaling (By similarity). Interacts with the phosphorylated form of IKBKB/IKKB (By similarity).By similarity

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000008575.

Structurei

3D structure databases

ProteinModelPortaliP35814.
SMRiP35814. Positions 2-368.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PP2C family.Curated

Phylogenomic databases

eggNOGiCOG0631.
HOGENOMiHOG000233895.
HOVERGENiHBG053647.
InParanoidiP35814.
KOiK04457.

Family and domain databases

Gene3Di1.10.10.430. 1 hit.
3.60.40.10. 1 hit.
InterProiIPR001932. PP2C-like_dom.
IPR012911. PP2C_C.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 1 hit.
PfamiPF00481. PP2C. 1 hit.
PF07830. PP2C_C. 1 hit.
[Graphical view]
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81601. SSF81601. 1 hit.
SSF81606. SSF81606. 1 hit.
PROSITEiPS01032. PP2C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35814-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGAFLDKPKM EKHNAQGQGN GLRYGLSSMQ GWRVEMEDAH TAVIGLPSGL
60 70 80 90 100
ETWSFFAVYD GHAGSQVAKY CCEHLLDHIT NNQDFKGSAG APSVENVKNG
110 120 130 140 150
IRTGFLEIDE HMRVMSEKKH GADRSGSTAV GVLISPQHTY FINCGDSRGL
160 170 180 190 200
LCRNRKVHFF TQDHKPSNPL EKERIQNAGG SVMIQRVNGS LAVSRALGDF
210 220 230 240 250
DYKCVHGKGP TEQLVSPEPE VHDIERSEED DQFIILACDG IWDVMGNEEL
260 270 280 290 300
CDFVRSRLEV TDDLEKVCNE VVDTCLYKGS RDNMSVILIC FPNAPKVSPE
310 320 330 340 350
AVKKEAELDK YLECRVEEIL KKQGEGVPDL VHVMRTLASE NIPSLPPGGE
360 370 380
LASKRNVIEA VYNRLNPYKN DDTDSTSTDD MW
Length:382
Mass (Da):42,462
Last modified:June 1, 1994 - v1
Checksum:i46BCF1854FD1CA86
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S87757 mRNA. Translation: AAB21783.1.
PIRiS22422.
RefSeqiNP_001076167.1. NM_001082698.1.
XP_008270042.1. XM_008271820.1.
UniGeneiOcu.3308.

Genome annotation databases

GeneIDi100009431.
KEGGiocu:100009431.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S87757 mRNA. Translation: AAB21783.1.
PIRiS22422.
RefSeqiNP_001076167.1. NM_001082698.1.
XP_008270042.1. XM_008271820.1.
UniGeneiOcu.3308.

3D structure databases

ProteinModelPortaliP35814.
SMRiP35814. Positions 2-368.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000008575.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009431.
KEGGiocu:100009431.

Organism-specific databases

CTDi5494.

Phylogenomic databases

eggNOGiCOG0631.
HOGENOMiHOG000233895.
HOVERGENiHBG053647.
InParanoidiP35814.
KOiK04457.

Family and domain databases

Gene3Di1.10.10.430. 1 hit.
3.60.40.10. 1 hit.
InterProiIPR001932. PP2C-like_dom.
IPR012911. PP2C_C.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 1 hit.
PfamiPF00481. PP2C. 1 hit.
PF07830. PP2C_C. 1 hit.
[Graphical view]
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81601. SSF81601. 1 hit.
SSF81606. SSF81606. 1 hit.
PROSITEiPS01032. PP2C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Mammalian protein serine/threonine phosphatase 2C: cDNA cloning and comparative analysis of amino acid sequences."
    Mann D.J., Campbell D.G., McGowan C.H., Cohen P.T.W.
    Biochim. Biophys. Acta 1130:100-104(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.

Entry informationi

Entry nameiPPM1A_RABIT
AccessioniPrimary (citable) accession number: P35814
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: February 4, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.