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P35814

- PPM1A_RABIT

UniProt

P35814 - PPM1A_RABIT

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Protein
Protein phosphatase 1A
Gene
PPM1A, PPPM1A
Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - 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.

Catalytic activityi

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

Cofactori

Binds 2 magnesium or manganese ions per subunit.

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. N-terminal protein myristoylation Source: UniProtKB
  2. Wnt signaling pathway Source: Ensembl
  3. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  4. negative regulation of NF-kappaB import into nucleus Source: UniProtKB
  5. negative regulation of SMAD protein complex assembly Source: Ensembl
  6. negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
  7. peptidyl-threonine dephosphorylation Source: Ensembl
  8. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: AgBase
  9. positive regulation of Wnt signaling pathway Source: Ensembl
  10. positive regulation of transcription, DNA-templated Source: Ensembl
  11. protein dephosphorylation Source: UniProtKB
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 – 11Removed By similarity
Chaini2 – 382381Protein phosphatase 1A
PRO_0000057743Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine By similarity
Modified residuei375 – 3751Phosphoserine By 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.

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000008575.

Structurei

3D structure databases

ProteinModelPortaliP35814.
SMRiP35814. Positions 2-368.

Family & Domainsi

Sequence similaritiesi

Belongs to the PP2C family.

Phylogenomic databases

eggNOGiCOG0631.
HOGENOMiHOG000233895.
HOVERGENiHBG053647.

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

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MGAFLDKPKM EKHNAQGQGN GLRYGLSSMQ GWRVEMEDAH TAVIGLPSGL    50
ETWSFFAVYD GHAGSQVAKY CCEHLLDHIT NNQDFKGSAG APSVENVKNG 100
IRTGFLEIDE HMRVMSEKKH GADRSGSTAV GVLISPQHTY FINCGDSRGL 150
LCRNRKVHFF TQDHKPSNPL EKERIQNAGG SVMIQRVNGS LAVSRALGDF 200
DYKCVHGKGP TEQLVSPEPE VHDIERSEED DQFIILACDG IWDVMGNEEL 250
CDFVRSRLEV TDDLEKVCNE VVDTCLYKGS RDNMSVILIC FPNAPKVSPE 300
AVKKEAELDK YLECRVEEIL KKQGEGVPDL VHVMRTLASE NIPSLPPGGE 350
LASKRNVIEA VYNRLNPYKN DDTDSTSTDD MW 382
Length:382
Mass (Da):42,462
Last modified:June 1, 1994 - v1
Checksum:i46BCF1854FD1CA86
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S87757 mRNA. Translation: AAB21783.1.
PIRiS22422.
RefSeqiNP_001076167.1. NM_001082698.1.
UniGeneiOcu.3308.

Genome annotation databases

GeneIDi100009431.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S87757 mRNA. Translation: AAB21783.1 .
PIRi S22422.
RefSeqi NP_001076167.1. NM_001082698.1.
UniGenei Ocu.3308.

3D structure databases

ProteinModelPortali P35814.
SMRi P35814. Positions 2-368.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9986.ENSOCUP00000008575.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100009431.

Organism-specific databases

CTDi 5494.

Phylogenomic databases

eggNOGi COG0631.
HOGENOMi HOG000233895.
HOVERGENi HBG053647.

Family and domain databases

Gene3Di 1.10.10.430. 1 hit.
3.60.40.10. 1 hit.
InterProi IPR001932. PP2C-like_dom.
IPR012911. PP2C_C.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view ]
PANTHERi PTHR13832. PTHR13832. 1 hit.
Pfami PF00481. PP2C. 1 hit.
PF07830. PP2C_C. 1 hit.
[Graphical view ]
SMARTi SM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view ]
SUPFAMi SSF81601. SSF81601. 1 hit.
SSF81606. SSF81606. 1 hit.
PROSITEi PS01032. PP2C. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 19, 2014
This is version 97 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

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