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O62829 (PPM1A_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein phosphatase 1A

EC=3.1.3.16
Alternative name(s):
Protein phosphatase 2C isoform alpha
Short name=PP2C-alpha
Gene names
Name:PPM1A
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

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

Cofactor

Binds 2 magnesium or manganese ions per subunit.

Subunit structure

Monomer. 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.

Subcellular location

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

Post-translational modification

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

Sequence similarities

Belongs to the PP2C family.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
Nucleus
   LigandMagnesium
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMLipoprotein
Myristate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processN-terminal protein myristoylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of NF-kappaB import into nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from sequence or structural similarity. Source: AgBase

protein dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Inferred from sequence or structural similarity. Source: GOC

   Cellular_componentcytosol

Inferred from sequence or structural similarity. Source: UniProtKB

membrane

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionR-SMAD binding

Inferred from sequence or structural similarity. Source: UniProtKB

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

manganese ion binding

Inferred from electronic annotation. Source: InterPro

phosphoprotein phosphatase activity

Inferred from sequence or structural similarity. Source: AgBase

protein serine/threonine phosphatase activity

Inferred from electronic annotation. Source: InterPro

signal transducer activity

Inferred from sequence or structural similarity. Source: AgBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 382381Protein phosphatase 1A
PRO_0000057740

Sites

Metal binding601Manganese 1 By similarity
Metal binding601Manganese 2 By similarity
Metal binding611Manganese 1; via carbonyl oxygen By similarity
Metal binding2391Manganese 2 By similarity
Metal binding2821Manganese 2 By similarity

Amino acid modifications

Modified residue3751Phosphoserine By similarity
Lipidation21N-myristoyl glycine By similarity

Sequences

Sequence LengthMass (Da)Tools
O62829 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: A716B3FA0E7E21C2

FASTA38242,530
        10         20         30         40         50         60 
MGAFLDKPKM EKHNAQGQGN GLRYGLSSMQ GWRVEMEDAH TAVIGLPSGL ETWSFFAVYD 

        70         80         90        100        110        120 
GHAGSQVAKY CCEHLLDHIT NNQDFKGSAG APSVENVKNG IRTGFLEIDE HMRVMSEKKH 

       130        140        150        160        170        180 
GADRSGSTAV GVLISPQHTY FINCGDSRGL LCRNRKVYFF TQDHKPSNPL EKERIQNAGG 

       190        200        210        220        230        240 
SVMIQRVNGS LAVSRALGDF DYKCVHGKGP TEQLVSPEPE VHDIERSEED DQFIILACDG 

       250        260        270        280        290        300 
IWDVMGNEEL CDFVRSRLEV TDDLEKVCNE VVDTCLYKGS RDNMSVILIC FPNAPKVSPE 

       310        320        330        340        350        360 
AVKKEEELDK YLESRVEEII KKQGEGVPDL VHVMRTLASE NIPSLPPGGE LASKRNVIEA 

       370        380 
VYNRLNPYKN DDTDSTSTDD MW 

« Hide

References

[1]"Protein phosphatase type-2C isozymes present in vertebrate retinae: purification, characterization, and localization in photoreceptors."
Klumpp S., Selke D., Fischer D., Baumann A., Mueller F., Thanos S.
J. Neurosci. Res. 51:328-338(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Retina.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ005457 mRNA. Translation: CAA06554.1.
RefSeqNP_776854.1. NM_174429.2.
UniGeneBt.4671.

3D structure databases

ProteinModelPortalO62829.
SMRO62829. Positions 2-368.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000024128.

Proteomic databases

PRIDEO62829.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000024128; ENSBTAP00000024128; ENSBTAG00000018127.
GeneID281994.
KEGGbta:281994.

Organism-specific databases

CTD5494.

Phylogenomic databases

eggNOGCOG0631.
GeneTreeENSGT00740000115384.
HOGENOMHOG000233895.
HOVERGENHBG053647.
InParanoidO62829.
KOK04457.
OMAEVYAIER.
OrthoDBEOG7WMCJH.
TreeFamTF313590.

Family and domain databases

Gene3D1.10.10.430. 1 hit.
3.60.40.10. 1 hit.
InterProIPR001932. PP2C-like_dom.
IPR012911. PP2C_C.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERPTHR13832. PTHR13832. 1 hit.
PfamPF00481. PP2C. 1 hit.
PF07830. PP2C_C. 1 hit.
[Graphical view]
SMARTSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81601. SSF81601. 1 hit.
SSF81606. SSF81606. 1 hit.
PROSITEPS01032. PP2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20805862.

Entry information

Entry namePPM1A_BOVIN
AccessionPrimary (citable) accession number: O62829
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families