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O62829

- PPM1A_BOVIN

UniProt

O62829 - PPM1A_BOVIN

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Protein

Protein phosphatase 1A

Gene

PPM1A

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 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

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. magnesium ion binding Source: InterPro
  2. manganese ion binding Source: InterPro
  3. phosphoprotein phosphatase activity Source: AgBase
  4. protein serine/threonine phosphatase activity Source: InterPro
  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. N-terminal protein myristoylation Source: UniProtKB
  4. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: AgBase
  5. protein dephosphorylation Source: UniProtKB
  6. signal transduction Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_203853. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_209268. Regulation of AMPK activity via LKB1.

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
Gene namesi
Name:PPM1A
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 10

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-KW
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_0000057740Add
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

Proteomic databases

PRIDEiO62829.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000024128.

Structurei

3D structure databases

ProteinModelPortaliO62829.
SMRiO62829. Positions 2-368.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PP2C family.Curated

Phylogenomic databases

eggNOGiCOG0631.
GeneTreeiENSGT00740000115384.
HOGENOMiHOG000233895.
HOVERGENiHBG053647.
InParanoidiO62829.
KOiK04457.
OMAiEVYAIER.
OrthoDBiEOG7WMCJH.
TreeFamiTF313590.

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.

O62829 [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
LCRNRKVYFF 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
AVKKEEELDK YLESRVEEII KKQGEGVPDL VHVMRTLASE NIPSLPPGGE
360 370 380
LASKRNVIEA VYNRLNPYKN DDTDSTSTDD MW
Length:382
Mass (Da):42,530
Last modified:August 1, 1998 - v1
Checksum:iA716B3FA0E7E21C2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ005457 mRNA. Translation: CAA06554.1.
RefSeqiNP_776854.1. NM_174429.2.
UniGeneiBt.4671.

Genome annotation databases

EnsembliENSBTAT00000024128; ENSBTAP00000024128; ENSBTAG00000018127.
GeneIDi281994.
KEGGibta:281994.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ005457 mRNA. Translation: CAA06554.1 .
RefSeqi NP_776854.1. NM_174429.2.
UniGenei Bt.4671.

3D structure databases

ProteinModelPortali O62829.
SMRi O62829. Positions 2-368.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000024128.

Proteomic databases

PRIDEi O62829.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000024128 ; ENSBTAP00000024128 ; ENSBTAG00000018127 .
GeneIDi 281994.
KEGGi bta:281994.

Organism-specific databases

CTDi 5494.

Phylogenomic databases

eggNOGi COG0631.
GeneTreei ENSGT00740000115384.
HOGENOMi HOG000233895.
HOVERGENi HBG053647.
InParanoidi O62829.
KOi K04457.
OMAi EVYAIER.
OrthoDBi EOG7WMCJH.
TreeFami TF313590.

Enzyme and pathway databases

Reactomei REACT_203853. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_209268. Regulation of AMPK activity via LKB1.

Miscellaneous databases

NextBioi 20805862.

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. "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.

Entry informationi

Entry nameiPPM1A_BOVIN
AccessioniPrimary (citable) accession number: O62829
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: October 29, 2014
This is version 109 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