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Q3T0E7

- PP1A_BOVIN

UniProt

Q3T0E7 - PP1A_BOVIN

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Protein

Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Gene
PPP1CA
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca2+/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E By similarity.

Catalytic activityi

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

Cofactori

Binds 2 manganese ions per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Manganese 1 By similarity
Metal bindingi66 – 661Manganese 1 By similarity
Metal bindingi92 – 921Manganese 1 By similarity
Metal bindingi92 – 921Manganese 2 By similarity
Metal bindingi124 – 1241Manganese 2 By similarity
Active sitei125 – 1251Proton donor By similarity
Metal bindingi173 – 1731Manganese 2 By similarity
Metal bindingi248 – 2481Manganese 2 By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphatase activity Source: UniProtKB
  3. phosphoprotein phosphatase activity Source: UniProtKB-KW

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. circadian regulation of gene expression Source: UniProtKB
  4. entrainment of circadian clock by photoperiod Source: UniProtKB
  5. glycogen metabolic process Source: UniProtKB-KW
  6. protein dephosphorylation Source: UniProtKB
  7. regulation of circadian rhythm Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Biological rhythms, Carbohydrate metabolism, Cell cycle, Cell division, Glycogen metabolism

Keywords - Ligandi

Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (EC:3.1.3.16)
Short name:
PP-1A
Gene namesi
Name:PPP1CA
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity. Nucleusnucleoplasm By similarity. Nucleusnucleolus By similarity
Note: Primarily nuclear and largely excluded from the nucleolus. Highly mobile in cells and can be relocalized through interaction with targeting subunits. NOM1 plays a role in targeting this protein to the nucleolus. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles By similarity.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleolus Source: UniProtKB-SubCell
  3. nucleoplasm Source: UniProtKB-SubCell
  4. PTW/PP1 phosphatase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 330329Serine/threonine-protein phosphatase PP1-alpha catalytic subunitPRO_0000240131Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei305 – 3051N6-acetyllysine By similarity
Modified residuei306 – 3061Phosphotyrosine By similarity
Modified residuei320 – 3201Phosphothreonine By similarity

Post-translational modificationi

Phosphorylated. Dephosphorylated at Thr-320 in the presence of ionizing radiation By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ3T0E7.
PRIDEiQ3T0E7.

Interactioni

Subunit structurei

PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then complexed to one or several targeting or regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. Interacts with PPP1R15A and PPP1R15B; the interactions mediate binding to EIF2S1. Part of a complex containing PPP1R15B, PP1 and NCK1/2. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R9A, PPP1R9B and PPP1R7. Interacts with YLPM1. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and NCOA5. Interacts with NOM1 and PPP1R8. Interacts with PPP1R16B. Interacts with RPSA only in the presence of PPP1R16B. Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R10/PNUTS and PPP1R8. Interacts with WDR82 in the presence of PPP1R10/PNUTS. Interacts with PPP1R39. transition from mitosis into interphase. Interacts with TRIM28; the interaction dephosphorylates TRIM28 on 'Ser-824' and forms a complex at the p21 promoter site. Interacts with NEK2. Interacts with PHACTR4; which acts as an activator of PP1 activity. Interacts with FER; this promotes phosphorylation at Thr-320 By similarity.

Protein-protein interaction databases

BioGridi172796. 3 interactions.
IntActiQ3T0E7. 3 interactions.
STRINGi9913.ENSBTAP00000016111.

Structurei

3D structure databases

ProteinModelPortaliQ3T0E7.
SMRiQ3T0E7. Positions 7-299.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172697.
HOVERGENiHBG000216.
InParanoidiQ3T0E7.
KOiK06269.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q3T0E7-1 [UniParc]FASTAAdd to Basket

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MSDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL KSREIFLSQP    50
ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS 100
LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK 150
TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL 200
LCDLLWSDPD KDVQGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV 250
VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAD 300
KNKGKYGQFS GLNPGGRPIT PPRNSAKAKK 330
Length:330
Mass (Da):37,512
Last modified:October 11, 2005 - v1
Checksum:i60C37E1AD9831DAC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC102424 mRNA. Translation: AAI02425.1.
RefSeqiNP_001030393.1. NM_001035316.2.
UniGeneiBt.48845.

Genome annotation databases

GeneIDi516175.
KEGGibta:516175.

Cross-referencesi

Web resourcesi

Protein Spotlight

The things we forget - Issue 32 of March 2003

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC102424 mRNA. Translation: AAI02425.1 .
RefSeqi NP_001030393.1. NM_001035316.2.
UniGenei Bt.48845.

3D structure databases

ProteinModelPortali Q3T0E7.
SMRi Q3T0E7. Positions 7-299.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 172796. 3 interactions.
IntActi Q3T0E7. 3 interactions.
STRINGi 9913.ENSBTAP00000016111.

Chemistry

BindingDBi Q3T0E7.

Proteomic databases

PaxDbi Q3T0E7.
PRIDEi Q3T0E7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 516175.
KEGGi bta:516175.

Organism-specific databases

CTDi 5499.

Phylogenomic databases

eggNOGi COG0639.
HOGENOMi HOG000172697.
HOVERGENi HBG000216.
InParanoidi Q3T0E7.
KOi K06269.

Miscellaneous databases

NextBioi 20872154.

Family and domain databases

Gene3Di 3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view ]
Pfami PF00149. Metallophos. 1 hit.
[Graphical view ]
PRINTSi PR00114. STPHPHTASE.
SMARTi SM00156. PP2Ac. 1 hit.
[Graphical view ]
SUPFAMi SSF56300. SSF56300. 1 hit.
PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.

Entry informationi

Entry nameiPP1A_BOVIN
AccessioniPrimary (citable) accession number: Q3T0E7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: October 11, 2005
Last modified: July 9, 2014
This is version 76 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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