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Protein

Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Gene

PPP1CA

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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). Dephosphorylates CENPA (By similarity). Dephosphorylates the 'Ser-139' residue of ATG16L1 causing dissociation of ATG12-ATG5-ATG16L1 complex, thereby inhibiting autophagy (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mn2+1 PublicationNote: Binds 2 manganese ions per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi64Manganese 11
Metal bindingi66Manganese 11
Metal bindingi92Manganese 11
Metal bindingi92Manganese 21
Metal bindingi124Manganese 21
Active sitei125Proton donorBy similarity1
Metal bindingi173Manganese 21
Metal bindingi248Manganese 21

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • phosphatase activity Source: UniProtKB
  • phosphoprotein phosphatase activity Source: ParkinsonsUK-UCL
  • protein serine/threonine phosphatase activity Source: ParkinsonsUK-UCL

GO - Biological processi

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
Synonyms:PPP1A
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: 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).By similarity

GO - Cellular componenti

  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: UniProtKB-SubCell
  • protein phosphatase type 1 complex Source: ParkinsonsUK-UCL
  • PTW/PP1 phosphatase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000587762 – 330Serine/threonine-protein phosphatase PP1-alpha catalytic subunitAdd BLAST329

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei2PhosphoserineBy similarity1
Modified residuei22PhosphoserineBy similarity1
Modified residuei305N6-acetyllysineBy similarity1
Modified residuei306PhosphotyrosineBy similarity1
Modified residuei320PhosphothreonineBy similarity1
Modified residuei325PhosphoserineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP62139.

PTM databases

iPTMnetiP62139.

Expressioni

Tissue specificityi

Detected in skeletal muscle (at protein level). Detected in skeletal muscle.1 Publication

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 TRIM28; the interaction dephosphorylates TRIM28 on 'Ser-824' and forms a complex at the p21 promoter site (By similarity). Interacts with PPP1R39. 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). Interacts with BTBD10 (By similarity). Interacts with KCTD20 (By similarity). Interacts with FOXP3 (By similarity). Interacts with CENPA (By similarity). Interacts with ATG16L1 (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GRIN2BQ132242EBI-2008988,EBI-2256942From a different organism.
PPP1R11O609272EBI-2008988,EBI-1048104From a different organism.

Protein-protein interaction databases

BioGridi1172319. 80 interactors.
IntActiP62139. 5 interactors.
MINTiMINT-106725.

Structurei

Secondary structure

1330
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 18Combined sources10
Turni19 – 22Combined sources4
Helixi32 – 48Combined sources17
Beta strandi51 – 55Combined sources5
Beta strandi57 – 62Combined sources6
Helixi69 – 79Combined sources11
Beta strandi87 – 89Combined sources3
Beta strandi94 – 98Combined sources5
Helixi100 – 113Combined sources14
Turni115 – 117Combined sources3
Beta strandi118 – 120Combined sources3
Helixi128 – 134Combined sources7
Helixi136 – 143Combined sources8
Helixi146 – 156Combined sources11
Beta strandi162 – 165Combined sources4
Turni166 – 168Combined sources3
Beta strandi169 – 174Combined sources6
Helixi183 – 188Combined sources6
Beta strandi197 – 199Combined sources3
Helixi200 – 206Combined sources7
Beta strandi214 – 218Combined sources5
Beta strandi222 – 227Combined sources6
Helixi229 – 239Combined sources11
Beta strandi242 – 246Combined sources5
Beta strandi254 – 258Combined sources5
Turni259 – 262Combined sources4
Beta strandi263 – 267Combined sources5
Beta strandi274 – 276Combined sources3
Beta strandi280 – 285Combined sources6
Beta strandi291 – 296Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FJMX-ray2.10A/B1-330[»]
ProteinModelPortaliP62139.
SMRiP62139.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62139.

Family & Domainsi

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-1 subfamily.Curated

Phylogenomic databases

HOVERGENiHBG000216.
InParanoidiP62139.
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.
IPR031675. STPPase_N.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
PF16891. STPPase_N. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2 (identifier: P62139-1) [UniParc]FASTAAdd to basket
Also known as: 1-alpha-2

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL KSREIFLSQP
60 70 80 90 100
ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS
110 120 130 140 150
LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK
160 170 180 190 200
TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL
210 220 230 240 250
LCDLLWSDPD KDVQGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV
260 270 280 290 300
VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAD
310 320 330
KNKGKYGQFS GLNPGGRPIT PPRNSAKAKK
Length:330
Mass (Da):37,512
Last modified:June 21, 2004 - v1
Checksum:i60C37E1AD9831DAC
GO
Isoform 1 (identifier: P62139-2) [UniParc] [UniParc]FASTAAdd to basket
Also known as: 1-alpha-1

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTEN → MVTIMTTSEYLSGY

Note: No experimental confirmation available.
Show »
Length:311
Mass (Da):35,466
Checksum:iDACB568733E12EC3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti309F → L in CAA68693 (PubMed:2822491).Curated1
Sequence conflicti309F → L in CAA30645 (PubMed:2835264).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0106421 – 33MSDSE…QLTEN → MVTIMTTSEYLSGY in isoform 1. 1 PublicationAdd BLAST33

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00701 mRNA. Translation: CAA68693.1.
X07798 mRNA. Translation: CAA30645.1.
X14832 mRNA. Translation: CAA32941.1.
PIRiS04335. PARB11.
RefSeqiNP_001095176.1. NM_001101706.1.
UniGeneiOcu.2075.

Genome annotation databases

GeneIDi100009298.
KEGGiocu:100009298.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Protein Spotlight

The things we forget - Issue 32 of March 2003

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00701 mRNA. Translation: CAA68693.1.
X07798 mRNA. Translation: CAA30645.1.
X14832 mRNA. Translation: CAA32941.1.
PIRiS04335. PARB11.
RefSeqiNP_001095176.1. NM_001101706.1.
UniGeneiOcu.2075.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FJMX-ray2.10A/B1-330[»]
ProteinModelPortaliP62139.
SMRiP62139.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1172319. 80 interactors.
IntActiP62139. 5 interactors.
MINTiMINT-106725.

PTM databases

iPTMnetiP62139.

Proteomic databases

PRIDEiP62139.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009298.
KEGGiocu:100009298.

Organism-specific databases

CTDi5499.

Phylogenomic databases

HOVERGENiHBG000216.
InParanoidiP62139.
KOiK06269.

Miscellaneous databases

EvolutionaryTraceiP62139.

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.
IPR031675. STPPase_N.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
PF16891. STPPase_N. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPP1A_RABIT
AccessioniPrimary (citable) accession number: P62139
Secondary accession number(s): P08128
, P08129, P20653, P22802
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: June 21, 2004
Last modified: November 30, 2016
This is version 113 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.