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P62139

- PP1A_RABIT

UniProt

P62139 - PP1A_RABIT

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Protein

Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Gene

PPP1CA

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - 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.By similarity

Catalytic activityi

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

Cofactori

Binds 2 manganese ions per subunit.1 Publication

Sites

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

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
Synonyms:PPP1A
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: 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

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
  3. 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 – 11RemovedBy similarity
Chaini2 – 330329Serine/threonine-protein phosphatase PP1-alpha catalytic subunitPRO_0000058776Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei305 – 3051N6-acetyllysineBy similarity
Modified residuei306 – 3061PhosphotyrosineBy similarity
Modified residuei320 – 3201PhosphothreonineBy similarity

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.

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.By similarity

Binary interactionsi

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

Protein-protein interaction databases

BioGridi1172319. 78 interactions.
IntActiP62139. 3 interactions.
MINTiMINT-106725.

Structurei

Secondary structure

1
330
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 1810Combined sources
Turni19 – 224Combined sources
Helixi32 – 4817Combined sources
Beta strandi51 – 555Combined sources
Beta strandi57 – 626Combined sources
Helixi69 – 7911Combined sources
Beta strandi87 – 893Combined sources
Beta strandi94 – 985Combined sources
Helixi100 – 11314Combined sources
Turni115 – 1173Combined sources
Beta strandi118 – 1203Combined sources
Helixi128 – 1347Combined sources
Helixi136 – 1438Combined sources
Helixi146 – 15611Combined sources
Beta strandi162 – 1654Combined sources
Turni166 – 1683Combined sources
Beta strandi169 – 1746Combined sources
Helixi183 – 1886Combined sources
Beta strandi197 – 1993Combined sources
Helixi200 – 2067Combined sources
Beta strandi214 – 2185Combined sources
Beta strandi222 – 2276Combined sources
Helixi229 – 23911Combined sources
Beta strandi242 – 2465Combined sources
Beta strandi254 – 2585Combined sources
Turni259 – 2624Combined sources
Beta strandi263 – 2675Combined sources
Beta strandi274 – 2763Combined sources
Beta strandi280 – 2856Combined sources
Beta strandi291 – 2966Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJMX-ray2.10A/B1-330[»]
ProteinModelPortaliP62139.
SMRiP62139. Positions 7-299.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62139.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0639.
HOVERGENiHBG000216.
InParanoidiP62139.

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]

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. Align

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:
     2-33: SDSEKLNLDSIIGRLLEVQGSRPGKNVQLTEN → MVTIMTTSEYLSGY

Note: No experimental confirmation available.

Show »
Length:312
Mass (Da):35,597
Checksum:iF8F24487D1110507
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti309 – 3091F → L in CAA68693. (PubMed:2822491)Curated
Sequence conflicti309 – 3091F → L in CAA30645. (PubMed:2835264)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 3332SDSEK…QLTEN → MVTIMTTSEYLSGY in isoform 1. 1 PublicationVSP_010642Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

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:
EMBL
GenBank
DDBJ
Links Updated
Y00701 mRNA. Translation: CAA68693.1 .
X07798 mRNA. Translation: CAA30645.1 .
X14832 mRNA. Translation: CAA32941.1 .
PIRi S04335. PARB11.
RefSeqi NP_001095176.1. NM_001101706.1.
UniGenei Ocu.2075.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FJM X-ray 2.10 A/B 1-330 [» ]
ProteinModelPortali P62139.
SMRi P62139. Positions 7-299.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 1172319. 78 interactions.
IntActi P62139. 3 interactions.
MINTi MINT-106725.

Chemistry

BindingDBi P62139.

Proteomic databases

PRIDEi P62139.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100009298.

Organism-specific databases

CTDi 5499.

Phylogenomic databases

eggNOGi COG0639.
HOVERGENi HBG000216.
InParanoidi P62139.

Miscellaneous databases

EvolutionaryTracei P62139.

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. "Isolation and sequence analysis of a cDNA clone encoding a type-1 protein phosphatase catalytic subunit: homology with protein phosphatase 2A."
    Berndt N., Campbell D.G., Caudwell F.B., Cohen P., da Cruz e Silva E.F., da Cruz e Silva O.B., Cohen P.T.W.
    FEBS Lett. 223:340-346(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY.
    Strain: New Zealand white.
    Tissue: Skeletal muscle.
  2. "Molecular cloning of a cDNA for the catalytic subunit of rabbit muscle phosphorylase phosphatase."
    Bai G., Zhang Z., Amin J., Deans-Zirattu S.A., Lee E.Y.C.
    FASEB J. 2:3010-3016(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Muscle.
  3. "Two isoforms of protein phosphatase 1 may be produced from the same gene."
    Cohen P.T.W.
    FEBS Lett. 232:17-23(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: New Zealand white.
    Tissue: Skeletal muscle.
  4. "The major type-1 protein phosphatase catalytic subunits are the same gene products in rabbit skeletal muscle and rabbit liver."
    Cohen P.T.W., Schelling D.L., da Cruz e Silva O.B., Barker H.M., Cohen P.
    Biochim. Biophys. Acta 1008:125-128(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: New Zealand white.
    Tissue: Liver.
  5. "FLJ23654 encodes a heart protein phosphatase 1-binding protein (Hepp1)."
    Chen C.Y., Lai N.S., Yang J.J., Huang H.L., Hung W.C., Li C., Lin T.H., Huang H.B.
    Biochem. Biophys. Res. Commun. 391:698-702(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP1R39.
  6. "Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1."
    Goldberg J., Huang H.B., Kwon Y.G., Greengard P., Nairn A.C., Kuriyan J.
    Nature 376:745-753(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS, COFACTOR.

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: October 29, 2014
This is version 96 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

External Data

Dasty 3