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Protein

Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Gene

PPP1CA

Organism
Homo sapiens (Human)
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. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). Dephosphorylates CENPA (PubMed:25556658). Dephosphorylates the 'Ser-139' residue of ATG16L1 causing dissociation of ATG12-ATG5-ATG16L1 complex, thereby inhibiting autophagy (PubMed:26083323).5 Publications

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Fe cationBy similarityNote: Binds 1 Fe cation per subunit.By similarity
  • Mn2+1 PublicationNote: Binds 2 manganese ions per subunit.1 Publication

Enzyme regulationi

The phosphatase activity of the PPP1R15A-PP1 complex toward EIF2S1 is specifically inhibited by Salubrinal, a drug that protects cells from endoplasmic reticulum stress.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi64Manganese 1By similarity1
Metal bindingi66Manganese 1By similarity1
Metal bindingi92Manganese1
Metal bindingi92Manganese 1By similarity1
Metal bindingi92Manganese 2By similarity1
Metal bindingi124Manganese1
Metal bindingi124Manganese 2By similarity1
Active sitei125Proton donorBy similarity1
Metal bindingi173Manganese1
Metal bindingi173Manganese 2By similarity1
Metal bindingi248Manganese1
Metal bindingi248Manganese 2By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Carbohydrate metabolism, Cell cycle, Cell division, Glycogen metabolism

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS10534-MONOMER.
BRENDAi3.1.3.16. 2681.
ReactomeiR-HSA-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-HSA-180024. DARPP-32 events.
R-HSA-2173788. Downregulation of TGF-beta receptor signaling.
R-HSA-400253. Circadian Clock.
SignaLinkiP62136.
SIGNORiP62136.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (EC:3.1.3.161 Publication)
Short name:
PP-1A
Gene namesi
Name:PPP1CA
Synonyms:PPP1A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:9281. PPP1CA.

Subcellular locationi

  • Cytoplasm
  • Nucleus
  • Nucleusnucleoplasm
  • Nucleusnucleolus

  • 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.

GO - Cellular componenti

  • cell-cell junction Source: BHF-UCL
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • dendritic spine Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • glycogen granule Source: Ensembl
  • MLL5-L complex Source: UniProtKB
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • perikaryon Source: Ensembl
  • plasma membrane Source: HPA
  • protein phosphatase type 1 complex Source: Ensembl
  • PTW/PP1 phosphatase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi5499.
OpenTargetsiENSG00000172531.
PharmGKBiPA33609.

Chemistry databases

ChEMBLiCHEMBL2164.

Polymorphism and mutation databases

BioMutaiPPP1CA.
DMDMi49065811.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000587742 – 330Serine/threonine-protein phosphatase PP1-alpha catalytic subunitAdd BLAST329

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei2PhosphoserineCombined sources1
Modified residuei22PhosphoserineCombined sources1
Modified residuei305N6-acetyllysineBy similarity1
Modified residuei306PhosphotyrosineBy similarity1
Modified residuei320PhosphothreonineCombined sources1 Publication1
Modified residuei325PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated. Dephosphorylated at Thr-320 in the presence of ionizing radiation.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP62136.
MaxQBiP62136.
PaxDbiP62136.
PeptideAtlasiP62136.
PRIDEiP62136.
TopDownProteomicsiP62136-1. [P62136-1]

2D gel databases

OGPiP08129.

PTM databases

DEPODiP62136.
iPTMnetiP62136.
PhosphoSitePlusiP62136.
SwissPalmiP62136.

Expressioni

Inductioni

Up-regulated in synovial fluid mononuclear cells and peripheral blood mononuclear cells from patients with rheumatoid arthritis.1 Publication

Gene expression databases

BgeeiENSG00000172531.
CleanExiHS_PPP1CA.
ExpressionAtlasiP62136. baseline and differential.
GenevisibleiP62136. HS.

Organism-specific databases

HPAiCAB004545.
HPA046833.

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 PPP1R39 (By similarity). Interacts with BTBD10 (By similarity). Interacts with KCTD20 (By similarity). Interacts with PPP1R9A and PPP1R9B. Part of a complex containing PPP1R15B, PP1 and NCK1/2. Interacts with PHACTR4; which acts as an activator of PP1 activity (By similarity). Interacts with PPP1R15A and PPP1R15B; the interactions mediate binding to EIF2S1. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R7. Interacts with YLPM1. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and NCOA5. Interacts with NOM1 and PPP1R8. Interacts with HHV-1 ICP34.5. 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. Interacts with isoform 1 and isoform 4 of NEK2. Interacts with FER; this promotes phosphorylation at Thr-320. Interacts with DAB2; the interaction is mutually exclusive with the AXIN1:PPP1CA interaction. Interacts with FOXP3 (PubMed:23396208). Interacts with CENPA (PubMed:25556658). Interacts with ATG16L1 (PubMed:26083323).By similarity19 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AKT1P317494EBI-357253,EBI-296087
APAF1O147272EBI-357253,EBI-446492
AXIN1O151694EBI-357253,EBI-710484
BRCA1P383982EBI-357253,EBI-349905
CASC5Q8NG312EBI-357253,EBI-1001161
CD2BP2O954002EBI-357253,EBI-768015
CDH1P128302EBI-357253,EBI-727477
CEP192Q8TEP82EBI-357253,EBI-2339778
CHCHD3Q9NX632EBI-357253,EBI-743375
ClockO087852EBI-357253,EBI-79859From a different organism.
CNSTQ6PJW83EBI-357253,EBI-750390
CSRNP1Q96S656EBI-357253,EBI-4311573
CSRNP2Q9H1756EBI-357253,EBI-5235958
DLG3Q927962EBI-357253,EBI-80440
ELLP551992EBI-357253,EBI-1245868
FOXP3Q9BZS12EBI-357253,EBI-983719
LRRK2Q5S0076EBI-357253,EBI-5323863
MPHOSPH10O005662EBI-357253,EBI-5235884
PPP1R13BQ96KQ47EBI-357253,EBI-1105153
PPP1R13LQ8WUF55EBI-357253,EBI-5550163
PPP1R15BQ5SWA13EBI-357253,EBI-2815482
PPP1R2P412363EBI-357253,EBI-1056517
PPP1R26Q5T8A72EBI-357253,EBI-308500
PPP1R27Q86WC62EBI-357253,EBI-5235602
PPP1R2P3Q6NXS15EBI-357253,EBI-10251630
PPP1R32Q7Z5V63EBI-357253,EBI-4311771
PPP1R37O758642EBI-357253,EBI-5235692
PPP1R8Q129724EBI-357253,EBI-716633
PPP1R9BQ96SB35EBI-357253,EBI-351275
PTENP604842EBI-357253,EBI-696162
RB1P064002EBI-357253,EBI-491274
RL1P363134EBI-357253,EBI-6149234From a different organism.
SFI1A8K8P32EBI-357253,EBI-743371
SGO2Q562F64EBI-357253,EBI-989213
SH2D4AQ9H7882EBI-357253,EBI-747035
SH3RF2Q8TEC53EBI-357253,EBI-2130111
SKP1P632083EBI-357253,EBI-307486
SPRED1Q7Z6994EBI-357253,EBI-5235340
SYTL2Q9HCH52EBI-357253,EBI-2690103
TMEM132DQ14C872EBI-357253,EBI-5235567
TP53BP2Q136257EBI-357253,EBI-77642
TRPC4APQ8TEL62EBI-357253,EBI-2559060
TSC2P498152EBI-357253,EBI-396587
WBP11Q9Y2W23EBI-357253,EBI-714455
WNK1Q9H4A32EBI-357253,EBI-457907
ZFYVE1Q9HBF42EBI-357253,EBI-4401611
ZFYVE9O954053EBI-357253,EBI-296817

Protein-protein interaction databases

BioGridi111493. 309 interactors.
DIPiDIP-221N.
DIP-38195N.
IntActiP62136. 273 interactors.
MINTiMINT-5001223.
STRINGi9606.ENSP00000326031.

Chemistry databases

BindingDBiP62136.

Structurei

Secondary structure

1330
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 18Combined sources10
Turni19 – 21Combined sources3
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 – 171Combined sources3
Helixi184 – 187Combined sources4
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
Helixi272 – 274Combined 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
3E7AX-ray1.63A/B7-300[»]
3E7BX-ray1.70A/B7-300[»]
3EGGX-ray1.85A/B7-330[»]
3EGHX-ray2.00A/B7-330[»]
3HVQX-ray2.20A/B7-330[»]
3N5UX-ray3.20A/B1-300[»]
3V4YX-ray2.10A/C/E/G7-307[»]
4G9JX-ray3.10A/B1-330[»]
4MOVX-ray1.45A/B7-300[»]
4MOYX-ray2.20A7-300[»]
4MP0X-ray2.10A/C7-300[»]
4XPNX-ray2.29A/C7-300[»]
5IOHX-ray2.57A/C7-300[»]
ProteinModelPortaliP62136.
SMRiP62136.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62136.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410IN85. Eukaryota.
ENOG410XPVF. LUCA.
GeneTreeiENSGT00530000062911.
HOGENOMiHOG000172697.
HOVERGENiHBG000216.
InParanoidiP62136.
KOiK06269.
OMAiGKFLHKH.
OrthoDBiEOG091G0EKF.
PhylomeDBiP62136.
TreeFamiTF354243.

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 (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P62136-1) [UniParc]FASTAAdd to basket

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 2 (identifier: P62136-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     18-18: E → EGSRVLTPHCAP

Note: No experimental confirmation available.
Show »
Length:341
Mass (Da):38,631
Checksum:iCE50F8B9DC84AB6F
GO
Isoform 3 (identifier: P62136-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     19-62: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:286
Mass (Da):32,595
Checksum:iE0560E7C422C353C
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04337718E → EGSRVLTPHCAP in isoform 2. 1 Publication1
Alternative sequenceiVSP_04675419 – 62Missing in isoform 3. CuratedAdd BLAST44

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70848 mRNA. Translation: CAA50197.1.
S57501 mRNA. Translation: AAB26015.1.
M63960 mRNA. Translation: AAA36508.1.
AK313586 mRNA. Translation: BAG36355.1.
BT006629 mRNA. Translation: AAP35275.1.
AP003419 Genomic DNA. No translation available.
BC001888 mRNA. Translation: AAH01888.1.
BC004482 mRNA. Translation: AAH04482.1.
BC008010 mRNA. Translation: AAH08010.1.
J04759 mRNA. Translation: AAA36475.1.
CCDSiCCDS31618.1. [P62136-2]
CCDS8160.1. [P62136-1]
CCDS8161.1. [P62136-3]
RefSeqiNP_001008709.1. NM_001008709.1. [P62136-2]
NP_002699.1. NM_002708.3. [P62136-1]
NP_996756.1. NM_206873.1. [P62136-3]
UniGeneiHs.183994.

Genome annotation databases

EnsembliENST00000312989; ENSP00000326031; ENSG00000172531. [P62136-2]
ENST00000358239; ENSP00000350974; ENSG00000172531. [P62136-3]
ENST00000376745; ENSP00000365936; ENSG00000172531. [P62136-1]
GeneIDi5499.
KEGGihsa:5499.
UCSCiuc001oku.2. human. [P62136-1]

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
X70848 mRNA. Translation: CAA50197.1.
S57501 mRNA. Translation: AAB26015.1.
M63960 mRNA. Translation: AAA36508.1.
AK313586 mRNA. Translation: BAG36355.1.
BT006629 mRNA. Translation: AAP35275.1.
AP003419 Genomic DNA. No translation available.
BC001888 mRNA. Translation: AAH01888.1.
BC004482 mRNA. Translation: AAH04482.1.
BC008010 mRNA. Translation: AAH08010.1.
J04759 mRNA. Translation: AAA36475.1.
CCDSiCCDS31618.1. [P62136-2]
CCDS8160.1. [P62136-1]
CCDS8161.1. [P62136-3]
RefSeqiNP_001008709.1. NM_001008709.1. [P62136-2]
NP_002699.1. NM_002708.3. [P62136-1]
NP_996756.1. NM_206873.1. [P62136-3]
UniGeneiHs.183994.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3E7AX-ray1.63A/B7-300[»]
3E7BX-ray1.70A/B7-300[»]
3EGGX-ray1.85A/B7-330[»]
3EGHX-ray2.00A/B7-330[»]
3HVQX-ray2.20A/B7-330[»]
3N5UX-ray3.20A/B1-300[»]
3V4YX-ray2.10A/C/E/G7-307[»]
4G9JX-ray3.10A/B1-330[»]
4MOVX-ray1.45A/B7-300[»]
4MOYX-ray2.20A7-300[»]
4MP0X-ray2.10A/C7-300[»]
4XPNX-ray2.29A/C7-300[»]
5IOHX-ray2.57A/C7-300[»]
ProteinModelPortaliP62136.
SMRiP62136.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111493. 309 interactors.
DIPiDIP-221N.
DIP-38195N.
IntActiP62136. 273 interactors.
MINTiMINT-5001223.
STRINGi9606.ENSP00000326031.

Chemistry databases

BindingDBiP62136.
ChEMBLiCHEMBL2164.

PTM databases

DEPODiP62136.
iPTMnetiP62136.
PhosphoSitePlusiP62136.
SwissPalmiP62136.

Polymorphism and mutation databases

BioMutaiPPP1CA.
DMDMi49065811.

2D gel databases

OGPiP08129.

Proteomic databases

EPDiP62136.
MaxQBiP62136.
PaxDbiP62136.
PeptideAtlasiP62136.
PRIDEiP62136.
TopDownProteomicsiP62136-1. [P62136-1]

Protocols and materials databases

DNASUi5499.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312989; ENSP00000326031; ENSG00000172531. [P62136-2]
ENST00000358239; ENSP00000350974; ENSG00000172531. [P62136-3]
ENST00000376745; ENSP00000365936; ENSG00000172531. [P62136-1]
GeneIDi5499.
KEGGihsa:5499.
UCSCiuc001oku.2. human. [P62136-1]

Organism-specific databases

CTDi5499.
DisGeNETi5499.
GeneCardsiPPP1CA.
HGNCiHGNC:9281. PPP1CA.
HPAiCAB004545.
HPA046833.
MIMi176875. gene.
neXtProtiNX_P62136.
OpenTargetsiENSG00000172531.
PharmGKBiPA33609.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IN85. Eukaryota.
ENOG410XPVF. LUCA.
GeneTreeiENSGT00530000062911.
HOGENOMiHOG000172697.
HOVERGENiHBG000216.
InParanoidiP62136.
KOiK06269.
OMAiGKFLHKH.
OrthoDBiEOG091G0EKF.
PhylomeDBiP62136.
TreeFamiTF354243.

Enzyme and pathway databases

BioCyciZFISH:HS10534-MONOMER.
BRENDAi3.1.3.16. 2681.
ReactomeiR-HSA-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-HSA-180024. DARPP-32 events.
R-HSA-2173788. Downregulation of TGF-beta receptor signaling.
R-HSA-400253. Circadian Clock.
SignaLinkiP62136.
SIGNORiP62136.

Miscellaneous databases

ChiTaRSiPPP1CA. human.
EvolutionaryTraceiP62136.
GeneWikiiPPP1CA.
GenomeRNAii5499.
PROiP62136.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000172531.
CleanExiHS_PPP1CA.
ExpressionAtlasiP62136. baseline and differential.
GenevisibleiP62136. HS.

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.
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Entry informationi

Entry nameiPP1A_HUMAN
AccessioniPrimary (citable) accession number: P62136
Secondary accession number(s): A6NNR3
, B2R908, P08129, P20653, P22802, Q07161
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: June 21, 2004
Last modified: November 30, 2016
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  5. 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.