PPP1R8
entrez
5511
canonical
uniprot
Q12972
canonical
ensembl
ENSG00000117751
resolver
ensp
ENSP00000236412
resolver
ensp
ENSP00000311677
resolver
ensp
ENSP00000363042
resolver
genesymbol
PPP1R8
resolver
genesymbol_syn
ARD1
resolver
genesymbol_syn
NIPP1
resolver
hgnc
HGNC:9296
resolver
uniprot
Q5TEJ2
resolver
uniprot
Q5TEJ4
resolver
uniprot
Q5TIF2
resolver
uniprot
Q6ICT4
resolver
uniprot
Q6PKF6
resolver
uniprot
Q9UBH1
resolver
uniprot
Q9UBZ0
resolver
uniprot_entry
PP1R8_HUMAN
resolver
uniprot_entry
Q6ICT4_HUMAN
resolver
uniprot_sec
Q5TEJ2
resolver
uniprot_sec
Q5TEJ4
resolver
uniprot_sec
Q5TIF2
resolver
uniprot_sec
Q6PKF6
resolver
uniprot_sec
Q9UBH1
resolver
uniprot_sec
Q9UBZ0
resolver
amino_acid_sequence
MAAAANSGSSLPLFDCPTWAGKPPPGLHLDVVKGDKLIEKLIIDEKKYYLFGRNPDLCDFTIDHQSCSRVHAALVYHKHLKRVFLIDLNSTHGTFLGHIRLEPHKPQQIPIDSTVSFGASTRAYTLREKPQTLPSAVKGDEKMGGEDDELKGLLGLPEEETELDNLTEFNTAHNKRISTLTIEEGNLDIQRPKRKRKNSRVTFSEDDEIINPEDVDPSVGRFRNMVQTAVVPVKKKRVEGPGSLGLEESGSRRMQNFAFSGGLYGGLPPTHSEAGSQPHGIHGTALIGGLPMPYPNLAPDVDLTPVVPSAVNMNPAPNPAVYNPEAVNEPKKKKYAKEAWPGKKPTPSLLI
uniprot
proteins
ec_number
3.1.4.-
uniprot
proteins
function
FUNCTION: Inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. May also be involved in pre-mRNA splicing. Binds DNA and might act as a transcriptional repressor. Seems to be required for cell proliferation.; FUNCTION: Isoform Gamma is a site-specific single-strand endoribonuclease that cleaves single strand RNA 3' to purines and pyrimidines in A+U-rich regions. It generates 5'-phosphate termini at the site of cleavage. This isoform does not inhibit PP-1. May be implicated in mRNA splicing.
uniprot
proteins
mass_dalton
38479
uniprot
proteins
mutagenesis
MUTAGEN 68..71; /note="SRVH->AAAA: Abolishes interaction with CDC5L, SF3B1 and MELK, and localization in nuclear speckles. No effect on repressor activity."; /evidence="ECO:0000269|PubMed:10827081, ECO:0000269|PubMed:11034904, ECO:0000269|PubMed:12105215, ECO:0000269|PubMed:12788942, ECO:0000269|PubMed:14699119"; MUTAGEN 193..197; /note="KRKRK->AAAAA: No effect on interaction with EED."; /evidence="ECO:0000269|PubMed:12788942"; MUTAGEN 195..197; /note="KRK->AAA: Abolishes nuclear import; when associated with A-234--237-A."; /evidence="ECO:0000269|PubMed:11034904"; MUTAGEN 199; /note="S->A,D: No change in subcellular location, no effect on interaction with EED or repressor activity; when associated with A-204 or D-204."; /evidence="ECO:0000269|PubMed:11034904, ECO:0000269|PubMed:12788942"; MUTAGEN 201; /note="V->A: Reduces PP-1 binding, no effect on subcellular location or repressor activity and prevents retargeting of PPP1CA and PPP1CC to nuclear speckles; when associated with A-203."; /evidence="ECO:0000269|PubMed:11034904, ECO:0000269|PubMed:11739654, ECO:0000269|PubMed:12788942"; MUTAGEN 203; /note="F->A: Reduces PP-1 binding, no effect on subcellular location or repressor activity and prevents retargeting of PPP1CA and PPP1CC to nuclear speckles; when associated with A-201."; /evidence="ECO:0000269|PubMed:11034904, ECO:0000269|PubMed:11739654, ECO:0000269|PubMed:12788942"; MUTAGEN 204; /note="S->A,D: No change in subcellular location, no effect on interaction with EED or repressor activity; when associated with A-199 or D-199."; /evidence="ECO:0000269|PubMed:11034904, ECO:0000269|PubMed:12788942"; MUTAGEN 234..237; /note="KKKR->AAAA: Abolishes nuclear import; when associated with A-195-197-A."; /evidence="ECO:0000269|PubMed:11034904"; MUTAGEN 264; /note="Y->D: Abolishes in vitro phosphorylation of isoform gamma by Lyn."; /evidence="ECO:0000269|PubMed:11104670"; MUTAGEN 335; /note="Y->D: Decreases the ability of isoform Gamma to bind and inhibit PP-1."; /evidence="ECO:0000269|PubMed:11104670"; MUTAGEN 346; /note="T->D: No effect on the ability of isoform Gamma to inhibit PP-1."; /evidence="ECO:0000269|PubMed:11104670"; MUTAGEN 348; /note="S->D: No effect on the ability of isoform Gamma to inhibit PP-1."; /evidence="ECO:0000269|PubMed:11104670
uniprot
proteins
post_translational_modification
PTM: May be inactivated by phosphorylation on Ser-199 or Ser-204 (By similarity). Phosphorylated by Lyn in vitro on Tyr-264, and also on Tyr-335 in the presence of RNA. {ECO:0000250, ECO:0000269|PubMed:11104670}.
uniprot
proteins
pubmed
10103062
uniprot
proteins
pubmed
10432294
uniprot
proteins
pubmed
10564811
uniprot
proteins
pubmed
10827081
uniprot
proteins
pubmed
11034904
uniprot
proteins
pubmed
11104670
uniprot
proteins
pubmed
11739654
uniprot
proteins
pubmed
11909864
uniprot
proteins
pubmed
12105215
uniprot
proteins
pubmed
12788942
uniprot
proteins
pubmed
14699119
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20516061
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
7499293
uniprot
proteins
pubmed
7524097
uniprot
proteins
pubmed
9153239
uniprot
proteins
sequence_length
351
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Note=Primarily, but not exclusively, nuclear.; SUBCELLULAR LOCATION: [Isoform Gamma]: Cytoplasm. Note=Found mainly in the cytoplasm.
uniprot
proteins