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Nuclear inhibitor of protein phosphatase 1 (NIPP-1) (Protein phosphatase 1 regulatory inhibitor subunit 8)

 PP1R8_BOVIN             Reviewed;         351 AA.
Q28147;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-FEB-2018, entry version 122.
RecName: Full=Nuclear inhibitor of protein phosphatase 1;
Short=NIPP-1;
AltName: Full=Protein phosphatase 1 regulatory inhibitor subunit 8;
Name=PPP1R8; Synonyms=NIPP1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, PROTEIN SEQUENCE OF
163-171 AND 196-208, BLOCKAGE OF N-TERMINUS, SUBCELLULAR LOCATION, AND
PHOSPHORYLATION AT SER-199.
TISSUE=Thymus;
PubMed=7499293; DOI=10.1074/jbc.270.47.28068;
Van Eynde A., Wera S., Beullens M., Torrekens S., Van Leuven F.,
Stalmans W., Bollen M.;
"Molecular cloning of NIPP-1, a nuclear inhibitor of protein
phosphatase-1, reveals homology with polypeptides involved in RNA
processing.";
J. Biol. Chem. 270:28068-28074(1995).
[2]
PROTEIN SEQUENCE OF 152-191 AND 197-221, CHARACTERIZATION,
PHOSPHORYLATION AT THR-161; SER-178; SER-199 AND SER-204, LACK OF
PHOSPHORYLATION AT THR-202 AND THR-346, AND MASS SPECTROMETRY.
PubMed=9407077; DOI=10.1074/jbc.272.52.32972;
Vulsteke V., Beullens M., Waelkens E., Stalmans W., Bollen M.;
"Properties and phosphorylation sites of baculovirus-expressed nuclear
inhibitor of protein phosphatase-1 (NIPP-1).";
J. Biol. Chem. 272:32972-32978(1997).
[3]
RNA-BINDING, AND FUNCTION.
PubMed=9268347; DOI=10.1074/jbc.272.35.22067;
Jagiello I., Beullens M., Vulsteke V., Wera S., Sohlberg B.,
Stalmans W., von Gabain A., Bollen M.;
"NIPP-1, a nuclear inhibitory subunit of protein phosphatase-1, has
RNA-binding properties.";
J. Biol. Chem. 272:22067-22071(1997).
[4]
DOMAIN PP-1 BINDING, SYNTHESIS OF PEPTIDES IN THE 141-230 REGION, AND
PHOSPHORYLATION AT SER-204.
PubMed=10318819; DOI=10.1074/jbc.274.20.14053;
Beullens M., Van Eynde A., Vulsteke V., Connor J., Shenolikar S.,
Stalmans W., Bollen M.;
"Molecular determinants of nuclear protein phosphatase-1 regulation by
NIPP-1.";
J. Biol. Chem. 274:14053-14061(1999).
-!- 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. {ECO:0000269|PubMed:9268347}.
-!- SUBUNIT: Interacts with phosphorylated CDC5L, SF3B1 and MELK.
Interacts with EED. Part of a complex consisting of PPP1R8, EED,
HDAC2 and PP-1. Part of the spliceosome. Interacts with PPP1CA,
PPP1CB and PPP1CC (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle
{ECO:0000250}. Note=Mainly, but not exclusively, nuclear.
{ECO:0000269|PubMed:7499293}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A;
IsoId=Q28147-1; Sequence=Displayed;
Name=B;
IsoId=Q28147-2; Sequence=VSP_005118;
-!- DOMAIN: Has a basic N- and C-terminal and an acidic central
domain. {ECO:0000269|PubMed:10318819}.
-!- DOMAIN: The FHA domain mediates interactions with threonine-
phosphorylated MELK. {ECO:0000250}.
-!- PTM: The N-terminus is blocked.
-!- PTM: Inactivated by phosphorylation on Ser-199 or Ser-204.
{ECO:0000305|PubMed:10318819, ECO:0000305|PubMed:7499293,
ECO:0000305|PubMed:9407077}.
-!- MASS SPECTROMETRY: Mass=38520; Method=Electrospray; Range=1-351;
Note=Expressed in baculovirus.;
Evidence={ECO:0000269|PubMed:9407077};
-!- MISCELLANEOUS: A synthetic peptide, NIPP-1(191-200), is able to
inhibit PP-1. Alanine substitution of Val-201 and Phe-203 in NIPP-
1(191-210) prevents PP-1 binding (far-western assay) but do not
affect PP-1 inhibition. Phosphorylation of Ser-199 or Ser-204
prevents PP-1 binding (far-western assay) and reduces PP-1
inhibition.
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EMBL; Z50748; CAA90625.1; -; mRNA.
PIR; I46033; I46033.
RefSeq; NP_777007.1; NM_174582.2. [Q28147-1]
UniGene; Bt.22; -.
ProteinModelPortal; Q28147; -.
SMR; Q28147; -.
BioGrid; 159581; 4.
DIP; DIP-438N; -.
STRING; 9913.ENSBTAP00000005043; -.
iPTMnet; Q28147; -.
PaxDb; Q28147; -.
PRIDE; Q28147; -.
GeneID; 282319; -.
KEGG; bta:282319; -.
CTD; 5511; -.
eggNOG; KOG1880; Eukaryota.
eggNOG; ENOG410XTHZ; LUCA.
HOGENOM; HOG000231315; -.
HOVERGEN; HBG053645; -.
InParanoid; Q28147; -.
KO; K13216; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IBA:GO_Central.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0035308; P:negative regulation of protein dephosphorylation; IBA:GO_Central.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00060; FHA; 1.
InterPro; IPR000253; FHA_dom.
InterPro; IPR008984; SMAD_FHA_dom_sf.
Pfam; PF00498; FHA; 1.
SMART; SM00240; FHA; 1.
SUPFAM; SSF49879; SSF49879; 1.
PROSITE; PS50006; FHA_DOMAIN; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Direct protein sequencing;
DNA-binding; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
Protein phosphatase inhibitor; Reference proteome; Repressor;
RNA-binding; Spliceosome; Transcription; Transcription regulation.
CHAIN 1 351 Nuclear inhibitor of protein phosphatase
1.
/FTId=PRO_0000071504.
DOMAIN 49 101 FHA. {ECO:0000255|PROSITE-
ProRule:PRU00086}.
REGION 1 142 Interaction with CDC5L, SF3B1 and MELK.
{ECO:0000250}.
REGION 143 224 Interaction with EED. {ECO:0000250}.
REGION 191 200 Involved in PP-1 inhibition.
REGION 200 203 Involved in PP-1 binding.
REGION 310 329 Interaction with EED. {ECO:0000250}.
REGION 330 351 RNA-binding. {ECO:0000250}.
REGION 331 337 Involved in PP-1 inhibition.
{ECO:0000250}.
MOTIF 185 209 Nuclear localization signal 1.
{ECO:0000250}.
MOTIF 210 240 Nuclear localization signal 2.
{ECO:0000250}.
SITE 202 202 Not phosphorylated.
{ECO:0000269|PubMed:9407077}.
SITE 346 346 Not phosphorylated.
{ECO:0000269|PubMed:9407077}.
MOD_RES 161 161 Phosphothreonine; by CK2; in vitro.
{ECO:0000269|PubMed:9407077}.
MOD_RES 178 178 Phosphoserine; by PKA; in vitro.
{ECO:0000269|PubMed:9407077}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000269|PubMed:7499293,
ECO:0000269|PubMed:9407077}.
MOD_RES 204 204 Phosphoserine.
{ECO:0000305|PubMed:10318819,
ECO:0000305|PubMed:9407077}.
MOD_RES 249 249 Phosphoserine.
{ECO:0000250|UniProtKB:Q12972}.
MOD_RES 264 264 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q12972}.
MOD_RES 335 335 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q12972}.
VAR_SEQ 1 142 Missing (in isoform B). {ECO:0000305}.
/FTId=VSP_005118.
SEQUENCE 351 AA; 38521 MW; 7CD5F6E162A66210 CRC64;
MAAAANSGSS LPLFDCPTWA GKPPPGLHLD VVKGDKLIEK LIIDEKKYYL FGRNPDLCDF
TIDHQSCSRV HAALVYHKHL KRVFLIDLNS THGTFLGHIR LEPHKPQQIP IDSTVSFGAS
TRAYTLREKP QTLPSAVKGD EKMGGEDDEL KGLLGLPEEE TELDNLTEFN TAHNKRISTL
TIEEGNLDIQ RPKRKRKNSR VTFSEDDEII NPEDVDPSVG RFRNMVQTAV VPVKKKRVEG
PGSLVLEESG SRRMQNFAFS GGLYGGLPPT HSEAGSQPHG IHGTALIGGL PMPYPNLAPD
VDLTPVVPSA VNMNPAPNPA VYNPEAVNEP KKKKYAKEAW PGKKPTPSLL I


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