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Q12972 (PP1R8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear inhibitor of protein phosphatase 1

Short name=NIPP-1
Alternative name(s):
Protein phosphatase 1 regulatory inhibitor subunit 8

Including the following 1 domains:

  1. Activator of RNA decay
    EC=3.1.4.-
    Alternative name(s):
    ARD-1
Gene names
Name:PPP1R8
Synonyms:ARD1, NIPP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length351 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.10 Ref.12 Ref.13 Ref.16 Ref.18

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 doesnot inhibit PP-1. May be implicated in mRNA splicing. Ref.10 Ref.12 Ref.13 Ref.16 Ref.18

Cofactor

Magnesium. Endoribonuclease function is magnesium-dependent.

Subunit structure

Interacts with phosphorylated CDC5L, SF3B1 and MELK. Interacts with EED, in a nucleic acid-stimulated manner. Part of a complex consisting of PPP1R8, EED, HDAC2 and PP-1. Part of the spliceosome. Interacts with PPP1CA, PPP1CB and PPP1CC. Ref.13 Ref.15 Ref.17 Ref.18 Ref.19 Ref.21

Subcellular location

Nucleus. Nucleus speckle. Note: Primarily, but not exclusively, nuclear. Ref.13 Ref.14 Ref.15

Isoform Gamma: Cytoplasm. Note: Found mainly in the cytoplasm. Ref.13 Ref.14 Ref.15

Tissue specificity

Ubiquitously expressed, with highest levels in heart and skeletal muscle, followed by brain, placenta, lung, liver and pancreas. Less abundant in kidney. The concentration and ratio between isoforms is cell-type dependent. Isoform Alpha (>90%) and isoform Beta were found in brain, heart and kidney. Isoform Gamma is mainly found in B-cells and T-lymphocytes, and has been found in 293 embryonic kidney cells. Ref.2 Ref.8

Domain

Has a basic N- and C-terminal and an acidic central domain.

The FHA domain mediates interactions with threonine-phosphorylated MELK By similarity.

Post-translational modification

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. Ref.12

Miscellaneous

A synthetic peptide, NIPP-1(330-351), is able to inhibit PP-1. Phosphorylation of Tyr-335 reduces PP-1 inhibition, whereas phosphorylation of Thr-346 or Ser-348 has no effect.

Sequence similarities

Contains 1 FHA domain.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
Spliceosome
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandDNA-binding
Magnesium
RNA-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
Protein phosphatase inhibitor
Repressor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA catabolic process

Traceable author statement Ref.9. Source: ProtInc

RNA phosphodiester bond hydrolysis

Traceable author statement Ref.9. Source: GOC

RNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

cell proliferation

Inferred from electronic annotation. Source: Ensembl

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of catalytic activity

Traceable author statement Ref.8. Source: GOC

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear speck

Inferred from direct assay Ref.15. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

spliceosomal complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Traceable author statement Ref.9. Source: ProtInc

endonuclease activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein phosphatase type 1 regulator activity

Inferred from electronic annotation. Source: Ensembl

protein serine/threonine phosphatase inhibitor activity

Traceable author statement Ref.8. Source: ProtInc

ribonuclease E activity

Traceable author statement Ref.9. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PPP1CAP621363EBI-716633,EBI-357253

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform Alpha (identifier: Q12972-1)

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.
Isoform Beta (identifier: Q12972-2)

Also known as: Delta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-142: Missing.
Isoform Gamma (identifier: Q12972-3)

Also known as: ARD-1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-224: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 351351Nuclear inhibitor of protein phosphatase 1
PRO_0000071505

Regions

Domain49 – 10153FHA
Region1 – 142142Interaction with CDC5L, SF3B1 and MELK
Region143 – 22482Interaction with EED
Region191 – 20010Involved in PP-1 inhibition
Region200 – 2034Involved in PP-1 binding
Region310 – 32920Interaction with EED
Region330 – 35122RNA-binding
Region331 – 3377Involved in PP-1 inhibition
Motif185 – 20925Nuclear localization signal 1 Ref.14
Motif210 – 24031Nuclear localization signal 2 Ref.14

Amino acid modifications

Modified residue1611Phosphothreonine By similarity
Modified residue1781Phosphoserine By similarity
Modified residue1991Phosphoserine By similarity
Modified residue2641Phosphotyrosine; by LYN; in vitro Ref.12
Modified residue3351Phosphotyrosine Probable

Natural variations

Alternative sequence1 – 224224Missing in isoform Gamma.
VSP_005120
Alternative sequence1 – 142142Missing in isoform Beta.
VSP_005119

Experimental info

Mutagenesis68 – 714SRVH → AAAA: Abolishes interaction with CDC5L, SF3B1 and MELK, and localization in nuclear speckles. No effect on repressor activity. Ref.13 Ref.14 Ref.17 Ref.18 Ref.19
Mutagenesis193 – 1975KRKRK → AAAAA: No effect on interaction with EED. Ref.18
Mutagenesis195 – 1973KRK → AAA: Abolishes nuclear import; when associated with A-234--237-A. Ref.14
Mutagenesis1991S → A or D: No change in subcellular location, no effect on interaction with EED or repressor activity; when associated with A-204 or D-204. Ref.14 Ref.18
Mutagenesis2011V → 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. Ref.14 Ref.15 Ref.18
Mutagenesis2031F → 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. Ref.14 Ref.15 Ref.18
Mutagenesis2041S → A or D: No change in subcellular location, no effect on interaction with EED or repressor activity; when associated with A-199 or D-199. Ref.14 Ref.18
Mutagenesis234 – 2374KKKR → AAAA: Abolishes nuclear import; when associated with A-195-197-A. Ref.14
Mutagenesis2641Y → D: Abolishes in vitro phosphorylation of isoform gamma by Lyn. Ref.12
Mutagenesis3351Y → D: Decreases the ability of isoform Gamma to bind and inhibit PP-1. Ref.12
Mutagenesis3461T → D: No effect on the ability of isoform Gamma to inhibit PP-1. Ref.12
Mutagenesis3481S → D: No effect on the ability of isoform Gamma to inhibit PP-1. Ref.12

Secondary structure

..... 351
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 0A0E92B033E37641

FASTA35138,479
        10         20         30         40         50         60 
MAAAANSGSS LPLFDCPTWA GKPPPGLHLD VVKGDKLIEK LIIDEKKYYL FGRNPDLCDF 

        70         80         90        100        110        120 
TIDHQSCSRV HAALVYHKHL KRVFLIDLNS THGTFLGHIR LEPHKPQQIP IDSTVSFGAS 

       130        140        150        160        170        180 
TRAYTLREKP QTLPSAVKGD EKMGGEDDEL KGLLGLPEEE TELDNLTEFN TAHNKRISTL 

       190        200        210        220        230        240 
TIEEGNLDIQ RPKRKRKNSR VTFSEDDEII NPEDVDPSVG RFRNMVQTAV VPVKKKRVEG 

       250        260        270        280        290        300 
PGSLGLEESG SRRMQNFAFS GGLYGGLPPT HSEAGSQPHG IHGTALIGGL PMPYPNLAPD 

       310        320        330        340        350 
VDLTPVVPSA VNMNPAPNPA VYNPEAVNEP KKKKYAKEAW PGKKPTPSLL I 

« Hide

Isoform Beta (Delta) [UniParc].

Checksum: B8A896191A4AB026
Show »

FASTA20922,711
Isoform Gamma (ARD-1) [UniParc].

Checksum: D29E123EA36C9F94
Show »

FASTA12713,344

References

« Hide 'large scale' references
[1]"ard-1: a human gene that reverses the effects of temperature-sensitive and deletion mutations in the Escherichia coli rne gene and encodes an activity producing RNase E-like cleavages."
Wang M., Cohen S.N.
Proc. Natl. Acad. Sci. U.S.A. 91:10591-10595(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA).
Tissue: B-cell.
[2]"Organization and alternate splice products of the gene encoding nuclear inhibitor of protein phosphatase-1 (NIPP-1)."
Van Eynde A., Perez-Callejon E., Schoenmakers E., Jacquemin M., Stalmans W., Bollen M.
Eur. J. Biochem. 261:291-300(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS ALPHA AND BETA), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
Tissue: Parathyroid and T-cell.
[3]"Complete cDNA sequence of NIPP-1 from human breast cancer cells."
Liu J.P., Yang Z., Li H.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
Tissue: Mammary cancer.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
Tissue: Synovium.
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-351 (ISOFORM ALPHA).
Tissue: Lymph.
[8]"Molecular cloning of NIPP-1, a nuclear inhibitor of protein phosphatase-1, reveals homology with polypeptides involved in RNA processing."
Van Eynde A., Wera S., Beullens M., Torrekens S., Van Leuven F., Stalmans W., Bollen M.
J. Biol. Chem. 270:28068-28074(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[9]"ARD-1 cDNA from human cells encodes a site-specific single-strand endoribonuclease that functionally resembles Escherichia coli RNase E."
Claverie-Martin F., Wang M., Cohen S.N.
J. Biol. Chem. 272:13823-13828(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION (ISOFORM GAMMA).
[10]"Mapping of the RNA-binding and endoribonuclease domains of NIPP1, a nuclear targeting subunit of protein phosphatase 1."
Jin Q., Beullens M., Jagiello I., Van Eynde A., Vulsteke V., Stalmans W., Bollen M.
Biochem. J. 342:13-19(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING, CHARACTERIZATION (ISOFORM GAMMA), FUNCTION.
[11]"Alternative splicing regulates the production of ARD-1 endoribonuclease and NIPP-1, an inhibitor of protein phosphatase-1, as isoforms encoded by the same gene."
Chang A.C.Y., Sohlberg B., Trinkle-Mulcahy L., Claverie-Martin F., Cohen P., Cohen S.N.
Gene 240:45-55(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF ALTERNATIVE SPLICING IN ISOFORM GAMMA.
[12]"The C-terminus of NIPP1 (nuclear inhibitor of protein phosphatase-1) contains a novel binding site for protein phosphatase-1 that is controlled by tyrosine phosphorylation and RNA binding."
Beullens M., Vulsteke V., Van Eynde A., Jagiello I., Stalmans W., Bollen M.
Biochem. J. 352:651-658(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF TYR-264; TYR-335; THR-346 AND SER-348, PHOSPHORYLATION AT TYR-264 AND TYR-335.
[13]"NIPP1-mediated interaction of protein phosphatase-1 with CDC5L, a regulator of pre-mRNA splicing and mitotic entry."
Boudrez A., Beullens M., Groenen P.M.A., Van Eynde A., Vulsteke V., Jagiello I., Murray M., Krainer A.R., Stalmans W., Bollen M.
J. Biol. Chem. 275:25411-25417(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDC5L, SUBCELLULAR LOCATION, MUTAGENESIS OF 68-SER--HIS-71, FUNCTION.
[14]"Nuclear and subnuclear targeting sequences of the protein phosphatase-1 regulator NIPP1."
Jagiello I., Van Eynde A., Vulsteke V., Beullens M., Boudrez A., Keppens S., Stalmans W., Bollen M.
J. Cell Sci. 113:3761-3768(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEAR LOCALIZATION SIGNALS, MUTAGENESIS OF 68-SER--HIS-71; 195-LYS--LYS-197; SER-199; VAL-201; PHE-203; SER-204 AND 234-LYS--ARG-237, SUBCELLULAR LOCATION.
[15]"Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells."
Trinkle-Mulcahy L., Sleeman J.E., Lamond A.I.
J. Cell Sci. 114:4219-4228(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PPP1CA AND PPP1CC, MUTAGENESIS OF VAL-201 AND PHE-203.
[16]"The protein phosphatase-1 regulator NIPP1 is also a splicing factor involved in a late step of spliceosome assembly."
Beullens M., Bollen M.
J. Biol. Chem. 277:19855-19860(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS PART OF THE SPLICEOSOME, FUNCTION.
[17]"Phosphorylation-dependent interaction between the splicing factors SAP155 and NIPP1."
Boudrez A., Beullens M., Waelkens E., Stalmans W., Bollen M.
J. Biol. Chem. 277:31834-31841(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SF3B1, MUTAGENESIS OF 68-SER--HIS-71.
[18]"The protein phosphatase-1 (PP1) regulator, nuclear inhibitor of PP1 (NIPP1), interacts with the polycomb group protein, embryonic ectoderm development (EED), and functions as a transcriptional repressor."
Jin Q., van Eynde A., Beullens M., Roy N., Thiel G., Stalmans W., Bollen M.
J. Biol. Chem. 278:30677-30685(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING, INTERACTION WITH EED, IDENTIFICATION IN A COMPLEX WITH EED; HDAC2 AND PP1, MUTAGENESIS OF 68-SER--HIS-71; 193-LYS--LYS-197; SER-199; VAL-201; PHE-203 AND SER-204, FUNCTION.
[19]"Inhibition of spliceosome assembly by the cell cycle-regulated protein kinase MELK and involvement of splicing factor NIPP1."
Vulsteke V., Beullens M., Boudrez A., Keppens S., Van Eynde A., Rider M.H., Stalmans W., Bollen M.
J. Biol. Chem. 279:8642-8647(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MELK, MUTAGENESIS OF 68-SER--HIS-71.
[20]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"Identification and characterization of a novel human PP1 phosphatase complex."
Lee J.H., You J., Dobrota E., Skalnik D.G.
J. Biol. Chem. 285:24466-24476(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP1CA; PPP1CB AND PPP1CC.
[22]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14575 mRNA. Translation: AAA64749.1.
AF061958 mRNA. Translation: AAD31541.1.
AF061959 mRNA. Translation: AAD31542.1.
AF064757 expand/collapse EMBL AC list , AF064751, AF064752, AF064753, AF064754, AF064755, AF064756 Genomic DNA. Translation: AAD24669.1.
AF064757 expand/collapse EMBL AC list , AF064754, AF064755, AF064756 Genomic DNA. Translation: AAD24670.1.
AF126488 mRNA. Translation: AAD22486.1.
AK292077 mRNA. Translation: BAF84766.1.
AL020997, AL109927 Genomic DNA. Translation: CAI20576.1.
AL020997, AL109927 Genomic DNA. Translation: CAI20577.1.
AL020997, AL109927 Genomic DNA. Translation: CAI20578.1.
AL109927, AL020997 Genomic DNA. Translation: CAI21779.1.
AL109927, AL020997 Genomic DNA. Translation: CAI21780.1.
AL109927, AL020997 Genomic DNA. Translation: CAI21781.1.
CH471059 Genomic DNA. Translation: EAX07731.1.
CH471059 Genomic DNA. Translation: EAX07732.1.
BC001597 mRNA. Translation: AAH01597.1.
BC013360 mRNA. Translation: AAH13360.1.
PIRI38856.
RefSeqNP_002704.1. NM_002713.3.
NP_054829.2. NM_014110.4.
NP_612568.1. NM_138558.2.
UniGeneHs.533474.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3V4YX-ray2.10B/D/F/H158-216[»]
ProteinModelPortalQ12972.
SMRQ12972. Positions 1-132, 158-212.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111503. 29 interactions.
DIPDIP-40815N.
IntActQ12972. 15 interactions.
MINTMINT-133673.
STRING9606.ENSP00000311677.

PTM databases

PhosphoSiteQ12972.

Polymorphism databases

DMDM19863082.

Proteomic databases

PaxDbQ12972.
PeptideAtlasQ12972.
PRIDEQ12972.

Protocols and materials databases

DNASU5511.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000236412; ENSP00000236412; ENSG00000117751. [Q12972-3]
ENST00000311772; ENSP00000311677; ENSG00000117751. [Q12972-1]
ENST00000373931; ENSP00000363042; ENSG00000117751. [Q12972-2]
GeneID5511.
KEGGhsa:5511.
UCSCuc001bov.2. human. [Q12972-1]

Organism-specific databases

CTD5511.
GeneCardsGC01P028157.
HGNCHGNC:9296. PPP1R8.
HPAHPA027406.
HPA027417.
HPA027452.
MIM602636. gene.
neXtProtNX_Q12972.
PharmGKBPA33659.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG275265.
HOGENOMHOG000231315.
HOVERGENHBG053645.
InParanoidQ12972.
KOK13216.
OMAPVKKKRM.
OrthoDBEOG7PS1FR.
PhylomeDBQ12972.
TreeFamTF105539.

Gene expression databases

ArrayExpressQ12972.
BgeeQ12972.
CleanExHS_PPP1R8.
GenevestigatorQ12972.

Family and domain databases

Gene3D2.60.200.20. 1 hit.
InterProIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamPF00498. FHA. 1 hit.
[Graphical view]
SMARTSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMSSF49879. SSF49879. 1 hit.
PROSITEPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPP1R8. human.
GeneWikiPPP1R8.
GenomeRNAi5511.
NextBio21316.
PROQ12972.
SOURCESearch...

Entry information

Entry namePP1R8_HUMAN
AccessionPrimary (citable) accession number: Q12972
Secondary accession number(s): Q5TEJ2 expand/collapse secondary AC list , Q5TEJ4, Q5TIF2, Q6PKF6, Q9UBH1, Q9UBZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: December 1, 2000
Last modified: April 16, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM