Q12972 (PP1R8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
Protein existence	Evidence 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 does not 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 process	Transcription Transcription regulation mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	DNA-binding Magnesium RNA-binding
Molecular function	Endonuclease Hydrolase Nuclease Protein phosphatase inhibitor Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA catabolic process Traceable author statement Ref.9. Source: ProtInc RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW cell proliferation Inferred from electronic annotation. Source: Compara mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear speck Inferred from direct assay Ref.15. Source: UniProtKB spliceosomal complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	DNA 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: Compara 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...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 351

351

Nuclear inhibitor of protein phosphatase 1

PRO_0000071505

Regions

Domain

49 – 101

53

FHA

Region

1 – 142

142

Interaction with CDC5L, SF3B1 and MELK

Region

143 – 224

82

Interaction with EED

Region

191 – 200

10

Involved in PP-1 inhibition

Region

200 – 203

4

Involved in PP-1 binding

Region

310 – 329

20

Interaction with EED

Region

330 – 351

22

RNA-binding

Region

331 – 337

7

Involved in PP-1 inhibition

Motif

185 – 209

25

Nuclear localization signal 1 Ref.14

Motif

210 – 240

31

Nuclear localization signal 2 Ref.14

Amino acid modifications

Modified residue

161

1

Phosphothreonine By similarity

Modified residue

178

1

Phosphoserine By similarity

Modified residue

199

1

Phosphoserine By similarity

Modified residue

264

1

Phosphotyrosine; by LYN; in vitro Ref.12

Modified residue

335

1

Phosphotyrosine Probable

Natural variations

Alternative sequence

1 – 224

224

Missing in isoform Gamma.

VSP_005120

Alternative sequence

1 – 142

142

Missing in isoform Beta.

VSP_005119

Experimental info

Mutagenesis

68 – 71

4

SRVH → 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

Mutagenesis

193 – 197

5

KRKRK → AAAAA: No effect on interaction with EED. Ref.18

Mutagenesis

195 – 197

3

KRK → AAA: Abolishes nuclear import; when associated with A-234--237-A. Ref.14

Mutagenesis

199

1

S → 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

Mutagenesis

201

1

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. Ref.14 Ref.15 Ref.18

Mutagenesis

203

1

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. Ref.14 Ref.15 Ref.18

Mutagenesis

204

1

S → 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

Mutagenesis

234 – 237

4

KKKR → AAAA: Abolishes nuclear import; when associated with A-195-197-A. Ref.14

Mutagenesis

264

1

Y → D: Abolishes in vitro phosphorylation of isoform gamma by Lyn. Ref.12

Mutagenesis

335

1

Y → D: Decreases the ability of isoform Gamma to bind and inhibit PP-1. Ref.12

Mutagenesis

346

1

T → D: No effect on the ability of isoform Gamma to inhibit PP-1. Ref.12

Mutagenesis

348

1

S → D: No effect on the ability of isoform Gamma to inhibit PP-1. Ref.12

Secondary structure

1

.

.

.

.

.

351

Helix Strand Turn

Details...

Helix

162 – 174

13

Beta strand

208 – 210

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 0A0E92B033E37641	FASTA	351	38,479
	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
	Isoform Beta (Delta) [UniParc]. Checksum: B8A896191A4AB026	FASTA	209	22,711
	10 20 30 40 50 60 MGGEDDELKG LLGLPEEETE LDNLTEFNTA HNKRISTLTI EEGNLDIQRP KRKRKNSRVT 70 80 90 100 110 120 FSEDDEIINP EDVDPSVGRF RNMVQTAVVP VKKKRVEGPG SLGLEESGSR RMQNFAFSGG 130 140 150 160 170 180 LYGGLPPTHS EAGSQPHGIH GTALIGGLPM PYPNLAPDVD LTPVVPSAVN MNPAPNPAVY 190 200 NPEAVNEPKK KKYAKEAWPG KKPTPSLLI
	Isoform Gamma (ARD-1) [UniParc]. Checksum: D29E123EA36C9F94	FASTA	127	13,344
	10 20 30 40 50 60 MVQTAVVPVK KKRVEGPGSL GLEESGSRRM QNFAFSGGLY GGLPPTHSEA GSQPHGIHGT 70 80 90 100 110 120 ALIGGLPMPY PNLAPDVDLT PVVPSAVNMN PAPNPAVYNP EAVNEPKKKK YAKEAWPGKK PTPSLLI

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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 , AF064751, AF064752, AF064753, AF064754, AF064755, AF064756 Genomic DNA. Translation: AAD24669.1.
AF064757 , 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.

IPI

IPI00030383.
IPI00142629.
IPI00218794.

PIR

I38856.

RefSeq

NP_002704.1. NM_002713.3.
NP_054829.2. NM_014110.4.
NP_612568.1. NM_138558.2.

UniGene

Hs.533474.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3V4Y	X-ray	2.10	B/D/F/H	158-216	[»]

ProteinModelPortal

Q12972.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-40815N.

IntAct

Q12972. 8 interactions.

MINT

MINT-133673.

STRING

9606.ENSP00000311677.

PTM databases

PhosphoSite

Q12972.

Polymorphism databases

DMDM

19863082.

Proteomic databases

PaxDb

Q12972.

PeptideAtlas

Q12972.

PRIDE

Q12972.

Protocols and materials databases

DNASU

5511.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000236412; ENSP00000236412; ENSG00000117751.
ENST00000311772; ENSP00000311677; ENSG00000117751.
ENST00000373931; ENSP00000363042; ENSG00000117751.
ENST00000431586; ENSP00000410206; ENSG00000117751.

GeneID

5511.

KEGG

hsa:5511.

UCSC

uc001bov.2. human.

Organism-specific databases

CTD

5511.

GeneCards

GC01P028157.

HGNC

HGNC:9296. PPP1R8.

HPA

HPA027406.
HPA027417.
HPA027452.

MIM

602636. gene.

neXtProt

NX_Q12972.

PharmGKB

PA33659.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG275265.

HOGENOM

HOG000231315.

HOVERGEN

HBG053645.

InParanoid

Q12972.

KO

K13216.

OMA

VKKKRME.

OrthoDB

EOG45HRXT.

PhylomeDB

Q12972.

Gene expression databases

ArrayExpress

Q12972.

Bgee

Q12972.

CleanEx

HS_PPP1R8.

Genevestigator

Q12972.

Family and domain databases

Gene3D

2.60.200.20. 1 hit.

InterPro

IPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]

Pfam

PF00498. FHA. 1 hit.
[Graphical view]

SMART

SM00240. FHA. 1 hit.
[Graphical view]

SUPFAM

SSF49879. SMAD_FHA. 1 hit.

PROSITE

PS50006. FHA_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PPP1R8. human.

GenomeRNAi

5511.

NextBio

21316.

SOURCE

Search...

Entry information

Entry name

PP1R8_HUMAN

Accession

Primary (citable) accession number: Q12972
Secondary accession number(s): Q5TEJ2 , Q5TEJ4, Q5TIF2, Q6PKF6, Q9UBH1, Q9UBZ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 127 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.