PP1R7_HUMAN
ID PP1R7_HUMAN Reviewed; 360 AA.
AC Q15435; B4DFD4; B5MCY6; Q9UQE5; Q9UQE6; Q9Y6K4;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 7;
DE AltName: Full=Protein phosphatase 1 regulatory subunit 22;
GN Name=PPP1R7; Synonyms=SDS22;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=7498485; DOI=10.1016/0014-5793(95)01180-m;
RA Renouf S., Beullens M., Wera S., Van Eynde A., Sikela J., Stalmans W.,
RA Bollen M.;
RT "Molecular cloning of a human polypeptide related to yeast sds22, a
RT regulator of protein phosphatase-1.";
RL FEBS Lett. 375:75-78(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=10231361; DOI=10.1046/j.1432-1327.1999.00344.x;
RA Ceulemans H., Van Eynde A., Perez-Callejon E., Beullens M., Stalmans W.,
RA Bollen M.;
RT "Structure and splice products of the human gene encoding sds22, a putative
RT mitotic regulator of protein phosphatase-1.";
RL Eur. J. Biochem. 262:36-42(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH PPP1CA; PPP1CB AND PPP1CC ISOFORM 1, AND MUTAGENESIS OF
RP ASP-148; PHE-170; GLU-192; PHE-214; ASP-280; GLU-300; TRP-302 AND TYR-327.
RX PubMed=12226088; DOI=10.1074/jbc.m206838200;
RA Ceulemans H., Vulsteke V., De Maeyer M., Tatchell K., Stalmans W.,
RA Bollen M.;
RT "Binding of the concave surface of the Sds22 superhelix to the alpha
RT 4/alpha 5/alpha 6-triangle of protein phosphatase-1.";
RL J. Biol. Chem. 277:47331-47337(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-27, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-27; SER-44 AND
RP SER-47, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-24 AND SER-27, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-322, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-44 AND SER-47, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Regulatory subunit of protein phosphatase 1. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PPP1CA, PPP1CB and PPP1CC/PPP1G isoform 1.
CC {ECO:0000269|PubMed:12226088}.
CC -!- INTERACTION:
CC Q15435; P62136: PPP1CA; NbExp=7; IntAct=EBI-1024281, EBI-357253;
CC Q15435; P62140: PPP1CB; NbExp=10; IntAct=EBI-1024281, EBI-352350;
CC Q15435; P36873: PPP1CC; NbExp=5; IntAct=EBI-1024281, EBI-356283;
CC Q15435; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-1024281, EBI-739895;
CC Q15435-3; P01112: HRAS; NbExp=3; IntAct=EBI-10695066, EBI-350145;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=sds22alpha1;
CC IsoId=Q15435-1; Sequence=Displayed;
CC Name=2; Synonyms=sds22alpha2;
CC IsoId=Q15435-2; Sequence=VSP_019244;
CC Name=3; Synonyms=sds22beta1;
CC IsoId=Q15435-3; Sequence=VSP_019245, VSP_019246;
CC Name=4; Synonyms=sds22beta2;
CC IsoId=Q15435-4; Sequence=VSP_019244, VSP_019245, VSP_019246;
CC Name=5;
CC IsoId=Q15435-5; Sequence=VSP_055672, VSP_019245, VSP_019246;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:7498485}.
CC -!- SIMILARITY: Belongs to the SDS22 family. {ECO:0000305}.
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DR EMBL; Z50749; CAA90626.1; -; mRNA.
DR EMBL; AF067136; AAD26610.1; -; Genomic_DNA.
DR EMBL; AF067130; AAD26610.1; JOINED; Genomic_DNA.
DR EMBL; AF067132; AAD26610.1; JOINED; Genomic_DNA.
DR EMBL; AF067133; AAD26610.1; JOINED; Genomic_DNA.
DR EMBL; AF067134; AAD26610.1; JOINED; Genomic_DNA.
DR EMBL; AF067135; AAD26610.1; JOINED; Genomic_DNA.
DR EMBL; AF067136; AAD26611.1; -; Genomic_DNA.
DR EMBL; AF067130; AAD26611.1; JOINED; Genomic_DNA.
DR EMBL; AF067132; AAD26611.1; JOINED; Genomic_DNA.
DR EMBL; AF067134; AAD26611.1; JOINED; Genomic_DNA.
DR EMBL; AF067135; AAD26611.1; JOINED; Genomic_DNA.
DR EMBL; AF067133; AAD26611.1; JOINED; Genomic_DNA.
DR EMBL; AF067131; AAD26611.1; JOINED; Genomic_DNA.
DR EMBL; AF067134; AAD26612.1; -; Genomic_DNA.
DR EMBL; AF067130; AAD26612.1; JOINED; Genomic_DNA.
DR EMBL; AF067131; AAD26612.1; JOINED; Genomic_DNA.
DR EMBL; AF067132; AAD26612.1; JOINED; Genomic_DNA.
DR EMBL; AF067133; AAD26612.1; JOINED; Genomic_DNA.
DR EMBL; AF067134; AAD26613.1; -; Genomic_DNA.
DR EMBL; AF067132; AAD26613.1; JOINED; Genomic_DNA.
DR EMBL; AF067130; AAD26613.1; JOINED; Genomic_DNA.
DR EMBL; AF067133; AAD26613.1; JOINED; Genomic_DNA.
DR EMBL; BT007296; AAP35960.1; -; mRNA.
DR EMBL; BT020134; AAV38936.1; -; mRNA.
DR EMBL; AK294043; BAG57395.1; -; mRNA.
DR EMBL; AC005237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471063; EAW71243.1; -; Genomic_DNA.
DR EMBL; BC000910; AAH00910.1; -; mRNA.
DR EMBL; BC012397; AAH12397.1; -; mRNA.
DR EMBL; BC013001; AAH13001.1; -; mRNA.
DR CCDS; CCDS2546.1; -. [Q15435-1]
DR CCDS; CCDS63190.1; -. [Q15435-5]
DR CCDS; CCDS63192.1; -. [Q15435-3]
DR CCDS; CCDS63193.1; -. [Q15435-4]
DR CCDS; CCDS63194.1; -. [Q15435-2]
DR PIR; S68209; S68209.
DR RefSeq; NP_001269338.1; NM_001282409.1. [Q15435-2]
DR RefSeq; NP_001269339.1; NM_001282410.1. [Q15435-3]
DR RefSeq; NP_001269340.1; NM_001282411.1. [Q15435-4]
DR RefSeq; NP_001269341.1; NM_001282412.1.
DR RefSeq; NP_001269342.1; NM_001282413.1.
DR RefSeq; NP_001269343.1; NM_001282414.1. [Q15435-5]
DR RefSeq; NP_002703.1; NM_002712.2. [Q15435-1]
DR PDB; 6HKW; X-ray; 3.09 A; A/B/C/D/E=1-360.
DR PDB; 6MKY; X-ray; 2.90 A; A/B=100-360.
DR PDB; 6OBN; X-ray; 2.70 A; C/D=56-360.
DR PDB; 6OBP; X-ray; 2.70 A; C=56-360.
DR PDBsum; 6HKW; -.
DR PDBsum; 6MKY; -.
DR PDBsum; 6OBN; -.
DR PDBsum; 6OBP; -.
DR AlphaFoldDB; Q15435; -.
DR SMR; Q15435; -.
DR BioGRID; 111502; 77.
DR DIP; DIP-1005N; -.
DR IntAct; Q15435; 50.
DR MINT; Q15435; -.
DR STRING; 9606.ENSP00000234038; -.
DR iPTMnet; Q15435; -.
DR MetOSite; Q15435; -.
DR PhosphoSitePlus; Q15435; -.
DR BioMuta; PPP1R7; -.
DR DMDM; 74762145; -.
DR REPRODUCTION-2DPAGE; IPI00033600; -.
DR EPD; Q15435; -.
DR jPOST; Q15435; -.
DR MassIVE; Q15435; -.
DR MaxQB; Q15435; -.
DR PaxDb; Q15435; -.
DR PeptideAtlas; Q15435; -.
DR PRIDE; Q15435; -.
DR ProteomicsDB; 60591; -. [Q15435-1]
DR ProteomicsDB; 60592; -. [Q15435-2]
DR ProteomicsDB; 60593; -. [Q15435-3]
DR ProteomicsDB; 60594; -. [Q15435-4]
DR ProteomicsDB; 6128; -.
DR Antibodypedia; 34547; 267 antibodies from 28 providers.
DR DNASU; 5510; -.
DR Ensembl; ENST00000234038.11; ENSP00000234038.6; ENSG00000115685.15. [Q15435-1]
DR Ensembl; ENST00000272983.12; ENSP00000272983.8; ENSG00000115685.15. [Q15435-2]
DR Ensembl; ENST00000401987.5; ENSP00000385466.1; ENSG00000115685.15. [Q15435-4]
DR Ensembl; ENST00000402734.5; ENSP00000385012.1; ENSG00000115685.15. [Q15435-5]
DR Ensembl; ENST00000406106.7; ENSP00000385022.3; ENSG00000115685.15. [Q15435-3]
DR Ensembl; ENST00000407025.5; ENSP00000385657.1; ENSG00000115685.15. [Q15435-1]
DR GeneID; 5510; -.
DR KEGG; hsa:5510; -.
DR MANE-Select; ENST00000234038.11; ENSP00000234038.6; NM_002712.3; NP_002703.1.
DR UCSC; uc002was.5; human. [Q15435-1]
DR CTD; 5510; -.
DR DisGeNET; 5510; -.
DR GeneCards; PPP1R7; -.
DR HGNC; HGNC:9295; PPP1R7.
DR HPA; ENSG00000115685; Low tissue specificity.
DR MIM; 602877; gene.
DR neXtProt; NX_Q15435; -.
DR OpenTargets; ENSG00000115685; -.
DR PharmGKB; PA33658; -.
DR VEuPathDB; HostDB:ENSG00000115685; -.
DR eggNOG; KOG0531; Eukaryota.
DR GeneTree; ENSGT00940000158551; -.
DR InParanoid; Q15435; -.
DR OMA; YDNLIAH; -.
DR PhylomeDB; Q15435; -.
DR TreeFam; TF105538; -.
DR PathwayCommons; Q15435; -.
DR SignaLink; Q15435; -.
DR BioGRID-ORCS; 5510; 662 hits in 1088 CRISPR screens.
DR ChiTaRS; PPP1R7; human.
DR GeneWiki; PPP1R7; -.
DR GenomeRNAi; 5510; -.
DR Pharos; Q15435; Tbio.
DR PRO; PR:Q15435; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q15435; protein.
DR Bgee; ENSG00000115685; Expressed in right testis and 203 other tissues.
DR ExpressionAtlas; Q15435; baseline and differential.
DR Genevisible; Q15435; HS.
DR GO; GO:0005694; C:chromosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; NAS:UniProtKB.
DR GO; GO:0019888; F:protein phosphatase regulator activity; TAS:ProtInc.
DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IBA:GO_Central.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IMP:MGI.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR003603; U2A'_phosphoprotein32A_C.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00446; LRRcap; 1.
DR PROSITE; PS51450; LRR; 12.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Leucine-rich repeat;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..360
FT /note="Protein phosphatase 1 regulatory subunit 7"
FT /id="PRO_0000239613"
FT REPEAT 77..98
FT /note="LRR 1"
FT REPEAT 99..120
FT /note="LRR 2"
FT REPEAT 121..142
FT /note="LRR 3"
FT REPEAT 143..164
FT /note="LRR 4"
FT REPEAT 165..186
FT /note="LRR 5"
FT REPEAT 187..208
FT /note="LRR 6"
FT REPEAT 209..230
FT /note="LRR 7"
FT REPEAT 231..252
FT /note="LRR 8"
FT REPEAT 253..274
FT /note="LRR 9"
FT REPEAT 275..296
FT /note="LRR 10"
FT REPEAT 297..318
FT /note="LRR 11"
FT DOMAIN 331..360
FT /note="LRRCT"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..60
FT /note="MAAERGAGQQQSQEMMEVDRRVESEESGDEEGKKHSSGIVADLSEQSLKDGE
FT ERGEEDPE -> M (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_055672"
FT VAR_SEQ 18..60
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_019244"
FT VAR_SEQ 274..280
FT /note="NKLTMLD -> VQDSLTY (in isoform 3, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_019245"
FT VAR_SEQ 281..360
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_019246"
FT MUTAGEN 148
FT /note="D->V: Completely abolishes the interaction with
FT protein phosphatase 1."
FT /evidence="ECO:0000269|PubMed:12226088"
FT MUTAGEN 170
FT /note="F->A: Severely impaired the binding of protein
FT phosphatase 1."
FT /evidence="ECO:0000269|PubMed:12226088"
FT MUTAGEN 192
FT /note="E->A: Completely abolishes the interaction with
FT protein phosphatase 1."
FT /evidence="ECO:0000269|PubMed:12226088"
FT MUTAGEN 214
FT /note="F->A: Completely abolishes the interaction with
FT protein phosphatase 1."
FT /evidence="ECO:0000269|PubMed:12226088"
FT MUTAGEN 280
FT /note="D->A: Severely impairs the binding of protein
FT phosphatase 1."
FT /evidence="ECO:0000269|PubMed:12226088"
FT MUTAGEN 300
FT /note="E->A: Completely abolishes the interaction with
FT protein phosphatase 1."
FT /evidence="ECO:0000269|PubMed:12226088"
FT MUTAGEN 302
FT /note="W->A: Completely abolishes the interaction with
FT protein phosphatase 1."
FT /evidence="ECO:0000269|PubMed:12226088"
FT MUTAGEN 327
FT /note="Y->A: Completely abolishes the interaction with
FT protein phosphatase 1."
FT /evidence="ECO:0000269|PubMed:12226088"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:6HKW"
FT HELIX 69..74
FT /evidence="ECO:0007829|PDB:6HKW"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:6HKW"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:6OBN"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:6OBN"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:6OBN"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:6OBN"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:6OBN"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:6OBN"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:6OBN"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:6OBN"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:6OBN"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:6OBN"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:6OBN"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:6OBN"
FT HELIX 311..317
FT /evidence="ECO:0007829|PDB:6OBN"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:6OBN"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:6OBN"
FT HELIX 339..346
FT /evidence="ECO:0007829|PDB:6OBN"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:6MKY"
SQ SEQUENCE 360 AA; 41564 MW; 49BCCF675EAA94D1 CRC64;
MAAERGAGQQ QSQEMMEVDR RVESEESGDE EGKKHSSGIV ADLSEQSLKD GEERGEEDPE
EEHELPVDME TINLDRDAED VDLNHYRIGK IEGFEVLKKV KTLCLRQNLI KCIENLEELQ
SLRELDLYDN QIKKIENLEA LTELEILDIS FNLLRNIEGV DKLTRLKKLF LVNNKISKIE
NLSNLHQLQM LELGSNRIRA IENIDTLTNL ESLFLGKNKI TKLQNLDALT NLTVLSMQSN
RLTKIEGLQN LVNLRELYLS HNGIEVIEGL ENNNKLTMLD IASNRIKKIE NISHLTELQE
FWMNDNLLES WSDLDELKGA RSLETVYLER NPLQKDPQYR RKVMLALPSV RQIDATFVRF
