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 27-MAR-2024, entry version 204. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8B5R; EM; 6.10 A; S=1-360. DR PDB; 8U5G; X-ray; 3.20 A; B=56-360. DR PDBsum; 6HKW; -. DR PDBsum; 6MKY; -. DR PDBsum; 6OBN; -. DR PDBsum; 6OBP; -. DR PDBsum; 8B5R; -. DR PDBsum; 8U5G; -. DR AlphaFoldDB; Q15435; -. DR EMDB; EMD-15774; -. DR EMDB; EMD-15778; -. DR EMDB; EMD-15846; -. DR EMDB; EMD-15847; -. DR EMDB; EMD-15861; -. DR SMR; Q15435; -. DR BioGRID; 111502; 105. DR DIP; DIP-1005N; -. DR IntAct; Q15435; 53. DR MINT; Q15435; -. DR STRING; 9606.ENSP00000234038; -. DR GlyGen; Q15435; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000234038; -. DR PeptideAtlas; 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 Pumba; Q15435; -. DR Antibodypedia; 34547; 290 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 AGR; HGNC:9295; -. 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; EVWASYN; -. DR OrthoDB; 8274at2759; -. DR PhylomeDB; Q15435; -. DR TreeFam; TF105538; -. DR PathwayCommons; Q15435; -. DR SignaLink; Q15435; -. DR BioGRID-ORCS; 5510; 678 hits in 1171 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 205 other cell types or tissues. DR ExpressionAtlas; Q15435; baseline and differential. 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:0030234; F:enzyme regulator activity; NAS:UniProtKB. DR GO; GO:0019888; F:protein phosphatase regulator activity; TAS:ProtInc. DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IMP:MGI. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR025875; Leu-rich_rpt_4. DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp. DR InterPro; IPR032675; LRR_dom_sf. DR InterPro; IPR003603; U2A'_phosphoprotein32A_C. DR PANTHER; PTHR45973:SF23; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 7; 1. DR PANTHER; PTHR45973; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT SDS22-RELATED; 1. DR Pfam; PF12799; LRR_4; 3. DR Pfam; PF14580; LRR_9; 1. DR SMART; SM00365; LRR_SD22; 10. DR SMART; SM00369; LRR_TYP; 7. DR SMART; SM00446; LRRcap; 1. DR SUPFAM; SSF52058; L domain-like; 1. DR PROSITE; PS51450; LRR; 12. DR Genevisible; Q15435; HS. 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 //