ID PP6R3_HUMAN Reviewed; 873 AA. AC Q5H9R7; Q3B7I1; Q3I4Y0; Q3KR35; Q68CR3; Q7L4R8; Q8N3B2; Q96MB2; Q9H2K5; AC Q9H2K6; Q9HCL4; Q9NUY3; DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 2. DT 27-MAR-2024, entry version 167. DE RecName: Full=Serine/threonine-protein phosphatase 6 regulatory subunit 3; DE AltName: Full=SAPS domain family member 3; DE AltName: Full=Sporulation-induced transcript 4-associated protein SAPL; GN Name=PPP6R3; Synonyms=C11orf23, KIAA1558, PP6R3, SAPL, SAPS3; 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] (ISOFORMS 3 AND 4), FUNCTION, AND TISSUE RP SPECIFICITY. RX PubMed=11401438; DOI=10.1006/geno.2000.6492; RA Twells R.C.J., Metzker M.L., Brown S.D., Cox R., Garey C., Hammond H., RA Hey P.J., Levy E., Nakagawa Y., Philips M.S., Todd J.A., Hess J.F.; RT "The sequence and gene characterization of a 400-kb candidate region for RT IDDM4 on chromosome 11q13."; RL Genomics 72:231-242(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SEQUENCE REVISION. RA Guergnon J., Stefansson B., Brautigan D.L.; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 226-873 (ISOFORM 1), FUNCTION, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RX PubMed=16769727; DOI=10.1074/jbc.m601772200; RA Stefansson B., Brautigan D.L.; RT "Protein phosphatase 6 subunit with conserved Sit4-associated protein RT domain targets IkappaBepsilon."; RL J. Biol. Chem. 281:22624-22634(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RC TISSUE=Brain; RX PubMed=10997877; DOI=10.1093/dnares/7.4.271; RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVIII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:273-281(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 620-873 (ISOFORMS 1/2/4/6). RC TISSUE=Colon carcinoma, Melanoma, and Seminal plasma; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 650-873 (ISOFORMS 1/2/4/6). RC TISSUE=Muscle; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 221-873 (ISOFORM 1). RC TISSUE=Placenta, and Testis; 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [10] RP SUBCELLULAR LOCATION, AND INTERACTION WITH PPP6C AND ANKRD28. RX PubMed=18186651; DOI=10.1021/bi7022877; RA Stefansson B., Ohama T., Daugherty A.E., Brautigan D.L.; RT "Protein phosphatase 6 regulatory subunits composed of ankyrin repeat RT domains."; RL Biochemistry 47:1442-1451(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-722, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579 AND SER-617, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579 AND SER-617, AND RP 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 [17] 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579 AND SER-617, 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579; SER-617; THR-631; RP SER-634 AND SER-853, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND IDENTIFICATION BY RP 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 6 (PP6). May CC function as a scaffolding PP6 subunit. May have an important role in CC maintaining immune self-tolerance. {ECO:0000269|PubMed:11401438, CC ECO:0000269|PubMed:16769727}. CC -!- SUBUNIT: Protein phosphatase 6 (PP6) holoenzyme is proposed to be a CC heterotrimeric complex formed by the catalytic subunit, a SAPS domain- CC containing subunit (PP6R) and an ankyrin repeat-domain containing CC regulatory subunit (ARS). Interacts with PPP6C and ANKRD28. CC {ECO:0000269|PubMed:18186651}. CC -!- INTERACTION: CC Q5H9R7; O15084: ANKRD28; NbExp=5; IntAct=EBI-355498, EBI-359567; CC Q5H9R7; O00743: PPP6C; NbExp=6; IntAct=EBI-355498, EBI-359751; CC Q5H9R7; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-355498, EBI-750109; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=Q5H9R7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5H9R7-2; Sequence=VSP_017142; CC Name=3; Synonyms=B, C11orf23b, SAPLb; CC IsoId=Q5H9R7-3; Sequence=VSP_017140, VSP_017141, VSP_017144; CC Name=4; Synonyms=A, C11orf23a, SAPLa; CC IsoId=Q5H9R7-4; Sequence=VSP_017140, VSP_017141; CC Name=5; CC IsoId=Q5H9R7-5; Sequence=VSP_017143; CC Name=6; CC IsoId=Q5H9R7-6; Sequence=VSP_017141; CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, placenta, heart, CC pancreas, testis, brain, lung, liver, kidney, spleen, thymus, prostate, CC small intestine, colon and leukocytes. {ECO:0000269|PubMed:11401438, CC ECO:0000269|PubMed:16769727}. CC -!- SIMILARITY: Belongs to the SAPS family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAZ99639.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA91978.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB13384.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB71396.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AF264779; AAG36934.1; -; mRNA. DR EMBL; AF264780; AAG36935.1; -; mRNA. DR EMBL; DQ111954; AAZ99639.2; ALT_INIT; mRNA. DR EMBL; AB046778; BAB13384.2; ALT_INIT; mRNA. DR EMBL; AL834471; CAD39130.1; -; mRNA. DR EMBL; CR749815; CAH18675.1; -; mRNA. DR EMBL; CR933658; CAI45957.1; -; mRNA. DR EMBL; BC007738; AAH07738.2; -; mRNA. DR EMBL; BC105933; AAI05934.1; -; mRNA. DR EMBL; BC105934; AAI05935.1; -; mRNA. DR EMBL; BC107599; AAI07600.1; -; mRNA. DR EMBL; AK001920; BAA91978.1; ALT_INIT; mRNA. DR EMBL; AK057250; BAB71396.1; ALT_INIT; mRNA. DR CCDS; CCDS53671.1; -. [Q5H9R7-5] DR CCDS; CCDS53672.1; -. [Q5H9R7-1] DR CCDS; CCDS53673.1; -. [Q5H9R7-2] DR CCDS; CCDS53674.1; -. [Q5H9R7-6] DR CCDS; CCDS53675.1; -. [Q5H9R7-3] DR CCDS; CCDS8182.1; -. [Q5H9R7-4] DR RefSeq; NP_001157632.1; NM_001164160.1. [Q5H9R7-5] DR RefSeq; NP_001157633.1; NM_001164161.1. [Q5H9R7-1] DR RefSeq; NP_001157634.1; NM_001164162.1. [Q5H9R7-2] DR RefSeq; NP_001157635.1; NM_001164163.1. [Q5H9R7-6] DR RefSeq; NP_001157636.1; NM_001164164.1. [Q5H9R7-3] DR RefSeq; NP_060782.2; NM_018312.4. [Q5H9R7-4] DR RefSeq; XP_006718676.1; XM_006718613.2. DR RefSeq; XP_006718677.1; XM_006718614.2. [Q5H9R7-2] DR RefSeq; XP_006718681.1; XM_006718618.3. DR RefSeq; XP_006718687.1; XM_006718624.2. [Q5H9R7-4] DR RefSeq; XP_011543442.1; XM_011545140.2. DR RefSeq; XP_016873451.1; XM_017017962.1. DR RefSeq; XP_016873452.1; XM_017017963.1. DR RefSeq; XP_016873455.1; XM_017017966.1. DR AlphaFoldDB; Q5H9R7; -. DR SMR; Q5H9R7; -. DR BioGRID; 120579; 264. DR CORUM; Q5H9R7; -. DR IntAct; Q5H9R7; 67. DR MINT; Q5H9R7; -. DR STRING; 9606.ENSP00000377390; -. DR ChEMBL; CHEMBL4105773; -. DR GlyConnect; 2073; 8 N-Linked glycans (1 site). DR GlyCosmos; Q5H9R7; 1 site, 16 glycans. DR GlyGen; Q5H9R7; 2 sites, 16 N-linked glycans (1 site), 1 O-linked glycan (1 site). DR iPTMnet; Q5H9R7; -. DR MetOSite; Q5H9R7; -. DR PhosphoSitePlus; Q5H9R7; -. DR SwissPalm; Q5H9R7; -. DR BioMuta; PPP6R3; -. DR DMDM; 88941982; -. DR CPTAC; CPTAC-1002; -. DR EPD; Q5H9R7; -. DR jPOST; Q5H9R7; -. DR MassIVE; Q5H9R7; -. DR MaxQB; Q5H9R7; -. DR PaxDb; 9606-ENSP00000377390; -. DR PeptideAtlas; Q5H9R7; -. DR ProteomicsDB; 62903; -. [Q5H9R7-1] DR ProteomicsDB; 62904; -. [Q5H9R7-2] DR ProteomicsDB; 62905; -. [Q5H9R7-3] DR ProteomicsDB; 62906; -. [Q5H9R7-4] DR ProteomicsDB; 62907; -. [Q5H9R7-5] DR ProteomicsDB; 62908; -. [Q5H9R7-6] DR Pumba; Q5H9R7; -. DR Antibodypedia; 30575; 99 antibodies from 20 providers. DR DNASU; 55291; -. DR Ensembl; ENST00000265636.9; ENSP00000265636.4; ENSG00000110075.15. [Q5H9R7-4] DR Ensembl; ENST00000393800.7; ENSP00000377389.2; ENSG00000110075.15. [Q5H9R7-1] DR Ensembl; ENST00000393801.7; ENSP00000377390.3; ENSG00000110075.15. [Q5H9R7-5] DR Ensembl; ENST00000524845.5; ENSP00000431415.1; ENSG00000110075.15. [Q5H9R7-6] DR Ensembl; ENST00000524904.5; ENSP00000433058.1; ENSG00000110075.15. [Q5H9R7-2] DR Ensembl; ENST00000529710.5; ENSP00000437329.1; ENSG00000110075.15. [Q5H9R7-3] DR GeneID; 55291; -. DR KEGG; hsa:55291; -. DR MANE-Select; ENST00000393800.7; ENSP00000377389.2; NM_001164161.2; NP_001157633.1. DR UCSC; uc001onu.4; human. [Q5H9R7-1] DR AGR; HGNC:1173; -. DR CTD; 55291; -. DR DisGeNET; 55291; -. DR GeneCards; PPP6R3; -. DR HGNC; HGNC:1173; PPP6R3. DR HPA; ENSG00000110075; Low tissue specificity. DR MIM; 610879; gene. DR neXtProt; NX_Q5H9R7; -. DR OpenTargets; ENSG00000110075; -. DR PharmGKB; PA25487; -. DR VEuPathDB; HostDB:ENSG00000110075; -. DR eggNOG; KOG2073; Eukaryota. DR GeneTree; ENSGT00390000009899; -. DR HOGENOM; CLU_012598_0_0_1; -. DR InParanoid; Q5H9R7; -. DR OMA; MNMEEND; -. DR PhylomeDB; Q5H9R7; -. DR TreeFam; TF313227; -. DR PathwayCommons; Q5H9R7; -. DR Reactome; R-HSA-171319; Telomere Extension By Telomerase. DR Reactome; R-HSA-204005; COPII-mediated vesicle transport. DR SignaLink; Q5H9R7; -. DR BioGRID-ORCS; 55291; 136 hits in 1158 CRISPR screens. DR ChiTaRS; PPP6R3; human. DR GenomeRNAi; 55291; -. DR Pharos; Q5H9R7; Tbio. DR PRO; PR:Q5H9R7; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q5H9R7; Protein. DR Bgee; ENSG00000110075; Expressed in calcaneal tendon and 204 other cell types or tissues. DR ExpressionAtlas; Q5H9R7; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0019903; F:protein phosphatase binding; IEA:InterPro. DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central. DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IDA:MGI. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR007587; SAPS. DR PANTHER; PTHR12634:SF12; SERINE_THREONINE-PROTEIN PHOSPHATASE 6 REGULATORY SUBUNIT 3; 1. DR PANTHER; PTHR12634; SIT4 YEAST -ASSOCIATING PROTEIN-RELATED; 1. DR Pfam; PF04499; SAPS; 2. DR SUPFAM; SSF48371; ARM repeat; 1. DR Genevisible; Q5H9R7; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein; KW Reference proteome. FT CHAIN 1..873 FT /note="Serine/threonine-protein phosphatase 6 regulatory FT subunit 3" FT /id="PRO_0000046100" FT REGION 628..873 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 720..753 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 789..810 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 851..873 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 315 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q922D4" FT MOD_RES 579 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 617 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 631 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 634 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 722 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 853 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 326..376 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:11401438" FT /id="VSP_017140" FT VAR_SEQ 516..544 FT /note="Missing (in isoform 3, isoform 4 and isoform 6)" FT /evidence="ECO:0000303|PubMed:11401438, FT ECO:0000303|PubMed:15489334" FT /id="VSP_017141" FT VAR_SEQ 544..549 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_017142" FT VAR_SEQ 817 FT /note="S -> RVLKSYR (in isoform 5)" FT /evidence="ECO:0000303|PubMed:10997877" FT /id="VSP_017143" FT VAR_SEQ 857..873 FT /note="RTGQPSAPGDTSVNGPV -> SGVEIPALPGQWSQQ (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11401438" FT /id="VSP_017144" FT VARIANT 842 FT /note="A -> V (in dbSNP:rs34009811)" FT /id="VAR_057720" FT CONFLICT 292 FT /note="P -> S (in Ref. 5; CAH18675)" FT /evidence="ECO:0000305" FT CONFLICT 443 FT /note="M -> V (in Ref. 7; BAB71396)" FT /evidence="ECO:0000305" FT CONFLICT 477 FT /note="N -> S (in Ref. 5; CAI45957)" FT /evidence="ECO:0000305" FT CONFLICT 677 FT /note="L -> P (in Ref. 5; CAI45957)" FT /evidence="ECO:0000305" SQ SEQUENCE 873 AA; 97669 MW; 5B4C69991E7DE16F CRC64; MFWKFDLHSS SHIDTLLERE DVTLKELMDE EDVLQECKAQ NRKLIEFLLK AECLEDLVSF IIEEPPQDMD EKIRYKYPNI SCELLTSDVS QMNDRLGEDE SLLMKLYSFL LNDSPLNPLL ASFFSKVLSI LISRKPEQIV DFLKKKHDFV DLIIKHIGTS AIMDLLLRLL TCIEPPQPRQ DVLNWLNEEK IIQRLVEIVH PSQEEDRHSN ASQSLCEIVR LSRDQMLQIQ NSTEPDPLLA TLEKQEIIEQ LLSNIFHKEK NESAIVSAIQ ILLTLLETRR PTFEGHIEIC PPGMSHSACS VNKSVLEAIR GRLGSFHELL LEPPKKSVMK TTWGVLDPPV GNTRLNVIRL ISSLLQTNTS SINGDLMELN SIGVILNMFF KYTWNNFLHT QVEICIALIL ASPFENTENA TITDQDSTGD NLLLKHLFQK CQLIERILEA WEMNEKKQAE GGRRHGYMGH LTRIANCIVH STDKGPNSAL VQQLIKDLPD EVRERWETFC TSSLGETNKR NTVDLVTTCH IHSSSDDEID FKETGFSQDS SLQQAFSDYQ MQQMTSNFID QFGFNDEKFA DQDDIGNVSF DRVSDINFTL NTNESGNIAL FEACCKERIQ QFDDGGSDEE DIWEEKHIAF TPESQRRSSS GSTDSEESTD SEEEDGAKQD LFEPSSANTE DKMEVDLSEP PNWSANFDVP METTHGAPLD SVGSDVWSTE EPMPTKETGW ASFSEFTSSL STKDSLRSNS PVEMETSTEP MDPLTPSAAA LAVQPEAAGS VAMEASSDGE EDAESTDKVT ETVMNGGMKE TLSLTVDAKT ETAVFKSEEG KLSTSQDAAC KDAEECPETA EAKCAAPRPP SSSPEQRTGQ PSAPGDTSVN GPV //