PP6R3_HUMAN
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 03-AUG-2022, entry version 158.
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};
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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; 163.
DR CORUM; Q5H9R7; -.
DR IntAct; Q5H9R7; 64.
DR MINT; Q5H9R7; -.
DR STRING; 9606.ENSP00000377390; -.
DR ChEMBL; CHEMBL4105773; -.
DR GlyConnect; 2073; 8 N-Linked glycans (1 site).
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; Q5H9R7; -.
DR PeptideAtlas; Q5H9R7; -.
DR PRIDE; 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 Antibodypedia; 30575; 78 antibodies from 19 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 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; NEMRHAD; -.
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; 130 hits in 1080 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 203 other tissues.
DR ExpressionAtlas; Q5H9R7; baseline and differential.
DR Genevisible; Q5H9R7; HS.
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; IPI:MGI.
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; PTHR12634; 1.
DR Pfam; PF04499; SAPS; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
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
