Full text data of PPP6R3
PPP6R3
(C11orf23, KIAA1558, PP6R3, SAPL, SAPS3)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Serine/threonine-protein phosphatase 6 regulatory subunit 3 (SAPS domain family member 3; Sporulation-induced transcript 4-associated protein SAPL)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Serine/threonine-protein phosphatase 6 regulatory subunit 3 (SAPS domain family member 3; Sporulation-induced transcript 4-associated protein SAPL)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q5H9R7
ID PP6R3_HUMAN Reviewed; 873 AA.
AC Q5H9R7; Q3B7I1; Q3I4Y0; Q3KR35; Q68CR3; Q7L4R8; Q8N3B2; Q96MB2;
read moreAC Q9H2K5; Q9H2K6; Q9HCL4; Q9NUY3;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 2.
DT 22-JAN-2014, entry version 88.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT for 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,
RP SUBCELLULAR 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.
RT XVIII. The complete sequences of 100 new cDNA clones from brain which
RT code for large proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
RP NUCLEOTIDE 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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
RP NUCLEOTIDE 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
RT project: 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation 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 MASS
RP SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-722, AND MASS
RP SPECTROMETRY.
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6). May
CC function as a scaffolding PP6 subunit. May have an important role
CC in maintaining immune self-tolerance.
CC -!- SUBUNIT: Protein phosphatase 6 (PP6) holoenzyme is proposed to be
CC a heterotrimeric complex formed by the catalytic subunit, a SAPS
CC domain-containing subunit (PP6R) and an ankyrin repeat-domain
CC containing regulatory subunit (ARS). Interacts with PPP6C and
CC ANKRD28.
CC -!- INTERACTION:
CC O15084:ANKRD28; NbExp=5; IntAct=EBI-355498, EBI-359567;
CC O00743:PPP6C; NbExp=5; IntAct=EBI-355498, EBI-359751;
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,
CC prostate, small intestine, colon and leukocytes.
CC -!- SIMILARITY: Belongs to the SAPS family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAZ99639.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAA91978.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB13384.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAB71396.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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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 RefSeq; NP_001157632.1; NM_001164160.1.
DR RefSeq; NP_001157633.1; NM_001164161.1.
DR RefSeq; NP_001157634.1; NM_001164162.1.
DR RefSeq; NP_001157635.1; NM_001164163.1.
DR RefSeq; NP_001157636.1; NM_001164164.1.
DR RefSeq; NP_060782.2; NM_018312.4.
DR RefSeq; XP_005274141.1; XM_005274084.1.
DR UniGene; Hs.503022; -.
DR ProteinModelPortal; Q5H9R7; -.
DR IntAct; Q5H9R7; 14.
DR MINT; MINT-5004961; -.
DR PhosphoSite; Q5H9R7; -.
DR DMDM; 88941982; -.
DR PaxDb; Q5H9R7; -.
DR PRIDE; Q5H9R7; -.
DR Ensembl; ENST00000265636; ENSP00000265636; ENSG00000110075.
DR Ensembl; ENST00000393800; ENSP00000377389; ENSG00000110075.
DR Ensembl; ENST00000393801; ENSP00000377390; ENSG00000110075.
DR Ensembl; ENST00000524845; ENSP00000431415; ENSG00000110075.
DR Ensembl; ENST00000524904; ENSP00000433058; ENSG00000110075.
DR Ensembl; ENST00000529710; ENSP00000437329; ENSG00000110075.
DR GeneID; 55291; -.
DR KEGG; hsa:55291; -.
DR UCSC; uc001onw.3; human.
DR CTD; 55291; -.
DR GeneCards; GC11P068229; -.
DR HGNC; HGNC:1173; PPP6R3.
DR HPA; CAB017183; -.
DR MIM; 610879; gene.
DR neXtProt; NX_Q5H9R7; -.
DR PharmGKB; PA25487; -.
DR eggNOG; NOG303042; -.
DR HOVERGEN; HBG069733; -.
DR KO; K15501; -.
DR OrthoDB; EOG7PGDQ3; -.
DR ChiTaRS; PPP6R3; human.
DR GenomeRNAi; 55291; -.
DR NextBio; 59478; -.
DR PRO; PR:Q5H9R7; -.
DR ArrayExpress; Q5H9R7; -.
DR Bgee; Q5H9R7; -.
DR Genevestigator; Q5H9R7; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; Complete proteome; Cytoplasm; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 873 Serine/threonine-protein phosphatase 6
FT regulatory subunit 3.
FT /FTId=PRO_0000046100.
FT MOD_RES 579 579 Phosphoserine.
FT MOD_RES 617 617 Phosphoserine.
FT MOD_RES 722 722 Phosphoserine.
FT MOD_RES 853 853 Phosphoserine (By similarity).
FT VAR_SEQ 326 376 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_017140.
FT VAR_SEQ 516 544 Missing (in isoform 3, isoform 4 and
FT isoform 6).
FT /FTId=VSP_017141.
FT VAR_SEQ 544 549 Missing (in isoform 2).
FT /FTId=VSP_017142.
FT VAR_SEQ 817 817 S -> RVLKSYR (in isoform 5).
FT /FTId=VSP_017143.
FT VAR_SEQ 857 873 RTGQPSAPGDTSVNGPV -> SGVEIPALPGQWSQQ (in
FT isoform 3).
FT /FTId=VSP_017144.
FT VARIANT 842 842 A -> V (in dbSNP:rs34009811).
FT /FTId=VAR_057720.
FT CONFLICT 292 292 P -> S (in Ref. 5; CAH18675).
FT CONFLICT 443 443 M -> V (in Ref. 7; BAB71396).
FT CONFLICT 477 477 N -> S (in Ref. 5; CAI45957).
FT CONFLICT 677 677 L -> P (in Ref. 5; CAI45957).
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
//
ID PP6R3_HUMAN Reviewed; 873 AA.
AC Q5H9R7; Q3B7I1; Q3I4Y0; Q3KR35; Q68CR3; Q7L4R8; Q8N3B2; Q96MB2;
read moreAC Q9H2K5; Q9H2K6; Q9HCL4; Q9NUY3;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 2.
DT 22-JAN-2014, entry version 88.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT for 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,
RP SUBCELLULAR 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.
RT XVIII. The complete sequences of 100 new cDNA clones from brain which
RT code for large proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
RP NUCLEOTIDE 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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
RP NUCLEOTIDE 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
RT project: 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation 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 MASS
RP SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-722, AND MASS
RP SPECTROMETRY.
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6). May
CC function as a scaffolding PP6 subunit. May have an important role
CC in maintaining immune self-tolerance.
CC -!- SUBUNIT: Protein phosphatase 6 (PP6) holoenzyme is proposed to be
CC a heterotrimeric complex formed by the catalytic subunit, a SAPS
CC domain-containing subunit (PP6R) and an ankyrin repeat-domain
CC containing regulatory subunit (ARS). Interacts with PPP6C and
CC ANKRD28.
CC -!- INTERACTION:
CC O15084:ANKRD28; NbExp=5; IntAct=EBI-355498, EBI-359567;
CC O00743:PPP6C; NbExp=5; IntAct=EBI-355498, EBI-359751;
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,
CC prostate, small intestine, colon and leukocytes.
CC -!- SIMILARITY: Belongs to the SAPS family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAZ99639.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAA91978.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB13384.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAB71396.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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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 RefSeq; NP_001157632.1; NM_001164160.1.
DR RefSeq; NP_001157633.1; NM_001164161.1.
DR RefSeq; NP_001157634.1; NM_001164162.1.
DR RefSeq; NP_001157635.1; NM_001164163.1.
DR RefSeq; NP_001157636.1; NM_001164164.1.
DR RefSeq; NP_060782.2; NM_018312.4.
DR RefSeq; XP_005274141.1; XM_005274084.1.
DR UniGene; Hs.503022; -.
DR ProteinModelPortal; Q5H9R7; -.
DR IntAct; Q5H9R7; 14.
DR MINT; MINT-5004961; -.
DR PhosphoSite; Q5H9R7; -.
DR DMDM; 88941982; -.
DR PaxDb; Q5H9R7; -.
DR PRIDE; Q5H9R7; -.
DR Ensembl; ENST00000265636; ENSP00000265636; ENSG00000110075.
DR Ensembl; ENST00000393800; ENSP00000377389; ENSG00000110075.
DR Ensembl; ENST00000393801; ENSP00000377390; ENSG00000110075.
DR Ensembl; ENST00000524845; ENSP00000431415; ENSG00000110075.
DR Ensembl; ENST00000524904; ENSP00000433058; ENSG00000110075.
DR Ensembl; ENST00000529710; ENSP00000437329; ENSG00000110075.
DR GeneID; 55291; -.
DR KEGG; hsa:55291; -.
DR UCSC; uc001onw.3; human.
DR CTD; 55291; -.
DR GeneCards; GC11P068229; -.
DR HGNC; HGNC:1173; PPP6R3.
DR HPA; CAB017183; -.
DR MIM; 610879; gene.
DR neXtProt; NX_Q5H9R7; -.
DR PharmGKB; PA25487; -.
DR eggNOG; NOG303042; -.
DR HOVERGEN; HBG069733; -.
DR KO; K15501; -.
DR OrthoDB; EOG7PGDQ3; -.
DR ChiTaRS; PPP6R3; human.
DR GenomeRNAi; 55291; -.
DR NextBio; 59478; -.
DR PRO; PR:Q5H9R7; -.
DR ArrayExpress; Q5H9R7; -.
DR Bgee; Q5H9R7; -.
DR Genevestigator; Q5H9R7; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; Complete proteome; Cytoplasm; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 873 Serine/threonine-protein phosphatase 6
FT regulatory subunit 3.
FT /FTId=PRO_0000046100.
FT MOD_RES 579 579 Phosphoserine.
FT MOD_RES 617 617 Phosphoserine.
FT MOD_RES 722 722 Phosphoserine.
FT MOD_RES 853 853 Phosphoserine (By similarity).
FT VAR_SEQ 326 376 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_017140.
FT VAR_SEQ 516 544 Missing (in isoform 3, isoform 4 and
FT isoform 6).
FT /FTId=VSP_017141.
FT VAR_SEQ 544 549 Missing (in isoform 2).
FT /FTId=VSP_017142.
FT VAR_SEQ 817 817 S -> RVLKSYR (in isoform 5).
FT /FTId=VSP_017143.
FT VAR_SEQ 857 873 RTGQPSAPGDTSVNGPV -> SGVEIPALPGQWSQQ (in
FT isoform 3).
FT /FTId=VSP_017144.
FT VARIANT 842 842 A -> V (in dbSNP:rs34009811).
FT /FTId=VAR_057720.
FT CONFLICT 292 292 P -> S (in Ref. 5; CAH18675).
FT CONFLICT 443 443 M -> V (in Ref. 7; BAB71396).
FT CONFLICT 477 477 N -> S (in Ref. 5; CAI45957).
FT CONFLICT 677 677 L -> P (in Ref. 5; CAI45957).
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
//
MIM
610879
*RECORD*
*FIELD* NO
610879
*FIELD* TI
*610879 SAPS DOMAIN FAMILY, MEMBER 3; SAPS3
;;PROTEIN PHOSPHATASE 6, REGULATORY SUBUNIT 3; PP6R3;;
read moreCHROMOSOME 11 OPEN READING FRAME 23; C11ORF23;;
KIAA1558
*FIELD* TX
DESCRIPTION
Protein phosphatase regulatory subunits, such as SAPS3, modulate the
activity of protein phosphatase catalytic subunits by restricting
substrate specificity, recruiting substrates, and determining the
intracellular localization of the holoenzyme. SAPS3 is a regulatory
subunit for the protein phosphatase-6 catalytic subunit (PPP6C; 612725)
(Stefansson and Brautigan, 2006).
CLONING
By sequencing clones obtained from a size-fractionated fetal brain cDNA
library, Nagase et al. (2000) cloned SAPS3, which they designated
KIAA1558. The 3-prime end of the transcript contains several repetitive
elements. RT-PCR ELISA detected moderate expression in all adult and
fetal tissues and specific brain regions examined.
By sequencing the IDDM4 (600319) region of chromosome 11, followed by
database analysis, Twells et al. (2001) cloned 2 splice variants of
SAPS3, which they called C11ORF23. The variants encode deduced 793- and
791-amino acid proteins, both of which have calculated molecular masses
of 89 kD. The first 776 amino acids are identical in the 2 isoforms and
include a tandem repeat of ser-thr-asp-ser-glu-glu. Both transcripts
have a second putative start methionine that would result in shorter
proteins if used. SAPS3 shares significant similarity with yeast Sap190
and Sap185, including conservation of several motifs. Northern blot
analysis detected highest expression of 4.9- and 4.1-kb transcripts in
skeletal muscle, placenta, heart, pancreas, and testis. Expression was
also detected in brain, lung, liver, kidney, spleen, thymus, prostate,
small intestine, colon, and leukocytes, but not in ovary. The 4.9-kb
transcript predominated in most tissues, but in testis the 4.1-kb
transcript was more abundant.
By searching databases for sequences similar to yeast Sap155, Sap185,
and Sap190, Stefansson and Brautigan (2006) identified multiple splice
variants of SAPS3, which they called PP6R3. The variants differ only in
their N termini, and all have a central alpha-helical SAPS domain of
about 400 amino acids. Northern blot analysis revealed high PP6R3
expression in heart, but little expression in other tissues examined.
Western blot analysis of fractionated HeLa and HEK293 cells showed PP6R3
in the cytosolic fraction.
GENE FUNCTION
Using protein pull-down assays, Stefansson and Brautigan (2006) showed
that epitope-tagged PP6R3 bound endogenous PPP6C, but not PPP2CA
(176915).
GENE STRUCTURE
Twells et al. (2001) determined that the SAPS3 gene contains 22 exons.
MAPPING
By PCR of a human-rodent hybrid panel, Nagase et al. (2000) mapped the
SAPS3 gene to chromosome 11. Twells et al. (2001) mapped the SAPS3 gene
to chromosome 11q13 by analysis of BAC and PAC clones.
*FIELD* RF
1. Nagase, T.; Kikuno, R.; Nakayama, M.; Hirosawa, M.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XVIII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 7: 273-281, 2000.
2. Stefansson, B.; Brautigan, D. L.: Protein phosphatase 6 subunit
with conserved Sit4-associated protein domain targets I-kappa-B-epsilon. J.
Biol. Chem. 281: 22624-22634, 2006.
3. Twells, R. C. J.; Metzker, M. L.; Brown, S. D.; Cox, R.; Garey,
C.; Hammond, H.; Hey, P. J.; Levy, E.; Nakagawa, Y.; Philips, M. S.;
Todd, J. A.; Hess, J. F.: The sequence and gene characterization
of a 400-kb candidate region for IDDM4 on chromosome 11q13. Genomics 72:
231-242, 2001.
*FIELD* CD
Patricia A. Hartz: 3/23/2007
*FIELD* ED
terry: 09/07/2010
mgross: 3/23/2007
*RECORD*
*FIELD* NO
610879
*FIELD* TI
*610879 SAPS DOMAIN FAMILY, MEMBER 3; SAPS3
;;PROTEIN PHOSPHATASE 6, REGULATORY SUBUNIT 3; PP6R3;;
read moreCHROMOSOME 11 OPEN READING FRAME 23; C11ORF23;;
KIAA1558
*FIELD* TX
DESCRIPTION
Protein phosphatase regulatory subunits, such as SAPS3, modulate the
activity of protein phosphatase catalytic subunits by restricting
substrate specificity, recruiting substrates, and determining the
intracellular localization of the holoenzyme. SAPS3 is a regulatory
subunit for the protein phosphatase-6 catalytic subunit (PPP6C; 612725)
(Stefansson and Brautigan, 2006).
CLONING
By sequencing clones obtained from a size-fractionated fetal brain cDNA
library, Nagase et al. (2000) cloned SAPS3, which they designated
KIAA1558. The 3-prime end of the transcript contains several repetitive
elements. RT-PCR ELISA detected moderate expression in all adult and
fetal tissues and specific brain regions examined.
By sequencing the IDDM4 (600319) region of chromosome 11, followed by
database analysis, Twells et al. (2001) cloned 2 splice variants of
SAPS3, which they called C11ORF23. The variants encode deduced 793- and
791-amino acid proteins, both of which have calculated molecular masses
of 89 kD. The first 776 amino acids are identical in the 2 isoforms and
include a tandem repeat of ser-thr-asp-ser-glu-glu. Both transcripts
have a second putative start methionine that would result in shorter
proteins if used. SAPS3 shares significant similarity with yeast Sap190
and Sap185, including conservation of several motifs. Northern blot
analysis detected highest expression of 4.9- and 4.1-kb transcripts in
skeletal muscle, placenta, heart, pancreas, and testis. Expression was
also detected in brain, lung, liver, kidney, spleen, thymus, prostate,
small intestine, colon, and leukocytes, but not in ovary. The 4.9-kb
transcript predominated in most tissues, but in testis the 4.1-kb
transcript was more abundant.
By searching databases for sequences similar to yeast Sap155, Sap185,
and Sap190, Stefansson and Brautigan (2006) identified multiple splice
variants of SAPS3, which they called PP6R3. The variants differ only in
their N termini, and all have a central alpha-helical SAPS domain of
about 400 amino acids. Northern blot analysis revealed high PP6R3
expression in heart, but little expression in other tissues examined.
Western blot analysis of fractionated HeLa and HEK293 cells showed PP6R3
in the cytosolic fraction.
GENE FUNCTION
Using protein pull-down assays, Stefansson and Brautigan (2006) showed
that epitope-tagged PP6R3 bound endogenous PPP6C, but not PPP2CA
(176915).
GENE STRUCTURE
Twells et al. (2001) determined that the SAPS3 gene contains 22 exons.
MAPPING
By PCR of a human-rodent hybrid panel, Nagase et al. (2000) mapped the
SAPS3 gene to chromosome 11. Twells et al. (2001) mapped the SAPS3 gene
to chromosome 11q13 by analysis of BAC and PAC clones.
*FIELD* RF
1. Nagase, T.; Kikuno, R.; Nakayama, M.; Hirosawa, M.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XVIII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 7: 273-281, 2000.
2. Stefansson, B.; Brautigan, D. L.: Protein phosphatase 6 subunit
with conserved Sit4-associated protein domain targets I-kappa-B-epsilon. J.
Biol. Chem. 281: 22624-22634, 2006.
3. Twells, R. C. J.; Metzker, M. L.; Brown, S. D.; Cox, R.; Garey,
C.; Hammond, H.; Hey, P. J.; Levy, E.; Nakagawa, Y.; Philips, M. S.;
Todd, J. A.; Hess, J. F.: The sequence and gene characterization
of a 400-kb candidate region for IDDM4 on chromosome 11q13. Genomics 72:
231-242, 2001.
*FIELD* CD
Patricia A. Hartz: 3/23/2007
*FIELD* ED
terry: 09/07/2010
mgross: 3/23/2007