Full text data of PPP6R2
PPP6R2
(KIAA0685, PP6R2, SAPS2)
[Confidence: low (only semi-automatic identification from reviews)]
Serine/threonine-protein phosphatase 6 regulatory subunit 2 (SAPS domain family member 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Serine/threonine-protein phosphatase 6 regulatory subunit 2 (SAPS domain family member 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O75170
ID PP6R2_HUMAN Reviewed; 966 AA.
AC O75170; A6PVG3; B7Z7T3; Q5U5P3; Q7Z2L2; Q7Z5G5; Q7Z731; Q9UGB9;
read moreDT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=Serine/threonine-protein phosphatase 6 regulatory subunit 2;
DE AltName: Full=SAPS domain family member 2;
GN Name=PPP6R2; Synonyms=KIAA0685, PP6R2, SAPS2;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 6).
RC TISSUE=Brain, Lymph, Muscle, Placenta, and Skin;
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 [5]
RP FUNCTION, INTERACTION WITH PPP6C AND NFKBIE, SUBCELLULAR LOCATION, AND
RP 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 [6]
RP 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 [7]
RP IDENTIFICATION BY 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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, 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 [9]
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND MASS
RP 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 [11]
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).
CC -!- FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6). May
CC function as a scaffolding PP6 subunit. Involved in the PP6-
CC mediated dephosphorylation of NFKBIE opposing its degradation in
CC response to TNF-alpha.
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 NFKBIE. Interacts with ANKRD28.
CC -!- INTERACTION:
CC O15084:ANKRD28; NbExp=7; IntAct=EBI-359739, EBI-359567;
CC O00743:PPP6C; NbExp=8; IntAct=EBI-359739, EBI-359751;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=O75170-1; Sequence=Displayed;
CC Note=No experimental confirmation available;
CC Name=2;
CC IsoId=O75170-2; Sequence=VSP_030758, VSP_030759, VSP_030760,
CC VSP_030761;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=O75170-3; Sequence=VSP_037768, VSP_030758, VSP_030760;
CC Name=4;
CC IsoId=O75170-4; Sequence=VSP_030758, VSP_030760;
CC Name=5;
CC IsoId=O75170-5; Sequence=VSP_030760;
CC Name=6;
CC IsoId=O75170-6; Sequence=VSP_037767, VSP_030758, VSP_030760;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with strongest
CC expression in the testis followed by liver, heart, kidney, brain
CC and placenta.
CC -!- SIMILARITY: Belongs to the SAPS family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31660.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AB014585; BAA31660.2; ALT_INIT; mRNA.
DR EMBL; AK302472; BAH13719.1; -; mRNA.
DR EMBL; AL096767; CAO03456.1; -; Genomic_DNA.
DR EMBL; AL671545; CAO03456.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03456.1; JOINED; Genomic_DNA.
DR EMBL; AL096767; CAO03457.1; -; Genomic_DNA.
DR EMBL; AL671545; CAO03457.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03457.1; JOINED; Genomic_DNA.
DR EMBL; AL096767; CAO03458.1; -; Genomic_DNA.
DR EMBL; AL671545; CAO03458.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03458.1; JOINED; Genomic_DNA.
DR EMBL; AL096767; CAO03459.1; -; Genomic_DNA.
DR EMBL; AL671545; CAO03459.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03459.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03561.1; -; Genomic_DNA.
DR EMBL; AL096767; CAO03561.1; JOINED; Genomic_DNA.
DR EMBL; AL671545; CAO03561.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03562.1; -; Genomic_DNA.
DR EMBL; AL096767; CAO03562.1; JOINED; Genomic_DNA.
DR EMBL; AL671545; CAO03562.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03563.1; -; Genomic_DNA.
DR EMBL; AL096767; CAO03563.1; JOINED; Genomic_DNA.
DR EMBL; AL671545; CAO03563.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03564.1; -; Genomic_DNA.
DR EMBL; AL096767; CAO03564.1; JOINED; Genomic_DNA.
DR EMBL; AL671545; CAO03564.1; JOINED; Genomic_DNA.
DR EMBL; AL671545; CAO03642.1; -; Genomic_DNA.
DR EMBL; AL096767; CAO03642.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03642.1; JOINED; Genomic_DNA.
DR EMBL; AL671545; CAO03643.1; -; Genomic_DNA.
DR EMBL; AL096767; CAO03643.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03643.1; JOINED; Genomic_DNA.
DR EMBL; AL671545; CAO03644.1; -; Genomic_DNA.
DR EMBL; AL096767; CAO03644.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03644.1; JOINED; Genomic_DNA.
DR EMBL; AL671545; CAO03645.1; -; Genomic_DNA.
DR EMBL; AL096767; CAO03645.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03645.1; JOINED; Genomic_DNA.
DR EMBL; BC000976; AAH00976.2; -; mRNA.
DR EMBL; BC006568; AAH06568.1; -; mRNA.
DR EMBL; BC032664; AAH32664.1; -; mRNA.
DR EMBL; BC041698; AAH41698.1; -; mRNA.
DR EMBL; BC052995; AAH52995.1; -; mRNA.
DR PIR; T00357; T00357.
DR RefSeq; NP_001229827.1; NM_001242898.1.
DR RefSeq; NP_001229828.1; NM_001242899.1.
DR RefSeq; NP_001229829.1; NM_001242900.1.
DR RefSeq; NP_055493.2; NM_014678.4.
DR UniGene; Hs.449098; -.
DR UniGene; Hs.733531; -.
DR UniGene; Hs.740776; -.
DR ProteinModelPortal; O75170; -.
DR DIP; DIP-27539N; -.
DR IntAct; O75170; 26.
DR MINT; MINT-1140941; -.
DR PhosphoSite; O75170; -.
DR PaxDb; O75170; -.
DR PRIDE; O75170; -.
DR Ensembl; ENST00000216061; ENSP00000216061; ENSG00000100239.
DR Ensembl; ENST00000359139; ENSP00000352051; ENSG00000100239.
DR Ensembl; ENST00000395741; ENSP00000379090; ENSG00000100239.
DR Ensembl; ENST00000395744; ENSP00000379093; ENSG00000100239.
DR GeneID; 9701; -.
DR KEGG; hsa:9701; -.
DR UCSC; uc003blb.2; human.
DR CTD; 9701; -.
DR GeneCards; GC22P050782; -.
DR HGNC; HGNC:19253; PPP6R2.
DR HPA; HPA030656; -.
DR MIM; 610877; gene.
DR neXtProt; NX_O75170; -.
DR PharmGKB; PA165378360; -.
DR eggNOG; NOG303042; -.
DR HOVERGEN; HBG069733; -.
DR InParanoid; O75170; -.
DR KO; K15500; -.
DR OMA; PPKKKAI; -.
DR OrthoDB; EOG7PGDQ3; -.
DR PhylomeDB; O75170; -.
DR ChiTaRS; PPP6R2; human.
DR GenomeRNAi; 9701; -.
DR NextBio; 36455; -.
DR PRO; PR:O75170; -.
DR ArrayExpress; O75170; -.
DR Bgee; O75170; -.
DR CleanEx; HS_SAPS2; -.
DR Genevestigator; O75170; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR007587; SAPS.
DR PANTHER; PTHR12634; PTHR12634; 1.
DR Pfam; PF04499; SAPS; 2.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT CHAIN 1 966 Serine/threonine-protein phosphatase 6
FT regulatory subunit 2.
FT /FTId=PRO_0000046098.
FT COMPBIAS 820 825 Poly-Ser.
FT MOD_RES 289 289 Phosphoserine.
FT VAR_SEQ 58 84 Missing (in isoform 6).
FT /FTId=VSP_037767.
FT VAR_SEQ 244 244 S -> SR (in isoform 3).
FT /FTId=VSP_037768.
FT VAR_SEQ 535 561 Missing (in isoform 2, isoform 3, isoform
FT 4 and isoform 6).
FT /FTId=VSP_030758.
FT VAR_SEQ 709 709 E -> EA (in isoform 2).
FT /FTId=VSP_030759.
FT VAR_SEQ 792 799 SQASYFAV -> F (in isoform 2, isoform 3,
FT isoform 4, isoform 5 and isoform 6).
FT /FTId=VSP_030760.
FT VAR_SEQ 952 966 KTDAPPEGAALNGPV -> QMPRQKELP (in isoform
FT 2).
FT /FTId=VSP_030761.
FT VARIANT 633 633 D -> E (in dbSNP:rs11555194).
FT /FTId=VAR_058402.
FT VARIANT 732 732 R -> K (in dbSNP:rs13057311).
FT /FTId=VAR_058403.
FT CONFLICT 224 224 D -> G (in Ref. 2; BAH13719).
FT CONFLICT 806 806 A -> T (in Ref. 2; BAH13719).
FT CONFLICT 835 835 Q -> H (in Ref. 4; AAH52995).
SQ SEQUENCE 966 AA; 104942 MW; D3BC10EADB98FB62 CRC64;
MFWKFDLNTT SHVDKLLDKE HVTLQELMDE DDILQECKAQ NQKLLDFLCR QQCMEELVSL
ITQDPPLDME EKVRFKYPNT ACELLTCDVP QISDRLGGDE SLLSLLYDFL DHEPPLNPLL
ASFFSKTIGN LIARKTEQVI TFLKKKDKFI SLVLKHIGTS ALMDLLLRLV SCVEPAGLRQ
DVLHWLNEEK VIQRLVELIH PSQDEDRQSN ASQTLCDIVR LGRDQGSQLQ EALEPDPLLT
ALESQDCVEQ LLKNMFDGDR TESCLVSGTQ VLLTLLETRR VGTEGLVDSF SQGLERSYAV
SSSVLHGIEP RLKDFHQLLL NPPKKKAILT TIGVLEEPLG NARLHGARLM AALLHTNTPS
INQELCRLNT MDLLLDLFFK YTWNNFLHFQ VELCIAAILS HAAREERTEA SGSESRVEPP
HENGNRSLET PQPAASLPDN TMVTHLFQKC CLVQRILEAW EANDHTQAAG GMRRGNMGHL
TRIANAVVQN LERGPVQTHI SEVIRGLPAD CRGRWESFVE ETLTETNRRN TVDLVSTHHL
HSSSEDEDIE GAFPNELSLQ QAFSDYQIQQ MTANFVDQFG FNDEEFADQD DNINAPFDRI
AEINFNIDAD EDSPSAALFE ACCSDRIQPF DDDEDEDIWE DSDTRCAARV MARPRFGAPH
ASESCSKNGP ERGGQDGKAS LEAHRDAPGA GAPPAPGKKE APPVEGDSEG AMWTAVFDEP
ANSTPTAPGV VRDVGSSVWA AGTSAPEEKG WAKFTDFQPF CCSESGPRCS SPVDTECSHA
EGSRSQGPEK ASQASYFAVS PASPCAWNVC VTRKAPLLAS DSSSSGGSHS EDGDQKAASA
MDAVSRGPGR EAPPLPTVAR TEEAVGRVGC ADSRLLSPAC PAPKEVTAAP AVAVPPEATV
AITTALSKAG PAIPTPAVSS ALAVAVPLGP IMAVTAAPAM VATLGTVTKD GKTDAPPEGA
ALNGPV
//
ID PP6R2_HUMAN Reviewed; 966 AA.
AC O75170; A6PVG3; B7Z7T3; Q5U5P3; Q7Z2L2; Q7Z5G5; Q7Z731; Q9UGB9;
read moreDT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=Serine/threonine-protein phosphatase 6 regulatory subunit 2;
DE AltName: Full=SAPS domain family member 2;
GN Name=PPP6R2; Synonyms=KIAA0685, PP6R2, SAPS2;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 6).
RC TISSUE=Brain, Lymph, Muscle, Placenta, and Skin;
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 [5]
RP FUNCTION, INTERACTION WITH PPP6C AND NFKBIE, SUBCELLULAR LOCATION, AND
RP 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 [6]
RP 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 [7]
RP IDENTIFICATION BY 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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, 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 [9]
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND MASS
RP 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 [11]
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).
CC -!- FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6). May
CC function as a scaffolding PP6 subunit. Involved in the PP6-
CC mediated dephosphorylation of NFKBIE opposing its degradation in
CC response to TNF-alpha.
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 NFKBIE. Interacts with ANKRD28.
CC -!- INTERACTION:
CC O15084:ANKRD28; NbExp=7; IntAct=EBI-359739, EBI-359567;
CC O00743:PPP6C; NbExp=8; IntAct=EBI-359739, EBI-359751;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=O75170-1; Sequence=Displayed;
CC Note=No experimental confirmation available;
CC Name=2;
CC IsoId=O75170-2; Sequence=VSP_030758, VSP_030759, VSP_030760,
CC VSP_030761;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=O75170-3; Sequence=VSP_037768, VSP_030758, VSP_030760;
CC Name=4;
CC IsoId=O75170-4; Sequence=VSP_030758, VSP_030760;
CC Name=5;
CC IsoId=O75170-5; Sequence=VSP_030760;
CC Name=6;
CC IsoId=O75170-6; Sequence=VSP_037767, VSP_030758, VSP_030760;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with strongest
CC expression in the testis followed by liver, heart, kidney, brain
CC and placenta.
CC -!- SIMILARITY: Belongs to the SAPS family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31660.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC -----------------------------------------------------------------------
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DR EMBL; AB014585; BAA31660.2; ALT_INIT; mRNA.
DR EMBL; AK302472; BAH13719.1; -; mRNA.
DR EMBL; AL096767; CAO03456.1; -; Genomic_DNA.
DR EMBL; AL671545; CAO03456.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03456.1; JOINED; Genomic_DNA.
DR EMBL; AL096767; CAO03457.1; -; Genomic_DNA.
DR EMBL; AL671545; CAO03457.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03457.1; JOINED; Genomic_DNA.
DR EMBL; AL096767; CAO03458.1; -; Genomic_DNA.
DR EMBL; AL671545; CAO03458.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03458.1; JOINED; Genomic_DNA.
DR EMBL; AL096767; CAO03459.1; -; Genomic_DNA.
DR EMBL; AL671545; CAO03459.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03459.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03561.1; -; Genomic_DNA.
DR EMBL; AL096767; CAO03561.1; JOINED; Genomic_DNA.
DR EMBL; AL671545; CAO03561.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03562.1; -; Genomic_DNA.
DR EMBL; AL096767; CAO03562.1; JOINED; Genomic_DNA.
DR EMBL; AL671545; CAO03562.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03563.1; -; Genomic_DNA.
DR EMBL; AL096767; CAO03563.1; JOINED; Genomic_DNA.
DR EMBL; AL671545; CAO03563.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03564.1; -; Genomic_DNA.
DR EMBL; AL096767; CAO03564.1; JOINED; Genomic_DNA.
DR EMBL; AL671545; CAO03564.1; JOINED; Genomic_DNA.
DR EMBL; AL671545; CAO03642.1; -; Genomic_DNA.
DR EMBL; AL096767; CAO03642.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03642.1; JOINED; Genomic_DNA.
DR EMBL; AL671545; CAO03643.1; -; Genomic_DNA.
DR EMBL; AL096767; CAO03643.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03643.1; JOINED; Genomic_DNA.
DR EMBL; AL671545; CAO03644.1; -; Genomic_DNA.
DR EMBL; AL096767; CAO03644.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03644.1; JOINED; Genomic_DNA.
DR EMBL; AL671545; CAO03645.1; -; Genomic_DNA.
DR EMBL; AL096767; CAO03645.1; JOINED; Genomic_DNA.
DR EMBL; AL954743; CAO03645.1; JOINED; Genomic_DNA.
DR EMBL; BC000976; AAH00976.2; -; mRNA.
DR EMBL; BC006568; AAH06568.1; -; mRNA.
DR EMBL; BC032664; AAH32664.1; -; mRNA.
DR EMBL; BC041698; AAH41698.1; -; mRNA.
DR EMBL; BC052995; AAH52995.1; -; mRNA.
DR PIR; T00357; T00357.
DR RefSeq; NP_001229827.1; NM_001242898.1.
DR RefSeq; NP_001229828.1; NM_001242899.1.
DR RefSeq; NP_001229829.1; NM_001242900.1.
DR RefSeq; NP_055493.2; NM_014678.4.
DR UniGene; Hs.449098; -.
DR UniGene; Hs.733531; -.
DR UniGene; Hs.740776; -.
DR ProteinModelPortal; O75170; -.
DR DIP; DIP-27539N; -.
DR IntAct; O75170; 26.
DR MINT; MINT-1140941; -.
DR PhosphoSite; O75170; -.
DR PaxDb; O75170; -.
DR PRIDE; O75170; -.
DR Ensembl; ENST00000216061; ENSP00000216061; ENSG00000100239.
DR Ensembl; ENST00000359139; ENSP00000352051; ENSG00000100239.
DR Ensembl; ENST00000395741; ENSP00000379090; ENSG00000100239.
DR Ensembl; ENST00000395744; ENSP00000379093; ENSG00000100239.
DR GeneID; 9701; -.
DR KEGG; hsa:9701; -.
DR UCSC; uc003blb.2; human.
DR CTD; 9701; -.
DR GeneCards; GC22P050782; -.
DR HGNC; HGNC:19253; PPP6R2.
DR HPA; HPA030656; -.
DR MIM; 610877; gene.
DR neXtProt; NX_O75170; -.
DR PharmGKB; PA165378360; -.
DR eggNOG; NOG303042; -.
DR HOVERGEN; HBG069733; -.
DR InParanoid; O75170; -.
DR KO; K15500; -.
DR OMA; PPKKKAI; -.
DR OrthoDB; EOG7PGDQ3; -.
DR PhylomeDB; O75170; -.
DR ChiTaRS; PPP6R2; human.
DR GenomeRNAi; 9701; -.
DR NextBio; 36455; -.
DR PRO; PR:O75170; -.
DR ArrayExpress; O75170; -.
DR Bgee; O75170; -.
DR CleanEx; HS_SAPS2; -.
DR Genevestigator; O75170; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR007587; SAPS.
DR PANTHER; PTHR12634; PTHR12634; 1.
DR Pfam; PF04499; SAPS; 2.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT CHAIN 1 966 Serine/threonine-protein phosphatase 6
FT regulatory subunit 2.
FT /FTId=PRO_0000046098.
FT COMPBIAS 820 825 Poly-Ser.
FT MOD_RES 289 289 Phosphoserine.
FT VAR_SEQ 58 84 Missing (in isoform 6).
FT /FTId=VSP_037767.
FT VAR_SEQ 244 244 S -> SR (in isoform 3).
FT /FTId=VSP_037768.
FT VAR_SEQ 535 561 Missing (in isoform 2, isoform 3, isoform
FT 4 and isoform 6).
FT /FTId=VSP_030758.
FT VAR_SEQ 709 709 E -> EA (in isoform 2).
FT /FTId=VSP_030759.
FT VAR_SEQ 792 799 SQASYFAV -> F (in isoform 2, isoform 3,
FT isoform 4, isoform 5 and isoform 6).
FT /FTId=VSP_030760.
FT VAR_SEQ 952 966 KTDAPPEGAALNGPV -> QMPRQKELP (in isoform
FT 2).
FT /FTId=VSP_030761.
FT VARIANT 633 633 D -> E (in dbSNP:rs11555194).
FT /FTId=VAR_058402.
FT VARIANT 732 732 R -> K (in dbSNP:rs13057311).
FT /FTId=VAR_058403.
FT CONFLICT 224 224 D -> G (in Ref. 2; BAH13719).
FT CONFLICT 806 806 A -> T (in Ref. 2; BAH13719).
FT CONFLICT 835 835 Q -> H (in Ref. 4; AAH52995).
SQ SEQUENCE 966 AA; 104942 MW; D3BC10EADB98FB62 CRC64;
MFWKFDLNTT SHVDKLLDKE HVTLQELMDE DDILQECKAQ NQKLLDFLCR QQCMEELVSL
ITQDPPLDME EKVRFKYPNT ACELLTCDVP QISDRLGGDE SLLSLLYDFL DHEPPLNPLL
ASFFSKTIGN LIARKTEQVI TFLKKKDKFI SLVLKHIGTS ALMDLLLRLV SCVEPAGLRQ
DVLHWLNEEK VIQRLVELIH PSQDEDRQSN ASQTLCDIVR LGRDQGSQLQ EALEPDPLLT
ALESQDCVEQ LLKNMFDGDR TESCLVSGTQ VLLTLLETRR VGTEGLVDSF SQGLERSYAV
SSSVLHGIEP RLKDFHQLLL NPPKKKAILT TIGVLEEPLG NARLHGARLM AALLHTNTPS
INQELCRLNT MDLLLDLFFK YTWNNFLHFQ VELCIAAILS HAAREERTEA SGSESRVEPP
HENGNRSLET PQPAASLPDN TMVTHLFQKC CLVQRILEAW EANDHTQAAG GMRRGNMGHL
TRIANAVVQN LERGPVQTHI SEVIRGLPAD CRGRWESFVE ETLTETNRRN TVDLVSTHHL
HSSSEDEDIE GAFPNELSLQ QAFSDYQIQQ MTANFVDQFG FNDEEFADQD DNINAPFDRI
AEINFNIDAD EDSPSAALFE ACCSDRIQPF DDDEDEDIWE DSDTRCAARV MARPRFGAPH
ASESCSKNGP ERGGQDGKAS LEAHRDAPGA GAPPAPGKKE APPVEGDSEG AMWTAVFDEP
ANSTPTAPGV VRDVGSSVWA AGTSAPEEKG WAKFTDFQPF CCSESGPRCS SPVDTECSHA
EGSRSQGPEK ASQASYFAVS PASPCAWNVC VTRKAPLLAS DSSSSGGSHS EDGDQKAASA
MDAVSRGPGR EAPPLPTVAR TEEAVGRVGC ADSRLLSPAC PAPKEVTAAP AVAVPPEATV
AITTALSKAG PAIPTPAVSS ALAVAVPLGP IMAVTAAPAM VATLGTVTKD GKTDAPPEGA
ALNGPV
//
MIM
610877
*RECORD*
*FIELD* NO
610877
*FIELD* TI
*610877 SAPS DOMAIN FAMILY, MEMBER 2; SAPS2
;;PROTEIN PHOSPHATASE 6, REGULATORY SUBUNIT 2; PP6R2;;
read moreKIAA0685
*FIELD* TX
DESCRIPTION
Protein phosphatase regulatory subunits, such as SAPS2, modulate the
activity of protein phosphatase catalytic subunits by restricting
substrate specificity, recruiting substrates, and determining the
intracellular localization of the holoenzyme. SAPS2 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 brain cDNA
library, Ishikawa et al. (1998) cloned SAPS2, which they designated
KIAA0685. The deduced 927-amino acid protein shares significant
similarity with yeast Sap190. RT-PCR detected strong SAPS2 expression in
all tissues examined.
By searching databases for sequences similar to yeast Sap155, Sap185,
and Sap190, Stefansson and Brautigan (2006) identified SAPS2, which they
called PP6R2. The deduced 966-amino acid protein has a calculated
molecular mass of 105 kD and contains a central alpha-helical SAPS
domain of about 400 amino acids. Northern blot analysis detected 2
transcripts in all tissues examined, with highest expression in testis,
followed by liver, heart, and brain.
GENE FUNCTION
Using coimmunoprecipitation and protein pull-down assays, Stefansson and
Brautigan (2006) showed that epitope-tagged PP6R2 bound endogenous
PPP6C, but not PPP2CA (176915). Immunoprecipitates containing PPP6C and
PP6R2 showed phosphatase activity against a test protein, and the
activity was inhibited by okadaic acid, a serine/threonine phosphatase
inhibitor. Stefansson and Brautigan (2006) found that PP6R2 and PPP6C
associated with I-kappa-B-epsilon (IKBE, or NFKBIE; 604548) in HeLa
cells. PP6R2 did not interact with epitope-tagged IKBA (NFKBIA; 164008)
or IKBB (NFKBIB; 604495).
MAPPING
By radiation hybrid analysis, Ishikawa et al. (1998) mapped the SAPS2
gene to chromosome 22.
*FIELD* RF
1. Ishikawa, K.; Nagase, T.; Suyama, M.; Miyajima, N.; Tanaka, A.;
Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the coding sequences
of unidentified human genes. X. The complete sequences of 100 new
cDNA clones from brain which can code for large proteins in vitro. DNA
Res. 5: 169-176, 1998.
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.
*FIELD* CD
Patricia A. Hartz: 3/23/2007
*FIELD* ED
terry: 09/07/2010
mgross: 3/23/2007
*RECORD*
*FIELD* NO
610877
*FIELD* TI
*610877 SAPS DOMAIN FAMILY, MEMBER 2; SAPS2
;;PROTEIN PHOSPHATASE 6, REGULATORY SUBUNIT 2; PP6R2;;
read moreKIAA0685
*FIELD* TX
DESCRIPTION
Protein phosphatase regulatory subunits, such as SAPS2, modulate the
activity of protein phosphatase catalytic subunits by restricting
substrate specificity, recruiting substrates, and determining the
intracellular localization of the holoenzyme. SAPS2 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 brain cDNA
library, Ishikawa et al. (1998) cloned SAPS2, which they designated
KIAA0685. The deduced 927-amino acid protein shares significant
similarity with yeast Sap190. RT-PCR detected strong SAPS2 expression in
all tissues examined.
By searching databases for sequences similar to yeast Sap155, Sap185,
and Sap190, Stefansson and Brautigan (2006) identified SAPS2, which they
called PP6R2. The deduced 966-amino acid protein has a calculated
molecular mass of 105 kD and contains a central alpha-helical SAPS
domain of about 400 amino acids. Northern blot analysis detected 2
transcripts in all tissues examined, with highest expression in testis,
followed by liver, heart, and brain.
GENE FUNCTION
Using coimmunoprecipitation and protein pull-down assays, Stefansson and
Brautigan (2006) showed that epitope-tagged PP6R2 bound endogenous
PPP6C, but not PPP2CA (176915). Immunoprecipitates containing PPP6C and
PP6R2 showed phosphatase activity against a test protein, and the
activity was inhibited by okadaic acid, a serine/threonine phosphatase
inhibitor. Stefansson and Brautigan (2006) found that PP6R2 and PPP6C
associated with I-kappa-B-epsilon (IKBE, or NFKBIE; 604548) in HeLa
cells. PP6R2 did not interact with epitope-tagged IKBA (NFKBIA; 164008)
or IKBB (NFKBIB; 604495).
MAPPING
By radiation hybrid analysis, Ishikawa et al. (1998) mapped the SAPS2
gene to chromosome 22.
*FIELD* RF
1. Ishikawa, K.; Nagase, T.; Suyama, M.; Miyajima, N.; Tanaka, A.;
Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the coding sequences
of unidentified human genes. X. The complete sequences of 100 new
cDNA clones from brain which can code for large proteins in vitro. DNA
Res. 5: 169-176, 1998.
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.
*FIELD* CD
Patricia A. Hartz: 3/23/2007
*FIELD* ED
terry: 09/07/2010
mgross: 3/23/2007