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PP6R2_MOUSE
ID   PP6R2_MOUSE             Reviewed;         923 AA.
AC   Q8R3Q2; Q9CXB7;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 127.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-206.
RC   STRAIN=C57BL/6J; TISSUE=Embryonic lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Lung, Pancreas, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6). May
CC       function as a scaffolding PP6 subunit. Involved in the PP6-mediated
CC       dephosphorylation of NFKBIE opposing its degradation in response to
CC       TNF-alpha.
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 NFKBIE. Interacts
CC       with ANKRD28 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Strongest expression in bladder and lower levels
CC       found in heart and pancreas. Very weak expression observed in all other
CC       tissues tested. {ECO:0000269|PubMed:16769727}.
CC   -!- SIMILARITY: Belongs to the SAPS family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AK018403; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BC024879; AAH24879.1; -; mRNA.
DR   EMBL; AK018403; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS27743.1; -.
DR   AlphaFoldDB; Q8R3Q2; -.
DR   SMR; Q8R3Q2; -.
DR   IntAct; Q8R3Q2; 3.
DR   STRING; 10090.ENSMUSP00000086167; -.
DR   iPTMnet; Q8R3Q2; -.
DR   PhosphoSitePlus; Q8R3Q2; -.
DR   EPD; Q8R3Q2; -.
DR   jPOST; Q8R3Q2; -.
DR   MaxQB; Q8R3Q2; -.
DR   PaxDb; Q8R3Q2; -.
DR   PRIDE; Q8R3Q2; -.
DR   ProteomicsDB; 289873; -.
DR   MGI; MGI:1918724; Ppp6r2.
DR   eggNOG; KOG2073; Eukaryota.
DR   InParanoid; Q8R3Q2; -.
DR   PhylomeDB; Q8R3Q2; -.
DR   ChiTaRS; Ppp6r2; mouse.
DR   PRO; PR:Q8R3Q2; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q8R3Q2; protein.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0019903; F:protein phosphatase binding; ISA:MGI.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR   GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; ISA: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   Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..923
FT                   /note="Serine/threonine-protein phosphatase 6 regulatory
FT                   subunit 2"
FT                   /id="PRO_0000046099"
FT   REGION          409..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          662..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          743..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..441
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        666..685
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         289
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75170"
FT   MOD_RES         746
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         796
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75170"
FT   CONFLICT        106
FT                   /note="L -> H (in Ref. 2; AK018403)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        167
FT                   /note="L -> C (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        195
FT                   /note="L -> I (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   923 AA;  100460 MW;  02F604745D69067B CRC64;
     MFWKFDLNTT SHVDKLLDKE HVTLQELMDE DDILQECKAQ NQKLLDFLCR QQCMEELVNL
     ITQDPPQDME EKVRFKYPNT ACELLTCDVP QISDRLGEDE SLLNLLYDFL DQEPPLNPLL
     ASFFSKTIGN LIARKTEQVI MFLKKKEKFI SQLLKHIGTS ALMDLLLRLV SCVEPVGLRQ
     EVLHWLNEEK IIQRLVALIH PHQDEDRQSN ASQALCDIIR LGRDQGSQLQ ETVEPDPLLI
     TLESQDCVEQ LLKNMFDGDQ TESCLVSGMQ VLLALLEPRR VGTEGLVDSF SQGLERSHSV
     SSSILRGIEP WLKNFHQLLL NPPKKKAILT TIGVLEEPLG NARLHGARLM AALLHTNTPG
     INQELCRLNT MDLLLDLFFK YTWNNFLHLQ VELCIAAILS HAAREEQAEA SGSDGKVEPL
     QGSGDGNGKL ETTPSITSPP ENTMVTHLFQ KCCLVQRILE AWEANDHTQA AGGMRRGNMG
     HLTRIANAVV QNLEQGPVQA HISEVIRGLP ADCRGRWESF VEETLMETNR RNTVDLAFSE
     YQIQQMTANF VDQFGFNDEE FADQDDNINA PFDRIAEINF NIEADEDSPS AALFEACCSD
     RIQPFDDDEE EDIWEDDETR CAARVMARAR FGAPHVSDNY SKNALEHGGQ DRKTGSAVAR
     NVPGLAAPSS PTQKEGPRSE SDSAGTTWTA VFDEPVNPLS ATPGAARDVG SSAWAAGPSV
     VEEKGWAKFT DFQPFCCSET GPRCSSPVDM DHSNAEGGQS PGPEKTFGPT SPCAWNVCVT
     RKAPLVASDS SSSGGSDSED DEKAAGAVEA VCTGHTGKVS PPPRTAEAAV GRAECPDSTV
     LAPACPAPSE VTISPAVATI APSKAGSPTA TIVVSSSVAA AVPPGPIVAV TTAAPAIVAT
     LGTMTKDRKA DALPEGAALN GPV
 
 
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