Full text data of PPP6R1
PPP6R1
(KIAA1115, PP6R1, SAPS1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Serine/threonine-protein phosphatase 6 regulatory subunit 1 (SAPS domain family member 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Serine/threonine-protein phosphatase 6 regulatory subunit 1 (SAPS domain family member 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UPN7
ID PP6R1_HUMAN Reviewed; 881 AA.
AC Q9UPN7; Q2M2H3; Q504V2; Q6NVJ6; Q9BU97;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-OCT-2009, sequence version 5.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Serine/threonine-protein phosphatase 6 regulatory subunit 1;
DE AltName: Full=SAPS domain family member 1;
GN Name=PPP6R1; Synonyms=KIAA1115, PP6R1, SAPS1;
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].
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph, Skin, and Testis;
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 [4]
RP IDENTIFICATION BY 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
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; ANKRD28; ANKRD44 AND ANKRD52, AND SUBCELLULAR
RP LOCATION.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635; SER-638 AND
RP SER-759, AND MASS 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635; SER-638; SER-702;
RP SER-726 AND SER-759, AND 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 [10]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-524; SER-635 AND
RP SER-638, AND 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. 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 of 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, ANKRD44 and ANKRD52.
CC -!- INTERACTION:
CC O15084:ANKRD28; NbExp=10; IntAct=EBI-359745, EBI-359567;
CC Q8N8A2:ANKRD44; NbExp=4; IntAct=EBI-359745, EBI-1245329;
CC Q8NB46:ANKRD52; NbExp=4; IntAct=EBI-359745, EBI-1996119;
CC O00743:PPP6C; NbExp=11; IntAct=EBI-359745, EBI-359751;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Ubiquitous with higher expression in testis.
CC -!- SIMILARITY: Belongs to the SAPS family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA83067.3; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB029038; BAA83067.3; ALT_INIT; mRNA.
DR EMBL; BC002799; AAH02799.2; -; mRNA.
DR EMBL; BC068014; AAH68014.1; -; mRNA.
DR EMBL; BC094753; AAH94753.2; -; mRNA.
DR RefSeq; NP_055746.3; NM_014931.3.
DR RefSeq; XP_005258726.1; XM_005258669.1.
DR RefSeq; XP_005258727.1; XM_005258670.1.
DR UniGene; Hs.515610; -.
DR ProteinModelPortal; Q9UPN7; -.
DR DIP; DIP-27589N; -.
DR IntAct; Q9UPN7; 37.
DR MINT; MINT-1154650; -.
DR PhosphoSite; Q9UPN7; -.
DR DMDM; 261260102; -.
DR PaxDb; Q9UPN7; -.
DR PRIDE; Q9UPN7; -.
DR Ensembl; ENST00000412770; ENSP00000414202; ENSG00000105063.
DR Ensembl; ENST00000587283; ENSP00000467521; ENSG00000105063.
DR GeneID; 22870; -.
DR KEGG; hsa:22870; -.
DR UCSC; uc002qjv.3; human.
DR CTD; 22870; -.
DR GeneCards; GC19M055742; -.
DR HGNC; HGNC:29195; PPP6R1.
DR HPA; HPA043989; -.
DR MIM; 610875; gene.
DR neXtProt; NX_Q9UPN7; -.
DR PharmGKB; PA165394108; -.
DR eggNOG; NOG303042; -.
DR HOVERGEN; HBG069733; -.
DR InParanoid; Q9UPN7; -.
DR KO; K15499; -.
DR OMA; GAWQGSQ; -.
DR OrthoDB; EOG7PGDQ3; -.
DR ChiTaRS; PPP6R1; human.
DR GenomeRNAi; 22870; -.
DR NextBio; 43399; -.
DR PMAP-CutDB; Q9UPN7; -.
DR PRO; PR:Q9UPN7; -.
DR ArrayExpress; Q9UPN7; -.
DR Bgee; Q9UPN7; -.
DR CleanEx; HS_SAPS1; -.
DR Genevestigator; Q9UPN7; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
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; 5.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1 881 Serine/threonine-protein phosphatase 6
FT regulatory subunit 1.
FT /FTId=PRO_0000046096.
FT REGION 10 403 Interaction with PPP6C.
FT COMPBIAS 624 685 Glu-rich.
FT COMPBIAS 624 631 Poly-Glu.
FT COMPBIAS 671 685 Poly-Glu.
FT COMPBIAS 697 878 Pro-rich.
FT MOD_RES 524 524 Phosphothreonine.
FT MOD_RES 529 529 Phosphoserine (By similarity).
FT MOD_RES 530 530 Phosphoserine (By similarity).
FT MOD_RES 531 531 Phosphoserine (By similarity).
FT MOD_RES 635 635 Phosphoserine.
FT MOD_RES 638 638 Phosphoserine.
FT MOD_RES 702 702 Phosphoserine.
FT MOD_RES 726 726 Phosphoserine.
FT MOD_RES 759 759 Phosphoserine.
SQ SEQUENCE 881 AA; 96724 MW; 36DDA2E945ED599A CRC64;
MFWKFDLHTS SHLDTLLERE DLSLPELLDE EDVLQECKVV NRKLLDFLLQ PPHLQAMVAW
VTQEPPDSGE ERLRYKYPSV ACEILTSDVP QINDALGADE SLLNRLYGFL QSTGSLNPLL
ASFFSKVMGI LINRKTDQLV SFLRKKDDFV DLLLQHIGTS AIMDLLLRLL TCVERPQLRQ
DVVNWLNEEK IVQRLIEQIH PSKDENQHSN ASQSLCDIIR LSREQMIQVQ DSPEPDQLLA
TLEKQETIEQ LLSNMFEGEQ SQSVIVSGIQ VLLTLLEPRR PRSESVTVNS FFSSVDGQLE
LLAQGALEST VSSVGALHAL RPRLSCFHQL LLEPPKLEPL QMTWGMLAPP LGNTRLHVVK
LLASALSAND AALTHELLAL DVPNTMLDLF FHYVFNNFLH AQVEGCVSTM LSLGPPPDSS
PETPIQNPVV KHLLQQCRLV ERILTSWEEN DRVQCAGGPR KGYMGHLTRV AGALVQNTEK
GPNAEQLRQL LKELPSEQQE QWEAFVSGPL AETNKKNMVD LVNTHHLHSS SDDEDDRLKE
FNFPEEAVLQ QAFMDFQMQR MTSAFIDHFG FNDEEFGEQE ESVNAPFDKT ANITFSLNAD
DENPNANLLE ICYKDRIQQF DDDEEEEDEE EAQGSGESDG EDGAWQGSQL ARGARLGQPP
GVRSGGSTDS EDEEEEDEEE EEDEEGIGCA ARGGATPLSY PSPGPQPPGP SWTATFDPVP
TDAPTSPRVS GEEELHTGPP APQGPLSVPQ GLPTQSLASP PARDALQLRS QDPTPPSAPQ
EATEGSKVTE PSAPCQALVS IGDLQATFHG IRSAPSSSDS ATRDPSTSVP ASGAHQPPQT
TEGEKSPEPL GLPQSQSAQA LTPPPIPNGS APEGPASPGS Q
//
ID PP6R1_HUMAN Reviewed; 881 AA.
AC Q9UPN7; Q2M2H3; Q504V2; Q6NVJ6; Q9BU97;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-OCT-2009, sequence version 5.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Serine/threonine-protein phosphatase 6 regulatory subunit 1;
DE AltName: Full=SAPS domain family member 1;
GN Name=PPP6R1; Synonyms=KIAA1115, PP6R1, SAPS1;
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].
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph, Skin, and Testis;
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 [4]
RP IDENTIFICATION BY 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
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; ANKRD28; ANKRD44 AND ANKRD52, AND SUBCELLULAR
RP LOCATION.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635; SER-638 AND
RP SER-759, AND MASS 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635; SER-638; SER-702;
RP SER-726 AND SER-759, AND 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 [10]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-524; SER-635 AND
RP SER-638, AND 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. 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 of 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, ANKRD44 and ANKRD52.
CC -!- INTERACTION:
CC O15084:ANKRD28; NbExp=10; IntAct=EBI-359745, EBI-359567;
CC Q8N8A2:ANKRD44; NbExp=4; IntAct=EBI-359745, EBI-1245329;
CC Q8NB46:ANKRD52; NbExp=4; IntAct=EBI-359745, EBI-1996119;
CC O00743:PPP6C; NbExp=11; IntAct=EBI-359745, EBI-359751;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Ubiquitous with higher expression in testis.
CC -!- SIMILARITY: Belongs to the SAPS family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA83067.3; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB029038; BAA83067.3; ALT_INIT; mRNA.
DR EMBL; BC002799; AAH02799.2; -; mRNA.
DR EMBL; BC068014; AAH68014.1; -; mRNA.
DR EMBL; BC094753; AAH94753.2; -; mRNA.
DR RefSeq; NP_055746.3; NM_014931.3.
DR RefSeq; XP_005258726.1; XM_005258669.1.
DR RefSeq; XP_005258727.1; XM_005258670.1.
DR UniGene; Hs.515610; -.
DR ProteinModelPortal; Q9UPN7; -.
DR DIP; DIP-27589N; -.
DR IntAct; Q9UPN7; 37.
DR MINT; MINT-1154650; -.
DR PhosphoSite; Q9UPN7; -.
DR DMDM; 261260102; -.
DR PaxDb; Q9UPN7; -.
DR PRIDE; Q9UPN7; -.
DR Ensembl; ENST00000412770; ENSP00000414202; ENSG00000105063.
DR Ensembl; ENST00000587283; ENSP00000467521; ENSG00000105063.
DR GeneID; 22870; -.
DR KEGG; hsa:22870; -.
DR UCSC; uc002qjv.3; human.
DR CTD; 22870; -.
DR GeneCards; GC19M055742; -.
DR HGNC; HGNC:29195; PPP6R1.
DR HPA; HPA043989; -.
DR MIM; 610875; gene.
DR neXtProt; NX_Q9UPN7; -.
DR PharmGKB; PA165394108; -.
DR eggNOG; NOG303042; -.
DR HOVERGEN; HBG069733; -.
DR InParanoid; Q9UPN7; -.
DR KO; K15499; -.
DR OMA; GAWQGSQ; -.
DR OrthoDB; EOG7PGDQ3; -.
DR ChiTaRS; PPP6R1; human.
DR GenomeRNAi; 22870; -.
DR NextBio; 43399; -.
DR PMAP-CutDB; Q9UPN7; -.
DR PRO; PR:Q9UPN7; -.
DR ArrayExpress; Q9UPN7; -.
DR Bgee; Q9UPN7; -.
DR CleanEx; HS_SAPS1; -.
DR Genevestigator; Q9UPN7; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
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; 5.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1 881 Serine/threonine-protein phosphatase 6
FT regulatory subunit 1.
FT /FTId=PRO_0000046096.
FT REGION 10 403 Interaction with PPP6C.
FT COMPBIAS 624 685 Glu-rich.
FT COMPBIAS 624 631 Poly-Glu.
FT COMPBIAS 671 685 Poly-Glu.
FT COMPBIAS 697 878 Pro-rich.
FT MOD_RES 524 524 Phosphothreonine.
FT MOD_RES 529 529 Phosphoserine (By similarity).
FT MOD_RES 530 530 Phosphoserine (By similarity).
FT MOD_RES 531 531 Phosphoserine (By similarity).
FT MOD_RES 635 635 Phosphoserine.
FT MOD_RES 638 638 Phosphoserine.
FT MOD_RES 702 702 Phosphoserine.
FT MOD_RES 726 726 Phosphoserine.
FT MOD_RES 759 759 Phosphoserine.
SQ SEQUENCE 881 AA; 96724 MW; 36DDA2E945ED599A CRC64;
MFWKFDLHTS SHLDTLLERE DLSLPELLDE EDVLQECKVV NRKLLDFLLQ PPHLQAMVAW
VTQEPPDSGE ERLRYKYPSV ACEILTSDVP QINDALGADE SLLNRLYGFL QSTGSLNPLL
ASFFSKVMGI LINRKTDQLV SFLRKKDDFV DLLLQHIGTS AIMDLLLRLL TCVERPQLRQ
DVVNWLNEEK IVQRLIEQIH PSKDENQHSN ASQSLCDIIR LSREQMIQVQ DSPEPDQLLA
TLEKQETIEQ LLSNMFEGEQ SQSVIVSGIQ VLLTLLEPRR PRSESVTVNS FFSSVDGQLE
LLAQGALEST VSSVGALHAL RPRLSCFHQL LLEPPKLEPL QMTWGMLAPP LGNTRLHVVK
LLASALSAND AALTHELLAL DVPNTMLDLF FHYVFNNFLH AQVEGCVSTM LSLGPPPDSS
PETPIQNPVV KHLLQQCRLV ERILTSWEEN DRVQCAGGPR KGYMGHLTRV AGALVQNTEK
GPNAEQLRQL LKELPSEQQE QWEAFVSGPL AETNKKNMVD LVNTHHLHSS SDDEDDRLKE
FNFPEEAVLQ QAFMDFQMQR MTSAFIDHFG FNDEEFGEQE ESVNAPFDKT ANITFSLNAD
DENPNANLLE ICYKDRIQQF DDDEEEEDEE EAQGSGESDG EDGAWQGSQL ARGARLGQPP
GVRSGGSTDS EDEEEEDEEE EEDEEGIGCA ARGGATPLSY PSPGPQPPGP SWTATFDPVP
TDAPTSPRVS GEEELHTGPP APQGPLSVPQ GLPTQSLASP PARDALQLRS QDPTPPSAPQ
EATEGSKVTE PSAPCQALVS IGDLQATFHG IRSAPSSSDS ATRDPSTSVP ASGAHQPPQT
TEGEKSPEPL GLPQSQSAQA LTPPPIPNGS APEGPASPGS Q
//
MIM
610875
*RECORD*
*FIELD* NO
610875
*FIELD* TI
*610875 SAPS DOMAIN FAMILY, MEMBER 1; SAPS1
;;PROTEIN PHOSPHATASE 6, REGULATORY SUBUNIT 1; PP6R1;;
read moreKIAA1115
*FIELD* TX
DESCRIPTION
Protein phosphatase regulatory subunits, such as SAPS1, modulate the
activity of protein phosphatase catalytic subunits by restricting
substrate specificity, recruiting substrates, and determining the
intracellular localization of the holoenzyme. SAPS1 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, Kikuno et al. (1999) cloned SAPS1, which they designated
KIAA1115. The transcript contains a repetitive element in its 5-prime
end, and the deduced protein contains 754 amino acids. RT-PCR ELISA
detected moderate to high expression in all adult and fetal tissues
examined, with highest levels in heart, brain, lung, testis, and ovary.
Moderate to high expression was also detected in all brain regions
examined.
By searching databases for sequences similar to yeast Sap155, Sap185,
and Sap190, Stefansson and Brautigan (2006) identified SAPS1, which they
called PP6R1. The deduced 829-amino acid protein has a central
alpha-helical SAPS domain of about 400 amino acids. Northern blot
analysis detected a 4-kb transcript that was highly expressed in testis
and moderately expressed in all other tissues examined. Western blot
analysis of fractionated HeLa and HEK293 cells showed PP6R1 in the
cytosolic fraction.
GENE FUNCTION
Using coimmunoprecipitation and protein pull-down assays, Stefansson and
Brautigan (2006) showed that epitope-tagged PP6R1 bound endogenous
PPP6C, but not PPP2CA (176915). The SAPS domain of PP6R1 was sufficient
for its association with PPP6C. Immunoprecipitates containing PPP6C and
PP6R1 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 PP6R1 and PPP6C
associated with I-kappa-B-epsilon (IKBE, or NFKBIE; 604548) in HeLa
cells, and knockdown of PP6R1 enhanced degradation of endogenous IKBE in
response to TNF-alpha (191160). PP6R1 did not interact with
epitope-tagged IKBA (NFKBIA; 164008) or IKBB (NFKBIB; 604495).
MAPPING
By radiation hybrid analysis, Kikuno et al. (1999) mapped the SAPS1 gene
to chromosome 19.
*FIELD* RF
1. Kikuno, R.; Nagase, T.; Ishikawa, K.; Hirosawa, M.; Miyajima, N.;
Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the
coding sequences of unidentified human genes. XIV. The complete sequences
of 100 new cDNA clones from brain which code for large proteins in
vitro. DNA Res. 6: 197-205, 1999.
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
610875
*FIELD* TI
*610875 SAPS DOMAIN FAMILY, MEMBER 1; SAPS1
;;PROTEIN PHOSPHATASE 6, REGULATORY SUBUNIT 1; PP6R1;;
read moreKIAA1115
*FIELD* TX
DESCRIPTION
Protein phosphatase regulatory subunits, such as SAPS1, modulate the
activity of protein phosphatase catalytic subunits by restricting
substrate specificity, recruiting substrates, and determining the
intracellular localization of the holoenzyme. SAPS1 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, Kikuno et al. (1999) cloned SAPS1, which they designated
KIAA1115. The transcript contains a repetitive element in its 5-prime
end, and the deduced protein contains 754 amino acids. RT-PCR ELISA
detected moderate to high expression in all adult and fetal tissues
examined, with highest levels in heart, brain, lung, testis, and ovary.
Moderate to high expression was also detected in all brain regions
examined.
By searching databases for sequences similar to yeast Sap155, Sap185,
and Sap190, Stefansson and Brautigan (2006) identified SAPS1, which they
called PP6R1. The deduced 829-amino acid protein has a central
alpha-helical SAPS domain of about 400 amino acids. Northern blot
analysis detected a 4-kb transcript that was highly expressed in testis
and moderately expressed in all other tissues examined. Western blot
analysis of fractionated HeLa and HEK293 cells showed PP6R1 in the
cytosolic fraction.
GENE FUNCTION
Using coimmunoprecipitation and protein pull-down assays, Stefansson and
Brautigan (2006) showed that epitope-tagged PP6R1 bound endogenous
PPP6C, but not PPP2CA (176915). The SAPS domain of PP6R1 was sufficient
for its association with PPP6C. Immunoprecipitates containing PPP6C and
PP6R1 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 PP6R1 and PPP6C
associated with I-kappa-B-epsilon (IKBE, or NFKBIE; 604548) in HeLa
cells, and knockdown of PP6R1 enhanced degradation of endogenous IKBE in
response to TNF-alpha (191160). PP6R1 did not interact with
epitope-tagged IKBA (NFKBIA; 164008) or IKBB (NFKBIB; 604495).
MAPPING
By radiation hybrid analysis, Kikuno et al. (1999) mapped the SAPS1 gene
to chromosome 19.
*FIELD* RF
1. Kikuno, R.; Nagase, T.; Ishikawa, K.; Hirosawa, M.; Miyajima, N.;
Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the
coding sequences of unidentified human genes. XIV. The complete sequences
of 100 new cDNA clones from brain which code for large proteins in
vitro. DNA Res. 6: 197-205, 1999.
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