Full text data of PPP1R7
PPP1R7
(SDS22)
[Confidence: low (only semi-automatic identification from reviews)]
Protein phosphatase 1 regulatory subunit 7 (Protein phosphatase 1 regulatory subunit 22)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Protein phosphatase 1 regulatory subunit 7 (Protein phosphatase 1 regulatory subunit 22)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q15435
ID PP1R7_HUMAN Reviewed; 360 AA.
AC Q15435; B4DFD4; Q9UQE5; Q9UQE6; Q9Y6K4;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 7;
DE AltName: Full=Protein phosphatase 1 regulatory subunit 22;
GN Name=PPP1R7; Synonyms=SDS22;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=7498485; DOI=10.1016/0014-5793(95)01180-M;
RA Renouf S., Beullens M., Wera S., Van Eynde A., Sikela J., Stalmans W.,
RA Bollen M.;
RT "Molecular cloning of a human polypeptide related to yeast sds22, a
RT regulator of protein phosphatase-1.";
RL FEBS Lett. 375:75-78(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=10231361; DOI=10.1046/j.1432-1327.1999.00344.x;
RA Ceulemans H., Van Eynde A., Perez-Callejon E., Beullens M.,
RA Stalmans W., Bollen M.;
RT "Structure and splice products of the human gene encoding sds22, a
RT putative mitotic regulator of protein phosphatase-1.";
RL Eur. J. Biochem. 262:36-42(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Cervix;
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 INTERACTION WITH PPP1CA; PPP1CB AND PPP1CC ISOFORM 1, AND MUTAGENESIS
RP OF ASP-148; PHE-170; GLU-192; PHE-214; ASP-280; GLU-300; TRP-302 AND
RP TYR-327.
RX PubMed=12226088; DOI=10.1074/jbc.M206838200;
RA Ceulemans H., Vulsteke V., De Maeyer M., Tatchell K., Stalmans W.,
RA Bollen M.;
RT "Binding of the concave surface of the Sds22 superhelix to the alpha
RT 4/alpha 5/alpha 6-triangle of protein phosphatase-1.";
RL J. Biol. Chem. 277:47331-47337(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-27, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-27; SER-44 AND
RP SER-47, AND 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 [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 SER-12; SER-24 AND SER-27,
RP 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 1 (By
CC similarity).
CC -!- SUBUNIT: Interacts with PPP1CA, PPP1CB and PPP1CC/PPP1G isoform 1.
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=sds22alpha1;
CC IsoId=Q15435-1; Sequence=Displayed;
CC Name=2; Synonyms=sds22alpha2;
CC IsoId=Q15435-2; Sequence=VSP_019244;
CC Name=3; Synonyms=sds22beta1;
CC IsoId=Q15435-3; Sequence=VSP_019245, VSP_019246;
CC Name=4; Synonyms=sds22beta2;
CC IsoId=Q15435-4; Sequence=VSP_019244, VSP_019245, VSP_019246;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the SDS22 family.
CC -!- SIMILARITY: Contains 11 LRR (leucine-rich) repeats.
CC -!- SIMILARITY: Contains 1 LRRCT domain.
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DR EMBL; Z50749; CAA90626.1; -; mRNA.
DR EMBL; AF067136; AAD26610.1; -; Genomic_DNA.
DR EMBL; AF067130; AAD26610.1; JOINED; Genomic_DNA.
DR EMBL; AF067132; AAD26610.1; JOINED; Genomic_DNA.
DR EMBL; AF067133; AAD26610.1; JOINED; Genomic_DNA.
DR EMBL; AF067134; AAD26610.1; JOINED; Genomic_DNA.
DR EMBL; AF067135; AAD26610.1; JOINED; Genomic_DNA.
DR EMBL; AF067136; AAD26611.1; -; Genomic_DNA.
DR EMBL; AF067130; AAD26611.1; JOINED; Genomic_DNA.
DR EMBL; AF067132; AAD26611.1; JOINED; Genomic_DNA.
DR EMBL; AF067134; AAD26611.1; JOINED; Genomic_DNA.
DR EMBL; AF067135; AAD26611.1; JOINED; Genomic_DNA.
DR EMBL; AF067133; AAD26611.1; JOINED; Genomic_DNA.
DR EMBL; AF067131; AAD26611.1; JOINED; Genomic_DNA.
DR EMBL; AF067134; AAD26612.1; -; Genomic_DNA.
DR EMBL; AF067130; AAD26612.1; JOINED; Genomic_DNA.
DR EMBL; AF067131; AAD26612.1; JOINED; Genomic_DNA.
DR EMBL; AF067132; AAD26612.1; JOINED; Genomic_DNA.
DR EMBL; AF067133; AAD26612.1; JOINED; Genomic_DNA.
DR EMBL; AF067134; AAD26613.1; -; Genomic_DNA.
DR EMBL; AF067132; AAD26613.1; JOINED; Genomic_DNA.
DR EMBL; AF067130; AAD26613.1; JOINED; Genomic_DNA.
DR EMBL; AF067133; AAD26613.1; JOINED; Genomic_DNA.
DR EMBL; BT007296; AAP35960.1; -; mRNA.
DR EMBL; BT020134; AAV38936.1; -; mRNA.
DR EMBL; AK294043; BAG57395.1; -; mRNA.
DR EMBL; CH471063; EAW71243.1; -; Genomic_DNA.
DR EMBL; BC000910; AAH00910.1; -; mRNA.
DR EMBL; BC012397; AAH12397.1; -; mRNA.
DR EMBL; BC013001; AAH13001.1; -; mRNA.
DR PIR; S68209; S68209.
DR RefSeq; NP_001269338.1; NM_001282409.1.
DR RefSeq; NP_001269339.1; NM_001282410.1.
DR RefSeq; NP_001269340.1; NM_001282411.1.
DR RefSeq; NP_001269341.1; NM_001282412.1.
DR RefSeq; NP_001269342.1; NM_001282413.1.
DR RefSeq; NP_001269343.1; NM_001282414.1.
DR RefSeq; NP_002703.1; NM_002712.2.
DR UniGene; Hs.36587; -.
DR ProteinModelPortal; Q15435; -.
DR SMR; Q15435; 77-359.
DR DIP; DIP-1005N; -.
DR IntAct; Q15435; 11.
DR MINT; MINT-5004667; -.
DR STRING; 9606.ENSP00000234038; -.
DR PhosphoSite; Q15435; -.
DR DMDM; 74762145; -.
DR REPRODUCTION-2DPAGE; IPI00033600; -.
DR PaxDb; Q15435; -.
DR PRIDE; Q15435; -.
DR DNASU; 5510; -.
DR Ensembl; ENST00000234038; ENSP00000234038; ENSG00000115685.
DR Ensembl; ENST00000272983; ENSP00000272983; ENSG00000115685.
DR Ensembl; ENST00000401987; ENSP00000385466; ENSG00000115685.
DR Ensembl; ENST00000406106; ENSP00000385022; ENSG00000115685.
DR Ensembl; ENST00000407025; ENSP00000385657; ENSG00000115685.
DR GeneID; 5510; -.
DR KEGG; hsa:5510; -.
DR UCSC; uc002wat.1; human.
DR CTD; 5510; -.
DR GeneCards; GC02P242088; -.
DR HGNC; HGNC:9295; PPP1R7.
DR HPA; HPA034501; -.
DR MIM; 602877; gene.
DR neXtProt; NX_Q15435; -.
DR PharmGKB; PA33658; -.
DR eggNOG; COG4886; -.
DR HOGENOM; HOG000211189; -.
DR HOVERGEN; HBG082161; -.
DR InParanoid; Q15435; -.
DR KO; K17550; -.
DR OMA; QRICLRQ; -.
DR PhylomeDB; Q15435; -.
DR ChiTaRS; PPP1R7; human.
DR GeneWiki; PPP1R7; -.
DR GenomeRNAi; 5510; -.
DR NextBio; 21312; -.
DR PRO; PR:Q15435; -.
DR ArrayExpress; Q15435; -.
DR Bgee; Q15435; -.
DR CleanEx; HS_PPP1R7; -.
DR Genevestigator; Q15435; -.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0008599; F:protein phosphatase type 1 regulator activity; TAS:ProtInc.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR027733; PPP1R7.
DR InterPro; IPR003603; U2A'_phosphoprotein32A_C.
DR PANTHER; PTHR10588:SF96; PTHR10588:SF96; 1.
DR Pfam; PF12799; LRR_4; 2.
DR SMART; SM00446; LRRcap; 1.
DR PROSITE; PS51450; LRR; 12.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome;
KW Leucine-rich repeat; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 360 Protein phosphatase 1 regulatory subunit
FT 7.
FT /FTId=PRO_0000239613.
FT REPEAT 77 98 LRR 1.
FT REPEAT 99 120 LRR 2.
FT REPEAT 121 142 LRR 3.
FT REPEAT 143 164 LRR 4.
FT REPEAT 165 186 LRR 5.
FT REPEAT 187 208 LRR 6.
FT REPEAT 209 230 LRR 7.
FT REPEAT 231 252 LRR 8.
FT REPEAT 253 274 LRR 9.
FT REPEAT 275 296 LRR 10.
FT REPEAT 297 318 LRR 11.
FT DOMAIN 331 360 LRRCT.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 12 12 Phosphoserine.
FT MOD_RES 24 24 Phosphoserine.
FT MOD_RES 27 27 Phosphoserine.
FT MOD_RES 44 44 Phosphoserine.
FT MOD_RES 47 47 Phosphoserine.
FT VAR_SEQ 18 60 Missing (in isoform 2 and isoform 4).
FT /FTId=VSP_019244.
FT VAR_SEQ 274 280 NKLTMLD -> VQDSLTY (in isoform 3 and
FT isoform 4).
FT /FTId=VSP_019245.
FT VAR_SEQ 281 360 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_019246.
FT MUTAGEN 148 148 D->V: Completely abolishes the
FT interaction with protein phosphatase 1.
FT MUTAGEN 170 170 F->A: Severely impaired the binding of
FT protein phosphatase 1.
FT MUTAGEN 192 192 E->A: Completely abolishes the
FT interaction with protein phosphatase 1.
FT MUTAGEN 214 214 F->A: Completely abolishes the
FT interaction with protein phosphatase 1.
FT MUTAGEN 280 280 D->A: Severely impairs the binding of
FT protein phosphatase 1.
FT MUTAGEN 300 300 E->A: Completely abolishes the
FT interaction with protein phosphatase 1.
FT MUTAGEN 302 302 W->A: Completely abolishes the
FT interaction with protein phosphatase 1.
FT MUTAGEN 327 327 Y->A: Completely abolishes the
FT interaction with protein phosphatase 1.
SQ SEQUENCE 360 AA; 41564 MW; 49BCCF675EAA94D1 CRC64;
MAAERGAGQQ QSQEMMEVDR RVESEESGDE EGKKHSSGIV ADLSEQSLKD GEERGEEDPE
EEHELPVDME TINLDRDAED VDLNHYRIGK IEGFEVLKKV KTLCLRQNLI KCIENLEELQ
SLRELDLYDN QIKKIENLEA LTELEILDIS FNLLRNIEGV DKLTRLKKLF LVNNKISKIE
NLSNLHQLQM LELGSNRIRA IENIDTLTNL ESLFLGKNKI TKLQNLDALT NLTVLSMQSN
RLTKIEGLQN LVNLRELYLS HNGIEVIEGL ENNNKLTMLD IASNRIKKIE NISHLTELQE
FWMNDNLLES WSDLDELKGA RSLETVYLER NPLQKDPQYR RKVMLALPSV RQIDATFVRF
//
ID PP1R7_HUMAN Reviewed; 360 AA.
AC Q15435; B4DFD4; Q9UQE5; Q9UQE6; Q9Y6K4;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 7;
DE AltName: Full=Protein phosphatase 1 regulatory subunit 22;
GN Name=PPP1R7; Synonyms=SDS22;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=7498485; DOI=10.1016/0014-5793(95)01180-M;
RA Renouf S., Beullens M., Wera S., Van Eynde A., Sikela J., Stalmans W.,
RA Bollen M.;
RT "Molecular cloning of a human polypeptide related to yeast sds22, a
RT regulator of protein phosphatase-1.";
RL FEBS Lett. 375:75-78(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=10231361; DOI=10.1046/j.1432-1327.1999.00344.x;
RA Ceulemans H., Van Eynde A., Perez-Callejon E., Beullens M.,
RA Stalmans W., Bollen M.;
RT "Structure and splice products of the human gene encoding sds22, a
RT putative mitotic regulator of protein phosphatase-1.";
RL Eur. J. Biochem. 262:36-42(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Cervix;
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 INTERACTION WITH PPP1CA; PPP1CB AND PPP1CC ISOFORM 1, AND MUTAGENESIS
RP OF ASP-148; PHE-170; GLU-192; PHE-214; ASP-280; GLU-300; TRP-302 AND
RP TYR-327.
RX PubMed=12226088; DOI=10.1074/jbc.M206838200;
RA Ceulemans H., Vulsteke V., De Maeyer M., Tatchell K., Stalmans W.,
RA Bollen M.;
RT "Binding of the concave surface of the Sds22 superhelix to the alpha
RT 4/alpha 5/alpha 6-triangle of protein phosphatase-1.";
RL J. Biol. Chem. 277:47331-47337(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-27, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-27; SER-44 AND
RP SER-47, AND 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 [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 SER-12; SER-24 AND SER-27,
RP 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 1 (By
CC similarity).
CC -!- SUBUNIT: Interacts with PPP1CA, PPP1CB and PPP1CC/PPP1G isoform 1.
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=sds22alpha1;
CC IsoId=Q15435-1; Sequence=Displayed;
CC Name=2; Synonyms=sds22alpha2;
CC IsoId=Q15435-2; Sequence=VSP_019244;
CC Name=3; Synonyms=sds22beta1;
CC IsoId=Q15435-3; Sequence=VSP_019245, VSP_019246;
CC Name=4; Synonyms=sds22beta2;
CC IsoId=Q15435-4; Sequence=VSP_019244, VSP_019245, VSP_019246;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the SDS22 family.
CC -!- SIMILARITY: Contains 11 LRR (leucine-rich) repeats.
CC -!- SIMILARITY: Contains 1 LRRCT domain.
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DR EMBL; Z50749; CAA90626.1; -; mRNA.
DR EMBL; AF067136; AAD26610.1; -; Genomic_DNA.
DR EMBL; AF067130; AAD26610.1; JOINED; Genomic_DNA.
DR EMBL; AF067132; AAD26610.1; JOINED; Genomic_DNA.
DR EMBL; AF067133; AAD26610.1; JOINED; Genomic_DNA.
DR EMBL; AF067134; AAD26610.1; JOINED; Genomic_DNA.
DR EMBL; AF067135; AAD26610.1; JOINED; Genomic_DNA.
DR EMBL; AF067136; AAD26611.1; -; Genomic_DNA.
DR EMBL; AF067130; AAD26611.1; JOINED; Genomic_DNA.
DR EMBL; AF067132; AAD26611.1; JOINED; Genomic_DNA.
DR EMBL; AF067134; AAD26611.1; JOINED; Genomic_DNA.
DR EMBL; AF067135; AAD26611.1; JOINED; Genomic_DNA.
DR EMBL; AF067133; AAD26611.1; JOINED; Genomic_DNA.
DR EMBL; AF067131; AAD26611.1; JOINED; Genomic_DNA.
DR EMBL; AF067134; AAD26612.1; -; Genomic_DNA.
DR EMBL; AF067130; AAD26612.1; JOINED; Genomic_DNA.
DR EMBL; AF067131; AAD26612.1; JOINED; Genomic_DNA.
DR EMBL; AF067132; AAD26612.1; JOINED; Genomic_DNA.
DR EMBL; AF067133; AAD26612.1; JOINED; Genomic_DNA.
DR EMBL; AF067134; AAD26613.1; -; Genomic_DNA.
DR EMBL; AF067132; AAD26613.1; JOINED; Genomic_DNA.
DR EMBL; AF067130; AAD26613.1; JOINED; Genomic_DNA.
DR EMBL; AF067133; AAD26613.1; JOINED; Genomic_DNA.
DR EMBL; BT007296; AAP35960.1; -; mRNA.
DR EMBL; BT020134; AAV38936.1; -; mRNA.
DR EMBL; AK294043; BAG57395.1; -; mRNA.
DR EMBL; CH471063; EAW71243.1; -; Genomic_DNA.
DR EMBL; BC000910; AAH00910.1; -; mRNA.
DR EMBL; BC012397; AAH12397.1; -; mRNA.
DR EMBL; BC013001; AAH13001.1; -; mRNA.
DR PIR; S68209; S68209.
DR RefSeq; NP_001269338.1; NM_001282409.1.
DR RefSeq; NP_001269339.1; NM_001282410.1.
DR RefSeq; NP_001269340.1; NM_001282411.1.
DR RefSeq; NP_001269341.1; NM_001282412.1.
DR RefSeq; NP_001269342.1; NM_001282413.1.
DR RefSeq; NP_001269343.1; NM_001282414.1.
DR RefSeq; NP_002703.1; NM_002712.2.
DR UniGene; Hs.36587; -.
DR ProteinModelPortal; Q15435; -.
DR SMR; Q15435; 77-359.
DR DIP; DIP-1005N; -.
DR IntAct; Q15435; 11.
DR MINT; MINT-5004667; -.
DR STRING; 9606.ENSP00000234038; -.
DR PhosphoSite; Q15435; -.
DR DMDM; 74762145; -.
DR REPRODUCTION-2DPAGE; IPI00033600; -.
DR PaxDb; Q15435; -.
DR PRIDE; Q15435; -.
DR DNASU; 5510; -.
DR Ensembl; ENST00000234038; ENSP00000234038; ENSG00000115685.
DR Ensembl; ENST00000272983; ENSP00000272983; ENSG00000115685.
DR Ensembl; ENST00000401987; ENSP00000385466; ENSG00000115685.
DR Ensembl; ENST00000406106; ENSP00000385022; ENSG00000115685.
DR Ensembl; ENST00000407025; ENSP00000385657; ENSG00000115685.
DR GeneID; 5510; -.
DR KEGG; hsa:5510; -.
DR UCSC; uc002wat.1; human.
DR CTD; 5510; -.
DR GeneCards; GC02P242088; -.
DR HGNC; HGNC:9295; PPP1R7.
DR HPA; HPA034501; -.
DR MIM; 602877; gene.
DR neXtProt; NX_Q15435; -.
DR PharmGKB; PA33658; -.
DR eggNOG; COG4886; -.
DR HOGENOM; HOG000211189; -.
DR HOVERGEN; HBG082161; -.
DR InParanoid; Q15435; -.
DR KO; K17550; -.
DR OMA; QRICLRQ; -.
DR PhylomeDB; Q15435; -.
DR ChiTaRS; PPP1R7; human.
DR GeneWiki; PPP1R7; -.
DR GenomeRNAi; 5510; -.
DR NextBio; 21312; -.
DR PRO; PR:Q15435; -.
DR ArrayExpress; Q15435; -.
DR Bgee; Q15435; -.
DR CleanEx; HS_PPP1R7; -.
DR Genevestigator; Q15435; -.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0008599; F:protein phosphatase type 1 regulator activity; TAS:ProtInc.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR027733; PPP1R7.
DR InterPro; IPR003603; U2A'_phosphoprotein32A_C.
DR PANTHER; PTHR10588:SF96; PTHR10588:SF96; 1.
DR Pfam; PF12799; LRR_4; 2.
DR SMART; SM00446; LRRcap; 1.
DR PROSITE; PS51450; LRR; 12.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome;
KW Leucine-rich repeat; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 360 Protein phosphatase 1 regulatory subunit
FT 7.
FT /FTId=PRO_0000239613.
FT REPEAT 77 98 LRR 1.
FT REPEAT 99 120 LRR 2.
FT REPEAT 121 142 LRR 3.
FT REPEAT 143 164 LRR 4.
FT REPEAT 165 186 LRR 5.
FT REPEAT 187 208 LRR 6.
FT REPEAT 209 230 LRR 7.
FT REPEAT 231 252 LRR 8.
FT REPEAT 253 274 LRR 9.
FT REPEAT 275 296 LRR 10.
FT REPEAT 297 318 LRR 11.
FT DOMAIN 331 360 LRRCT.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 12 12 Phosphoserine.
FT MOD_RES 24 24 Phosphoserine.
FT MOD_RES 27 27 Phosphoserine.
FT MOD_RES 44 44 Phosphoserine.
FT MOD_RES 47 47 Phosphoserine.
FT VAR_SEQ 18 60 Missing (in isoform 2 and isoform 4).
FT /FTId=VSP_019244.
FT VAR_SEQ 274 280 NKLTMLD -> VQDSLTY (in isoform 3 and
FT isoform 4).
FT /FTId=VSP_019245.
FT VAR_SEQ 281 360 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_019246.
FT MUTAGEN 148 148 D->V: Completely abolishes the
FT interaction with protein phosphatase 1.
FT MUTAGEN 170 170 F->A: Severely impaired the binding of
FT protein phosphatase 1.
FT MUTAGEN 192 192 E->A: Completely abolishes the
FT interaction with protein phosphatase 1.
FT MUTAGEN 214 214 F->A: Completely abolishes the
FT interaction with protein phosphatase 1.
FT MUTAGEN 280 280 D->A: Severely impairs the binding of
FT protein phosphatase 1.
FT MUTAGEN 300 300 E->A: Completely abolishes the
FT interaction with protein phosphatase 1.
FT MUTAGEN 302 302 W->A: Completely abolishes the
FT interaction with protein phosphatase 1.
FT MUTAGEN 327 327 Y->A: Completely abolishes the
FT interaction with protein phosphatase 1.
SQ SEQUENCE 360 AA; 41564 MW; 49BCCF675EAA94D1 CRC64;
MAAERGAGQQ QSQEMMEVDR RVESEESGDE EGKKHSSGIV ADLSEQSLKD GEERGEEDPE
EEHELPVDME TINLDRDAED VDLNHYRIGK IEGFEVLKKV KTLCLRQNLI KCIENLEELQ
SLRELDLYDN QIKKIENLEA LTELEILDIS FNLLRNIEGV DKLTRLKKLF LVNNKISKIE
NLSNLHQLQM LELGSNRIRA IENIDTLTNL ESLFLGKNKI TKLQNLDALT NLTVLSMQSN
RLTKIEGLQN LVNLRELYLS HNGIEVIEGL ENNNKLTMLD IASNRIKKIE NISHLTELQE
FWMNDNLLES WSDLDELKGA RSLETVYLER NPLQKDPQYR RKVMLALPSV RQIDATFVRF
//
MIM
602877
*RECORD*
*FIELD* NO
602877
*FIELD* TI
*602877 PROTEIN PHOSPHATASE 1, REGULATORY SUBUNIT 7; PPP1R7
;;SDS22, S. POMBE, HOMOLOG OF
read more*FIELD* TX
CLONING
Type 1 serine/threonine phosphatases consist of a catalytic subunit and
one or more regulatory subunits. The noncatalytic subunits not only
determine the activity and substrate specificity of the holoenzyme, but
also target the phosphatase to a particular cellular location. S. pombe
sds22 is a regulatory polypeptide of protein phosphatase-1 that is
required for the completion of mitosis. By sequence analysis of a human
brain expressed sequence tag (EST) that is homologous to sds22, and by
5-prime RACE using oligonucleotides based on this EST, Renouf et al.
(1995) determined the complete cDNA sequence of a human homolog of
sds22, termed PPP1R7. The predicted 360-amino acid PPP1R7 protein
contains 11 leucine-rich repeats, which may participate in
protein-protein interactions, and multiple putative phosphorylation
sites. The amino acid sequences of PPP1R7 and sds22 are 46% identical.
Western blot analysis using antibodies against human PPP1R7 detected a
44-kD protein in both the cytoplasm and nucleus of rat liver cells.
Northern blot analysis showed a major 1.4-kb transcript in all human
tissues examined.
MAPPING
By PCR analysis of YACs and somatic cell hybrid DNAs using sequence
tagged sites derived from the 3-prime untranslated region of PPP1R7,
Berry et al. (1995) mapped the PPP1R7 gene to 2q37.3.
*FIELD* RF
1. Berry, R.; Stevens, T. J.; Walter, N. A. R.; Wilcox, A. S.; Rubano,
T.; Hopkins, J. A.; Weber, J.; Goold, R.; Soares, M. B.; Sikela, J.
M.: Gene-based sequence-tagged-sites (STSs) as the basis for a human
gene map. Nature Genet. 10: 415-423, 1995.
2. Renouf, S.; Beullens, M.; Wera, S.; Van Eynde, A.; Sikela, J.;
Stalmans, W.; Bollen, M.: Molecular cloning of a human polypeptide
related to yeast sds22, a regulator of protein phosphatase-1. FEBS
Lett. 375: 75-78, 1995.
*FIELD* CN
Patti M. Sherman - updated: 8/11/1998
*FIELD* CD
Patti M. Sherman: 7/22/1998
*FIELD* ED
carol: 06/12/2012
alopez: 2/4/2009
carol: 8/14/1998
carol: 8/11/1998
carol: 7/27/1998
dkim: 7/24/1998
carol: 7/23/1998
*RECORD*
*FIELD* NO
602877
*FIELD* TI
*602877 PROTEIN PHOSPHATASE 1, REGULATORY SUBUNIT 7; PPP1R7
;;SDS22, S. POMBE, HOMOLOG OF
read more*FIELD* TX
CLONING
Type 1 serine/threonine phosphatases consist of a catalytic subunit and
one or more regulatory subunits. The noncatalytic subunits not only
determine the activity and substrate specificity of the holoenzyme, but
also target the phosphatase to a particular cellular location. S. pombe
sds22 is a regulatory polypeptide of protein phosphatase-1 that is
required for the completion of mitosis. By sequence analysis of a human
brain expressed sequence tag (EST) that is homologous to sds22, and by
5-prime RACE using oligonucleotides based on this EST, Renouf et al.
(1995) determined the complete cDNA sequence of a human homolog of
sds22, termed PPP1R7. The predicted 360-amino acid PPP1R7 protein
contains 11 leucine-rich repeats, which may participate in
protein-protein interactions, and multiple putative phosphorylation
sites. The amino acid sequences of PPP1R7 and sds22 are 46% identical.
Western blot analysis using antibodies against human PPP1R7 detected a
44-kD protein in both the cytoplasm and nucleus of rat liver cells.
Northern blot analysis showed a major 1.4-kb transcript in all human
tissues examined.
MAPPING
By PCR analysis of YACs and somatic cell hybrid DNAs using sequence
tagged sites derived from the 3-prime untranslated region of PPP1R7,
Berry et al. (1995) mapped the PPP1R7 gene to 2q37.3.
*FIELD* RF
1. Berry, R.; Stevens, T. J.; Walter, N. A. R.; Wilcox, A. S.; Rubano,
T.; Hopkins, J. A.; Weber, J.; Goold, R.; Soares, M. B.; Sikela, J.
M.: Gene-based sequence-tagged-sites (STSs) as the basis for a human
gene map. Nature Genet. 10: 415-423, 1995.
2. Renouf, S.; Beullens, M.; Wera, S.; Van Eynde, A.; Sikela, J.;
Stalmans, W.; Bollen, M.: Molecular cloning of a human polypeptide
related to yeast sds22, a regulator of protein phosphatase-1. FEBS
Lett. 375: 75-78, 1995.
*FIELD* CN
Patti M. Sherman - updated: 8/11/1998
*FIELD* CD
Patti M. Sherman: 7/22/1998
*FIELD* ED
carol: 06/12/2012
alopez: 2/4/2009
carol: 8/14/1998
carol: 8/11/1998
carol: 7/27/1998
dkim: 7/24/1998
carol: 7/23/1998