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Protein phosphatase 1 regulatory subunit 3A (Protein phosphatase 1 glycogen-associated regulatory subunit) (Protein phosphatase type-1 glycogen targeting subunit) (RG1)

 PPR3A_HUMAN             Reviewed;        1122 AA.
Q16821; A0AVQ2; A4D0T6; O43476; Q75LN8; Q7KYM8; Q86UI6;
13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
15-JUN-2010, sequence version 3.
20-JUN-2018, entry version 134.
RecName: Full=Protein phosphatase 1 regulatory subunit 3A;
AltName: Full=Protein phosphatase 1 glycogen-associated regulatory subunit;
AltName: Full=Protein phosphatase type-1 glycogen targeting subunit;
Short=RG1;
Name=PPP1R3A; Synonyms=PP1G;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), TISSUE
SPECIFICITY, AND VARIANTS MET-451; LYS-476; HIS-882; SER-883 AND
TYR-905.
TISSUE=Skeletal muscle;
PubMed=9726244; DOI=10.2337/diabetes.47.9.1519;
Xia J., Scherer S.W., Cohen P.T.W., Majer M., Xi T., Norman R.A.,
Knowler W.C., Bogardus C., Prochazka M.;
"A common variant in PPP1R3 associated with insulin resistance and
type 2 diabetes.";
Diabetes 47:1519-1524(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS MET-451;
LYS-476 AND HIS-882.
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
MET-451; LYS-476 AND HIS-882.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-1122 (ISOFORM 1), VARIANTS MET-451;
LYS-476 AND HIS-882, AND VARIANT NIDDM GLU-931.
TISSUE=Skeletal muscle;
PubMed=7926294; DOI=10.2337/diabetes.43.10.1234;
Chen Y.H., Hansen L., Chen M.X., Bjorbaek C., Vestergaard H.,
Hansen T., Cohen P.T.W., Pederson O.;
"Sequence of the human glycogen-associated regulatory subunit of type
I protein phosphatase and analysis of its coding region and mRNA level
in muscle from patients with non-insulin-dependent diabetes.";
Diabetes 43:1234-1241(1994).
[6]
VARIANT TYR-905.
PubMed=7581368; DOI=10.1093/hmg/4.8.1313;
Hansen L., Hansen T., Vestergaard H., Bjorbaek C., Echwald S.M.,
Clausen J.O., Chen Y.H., Chen M.X., Cohen P.T.W., Pedersen O.;
"A widespread amino acid polymorphism at codon 905 of the glycogen-
associated regulatory subunit of protein phosphatase-1 is associated
with insulin resistance and hypersecretion of insulin.";
Hum. Mol. Genet. 4:1313-1320(1995).
[7]
VARIANT [LARGE SCALE ANALYSIS] ALA-554.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Seems to act as a glycogen-targeting subunit for PP1.
PP1 is essential for cell division, and participates in the
regulation of glycogen metabolism, muscle contractility and
protein synthesis. Plays an important role in glycogen synthesis
but is not essential for insulin activation of glycogen synthase
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with PPP1CC catalytic subunit of PP1, and
associates with glycogen. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane
protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q16821-1; Sequence=Displayed;
Name=2;
IsoId=Q16821-2; Sequence=VSP_011585, VSP_011586;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
-!- TISSUE SPECIFICITY: Skeletal muscle and heart.
{ECO:0000269|PubMed:9726244}.
-!- DOMAIN: The CBM21 domain is known to be involved in the
localization to glycogen and is characteristic of some regulatory
subunit of phosphatase complexes.
-!- PTM: Phosphorylation at Ser-46 by ISPK stimulates the
dephosphorylation of glycogen synthase and phosphorylase kinase.
{ECO:0000250}.
-!- DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM)
[MIM:125853]: A multifactorial disorder of glucose homeostasis
caused by a lack of sensitivity to the body's own insulin.
Affected individuals usually have an obese body habitus and
manifestations of a metabolic syndrome characterized by diabetes,
insulin resistance, hypertension and hypertriglyceridemia. The
disease results in long-term complications that affect the eyes,
kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:7926294}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAS07492.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF024578; AAB94596.1; -; Genomic_DNA.
EMBL; AF024576; AAB94596.1; JOINED; Genomic_DNA.
EMBL; AF024577; AAB94596.1; JOINED; Genomic_DNA.
EMBL; AF024579; AAB94597.1; -; mRNA.
EMBL; AC092465; AAS07492.1; ALT_SEQ; Genomic_DNA.
EMBL; AC093598; AAP22361.1; -; Genomic_DNA.
EMBL; CH236947; EAL24370.1; -; Genomic_DNA.
EMBL; BC126451; AAI26452.1; -; mRNA.
EMBL; BC126453; AAI26454.1; -; mRNA.
EMBL; X78578; CAA55316.1; -; mRNA.
CCDS; CCDS5759.1; -. [Q16821-1]
PIR; I38127; I38127.
RefSeq; NP_002702.2; NM_002711.3. [Q16821-1]
UniGene; Hs.458309; -.
ProteinModelPortal; Q16821; -.
SMR; Q16821; -.
BioGrid; 111499; 45.
IntAct; Q16821; 2.
STRING; 9606.ENSP00000284601; -.
CAZy; CBM21; Carbohydrate-Binding Module Family 21.
iPTMnet; Q16821; -.
PhosphoSitePlus; Q16821; -.
BioMuta; PPP1R3A; -.
DMDM; 298286906; -.
EPD; Q16821; -.
PaxDb; Q16821; -.
PeptideAtlas; Q16821; -.
PRIDE; Q16821; -.
ProteomicsDB; 61080; -.
ProteomicsDB; 61081; -. [Q16821-2]
DNASU; 5506; -.
Ensembl; ENST00000284601; ENSP00000284601; ENSG00000154415. [Q16821-1]
Ensembl; ENST00000284602; ENSP00000284602; ENSG00000154415. [Q16821-2]
GeneID; 5506; -.
KEGG; hsa:5506; -.
UCSC; uc010ljy.2; human. [Q16821-1]
CTD; 5506; -.
DisGeNET; 5506; -.
EuPathDB; HostDB:ENSG00000154415.7; -.
GeneCards; PPP1R3A; -.
H-InvDB; HIX0033522; -.
HGNC; HGNC:9291; PPP1R3A.
MalaCards; PPP1R3A; -.
MIM; 125853; phenotype.
MIM; 600917; gene.
neXtProt; NX_Q16821; -.
OpenTargets; ENSG00000154415; -.
PharmGKB; PA33651; -.
eggNOG; KOG3986; Eukaryota.
eggNOG; ENOG4111FT1; LUCA.
GeneTree; ENSGT00530000062978; -.
HOVERGEN; HBG053657; -.
InParanoid; Q16821; -.
KO; K07189; -.
OMA; LFTCQET; -.
OrthoDB; EOG091G00OC; -.
PhylomeDB; Q16821; -.
TreeFam; TF105537; -.
SIGNOR; Q16821; -.
ChiTaRS; PPP1R3A; human.
GeneWiki; PPP1R3A; -.
GenomeRNAi; 5506; -.
PRO; PR:Q16821; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000154415; -.
CleanEx; HS_PPP1R3A; -.
ExpressionAtlas; Q16821; baseline and differential.
Genevisible; Q16821; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
Gene3D; 2.60.40.2440; -; 1.
InterPro; IPR005036; CBM21_dom.
InterPro; IPR038175; CBM21_dom_sf.
Pfam; PF03370; CBM_21; 1.
PROSITE; PS51159; CBM21; 1.
1: Evidence at protein level;
Alternative splicing; Carbohydrate metabolism; Complete proteome;
Diabetes mellitus; Disease mutation; Glycogen metabolism; Membrane;
Phosphoprotein; Polymorphism; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 1122 Protein phosphatase 1 regulatory subunit
3A.
/FTId=PRO_0000071500.
TRANSMEM 1078 1098 Helical. {ECO:0000255}.
DOMAIN 122 230 CBM21. {ECO:0000255|PROSITE-
ProRule:PRU00491}.
MOTIF 62 65 PP1-binding motif.
MOD_RES 38 38 Phosphoserine; by GSK3.
{ECO:0000250|UniProtKB:Q00756}.
MOD_RES 42 42 Phosphoserine; by GSK3.
{ECO:0000250|UniProtKB:Q00756}.
MOD_RES 46 46 Phosphoserine; by PKA and ISPK.
{ECO:0000250|UniProtKB:Q00756}.
MOD_RES 49 49 Phosphoserine.
{ECO:0000250|UniProtKB:Q99MR9}.
MOD_RES 56 56 Phosphothreonine.
{ECO:0000250|UniProtKB:Q99MR9}.
MOD_RES 65 65 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:Q00756}.
MOD_RES 844 844 Phosphoserine.
{ECO:0000250|UniProtKB:Q99MR9}.
VAR_SEQ 60 74 GTRRVSFADSFGFNL -> ERTRAGACKTMERSS (in
isoform 2). {ECO:0000303|PubMed:9726244}.
/FTId=VSP_011585.
VAR_SEQ 75 1122 Missing (in isoform 2).
{ECO:0000303|PubMed:9726244}.
/FTId=VSP_011586.
VARIANT 45 45 G -> S (in dbSNP:rs8192687).
/FTId=VAR_027929.
VARIANT 231 231 C -> Y (in dbSNP:rs7801819).
/FTId=VAR_027930.
VARIANT 451 451 V -> M (in dbSNP:rs2974942).
{ECO:0000269|PubMed:12690205,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7926294,
ECO:0000269|PubMed:9726244}.
/FTId=VAR_027931.
VARIANT 476 476 N -> K (in dbSNP:rs2974944).
{ECO:0000269|PubMed:12690205,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7926294,
ECO:0000269|PubMed:9726244}.
/FTId=VAR_027932.
VARIANT 554 554 G -> A (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036287.
VARIANT 627 627 R -> K (in dbSNP:rs35067467).
/FTId=VAR_057128.
VARIANT 748 748 E -> K (in dbSNP:rs4304271).
/FTId=VAR_027933.
VARIANT 882 882 L -> H (in dbSNP:rs2974938).
{ECO:0000269|PubMed:12690205,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7926294,
ECO:0000269|PubMed:9726244}.
/FTId=VAR_027934.
VARIANT 883 883 R -> S (in dbSNP:rs1800000).
{ECO:0000269|PubMed:9726244}.
/FTId=VAR_019697.
VARIANT 905 905 D -> Y (common polymorphism; can be
associated with insulin resistance;
dbSNP:rs1799999).
{ECO:0000269|PubMed:7581368,
ECO:0000269|PubMed:9726244}.
/FTId=VAR_019698.
VARIANT 931 931 A -> E (in NIDDM; dbSNP:rs35449651).
{ECO:0000269|PubMed:7926294}.
/FTId=VAR_019699.
SEQUENCE 1122 AA; 125767 MW; FACB2CEA7C00E75B CRC64;
MEPSEVPSQI SKDNFLEVPN LSDSLCEDEE VTFQPGFSPQ PSRRGSDSSE DIYLDTPSSG
TRRVSFADSF GFNLVSVKEF DCWELPSAST TFDLGTDIFH TEEYVLAPLF DLPSSKEDLM
QQLQIQKAIL ESTESLLGST SIKGIIRVLN VSFEKLVYVR MSLDDWQTHY DILAEYVPNS
CDGETDQFSF KIVLVPPYQK DGSKVEFCIR YETSVGTFWS NNNGTNYTFI CQKKEQEPEP
VKPWKEVPNR QIKGCLKVKS SKEESSVTSE ENNFENPKNT DTYIPTIICS HEDKEDLEAS
NRNVKDVNRE HDEHNEKELE LMINQHLIRT RSTASRDERN TFSTDPVNFP NKAEGLEKKQ
IHGEICTDLF QRSLSPSSSA ESSVKGDFYC NEKYSSGDDC THQPSEETTS NMGEIKPSLG
DTSSDELVQL HTGSKEVLDD NANPAHGNGT VQIPCPSSDQ LMAGNLNKKH EGGAKNIEVK
DLGCLRRDFH SDTSACLKES TEEGSSKEDY YGNGKDDEEQ RIYLGVNEKQ RKNFQTILHD
QERKMGNPKI SVAGIGASNR DLATLLSEHT AIPTRAITAD VSHSPRTNLS WEEAVLTPEH
HHLTSEGSAL GGITGQVCSS RTGNVLRNDY LFQVEEKSGG INSEDQDNSP QHKQSWNVLE
SQGKSRENKT NITEHIKGQT DCEDVWGKRD NTRSLKATTE ELFTCQETVC CELSSLADHG
ITEKAEAGTA YIIKTTSEST PESMSAREKA IIAKLPQETA RSDRPIEVKE TAFDPHEGRN
DDSHYTLCQR DTVGVIYDND FEKESRLGIC NVRVDEMEKE ETMSMYNPRK THDREKCGTG
NITSVEESSW VITEYQKATS KLDLQLGMLP TDKTVFSENR DLRQVQELSK KTDSDAIVHS
AFNSDTNRAP QNSSPFSKHH TEISVSTNEQ AIAVENAVTT MASQPISTKS ENICNSTREI
QGIEKHPYPE SKPEEVSRSS GIVTSGSRKE RCIGQIFQTE EYSVEKSLGP MILINKPLEN
MEEARHENEG LVSSGQSLYT SGEKESDSSA STSLPVEESQ AQGNESLFSK YTNSKIPYFL
LFLIFLITVY HYDLMIGLTF YVLSLSWLSW EEGRQKESVK KK


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