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Q99MR9

- PPR3A_MOUSE

UniProt

Q99MR9 - PPR3A_MOUSE

Protein

Protein phosphatase 1 regulatory subunit 3A

Gene

Ppp1r3a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    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.1 Publication

    GO - Molecular functioni

    1. protein serine/threonine phosphatase activity Source: MGI

    GO - Biological processi

    1. dephosphorylation Source: GOC
    2. glycogen metabolic process Source: MGI

    Keywords - Biological processi

    Carbohydrate metabolism, Glycogen metabolism

    Protein family/group databases

    CAZyiCBM21. Carbohydrate-Binding Module Family 21.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein phosphatase 1 regulatory subunit 3A
    Alternative name(s):
    Protein phosphatase 1 glycogen-associated regulatory subunit
    Protein phosphatase type-1 glycogen targeting subunit
    Short name:
    RG1
    Gene namesi
    Name:Ppp1r3a
    Synonyms:Pp1g
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:2153588. Ppp1r3a.

    Subcellular locationi

    Membrane By similarity; Single-pass membrane protein By similarity

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10891089Protein phosphatase 1 regulatory subunit 3APRO_0000071501Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei40 – 401Phosphoserine; by GSK3By similarity
    Modified residuei44 – 441Phosphoserine; by GSK3By similarity
    Modified residuei48 – 481Phosphoserine; by PKA and ISPKBy similarity
    Modified residuei67 – 671Phosphoserine; by PKABy similarity

    Post-translational modificationi

    Phosphorylation at Ser-48 by ISPK stimulates the dephosphorylation of glycogen synthase and phosphorylase kinase.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ99MR9.
    PaxDbiQ99MR9.
    PRIDEiQ99MR9.

    PTM databases

    PhosphoSiteiQ99MR9.

    Expressioni

    Tissue specificityi

    Skeletal muscle and heart.1 Publication

    Gene expression databases

    BgeeiQ99MR9.
    GenevestigatoriQ99MR9.

    Interactioni

    Subunit structurei

    Interacts with PPP1CC catalytic subunit of PP1, and associates with glycogen.By similarity

    Protein-protein interaction databases

    IntActiQ99MR9. 2 interactions.
    MINTiMINT-4108485.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99MR9.
    SMRiQ99MR9. Positions 124-244.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1047 – 106721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini123 – 231109CBM21PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi64 – 674PP1-binding motif

    Domaini

    The CBM21 domain is known to be involved in the localization to glycogen and is characteristic of some regulatory subunit of phosphatase complexes.

    Sequence similaritiesi

    Contains 1 CBM21 (carbohydrate binding type-21) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG288354.
    GeneTreeiENSGT00530000062978.
    HOGENOMiHOG000115667.
    HOVERGENiHBG053657.
    InParanoidiQ32MS0.
    KOiK07189.
    OMAiAFDPHEG.
    OrthoDBiEOG769ZKR.
    TreeFamiTF105537.

    Family and domain databases

    InterProiIPR005036. CBM_21.
    [Graphical view]
    PfamiPF03370. CBM_21. 1 hit.
    [Graphical view]
    PROSITEiPS51159. CBM21. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q99MR9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEPAEEPGQI SKDNFLEVPN LSDSVCEDEE VKATFKPGFS PQPSRRGSGS     50
    SEDMYLDTPT SASRRVSFAD SLGFSLVSVK EFDCWELPSV STDFDLSGDV 100
    FHTDEYVLSP LFDLPSSKEK LMEQLQVQKA VLESAEHLPG SSMKGIIRVL 150
    NISFEKLVYV RMSLDDWQTH YDILAEYVPN SCDGETDQFS FKISLVPPYQ 200
    KEGGKVEFCI RYETSAGTFW SNNNGTNYIL VCQKKRKEPE PVKPLEEAPS 250
    RQIKGCLKVK SRSKEEPLLA PEENKFETLK FTESYIPTII CSHEDKDDLG 300
    ANHPNVDDIN KKHDEHNGKE LDLMINQRLI TSQDEKNTFA TDTVNFTNKA 350
    EGSEKKQAYH EINTDLFMGP LSPSLSAESS LKRDFYHSRS SSPGNEYGHP 400
    HSEEIISDMG EKGPSLGDTS SDELMQLELC SKEDLDDNAN PANGSGRVCS 450
    SFDQRMACGL KNNEAGIKKT GIQDYKYSHG DSTKLEESNA SSRDDYAKVD 500
    NKKEKQTCLG VNENPSKNFQ SVFQTQEGHM GYPKISTEGD KANNQDLTSL 550
    LSKDITANTW AVTVDPCPST NAKRSWREVG SGSNLEPGTS DLSSPRNFSP 600
    LTDDHLFQAD RENSDSSNPE NQNMNTRHRK KWNVLETQSE TSETESDIAK 650
    HTKEQAEYKD MWEKTDNSRN LKATPTEHLF TCRETECYGL SSLADHGITE 700
    KAQAVTAYII KTTLESTPES ASARGKAIIA KLPQETAGND RPIEVKETAF 750
    DPHEGRKDDS HYSLCHGDTA GVIHDNDFER ESHLDICNLR VDEMKKEKTT 800
    STCFPQKTYD KEKHGIGSVT SIDEPSQVIT GNQKATSKLD LHLGVLPTDR 850
    AIFQANADLE LLQELSRRTD FNAVPSAFNS DTASASRDSS QVYRHCSKKS 900
    VPSYGEEKAV TNTTLQSIPT KSEYNWHPES EVLGHAMSKP EDVFKSSEIM 950
    KSGSGGERGG GPILQQKEGS LENSQGPMFF TNEPLENLDE ASSENEGLMH 1000
    SGQSQCYLGD KGLVSSASAT VSTQELEAQG RESLLSISTN SKIPYFLLFL 1050
    IFLATVYYYD LMIGLAFYLF SLYWLYWEGG RQRESVKKK 1089
    Length:1,089
    Mass (Da):121,435
    Last modified:July 27, 2011 - v2
    Checksum:i85EC67FD90CC8FD2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti959 – 9591G → S in AAK31072. (PubMed:11361130)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF309629, AF309628 Genomic DNA. Translation: AAK31072.1.
    CH466533 Genomic DNA. Translation: EDL13902.1.
    BC109007 mRNA. Translation: AAI09008.1.
    AK084518 mRNA. Translation: BAC39208.2.
    AK084719 mRNA. Translation: BAC39262.2.
    CCDSiCCDS19917.1.
    RefSeqiNP_536712.2. NM_080464.2.
    UniGeneiMm.209429.

    Genome annotation databases

    EnsembliENSMUST00000045096; ENSMUSP00000049054; ENSMUSG00000042717.
    GeneIDi140491.
    KEGGimmu:140491.
    UCSCiuc009ayw.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF309629 , AF309628 Genomic DNA. Translation: AAK31072.1 .
    CH466533 Genomic DNA. Translation: EDL13902.1 .
    BC109007 mRNA. Translation: AAI09008.1 .
    AK084518 mRNA. Translation: BAC39208.2 .
    AK084719 mRNA. Translation: BAC39262.2 .
    CCDSi CCDS19917.1.
    RefSeqi NP_536712.2. NM_080464.2.
    UniGenei Mm.209429.

    3D structure databases

    ProteinModelPortali Q99MR9.
    SMRi Q99MR9. Positions 124-244.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q99MR9. 2 interactions.
    MINTi MINT-4108485.

    Protein family/group databases

    CAZyi CBM21. Carbohydrate-Binding Module Family 21.

    PTM databases

    PhosphoSitei Q99MR9.

    Proteomic databases

    MaxQBi Q99MR9.
    PaxDbi Q99MR9.
    PRIDEi Q99MR9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000045096 ; ENSMUSP00000049054 ; ENSMUSG00000042717 .
    GeneIDi 140491.
    KEGGi mmu:140491.
    UCSCi uc009ayw.1. mouse.

    Organism-specific databases

    CTDi 5506.
    MGIi MGI:2153588. Ppp1r3a.

    Phylogenomic databases

    eggNOGi NOG288354.
    GeneTreei ENSGT00530000062978.
    HOGENOMi HOG000115667.
    HOVERGENi HBG053657.
    InParanoidi Q32MS0.
    KOi K07189.
    OMAi AFDPHEG.
    OrthoDBi EOG769ZKR.
    TreeFami TF105537.

    Miscellaneous databases

    NextBioi 369808.
    PROi Q99MR9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q99MR9.
    Genevestigatori Q99MR9.

    Family and domain databases

    InterProi IPR005036. CBM_21.
    [Graphical view ]
    Pfami PF03370. CBM_21. 1 hit.
    [Graphical view ]
    PROSITEi PS51159. CBM21. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Gene structure and expression of the targeting subunit, RGL, of the muscle-specific glycogen-associated type 1 protein phosphatase, PP1G."
      Lanner C., Suzuki Y., Bi C., Zhang H., Cooper L.D., Bowker-Kinley M.M., DePaoli-Roach A.A.
      Arch. Biochem. Biophys. 388:135-145(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
      Strain: 129/Sv.
    2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-626.
      Strain: C57BL/6J.
      Tissue: Embryonic heart.
    5. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 259-264, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    6. "Insulin control of glycogen metabolism in knockout mice lacking the muscle-specific protein phosphatase PP1G/RGL."
      Suzuki Y., Lanner C., Kim J.-H., Vilardo P.G., Zhang H., Yang J., Cooper L.D., Steele M., Kennedy A., Bock C.B., Scrimgeour A., Lawrence J.C. Jr., DePaoli-Roach A.A.
      Mol. Cell. Biol. 21:2683-2694(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: 129/Sv.

    Entry informationi

    Entry nameiPPR3A_MOUSE
    AccessioniPrimary (citable) accession number: Q99MR9
    Secondary accession number(s): Q32MS0, Q8BUJ4, Q8BUL0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2004
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 88 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3