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Protein

Protein phosphatase 1 regulatory subunit 3B

Gene

Ppp1r3b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a glycogen-targeting subunit for phosphatase PP1. Facilitates interaction of the PP1 with enzymes of the glycogen metabolism and regulates its activity. Suppresses the rate at which PP1 dephosphorylates (inactivates) glycogen phosphorylase and enhances the rate at which it activates glycogen synthase and therefore limits glycogen breakdown. Its activity is inhibited by PYGL, resulting in inhibition of the glycogen synthase and glycogen phosphorylase phosphatase activities of PP1. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in hepatocytes (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

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 3B
Alternative name(s):
Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL
Protein phosphatase 1 regulatory subunit 4
Short name:
PP1 subunit R4
Protein phosphatase 1 subunit GL
Short name:
PTG
Gene namesi
Name:Ppp1r3b
Synonyms:Ppp1r4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2177268. Ppp1r3b.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 284284Protein phosphatase 1 regulatory subunit 3BPRO_0000324544Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei260 – 2601PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8C767.
PaxDbiQ8C767.
PRIDEiQ8C767.

PTM databases

iPTMnetiQ8C767.

Expressioni

Tissue specificityi

Highly expressed in liver (at protein level). Expressed predominantly in liver. Expressed moderately in heart. Expressed weakly in prostate, stomach, thyroid, lung, kidney, spleen and skeletal muscle.2 Publications

Developmental stagei

Expressed in lung at 12.5 and 16.5 dpc and declines thereafter. Expressed in epithelial cells of the bronchus and smooth muscle of the pulmonary artery at 13.5 and 16.5 dpc.1 Publication

Inductioni

Up-regulated by TITF1.1 Publication

Gene expression databases

BgeeiQ8C767.
GenevisibleiQ8C767. MM.

Interactioni

Subunit structurei

Interacts with glycogen, PPP1CC catalytic subunit of PP1 and PYGL. Associates with glycogen particles. Forms complexes with debranching enzyme, glycogen phosphorylase, glycogen synthase and phosphorylase kinase which is necessary for its regulation of PP1 activity (By similarity).By similarity

Protein-protein interaction databases

BioGridi232645. 9 interactions.
IntActiQ8C767. 10 interactions.
STRINGi10090.ENSMUSP00000065679.

Structurei

3D structure databases

ProteinModelPortaliQ8C767.
SMRiQ8C767. Positions 109-252.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini124 – 232109CBM21PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi61 – 644PP1-binding motif

Domaini

The N-terminal region is required for binding to PP1, the central region is required for binding to glycogen and the C-terminal region is required for binding to PYGL.By similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3986. Eukaryota.
ENOG4111FT1. LUCA.
GeneTreeiENSGT00530000062978.
HOGENOMiHOG000026799.
HOVERGENiHBG052744.
InParanoidiQ8C767.
KOiK07189.
OMAiMVKVFSE.
OrthoDBiEOG7H4DTW.
PhylomeDBiQ8C767.
TreeFamiTF105537.

Family and domain databases

InterProiIPR005036. CBM21_dom.
IPR017434. Pase-1_reg-su_3B/C/D_met.
[Graphical view]
PfamiPF03370. CBM_21. 1 hit.
[Graphical view]
PIRSFiPIRSF038207. PP1_GT_animal. 1 hit.
PROSITEiPS51159. CBM21. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8C767-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVDIQYSYS SMAPSLRRER FTFKISPKLS KPLRPCIQLG SKDEASGMVA
60 70 80 90 100
PAVQEKKVKK RVSFADNQGL ALTMVKVFSE FDDPLDIPFN ITELLDNIVS
110 120 130 140 150
LTTAESESFV LDFPQPSADY LDFRNRLQTN HVCLENCVLK DKAIAGTVKV
160 170 180 190 200
QNLAFEKVVK IRMTFDTWKS FTDFPCQYVK DTYAGSDRDT FSFDISLPEK
210 220 230 240 250
IQSYERMEFA VCYECNGQAY WDSNKGKNYR ITRAELRSSP GKIEPYNGPD
260 270 280
FGISFDQFGS PRCSFGLFPE WPSYLGYEKL GPYY
Length:284
Mass (Da):32,433
Last modified:March 1, 2003 - v1
Checksum:i193C1BAC1286D344
GO

Sequence cautioni

The sequence AAH60261.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK052438 mRNA. Translation: BAC34990.1.
BC060261 mRNA. Translation: AAH60261.1. Different initiation.
BC079666 mRNA. Translation: AAH79666.1.
CCDSiCCDS22243.1.
RefSeqiNP_808409.1. NM_177741.3.
XP_006509181.1. XM_006509118.2.
XP_006509182.1. XM_006509119.2.
UniGeneiMm.247126.

Genome annotation databases

EnsembliENSMUST00000070481; ENSMUSP00000065679; ENSMUSG00000046794.
GeneIDi244416.
KEGGimmu:244416.
UCSCiuc009lkw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK052438 mRNA. Translation: BAC34990.1.
BC060261 mRNA. Translation: AAH60261.1. Different initiation.
BC079666 mRNA. Translation: AAH79666.1.
CCDSiCCDS22243.1.
RefSeqiNP_808409.1. NM_177741.3.
XP_006509181.1. XM_006509118.2.
XP_006509182.1. XM_006509119.2.
UniGeneiMm.247126.

3D structure databases

ProteinModelPortaliQ8C767.
SMRiQ8C767. Positions 109-252.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi232645. 9 interactions.
IntActiQ8C767. 10 interactions.
STRINGi10090.ENSMUSP00000065679.

Protein family/group databases

CAZyiCBM21. Carbohydrate-Binding Module Family 21.

PTM databases

iPTMnetiQ8C767.

Proteomic databases

EPDiQ8C767.
PaxDbiQ8C767.
PRIDEiQ8C767.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000070481; ENSMUSP00000065679; ENSMUSG00000046794.
GeneIDi244416.
KEGGimmu:244416.
UCSCiuc009lkw.1. mouse.

Organism-specific databases

CTDi79660.
MGIiMGI:2177268. Ppp1r3b.

Phylogenomic databases

eggNOGiKOG3986. Eukaryota.
ENOG4111FT1. LUCA.
GeneTreeiENSGT00530000062978.
HOGENOMiHOG000026799.
HOVERGENiHBG052744.
InParanoidiQ8C767.
KOiK07189.
OMAiMVKVFSE.
OrthoDBiEOG7H4DTW.
PhylomeDBiQ8C767.
TreeFamiTF105537.

Miscellaneous databases

ChiTaRSiPpp1r3b. mouse.
NextBioi386258.
PROiQ8C767.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C767.
GenevisibleiQ8C767. MM.

Family and domain databases

InterProiIPR005036. CBM21_dom.
IPR017434. Pase-1_reg-su_3B/C/D_met.
[Graphical view]
PfamiPF03370. CBM_21. 1 hit.
[Graphical view]
PIRSFiPIRSF038207. PP1_GT_animal. 1 hit.
PROSITEiPS51159. CBM21. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Strain: C57BL/6J.
    Tissue: Lung.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Brain.
  3. "Human skeletal muscle expresses a glycogen-targeting subunit of PP1 that is identical to the insulin-sensitive glycogen-targeting subunit G(L) of liver."
    Munro S., Cuthbertson D.J., Cunningham J., Sales M., Cohen P.T.W.
    Diabetes 51:591-598(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  4. "Identification and expression of alternative splice variants of the mouse Ppp1r3b gene in lung epithelial cells."
    Niimi T., Kurotani R., Kimura S., Kitagawa Y.
    Biochem. Biophys. Res. Commun. 349:588-596(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue.

Entry informationi

Entry nameiPPR3B_MOUSE
AccessioniPrimary (citable) accession number: Q8C767
Secondary accession number(s): Q6PAJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 1, 2003
Last modified: April 13, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.