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Protein

Glucosidase 2 subunit beta

Gene

Prkcsh

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

Functioni

Regulatory subunit of glucosidase II that cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc2Man9GlcNAc2 oligosaccharide precursor of immature glycoproteins (PubMed:27462106, PubMed:9148925). Required for efficient PKD1/Polycystin-1 biogenesis and trafficking to the plasma membrane of the primary cilia (PubMed:21685914).3 Publications

Pathwayi: N-glycan metabolism

This protein is involved in the pathway N-glycan metabolism, which is part of Glycan metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway N-glycan metabolism and in Glycan metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei49Substrate; shared with catalytic subunitCombined sources1 Publication1
Metal bindingi50Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi53Calcium 1Combined sources1 Publication1
Binding sitei53Substrate; shared with catalytic subunitCombined sources1 Publication1
Metal bindingi55Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi57Calcium 1Combined sources1 Publication1
Metal bindingi63Calcium 1Combined sources1 Publication1
Metal bindingi64Calcium 1Combined sources1 Publication1
Metal bindingi91Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi94Calcium 2Combined sources1 Publication1
Metal bindingi96Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi98Calcium 2Combined sources1 Publication1
Metal bindingi104Calcium 2Combined sources1 Publication1
Metal bindingi105Calcium 2Combined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi222 – 2331PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

GO - Biological processi

  • in utero embryonic development Source: MGI
  • liver development Source: MGI
  • negative regulation of neuron projection development Source: MGI
  • N-glycan processing Source: UniProtKB
  • nitrogen compound metabolic process Source: MGI
  • protein heterooligomerization Source: MGI
  • renal system development Source: MGI

Keywordsi

LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-MMU-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-MMU-8957275 Post-translational protein phosphorylation
R-MMU-901042 Calnexin/calreticulin cycle
UniPathwayi
UPA00957

Names & Taxonomyi

Protein namesi
Recommended name:
Glucosidase 2 subunit beta
Alternative name(s):
80K-H protein
Glucosidase II subunit beta1 Publication
Protein kinase C substrate 60.1 kDa protein heavy chain
Short name:
PKCSH
Gene namesi
Name:PrkcshImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:107877 Prkcsh

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Disruption phenotypei

Knockout mice exhibit early embryonic lethality by E11.5. Conditional ubiquitous or kidney-specidic knockdown results in polycystic liver and kidney phenotypes, respectively.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 141 PublicationAdd BLAST14
ChainiPRO_000000414415 – 521Glucosidase 2 subunit betaAdd BLAST507

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei24PhosphoserineBy similarity1
Disulfide bondi39 ↔ 58Combined sources1 Publication
Disulfide bondi56 ↔ 70Combined sources1 Publication
Glycosylationi72N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi77 ↔ 99Combined sources1 Publication
Modified residuei89Phosphoserine; by PKCSequence analysis1
Disulfide bondi97 ↔ 112Combined sources1 Publication
Disulfide bondi100 ↔ 116Combined sources1 Publication
Modified residuei166N6-succinyllysineCombined sources1
Modified residuei168PhosphoserineBy similarity1
Modified residuei376Phosphoserine; by PKCSequence analysis1
Modified residuei383Phosphoserine; by PKCSequence analysis1
Modified residuei427Phosphoserine; by PKCSequence analysis1
Glycosylationi469N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiO08795
PeptideAtlasiO08795
PRIDEiO08795

PTM databases

iPTMnetiO08795
PhosphoSitePlusiO08795
SwissPalmiO08795

Expressioni

Tissue specificityi

Expressed in kidney (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000003402 Expressed in 288 organ(s), highest expression level in membranous labyrinth
CleanExiMM_PRKCSH
ExpressionAtlasiO08795 baseline and differential
GenevisibleiO08795 MM

Interactioni

Subunit structurei

Heterodimer of a catalytic alpha subunit (GANAB) and a beta subunit (PRKCSH) (PubMed:9148925, PubMed:27462106). Binds glycosylated PTPRC (PubMed:9148925).2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202370, 4 interactors
IntActiO08795, 5 interactors
MINTiO08795
STRINGi10090.ENSMUSP00000003493

Structurei

Secondary structure

1521
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliO08795
SMRiO08795
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini37 – 71LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST35
Domaini69 – 113LDL-receptor class A 2PROSITE-ProRule annotation