CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012378
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Neutral alpha-glucosidase AB 
Protein Synonyms/Alias
 Alpha-glucosidase 2; Glucosidase II subunit alpha 
Gene Name
 GANAB 
Gene Synonyms/Alias
 G2AN; KIAA0088 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
39AVDRSNFKTCEESSFubiquitination[1]
48CEESSFCKRQRSIRPubiquitination[1]
191PRVSQGSKDPAEGDGubiquitination[1, 2, 3, 4]
217KPEETQGKAEKDEPGubiquitination[2]
220ETQGKAEKDEPGAWEubiquitination[2]
237FKTHSDSKPYGPMSVubiquitination[1, 2]
269HADNLRLKVTEGGEPubiquitination[1, 2, 3, 4]
337AGKTLFGKMMDYLQGubiquitination[1, 2, 3, 4]
462RLASKRRKLVAIVDPubiquitination[1]
472AIVDPHIKVDSGYRVubiquitination[1, 2, 5]
491RNLGLYVKTRDGSDYubiquitination[1, 2, 3, 4, 6]
899VVIIGAGKPAAVVLQubiquitination[1, 2, 4, 5, 6]
908AAVVLQTKGSPESRLubiquitination[1, 2, 4, 5]
930TSVLVLRKPGINVASubiquitination[1, 2]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 Cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins. 
Sequence Annotation
 ACT_SITE 542 542 Nucleophile.
 ACT_SITE 545 545 By similarity.
 ACT_SITE 618 618 Proton donor (By similarity).
 CARBOHYD 97 97 N-linked (GlcNAc...).  
Keyword
 Alternative splicing; Complete proteome; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; Glycosidase; Golgi apparatus; Hydrolase; Polymorphism; Reference proteome; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 944 AA 
Protein Sequence
MAAVAAVAAR RRRSWASLVL AFLGVCLGIT LAVDRSNFKT CEESSFCKRQ RSIRPGLSPY 60
RALLDSLQLG PDSLTVHLIH EVTKVLLVLE LQGLQKNMTR FRIDELEPRR PRYRVPDVLV 120
ADPPIARLSV SGRDENSVEL TMAEGPYKII LTARPFRLDL LEDRSLLLSV NARGLLEFEH 180
QRAPRVSQGS KDPAEGDGAQ PEETPRDGDK PEETQGKAEK DEPGAWEETF KTHSDSKPYG 240
PMSVGLDFSL PGMEHVYGIP EHADNLRLKV TEGGEPYRLY NLDVFQYELY NPMALYGSVP 300
VLLAHNPHRD LGIFWLNAAE TWVDISSNTA GKTLFGKMMD YLQGSGETPQ TDVRWMSETG 360
IIDVFLLLGP SISDVFRQYA SLTGTQALPP LFSLGYHQSR WNYRDEADVL EVDQGFDDHN 420
LPCDVIWLDI EHADGKRYFT WDPSRFPQPR TMLERLASKR RKLVAIVDPH IKVDSGYRVH 480
EELRNLGLYV KTRDGSDYEG WCWPGSAGYP DFTNPTMRAW WANMFSYDNY EGSAPNLFVW 540
NDMNEPSVFN GPEVTMLKDA QHYGGWEHRD VHNIYGLYVH MATADGLRQR SGGMERPFVL 600
ARAFFAGSQR FGAVWTGDNT AEWDHLKISI PMCLSLGLVG LSFCGADVGG FFKNPEPELL 660
VRWYQMGAYQ PFFRAHAHLD TGRREPWLLP SQHNDIIRDA LGQRYSLLPF WYTLLYQAHR 720
EGIPVMRPLW VQYPQDVTTF NIDDQYLLGD ALLVHPVSDS GAHGVQVYLP GQGEVWYDIQ 780
SYQKHHGPQT LYLPVTLSSI PVFQRGGTIV PRWMRVRRSS ECMKDDPITL FVALSPQGTA 840
QGELFLDDGH TFNYQTRQEF LLRRFSFSGN TLVSSSADPE GHFETPIWIE RVVIIGAGKP 900
AAVVLQTKGS PESRLSFQHD PETSVLVLRK PGINVASDWS IHLR 944 
Gene Ontology
 GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
 GO:0017177; C:glucosidase II complex; IEA:Compara.
 GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0030246; F:carbohydrate binding; IEA:InterPro.
 GO:0033919; F:glucan 1,3-alpha-glucosidase activity; IEA:EC.
 GO:0043687; P:post-translational protein modification; TAS:Reactome.
 GO:0006457; P:protein folding; TAS:Reactome.
 GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome. 
Interpro
 IPR011013; Gal_mutarotase_SF_dom.
 IPR000322; Glyco_hydro_31.
 IPR025887; Glyco_hydro_31_N_dom.
 IPR017853; Glycoside_hydrolase_SF. 
Pfam
 PF13802; Gal_mutarotas_2
 PF01055; Glyco_hydro_31 
SMART
  
PROSITE
 PS00129; GLYCOSYL_HYDROL_F31_1
 PS00707; GLYCOSYL_HYDROL_F31_2 
PRINTS