CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-040015
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Neutral alpha-glucosidase AB 
Protein Synonyms/Alias
  
Gene Name
 GANAB 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
94PRVSQGSKDPAEGDGubiquitination[1, 2, 3, 4]
Reference
 [1] 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]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] 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]
 [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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 847 AA 
Protein Sequence
MTRFRIDELE PRRPRYRVPD VLVADPPIAR LSVSGRDENS VELTMAEGPY KIILTARPFR 60
LDLLEDRSLL LSVNARGLLE FEHQRAPRVS QGSKDPAEGD GAQPEETPRD GDKPEETQGK 120
AEKDEPGAWE ETFKTHSDSK PYGPMSVGLD FSLPGMEHVY GIPEHADNLR LKVTEGGEPY 180
RLYNLDVFQY ELYNPMALYG SVPVLLAHNP HRDLGIFWLN AAETWVDISS NTAGKTLFGK 240
MMDYLQGSGE TPQTDVRWMS ETGIIDVFLL LGPSISDVFR QYASLTGTQA LPPLFSLGYH 300
QSRWNYRDEA DVLEVDQGFD DHNLPCDVIW LDIEHADGKR YFTWDPSRFP QPRTMLERLA 360
SKRRKLVAIV DPHIKVDSGY RVHEELRNLG LYVKTRDGSD YEGWCWPGSA GYPDFTNPTM 420
RAWWANMFSY DNYEGSAPNL FVWNDMNEPS VFNGPEVTML KDAQHYGGWE HRDVHNIYGL 480
YVHMATADGL RQRSGGMERP FVLARAFFAG SQRFGAVWTG DNTAEWDHLK ISIPMCLSLG 540
LVGLSFCGAD VGGFFKNPEP ELLVRWYQMG AYQPFFRAHA HLDTGRREPW LLPSQHNDII 600
RDALGQRYSL LPFWYTLLYQ AHREGIPVMR PLWVQYPQDV TTFNIDDQYL LGDALLVHPV 660
SDSGAHGVQV YLPGQGEVWY DIQSYQKHHG PQTLYLPVTL SSIPVFQRGG TIVPRWMRVR 720
RSSECMKDDP ITLFVALSPQ GTAQGELFLD DGHTFNYQTR QEFLLRRFSF SGNTLVSSSA 780
DPEGHFETPI WIERVVIIGA GKPAAVVLQT KGSPESRLSF QHDPETSVLV LRKPGINVAS 840
DWSIHLR 847 
Gene Ontology
 GO:0030246; F:carbohydrate binding; IEA:InterPro.
 GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
 GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. 
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