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Sequence of GANAB_HUMAN

EC Number:3.2.1.207

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
mannosyl-oligosaccharide alpha-1,3-glucosidase
Q14697
Homo sapiens
944
106874
Reaction
Glc2Man9GlcNAc2-[protein] + H2O = GlcMan9GlcNAc2-[protein] + beta-D-glucopyranose
Other sequences found for EC No. 3.2.1.207

General information:

Sequence
show sequence in fasta format
  0 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
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
546949
Pelletier M.F.,Marcil A.,Sevigny G.,Jakob C.A.,Tessier D.C.,Chevet E.,Menard R.,Bergeron J.J.M.,Thomas D.Y.
The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo.
Glycobiology
10
815-827
2000
546950
Taylor T.D.,Noguchi H.,Totoki Y.,Toyoda A.,Kuroki Y.,Dewar K.,Lloyd C.,Itoh T.,Takeda T.,Kim D.-W.,She X.,Barlow K.F.,Bloom T.,Bruford E.,Chang J.L.,Cuomo C.A.,Eichler E.,FitzGerald M.G.,Jaffe D.B.,LaButti K.,Nicol R.,Park H.-S.,Seaman C.,Sougnez C.,Yang X.,Zimmer A.R.,Zody M.C.,Birren B.W.,Nusbaum C.,Fujiyama A.,Hattori M.,Rogers J.,Lander E.S.,Sakaki Y.
Human chromosome 11 DNA sequence and analysis including novel gene identification.
Nature
440
497-500
2006
546951
Nagase T.,Miyajima N.,Tanaka A.,Sazuka T.,Seki N.,Sato S.,Tabata S.,Ishikawa K.,Kawarabayasi Y.,Kotani H.,Nomura N.
Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1.
DNA Res.
2
37-43
1995
546952
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
546954
Martiniuk F.,Ellenbogen A.,Hirschhorn R.
Identity of neutral alpha-glucosidase AB and the glycoprotein processing enzyme glucosidase II. Biochemical and genetic studies.
J. Biol. Chem.
260
1238-1242
1985
546955
Trombetta E.S.,Simons J.F.,Helenius A.
Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit.
J. Biol. Chem.
271
27509-27516
1996
546956
Chi A.,Valencia J.C.,Hu Z.-Z.,Watabe H.,Yamaguchi H.,Mangini N.J.,Huang H.,Canfield V.A.,Cheng K.C.,Yang F.,Abe R.,Yamagishi S.,Shabanowitz J.,Hearing V.J.,Wu C.,Appella E.,Hunt D.F.
Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.
J. Proteome Res.
5
3135-3144
2006
546957
Burkard T.R.,Planyavsky M.,Kaupe I.,Breitwieser F.P.,Buerckstuemmer T.,Bennett K.L.,Superti-Furga G.,Colinge J.
Initial characterization of the human central proteome.
BMC Syst. Biol.
5
17-17
2011
546958
Zhou H.,Di Palma S.,Preisinger C.,Peng M.,Polat A.N.,Heck A.J.,Mohammed S.
Toward a comprehensive characterization of a human cancer cell phosphoproteome.
J. Proteome Res.
12
260-271
2013
546959
Bian Y.,Song C.,Cheng K.,Dong M.,Wang F.,Huang J.,Sun D.,Wang L.,Ye M.,Zou H.
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
J. Proteomics
96
253-262
2014
546960
Vaca Jacome A.S.,Rabilloud T.,Schaeffer-Reiss C.,Rompais M.,Ayoub D.,Lane L.,Bairoch A.,Van Dorsselaer A.,Carapito C.
N-terminome analysis of the human mitochondrial proteome.
Proteomics
15
2519-2524
2015
546961
Porath B.,Gainullin V.G.,Cornec-Le Gall E.,Dillinger E.K.,Heyer C.M.,Hopp K.,Edwards M.E.,Madsen C.D.,Mauritz S.R.,Banks C.J.,Baheti S.,Reddy B.,Herrero J.I.,Banales J.M.,Hogan M.C.,Tasic V.,Watnick T.J.,Chapman A.B.,Vigneau C.,Lavainne F.,Audrezet M.P.,Ferec C.,Le Meur Y.,Torres V.E.,Harris P.C.
Mutations in GANAB, encoding the glucosidase IIalpha subunit, cause autosomal-dominant polycystic kidney and liver disease.
Am. J. Hum. Genet.
98
1193-1207
2016
546962
Besse W.,Dong K.,Choi J.,Punia S.,Fedeles S.V.,Choi M.,Gallagher A.R.,Huang E.B.,Gulati A.,Knight J.,Mane S.,Tahvanainen E.,Tahvanainen P.,Sanna-Cherchi S.,Lifton R.P.,Watnick T.,Pei Y.P.,Torres V.E.,Somlo S.
Isolated polycystic liver disease genes define effectors of polycystin-1 function.
J. Clin. Invest.
127
1772-1785
2017
546963
van de Laarschot L.F.M.,Te Morsche R.H.M.,Hoischen A.,Venselaar H.,Roelofs H.M.,Cnossen W.R.,Banales J.M.,Roepman R.,Drenth J.P.H.
Novel GANAB variants associated with polycystic liver disease.
Orphanet J. Rare Dis.
15
302-302
2020