SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8BHN3

- GANAB_MOUSE

UniProt

Q8BHN3 - GANAB_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Neutral alpha-glucosidase AB
Gene
Ganab, G2an, Kiaa0088
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc2Man9GlcNAc2 oligosaccharide precursor of immature glycoproteins.

Catalytic activityi

Hydrolysis of terminal (1->3)-alpha-D-glucosidic links in (1->3)-alpha-D-glucans.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei542 – 5421Nucleophile By similarity
Active sitei545 – 5451 By similarity
Active sitei618 – 6181Proton donor By similarity

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. glucan 1,3-alpha-glucosidase activity Source: UniProtKB-EC
  3. glucosidase activity Source: MGI
  4. protein binding Source: MGI

GO - Biological processi

  1. N-glycan processing Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

ReactomeiREACT_198616. Calnexin/calreticulin cycle.
REACT_198618. N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
UniPathwayiUPA00957.

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
Neutral alpha-glucosidase AB (EC:3.2.1.84)
Alternative name(s):
Alpha-glucosidase 2
Glucosidase II subunit alpha
Gene namesi
Name:Ganab
Synonyms:G2an, Kiaa0088
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:1097667. Ganab.

Subcellular locationi

Endoplasmic reticulum By similarity. Golgi apparatus By similarity. Melanosome By similarity

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB-SubCell
  2. endoplasmic reticulum Source: MGI
  3. glucosidase II complex Source: MGI
  4. melanosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 32321 Publication
Add
BLAST
Chaini33 – 944912Neutral alpha-glucosidase AB
PRO_0000018572Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi97 – 971N-linked (GlcNAc...)

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ8BHN3.
PaxDbiQ8BHN3.
PRIDEiQ8BHN3.

PTM databases

PhosphoSiteiQ8BHN3.

Expressioni

Gene expression databases

ArrayExpressiQ8BHN3.
BgeeiQ8BHN3.
CleanExiMM_GANAB.
GenevestigatoriQ8BHN3.

Interactioni

Subunit structurei

Heterodimer of a catalytic alpha subunit (GANAB) and a beta subunit (PRKCSH). Binds glycosylated PTPRC.1 Publication

Protein-protein interaction databases

BioGridi199786. 1 interaction.
IntActiQ8BHN3. 6 interactions.
MINTiMINT-1863945.

Structurei

3D structure databases

ProteinModelPortaliQ8BHN3.
SMRiQ8BHN3. Positions 349-928.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1501.
GeneTreeiENSGT00740000115152.
HOGENOMiHOG000115864.
HOVERGENiHBG051683.
KOiK05546.
OMAiAIDDQLY.
OrthoDBiEOG7VQJDS.
PhylomeDBiQ8BHN3.
TreeFamiTF300337.

Family and domain databases

InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR025887. Glyco_hydro_31_N_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF13802. Gal_mutarotas_2. 1 hit.
PF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 2 hits.
PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8BHN3-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MAAIAAVAAR RRRSWLSLVL AYLGVCLGIT LAVDRSNFKT CDESSFCKRQ    50
RSIRPGLSPY RALLDTLQLG PDALTVHLIH EVTKVLLVLE LQGLQKNMTR 100
IRIDELEPRR PRYRVPDVLV ADPPTARLSV SGRDDNSVEL TVAEGPYKII 150
LTAQPFRLDL LEDRSLLLSV NARGLMAFEH QRAPRVPQES KDPAEGNGAQ 200
PEATPGDGDK PEETQEKAEK DEPGAWEETF KTHSDSKPYG PTSVGLDFSL 250
PGMEHVYGIP EHADSLRLKV TEGGEPYRLY NLDVFQYELN NPMALYGSVP 300
VLLAHSFHRD LGIFWLNAAE TWVDISSNTA GKTLFGKMLD YLQGSGETPQ 350
TDIRWMSESG IIDVFLMLGP SVFDVFRQYA SLTGTQALPP LFSLGYHQSR 400
WNYRDEADVL EVDQGFDDHN MPCDVIWLDI EHADGKRYFT WDPTRFPQPL 450
NMLEHLASKR RKLVAIVDPH IKVDSGYRVH EELRNHGLYV KTRDGSDYEG 500
WCWPGSASYP DFTNPRMRAW WSNMFSFDNY EGSAPNLYVW NDMNEPSVFN 550
GPEVTMLKDA VHYGGWEHRD IHNIYGLYVH MATADGLIQR SGGIERPFVL 600
SRAFFSGSQR FGAVWTGDNT AEWDHLKISI PMCLSLALVG LSFCGADVGG 650
FFKNPEPELL VRWYQMGAYQ PFFRAHAHLD TGRREPWLLA SQYQDAIRDA 700
LFQRYSLLPF WYTLFYQAHK EGFPVMRPLW VQYPEDMSTF SIEDQFMLGD 750
ALLIHPVSDA GAHGVQVYLP GQEEVWYDIQ SYQKHHGPQT LYLPVTLSSI 800
PVFQRGGTIV PRWMRVRRSS DCMKDDPITL FVALSPQGTA QGELFLDDGH 850
TFNYQTRHEF LLRRFSFSGS TLVSSSADPK GHLETPIWIE RVVIMGAGKP 900
AAVVLQTKGS PESRLSFQHD PETSVLILRK PGVSVASDWS IHLR 944
Length:944
Mass (Da):106,911
Last modified:March 1, 2003 - v1
Checksum:i01489861A537416E
GO
Isoform 2 (identifier: Q8BHN3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     187-187: P → PFSDKVSLALGSVWDKIKNLFSR

Show »
Length:966
Mass (Da):109,404
Checksum:iE3E507E2E2E68C75
GO
Isoform 3 (identifier: Q8BHN3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-252: Missing.

Note: May be due to an intron retention.

Show »
Length:692
Mass (Da):79,082
Checksum:iE4877A7B38966E3C
GO

Sequence cautioni

The sequence BAC65483.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 252252Missing in isoform 3.
VSP_010675Add
BLAST
Alternative sequencei187 – 1871P → PFSDKVSLALGSVWDKIKNL FSR in isoform 2.
VSP_010676

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti647 – 6471D → N in BAB30982. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U92793 mRNA. Translation: AAC53182.1.
AK017873 mRNA. Translation: BAB30982.1.
AK030722 mRNA. Translation: BAC27099.1.
AK081915 mRNA. Translation: BAC38370.1.
AK122201 mRNA. Translation: BAC65483.1. Different initiation.
BC094437 mRNA. Translation: AAH94437.1.
BC117888 mRNA. Translation: AAI17889.1.
BC117889 mRNA. Translation: AAI17890.1.
CCDSiCCDS29557.1. [Q8BHN3-2]
RefSeqiNP_032086.1. NM_008060.2. [Q8BHN3-2]
UniGeneiMm.3196.

Genome annotation databases

EnsembliENSMUST00000096246; ENSMUSP00000093965; ENSMUSG00000071650. [Q8BHN3-2]
GeneIDi14376.
KEGGimmu:14376.
UCSCiuc008gnx.1. mouse. [Q8BHN3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U92793 mRNA. Translation: AAC53182.1 .
AK017873 mRNA. Translation: BAB30982.1 .
AK030722 mRNA. Translation: BAC27099.1 .
AK081915 mRNA. Translation: BAC38370.1 .
AK122201 mRNA. Translation: BAC65483.1 . Different initiation.
BC094437 mRNA. Translation: AAH94437.1 .
BC117888 mRNA. Translation: AAI17889.1 .
BC117889 mRNA. Translation: AAI17890.1 .
CCDSi CCDS29557.1. [Q8BHN3-2 ]
RefSeqi NP_032086.1. NM_008060.2. [Q8BHN3-2 ]
UniGenei Mm.3196.

3D structure databases

ProteinModelPortali Q8BHN3.
SMRi Q8BHN3. Positions 349-928.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199786. 1 interaction.
IntActi Q8BHN3. 6 interactions.
MINTi MINT-1863945.

Protein family/group databases

CAZyi GH31. Glycoside Hydrolase Family 31.

PTM databases

PhosphoSitei Q8BHN3.

Proteomic databases

MaxQBi Q8BHN3.
PaxDbi Q8BHN3.
PRIDEi Q8BHN3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000096246 ; ENSMUSP00000093965 ; ENSMUSG00000071650 . [Q8BHN3-2 ]
GeneIDi 14376.
KEGGi mmu:14376.
UCSCi uc008gnx.1. mouse. [Q8BHN3-1 ]

Organism-specific databases

CTDi 23193.
MGIi MGI:1097667. Ganab.
Rougei Search...

Phylogenomic databases

eggNOGi COG1501.
GeneTreei ENSGT00740000115152.
HOGENOMi HOG000115864.
HOVERGENi HBG051683.
KOi K05546.
OMAi AIDDQLY.
OrthoDBi EOG7VQJDS.
PhylomeDBi Q8BHN3.
TreeFami TF300337.

Enzyme and pathway databases

UniPathwayi UPA00957 .
Reactomei REACT_198616. Calnexin/calreticulin cycle.
REACT_198618. N-glycan trimming in the ER and Calnexin/Calreticulin cycle.

Miscellaneous databases

NextBioi 285877.
PROi Q8BHN3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8BHN3.
Bgeei Q8BHN3.
CleanExi MM_GANAB.
Genevestigatori Q8BHN3.

Family and domain databases

InterProi IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR025887. Glyco_hydro_31_N_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF13802. Gal_mutarotas_2. 1 hit.
PF01055. Glyco_hydro_31. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 2 hits.
PROSITEi PS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of the CD45-associated 116-kDa and 80-kDa proteins as the alpha- and beta-subunits of alpha-glucosidase II."
    Arendt C.W., Ostergaard H.L.
    J. Biol. Chem. 272:13117-13125(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 33-50; 176-187; 823-839 AND 895-905, HETERODIMERIZATION WITH PRKCSH.
    Tissue: T-cell lymphoma.
  2. "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] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Embryo and Head.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  4. "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] (ISOFORM 1).
  5. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 62-96; 134-173; 338-354; 378-400; 438-459; 591-610; 654-662; 685-698; 785-805; 864-880; 892-908 AND 915-944, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  6. "Specific isoforms of the resident endoplasmic reticulum protein glucosidase II associate with the CD45 protein-tyrosine phosphatase via a lectin-like interaction."
    Baldwin T.A., Gogela-Spehar M., Ostergaard H.L.
    J. Biol. Chem. 275:32071-32076(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GLYCOSYLATED PTPRC, GLYCOSYLATION.

Entry informationi

Entry nameiGANAB_MOUSE
AccessioniPrimary (citable) accession number: Q8BHN3
Secondary accession number(s): O08794
, Q149A6, Q80U81, Q9CS53
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: March 1, 2003
Last modified: September 3, 2014
This is version 101 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, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi