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Q9DBE8 (ALG2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-1,3/1,6-mannosyltransferase ALG2

EC=2.4.1.132
EC=2.4.1.257
Alternative name(s):
Asparagine-linked glycosylation protein 2 homolog
GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase
GDP-Man:Man(1)GlcNAc(2)-PP-dolichol mannosyltransferase
GDP-Man:Man(2)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase
Gene names
Name:Alg2
ORF Names:MNCb-5081
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Mannosylates Man2GlcNAc(2)-dolichol diphosphate and Man1GlcNAc(2)-dolichol diphosphate to form Man3GlcNAc(2)-dolichol diphosphate By similarity.

Catalytic activity

GDP-D-mannose + D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = GDP + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-GlcNAc-diphosphodolichol.

GDP-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = GDP + D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Membrane; Single-pass membrane protein Potential.

Sequence similarities

Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 415415Alpha-1,3/1,6-mannosyltransferase ALG2
PRO_0000080261

Regions

Transmembrane85 – 10521Helical; Potential

Experimental info

Sequence conflict2961H → Y in BAB27106. Ref.3
Sequence conflict3761F → L in BAB23731. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9DBE8 [UniParc].

Last modified April 13, 2004. Version 2.
Checksum: 7462CA9DEF74BA13

FASTA41547,405
        10         20         30         40         50         60 
MAENLYRARS RVYSPSVLFL HPDMGIGGAE RLVLDAALAL QEYGCDVKIW TAHYDPNHCF 

        70         80         90        100        110        120 
IETRELSVQC AGDWLPRSLG WGGRGAAICS YVRMVFLALY VLFLSGEEFD VVVCDQVSAC 

       130        140        150        160        170        180 
IPVFKLARRR KRVLFYCHFP DLLLTQRNSA LKKFYRAPID WIEEYTTGMA DRILVNSQYT 

       190        200        210        220        230        240 
ASVFKETFKT LSHRNPDVLY PSLNIGSFDL AIPEKIDDLV PKGKQFLFLS INRYERKKNL 

       250        260        270        280        290        300 
PLALRSLVQL RNRLPSQEWD KVHLFMAGGY DDRIPENVEH YKELKKMVQE SDLERHVTFL 

       310        320        330        340        350        360 
RSFSDRQKIS LLHGCLCVLY TPSNEHFGIV PLEAMYMQCP VIAVNNGGPL ESIVHKVTGF 

       370        380        390        400        410 
LCEPDPVHFS EAMEKFIHKP SLKATMGLAG KARVAEKFSA DAFADQLYQY VTKLV 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of the mammalian genes which complement the defect of the yeast alg2 mutation."
Takahashi T., Ueda M., Itoh N., Okutomi S., Nishikawa Y.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method."
Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[3]"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. expand/collapse author list , 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].
Strain: C57BL/6J.
Tissue: Embryonic stem cell and Liver.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"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].
Strain: C57BL/6.
Tissue: Embryonic brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB161357 mRNA. Translation: BAD11906.1.
AB041604 mRNA. Translation: BAA95087.1.
AK004997 mRNA. Translation: BAB23731.1.
AK010673 mRNA. Translation: BAB27106.1.
AL772150 Genomic DNA. Translation: CAM24920.1.
BC051951 mRNA. Translation: AAH51951.1.
BC052411 mRNA. Translation: AAH52411.2.
CCDSCCDS18161.1.
RefSeqNP_064382.3. NM_019998.3.
UniGeneMm.22218.

3D structure databases

ProteinModelPortalQ9DBE8.
SMRQ9DBE8. Positions 153-407.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid208151. 3 interactions.
IntActQ9DBE8. 1 interaction.
MINTMINT-4998111.

Protein family/group databases

CAZyGT4. Glycosyltransferase Family 4.

PTM databases

PhosphoSiteQ9DBE8.

Proteomic databases

MaxQBQ9DBE8.
PaxDbQ9DBE8.
PRIDEQ9DBE8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000044148; ENSMUSP00000043580; ENSMUSG00000039740.
GeneID56737.
KEGGmmu:56737.
UCSCuc008suq.2. mouse.

Organism-specific databases

CTD85365.
MGIMGI:1914731. Alg2.

Phylogenomic databases

eggNOGCOG0438.
GeneTreeENSGT00550000075033.
HOGENOMHOG000177048.
HOVERGENHBG009445.
InParanoidQ9DBE8.
KOK03843.
OMAGETGWLR.
OrthoDBEOG7HTHH4.
PhylomeDBQ9DBE8.
TreeFamTF106000.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeQ9DBE8.
GenevestigatorQ9DBE8.

Family and domain databases

InterProIPR027054. ALG2.
IPR001296. Glyco_trans_1.
IPR028098. Glyco_trans_4_N.
[Graphical view]
PANTHERPTHR12526:SF221. PTHR12526:SF221. 1 hit.
PfamPF13579. Glyco_trans_4_4. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio313228.
PROQ9DBE8.
SOURCESearch...

Entry information

Entry nameALG2_MOUSE
AccessionPrimary (citable) accession number: Q9DBE8
Secondary accession number(s): Q7TN30, Q9CWI6, Q9JJA8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: July 9, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot