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Protein

Alpha-1,3/1,6-mannosyltransferase ALG2

Gene

Alg2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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.

Pathwayi

GO - Molecular functioni

  1. alpha-1,3-mannosyltransferase activity Source: MGI
  2. calcium-dependent protein binding Source: MGI
  3. GDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity Source: UniProtKB-EC
  4. glycolipid 6-alpha-mannosyltransferase activity Source: InterPro
  5. protein heterodimerization activity Source: MGI
  6. protein N-terminus binding Source: MGI

GO - Biological processi

  1. dolichol-linked oligosaccharide biosynthetic process Source: MGI
  2. mannosylation Source: MGI
  3. protein glycosylation in endoplasmic reticulum Source: MGI
  4. response to calcium ion Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_320215. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Alg2
ORF Names:MNCb-5081
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1914731. Alg2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei85 – 10521HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: MGI
  4. nucleus Source: MGI
  5. perinuclear region of cytoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 415415Alpha-1,3/1,6-mannosyltransferase ALG2PRO_0000080261Add
BLAST

Proteomic databases

MaxQBiQ9DBE8.
PaxDbiQ9DBE8.
PRIDEiQ9DBE8.

PTM databases

PhosphoSiteiQ9DBE8.

Expressioni

Gene expression databases

BgeeiQ9DBE8.
GenevestigatoriQ9DBE8.

Interactioni

Protein-protein interaction databases

BioGridi208151. 3 interactions.
IntActiQ9DBE8. 1 interaction.
MINTiMINT-4998111.

Structurei

3D structure databases

ProteinModelPortaliQ9DBE8.
SMRiQ9DBE8. Positions 153-407.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0438.
GeneTreeiENSGT00550000075033.
HOGENOMiHOG000177048.
HOVERGENiHBG009445.
InParanoidiQ9DBE8.
KOiK03843.
OMAiGETGWLR.
OrthoDBiEOG7HTHH4.
PhylomeDBiQ9DBE8.
TreeFamiTF106000.

Family and domain databases

InterProiIPR027054. ALG2.
IPR001296. Glyco_trans_1.
IPR028098. Glyco_trans_4_N.
[Graphical view]
PANTHERiPTHR12526:SF221. PTHR12526:SF221. 1 hit.
PfamiPF13579. Glyco_trans_4_4. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DBE8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAENLYRARS RVYSPSVLFL HPDMGIGGAE RLVLDAALAL QEYGCDVKIW
60 70 80 90 100
TAHYDPNHCF IETRELSVQC AGDWLPRSLG WGGRGAAICS YVRMVFLALY
110 120 130 140 150
VLFLSGEEFD VVVCDQVSAC IPVFKLARRR KRVLFYCHFP DLLLTQRNSA
160 170 180 190 200
LKKFYRAPID WIEEYTTGMA DRILVNSQYT ASVFKETFKT LSHRNPDVLY
210 220 230 240 250
PSLNIGSFDL AIPEKIDDLV PKGKQFLFLS INRYERKKNL PLALRSLVQL
260 270 280 290 300
RNRLPSQEWD KVHLFMAGGY DDRIPENVEH YKELKKMVQE SDLERHVTFL
310 320 330 340 350
RSFSDRQKIS LLHGCLCVLY TPSNEHFGIV PLEAMYMQCP VIAVNNGGPL
360 370 380 390 400
ESIVHKVTGF LCEPDPVHFS EAMEKFIHKP SLKATMGLAG KARVAEKFSA
410
DAFADQLYQY VTKLV
Length:415
Mass (Da):47,405
Last modified:April 13, 2004 - v2
Checksum:i7462CA9DEF74BA13
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti296 – 2961H → Y in BAB27106 (PubMed:16141072).Curated
Sequence conflicti376 – 3761F → L in BAB23731 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18161.1.
RefSeqiNP_064382.3. NM_019998.3.
UniGeneiMm.22218.

Genome annotation databases

EnsembliENSMUST00000044148; ENSMUSP00000043580; ENSMUSG00000039740.
GeneIDi56737.
KEGGimmu:56737.
UCSCiuc008suq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18161.1.
RefSeqiNP_064382.3. NM_019998.3.
UniGeneiMm.22218.

3D structure databases

ProteinModelPortaliQ9DBE8.
SMRiQ9DBE8. Positions 153-407.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208151. 3 interactions.
IntActiQ9DBE8. 1 interaction.
MINTiMINT-4998111.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

PTM databases

PhosphoSiteiQ9DBE8.

Proteomic databases

MaxQBiQ9DBE8.
PaxDbiQ9DBE8.
PRIDEiQ9DBE8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000044148; ENSMUSP00000043580; ENSMUSG00000039740.
GeneIDi56737.
KEGGimmu:56737.
UCSCiuc008suq.2. mouse.

Organism-specific databases

CTDi85365.
MGIiMGI:1914731. Alg2.

Phylogenomic databases

eggNOGiCOG0438.
GeneTreeiENSGT00550000075033.
HOGENOMiHOG000177048.
HOVERGENiHBG009445.
InParanoidiQ9DBE8.
KOiK03843.
OMAiGETGWLR.
OrthoDBiEOG7HTHH4.
PhylomeDBiQ9DBE8.
TreeFamiTF106000.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_320215. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.

Miscellaneous databases

NextBioi313228.
PROiQ9DBE8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBE8.
GenevestigatoriQ9DBE8.

Family and domain databases

InterProiIPR027054. ALG2.
IPR001296. Glyco_trans_1.
IPR028098. Glyco_trans_4_N.
[Graphical view]
PANTHERiPTHR12526:SF221. PTHR12526:SF221. 1 hit.
PfamiPF13579. Glyco_trans_4_4. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 (DEC-2003) 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 (MAR-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.
    , 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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryonic stem cell and Liver.
  4. 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Embryonic brain.

Entry informationi

Entry nameiALG2_MOUSE
AccessioniPrimary (citable) accession number: Q9DBE8
Secondary accession number(s): Q7TN30, Q9CWI6, Q9JJA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: April 1, 2015
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.