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Q9H553

- ALG2_HUMAN

UniProt

Q9H553 - ALG2_HUMAN

Protein

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

Gene

ALG2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Mannosylates Man2GlcNAc(2)-dolichol diphosphate and Man1GlcNAc(2)-dolichol diphosphate to form Man3GlcNAc(2)-dolichol diphosphate.1 Publication

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

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. dolichol-linked oligosaccharide biosynthetic process Source: UniProtKB
    3. mannosylation Source: GOC
    4. post-translational protein modification Source: Reactome
    5. protein glycosylation in endoplasmic reticulum Source: UniProtKB
    6. protein N-linked glycosylation via asparagine Source: Reactome
    7. response to calcium ion Source: UniProtKB

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    ReactomeiREACT_22433. 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:UNQ666/PRO1298
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:23159. ALG2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. endoplasmic reticulum membrane Source: Reactome
    3. integral component of membrane Source: UniProtKB-KW
    4. membrane Source: UniProtKB
    5. nucleus Source: UniProtKB
    6. perinuclear region of cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Congenital disorder of glycosylation 1I (CDG1I) [MIM:607906]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Congenital disorder of glycosylation

    Organism-specific databases

    MIMi607906. phenotype.
    Orphaneti79326. ALG2-CDG.
    353327. Congenital myasthenic syndromes with glycosylation defect.
    PharmGKBiPA134956849.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 416416Alpha-1,3/1,6-mannosyltransferase ALG2PRO_0000080260Add
    BLAST

    Proteomic databases

    MaxQBiQ9H553.
    PaxDbiQ9H553.
    PRIDEiQ9H553.

    PTM databases

    PhosphoSiteiQ9H553.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9H553.
    BgeeiQ9H553.
    CleanExiHS_ALG2.
    GenevestigatoriQ9H553.

    Organism-specific databases

    HPAiHPA041512.
    HPA041601.

    Interactioni

    Protein-protein interaction databases

    BioGridi124493. 16 interactions.
    STRINGi9606.ENSP00000417764.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H553.
    SMRiQ9H553. Positions 163-407.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

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

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0438.
    HOGENOMiHOG000177048.
    HOVERGENiHBG009445.
    InParanoidiQ9H553.
    KOiK03843.
    OMAiGETGWLR.
    OrthoDBiEOG7HTHH4.
    PhylomeDBiQ9H553.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H553-1) [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

    MAEEQGRERD SVPKPSVLFL HPDLGVGGAE RLVLDAALAL QARGCSVKIW    50
    TAHYDPGHCF AESRELPVRC AGDWLPRGLG WGGRGAAVCA YVRMVFLALY 100
    VLFLADEEFD VVVCDQVSAC IPVFRLARRR KKILFYCHFP DLLLTKRDSF 150
    LKRLYRAPID WIEEYTTGMA DCILVNSQFT AAVFKETFKS LSHIDPDVLY 200
    PSLNVTSFDS VVPEKLDDLV PKGKKFLLLS INRYERKKNL TLALEALVQL 250
    RGRLTSQDWE RVHLIVAGGY DERVLENVEH YQELKKMVQQ SDLGQYVTFL 300
    RSFSDKQKIS LLHSCTCVLY TPSNEHFGIV PLEAMYMQCP VIAVNSGGPL 350
    ESIDHSVTGF LCEPDPVHFS EAIEKFIREP SLKATMGLAG RARVKEKFSP 400
    EAFTEQLYRY VTKLLV 416
    Length:416
    Mass (Da):47,092
    Last modified:March 1, 2001 - v1
    Checksum:i778DB1FD069E7F29
    GO
    Isoform 2 (identifier: Q9H553-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-91: Missing.
         92-116: VRMVFLALYVLFLADEEFDVVVCDQ → MPLLKLVHGSPLVFGEKFKLFTL

    Show »
    Length:323
    Mass (Da):37,017
    Checksum:iC8506E37A7E15848
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti178 – 1781Q → R in BAC11449. (PubMed:12975309)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111S → P.
    Corresponds to variant rs11545137 [ dbSNP | Ensembl ].
    VAR_049351
    Natural varianti367 – 3671V → A.
    Corresponds to variant rs35626507 [ dbSNP | Ensembl ].
    VAR_049352

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9191Missing in isoform 2. 2 PublicationsVSP_013188Add
    BLAST
    Alternative sequencei92 – 11625VRMVF…VVCDQ → MPLLKLVHGSPLVFGEKFKL FTL in isoform 2. 2 PublicationsVSP_013189Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB161356 mRNA. Translation: BAD11905.1.
    AY358697 mRNA. Translation: AAQ89060.1.
    AK027417 mRNA. Translation: BAB55099.1.
    AK074704 mRNA. Translation: BAC11150.1.
    AK074988 mRNA. Translation: BAC11337.1.
    AK075172 mRNA. Translation: BAC11449.1.
    AL137067 Genomic DNA. Translation: CAC07999.1.
    BC017876 mRNA. Translation: AAH17876.1.
    CCDSiCCDS6739.1. [Q9H553-1]
    RefSeqiNP_149078.1. NM_033087.3. [Q9H553-1]
    UniGeneiHs.40919.

    Genome annotation databases

    EnsembliENST00000319033; ENSP00000326609; ENSG00000119523. [Q9H553-2]
    ENST00000476832; ENSP00000417764; ENSG00000119523. [Q9H553-1]
    GeneIDi85365.
    KEGGihsa:85365.
    UCSCiuc004azf.3. human. [Q9H553-1]
    uc004azg.3. human. [Q9H553-2]

    Polymorphism databases

    DMDMi46395991.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB161356 mRNA. Translation: BAD11905.1 .
    AY358697 mRNA. Translation: AAQ89060.1 .
    AK027417 mRNA. Translation: BAB55099.1 .
    AK074704 mRNA. Translation: BAC11150.1 .
    AK074988 mRNA. Translation: BAC11337.1 .
    AK075172 mRNA. Translation: BAC11449.1 .
    AL137067 Genomic DNA. Translation: CAC07999.1 .
    BC017876 mRNA. Translation: AAH17876.1 .
    CCDSi CCDS6739.1. [Q9H553-1 ]
    RefSeqi NP_149078.1. NM_033087.3. [Q9H553-1 ]
    UniGenei Hs.40919.

    3D structure databases

    ProteinModelPortali Q9H553.
    SMRi Q9H553. Positions 163-407.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124493. 16 interactions.
    STRINGi 9606.ENSP00000417764.

    Protein family/group databases

    CAZyi GT4. Glycosyltransferase Family 4.

    PTM databases

    PhosphoSitei Q9H553.

    Polymorphism databases

    DMDMi 46395991.

    Proteomic databases

    MaxQBi Q9H553.
    PaxDbi Q9H553.
    PRIDEi Q9H553.

    Protocols and materials databases

    DNASUi 85365.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000319033 ; ENSP00000326609 ; ENSG00000119523 . [Q9H553-2 ]
    ENST00000476832 ; ENSP00000417764 ; ENSG00000119523 . [Q9H553-1 ]
    GeneIDi 85365.
    KEGGi hsa:85365.
    UCSCi uc004azf.3. human. [Q9H553-1 ]
    uc004azg.3. human. [Q9H553-2 ]

    Organism-specific databases

    CTDi 85365.
    GeneCardsi GC09M101978.
    GeneReviewsi ALG2.
    H-InvDB HIX0019474.
    HGNCi HGNC:23159. ALG2.
    HPAi HPA041512.
    HPA041601.
    MIMi 607905. gene.
    607906. phenotype.
    neXtProti NX_Q9H553.
    Orphaneti 79326. ALG2-CDG.
    353327. Congenital myasthenic syndromes with glycosylation defect.
    PharmGKBi PA134956849.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0438.
    HOGENOMi HOG000177048.
    HOVERGENi HBG009445.
    InParanoidi Q9H553.
    KOi K03843.
    OMAi GETGWLR.
    OrthoDBi EOG7HTHH4.
    PhylomeDBi Q9H553.
    TreeFami TF106000.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.

    Miscellaneous databases

    ChiTaRSi ALG2. human.
    GeneWikii ALG2.
    GenomeRNAii 85365.
    NextBioi 75895.
    PROi Q9H553.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H553.
    Bgeei Q9H553.
    CleanExi HS_ALG2.
    Genevestigatori Q9H553.

    Family and domain databases

    InterProi IPR027054. ALG2.
    IPR001296. Glyco_trans_1.
    IPR028098. Glyco_trans_4_N.
    [Graphical view ]
    PANTHERi PTHR12526:SF221. PTHR12526:SF221. 1 hit.
    Pfami PF13579. Glyco_trans_4_4. 1 hit.
    PF00534. Glycos_transf_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of the mammalian genes which complement the defect of the yeast alg2 mutation."
      Takahashi T., Katoh R., Okutomi S., Suzuki Y., Mori H., Takizawa Y., Nishikawa Y.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Placenta.
    4. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1).
      Tissue: Embryonic testis carcinoma.
    6. "A new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesis."
      Thiel C., Schwarz M., Peng J., Grzmil M., Hasilik M., Braulke T., Kohlschuetter A., von Figura K., Lehle L., Koerner C.
      J. Biol. Chem. 278:22498-22505(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INVOLVEMENT IN CDG1I.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiALG2_HUMAN
    AccessioniPrimary (citable) accession number: Q9H553
    Secondary accession number(s): A2A2Y0, Q8NBX2, Q8NC39
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3