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Q2TAA5

- ALG11_HUMAN

UniProt

Q2TAA5 - ALG11_HUMAN

Protein

GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase

Gene

ALG11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 2 (24 Jul 2007)
      Previous versions | rss
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    Functioni

    Mannosyltransferase involved in the last steps of the synthesis of Man5GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum. Catalyzes the addition of the 4th and 5th mannose residues to the dolichol-linked oligosaccharide chain.1 Publication

    Catalytic activityi

    2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = 2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol.1 Publication

    GO - Molecular functioni

    1. GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. dolichol-linked oligosaccharide biosynthetic process Source: Reactome
    3. post-translational protein modification Source: Reactome
    4. protein N-linked glycosylation via asparagine Source: Reactome

    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.

    Protein family/group databases

    CAZyiGT4. Glycosyltransferase Family 4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase (EC:2.4.1.131)
    Alternative name(s):
    Asparagine-linked glycosylation protein 11 homolog
    Glycolipid 2-alpha-mannosyltransferase
    Gene namesi
    Name:ALG11
    Synonyms:GT8
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:32456. ALG11.

    Subcellular locationi

    Endoplasmic reticulum 1 Publication. Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Congenital disorder of glycosylation 1P (CDG1P) [MIM:613661]: 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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti86 – 861L → S in CDG1P; does not affect subcellular localization; results in the accumulation of under-glycosylated proteins. 1 Publication
    VAR_064908
    Natural varianti279 – 2791Y → S in CDG1P. 1 Publication
    VAR_068070
    Natural varianti318 – 3181Q → P in CDG1P. 1 Publication
    VAR_068071
    Natural varianti381 – 3811L → S in CDG1P. 1 Publication
    VAR_068072
    Natural varianti398 – 3981E → K in CDG1P. 1 Publication
    VAR_068073

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi86 – 861L → A: Does not affect function. 1 Publication
    Mutagenesisi86 – 861L → P: Loss of function. 1 Publication

    Keywords - Diseasei

    Congenital disorder of glycosylation, Disease mutation

    Organism-specific databases

    MIMi613661. phenotype.
    Orphaneti280071. ALG11-CDG.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 492492GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferasePRO_0000295616Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi257 – 2571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi273 – 2731N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ2TAA5.
    PaxDbiQ2TAA5.
    PRIDEiQ2TAA5.

    PTM databases

    PhosphoSiteiQ2TAA5.

    Expressioni

    Gene expression databases

    BgeeiQ2TAA5.
    CleanExiHS_ALG11.
    GenevestigatoriQ2TAA5.

    Organism-specific databases

    HPAiHPA047214.

    Interactioni

    Protein-protein interaction databases

    BioGridi136328. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2TAA5.
    SMRiQ2TAA5. Positions 251-475.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei20 – 4021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei234 – 25421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5644.
    HOGENOMiHOG000209670.
    HOVERGENiHBG057178.
    InParanoidiQ2TAA5.
    KOiK03844.
    OMAiGTVILAH.
    PhylomeDBiQ2TAA5.
    TreeFamiTF313056.

    Family and domain databases

    InterProiIPR001296. Glyco_trans_1.
    [Graphical view]
    PfamiPF00534. Glycos_transf_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q2TAA5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAGERSWCL CKLLRFFYSL FFPGLIVCGT LCVCLVIVLW GIRLLLQRKK    50
    KLVSTSKNGK NQMVIAFFHP YCNAGGGGER VLWCALRALQ KKYPEAVYVV 100
    YTGDVNVNGQ QILEGAFRRF NIRLIHPVQF VFLRKRYLVE DSLYPHFTLL 150
    GQSLGSIFLG WEALMQCVPD VYIDSMGYAF TLPLFKYIGG CQVGSYVHYP 200
    TISTDMLSVV KNQNIGFNNA AFITRNPFLS KVKLIYYYLF AFIYGLVGSC 250
    SDVVMVNSSW TLNHILSLWK VGNCTNIVYP PCDVQTFLDI PLHEKKMTPG 300
    HLLVSVGQFR PEKNHPLQIR AFAKLLNKKM VESPPSLKLV LIGGCRNKDD 350
    ELRVNQLRRL SEDLGVQEYV EFKINIPFDE LKNYLSEATI GLHTMWNEHF 400
    GIGVVECMAA GTIILAHNSG GPKLDIVVPH EGDITGFLAE SEEDYAETIA 450
    HILSMSAEKR LQIRKSARAS VSRFSDQEFE VTFLSSVEKL FK 492
    Length:492
    Mass (Da):55,651
    Last modified:July 24, 2007 - v2
    Checksum:i1B3B0789030777FC
    GO

    Sequence cautioni

    The sequence AAI11023.1 differs from that shown. Reason: Frameshift at position 16.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti96 – 961A → V in AAI42999. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti86 – 861L → S in CDG1P; does not affect subcellular localization; results in the accumulation of under-glycosylated proteins. 1 Publication
    VAR_064908
    Natural varianti108 – 1081N → S.
    Corresponds to variant rs17480245 [ dbSNP | Ensembl ].
    VAR_055902
    Natural varianti279 – 2791Y → S in CDG1P. 1 Publication
    VAR_068070
    Natural varianti318 – 3181Q → P in CDG1P. 1 Publication
    VAR_068071
    Natural varianti381 – 3811L → S in CDG1P. 1 Publication
    VAR_068072
    Natural varianti398 – 3981E → K in CDG1P. 1 Publication
    VAR_068073

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK296747 mRNA. Translation: BAG59331.1.
    AL139082 Genomic DNA. Translation: CAI12890.1.
    BC073862 mRNA. Translation: AAH73862.1.
    BC010857 mRNA. Translation: AAH10857.3.
    BC111022 mRNA. Translation: AAI11023.1. Sequence problems.
    BC142998 mRNA. Translation: AAI42999.1.
    CCDSiCCDS31977.1.
    RefSeqiNP_001004127.2. NM_001004127.2.
    UniGeneiHs.512963.
    Hs.732220.

    Genome annotation databases

    EnsembliENST00000521508; ENSP00000430236; ENSG00000253710.
    GeneIDi440138.
    KEGGihsa:440138.
    UCSCiuc001vga.3. human.

    Polymorphism databases

    DMDMi156631015.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK296747 mRNA. Translation: BAG59331.1 .
    AL139082 Genomic DNA. Translation: CAI12890.1 .
    BC073862 mRNA. Translation: AAH73862.1 .
    BC010857 mRNA. Translation: AAH10857.3 .
    BC111022 mRNA. Translation: AAI11023.1 . Sequence problems.
    BC142998 mRNA. Translation: AAI42999.1 .
    CCDSi CCDS31977.1.
    RefSeqi NP_001004127.2. NM_001004127.2.
    UniGenei Hs.512963.
    Hs.732220.

    3D structure databases

    ProteinModelPortali Q2TAA5.
    SMRi Q2TAA5. Positions 251-475.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 136328. 1 interaction.

    Protein family/group databases

    CAZyi GT4. Glycosyltransferase Family 4.

    PTM databases

    PhosphoSitei Q2TAA5.

    Polymorphism databases

    DMDMi 156631015.

    Proteomic databases

    MaxQBi Q2TAA5.
    PaxDbi Q2TAA5.
    PRIDEi Q2TAA5.

    Protocols and materials databases

    DNASUi 440138.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000521508 ; ENSP00000430236 ; ENSG00000253710 .
    GeneIDi 440138.
    KEGGi hsa:440138.
    UCSCi uc001vga.3. human.

    Organism-specific databases

    CTDi 440138.
    GeneCardsi GC13P052587.
    GeneReviewsi ALG11.
    H-InvDB HIX0011337.
    HGNCi HGNC:32456. ALG11.
    HPAi HPA047214.
    MIMi 613661. phenotype.
    613666. gene.
    neXtProti NX_Q2TAA5.
    Orphaneti 280071. ALG11-CDG.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5644.
    HOGENOMi HOG000209670.
    HOVERGENi HBG057178.
    InParanoidi Q2TAA5.
    KOi K03844.
    OMAi GTVILAH.
    PhylomeDBi Q2TAA5.
    TreeFami TF313056.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi ALG11. human.
    GeneWikii ALG11.
    GenomeRNAii 440138.
    NextBioi 108982.
    PROi Q2TAA5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q2TAA5.
    CleanExi HS_ALG11.
    Genevestigatori Q2TAA5.

    Family and domain databases

    InterProi IPR001296. Glyco_trans_1.
    [Graphical view ]
    Pfami PF00534. Glycos_transf_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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].
      Tissue: Tongue.
    2. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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].
      Tissue: Lung and Skin.
    4. "A severe human metabolic disease caused by deficiency of the endoplasmatic mannosyltransferase hALG11 leads to congenital disorder of glycosylation-Ip."
      Rind N., Schmeiser V., Thiel C., Absmanner B., Lubbehusen J., Hocks J., Apeshiotis N., Wilichowski E., Lehle L., Korner C.
      Hum. Mol. Genet. 19:1413-1424(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, VARIANT CDG1P SER-86, CHARACTERIZATION OF VARIANT CDG1P SER-86, MUTAGENESIS OF LEU-86.
    5. "Improved diagnostics lead to identification of three new patients with congenital disorder of glycosylation-Ip."
      Thiel C., Rind N., Popovici D., Hoffmann G.F., Hanson K., Conway R.L., Adamski C.R., Butler E., Scanlon R., Lambert M., Apeshiotis N., Thiels C., Matthijs G., Korner C.
      Hum. Mutat. 33:485-487(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CDG1P SER-279; PRO-318; SER-381 AND LYS-398.

    Entry informationi

    Entry nameiALG11_HUMAN
    AccessioniPrimary (citable) accession number: Q2TAA5
    Secondary accession number(s): A5PLP3
    , B4DKW9, Q5TAN9, Q6DKI6, Q96FI7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 24, 2007
    Last sequence update: July 24, 2007
    Last modified: October 1, 2014
    This is version 81 of the entry and version 2 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 13
      Human chromosome 13: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3