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Q96F25

- ALG14_HUMAN

UniProt

Q96F25 - ALG14_HUMAN

Protein

UDP-N-acetylglucosamine transferase subunit ALG14 homolog

Gene

ALG14

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    May be involved in protein N-glycosylation. May play a role in the second step of the dolichol-linked oligosaccharide pathway. May anchor the catalytic subunit ALG13 to the ER.1 Publication

    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

    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

    CAZyiGT1. Glycosyltransferase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-N-acetylglucosamine transferase subunit ALG14 homolog
    Gene namesi
    Name:ALG14
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:28287. ALG14.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti353327. Congenital myasthenic syndromes with glycosylation defect.
    PharmGKBiPA142672628.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 216216UDP-N-acetylglucosamine transferase subunit ALG14 homologPRO_0000265116Add
    BLAST

    Proteomic databases

    MaxQBiQ96F25.
    PaxDbiQ96F25.
    PRIDEiQ96F25.

    PTM databases

    PhosphoSiteiQ96F25.

    Expressioni

    Gene expression databases

    BgeeiQ96F25.
    CleanExiHS_ALG14.
    GenevestigatoriQ96F25.

    Organism-specific databases

    HPAiHPA031829.

    Interactioni

    Subunit structurei

    Heterodimer with ALG13 isoform 2 to form a functional enzyme.By similarity

    Protein-protein interaction databases

    BioGridi128278. 1 interaction.
    STRINGi9606.ENSP00000359224.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96F25.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 33LumenalSequence Analysis
    Topological domaini25 – 216192CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei4 – 2421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ALG14 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0707.
    HOGENOMiHOG000182099.
    HOVERGENiHBG059605.
    InParanoidiQ96F25.
    KOiK07441.
    OMAiCIPLCAS.
    OrthoDBiEOG7SN8DK.
    PhylomeDBiQ96F25.
    TreeFamiTF105628.

    Family and domain databases

    InterProiIPR013969. Oligosacch_biosynth_Alg14.
    [Graphical view]
    PANTHERiPTHR12154. PTHR12154. 1 hit.
    PfamiPF08660. Alg14. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q96F25-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVCVLVLAAA AGAVAVFLIL RIWVVLRSMD VTPRESLSIL VVAGSGGHTT    50
    EILRLLGSLS NAYSPRHYVI ADTDEMSANK INSFELDRAD RDPSNMYTKY 100
    YIHRIPRSRE VQQSWPSTVF TTLHSMWLSF PLIHRVKPDL VLCNGPGTCV 150
    PICVSALLLG ILGIKKVIIV YVESICRVET LSMSGKILFH LSDYFIVQWP 200
    ALKEKYPKSV YLGRIV 216
    Length:216
    Mass (Da):24,151
    Last modified:December 1, 2001 - v1
    Checksum:i0724FEAE33A841E8
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti14 – 141V → M.
    Corresponds to variant rs11165298 [ dbSNP | Ensembl ].
    VAR_029635

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK289395 mRNA. Translation: BAF82084.1.
    CH471097 Genomic DNA. Translation: EAW73027.1.
    BC011706 mRNA. Translation: AAH11706.1.
    CCDSiCCDS752.1.
    RefSeqiNP_659425.1. NM_144988.3.
    UniGeneiHs.408927.

    Genome annotation databases

    EnsembliENST00000370205; ENSP00000359224; ENSG00000172339.
    GeneIDi199857.
    KEGGihsa:199857.
    UCSCiuc001dra.2. human.

    Polymorphism databases

    DMDMi74731649.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK289395 mRNA. Translation: BAF82084.1 .
    CH471097 Genomic DNA. Translation: EAW73027.1 .
    BC011706 mRNA. Translation: AAH11706.1 .
    CCDSi CCDS752.1.
    RefSeqi NP_659425.1. NM_144988.3.
    UniGenei Hs.408927.

    3D structure databases

    ProteinModelPortali Q96F25.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 128278. 1 interaction.
    STRINGi 9606.ENSP00000359224.

    Protein family/group databases

    CAZyi GT1. Glycosyltransferase Family 1.

    PTM databases

    PhosphoSitei Q96F25.

    Polymorphism databases

    DMDMi 74731649.

    Proteomic databases

    MaxQBi Q96F25.
    PaxDbi Q96F25.
    PRIDEi Q96F25.

    Protocols and materials databases

    DNASUi 199857.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370205 ; ENSP00000359224 ; ENSG00000172339 .
    GeneIDi 199857.
    KEGGi hsa:199857.
    UCSCi uc001dra.2. human.

    Organism-specific databases

    CTDi 199857.
    GeneCardsi GC01M095449.
    HGNCi HGNC:28287. ALG14.
    HPAi HPA031829.
    MIMi 612866. gene.
    neXtProti NX_Q96F25.
    Orphaneti 353327. Congenital myasthenic syndromes with glycosylation defect.
    PharmGKBi PA142672628.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0707.
    HOGENOMi HOG000182099.
    HOVERGENi HBG059605.
    InParanoidi Q96F25.
    KOi K07441.
    OMAi CIPLCAS.
    OrthoDBi EOG7SN8DK.
    PhylomeDBi Q96F25.
    TreeFami TF105628.

    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 ALG14. human.
    GeneWikii ALG14.
    GenomeRNAii 199857.
    NextBioi 89753.
    PROi Q96F25.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q96F25.
    CleanExi HS_ALG14.
    Genevestigatori Q96F25.

    Family and domain databases

    InterProi IPR013969. Oligosacch_biosynth_Alg14.
    [Graphical view ]
    PANTHERi PTHR12154. PTHR12154. 1 hit.
    Pfami PF08660. Alg14. 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].
    2. 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: Pancreas.
    4. "Alg14 recruits Alg13 to the cytoplasmic face of the endoplasmic reticulum to form a novel bipartite UDP-N-acetylglucosamine transferase required for the second step of N-linked glycosylation."
      Gao X.-D., Tachikawa H., Sato T., Jigami Y., Dean N.
      J. Biol. Chem. 280:36254-36262(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiALG14_HUMAN
    AccessioniPrimary (citable) accession number: Q96F25
    Secondary accession number(s): A8K030
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 96 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 1
      Human chromosome 1: 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