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O60476

- MA1A2_HUMAN

UniProt

O60476 - MA1A2_HUMAN

Protein

Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB

Gene

MAN1A2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man9GlcNAc2 to produce Man5GlcNAc2.

    Catalytic activityi

    Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.

    Cofactori

    Calcium.

    Enzyme regulationi

    Inhibited by both 1-deoxymannojirimycin and kifunensine.

    Pathwayi

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Source: ProtInc

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. lung alveolus development Source: Ensembl
    3. N-glycan processing Source: ProtInc
    4. post-translational protein modification Source: Reactome
    5. protein N-linked glycosylation via asparagine Source: Reactome
    6. respiratory gaseous exchange Source: Ensembl

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_25396. Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGH47. Glycoside Hydrolase Family 47.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB (EC:3.2.1.113)
    Alternative name(s):
    Mannosidase alpha class 1A member 2
    Processing alpha-1,2-mannosidase IB
    Short name:
    Alpha-1,2-mannosidase IB
    Gene namesi
    Name:MAN1A2
    Synonyms:MAN1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6822. MAN1A2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. Golgi apparatus Source: HPA
    3. Golgi membrane Source: Reactome
    4. integral component of membrane Source: ProtInc
    5. membrane Source: UniProtKB
    6. nucleolus Source: HPA

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30571.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 641640Mannosyl-oligosaccharide 1,2-alpha-mannosidase IBPRO_0000210312Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine1 Publication
    Glycosylationi631 – 6311N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Acetylation, Glycoprotein

    Proteomic databases

    MaxQBiO60476.
    PaxDbiO60476.
    PRIDEiO60476.

    PTM databases

    PhosphoSiteiO60476.

    Expressioni

    Tissue specificityi

    Highest levels of expression in placenta and testis.

    Gene expression databases

    ArrayExpressiO60476.
    BgeeiO60476.
    CleanExiHS_MAN1A2.
    GenevestigatoriO60476.

    Organism-specific databases

    HPAiHPA034559.

    Interactioni

    Protein-protein interaction databases

    BioGridi116111. 2 interactions.
    IntActiO60476. 4 interactions.
    MINTiMINT-1184386.
    STRINGi9606.ENSP00000348959.

    Structurei

    3D structure databases

    ProteinModelPortaliO60476.
    SMRiO60476. Positions 156-627.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 3635CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini58 – 641584LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei37 – 5721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 47 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG300315.
    HOGENOMiHOG000181988.
    HOVERGENiHBG052389.
    InParanoidiO60476.
    KOiK01230.
    OMAiDPEDNDI.
    OrthoDBiEOG7X0VH1.
    PhylomeDBiO60476.
    TreeFamiTF313420.

    Family and domain databases

    Gene3Di1.50.10.50. 1 hit.
    InterProiIPR001382. Glyco_hydro_47.
    [Graphical view]
    PANTHERiPTHR11742. PTHR11742. 1 hit.
    PfamiPF01532. Glyco_hydro_47. 1 hit.
    [Graphical view]
    PRINTSiPR00747. GLYHDRLASE47.
    SUPFAMiSSF48225. SSF48225. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O60476-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTPALLPLS GRRIPPLNLG PPSFPHHRAT LRLSEKFILL LILSAFITLC    50
    FGAFFFLPDS SKHKRFDLGL EDVLIPHVDA GKGAKNPGVF LIHGPDEHRH 100
    REEEERLRNK IRADHEKALE EAKEKLRKSR EEIRAEIQTE KNKVVQEMKI 150
    KENKPLPPVP IPNLVGIRGG DPEDNDIREK REKIKEMMKH AWDNYRTYGW 200
    GHNELRPIAR KGHSPNIFGS SQMGATIVDA LDTLYIMGLH DEFLDGQRWI 250
    EDNLDFSVNS EVSVFEVNIR FIGGLLAAYY LSGEEIFKIK AVQLAEKLLP 300
    AFNTPTGIPW AMVNLKSGVG RNWGWASAGS SILAEFGTLH MEFIHLSYLT 350
    GDLTYYKKVM HIRKLLQKMD RPNGLYPNYL NPRTGRWGQY HTSVGGLGDS 400
    FYEYLLKAWL MSDKTDHEAR KMYDDAIEAI EKHLIKKSRG GLTFIGEWKN 450
    GHLEKKMGHL ACFAGGMFAL GADGSRADKA GHYLELGAEI ARTCHESYDR 500
    TALKLGPESF KFDGAVEAVA VRQAEKYYIL RPEVIETYWY LWRFTHDPRY 550
    RQWGWEAALA IEKYCRVNGG FSGVKDVYSS TPTHDDVQQS FFLAETLKYL 600
    YLLFSGDDLL PLDHWVFNTE AHPLPVLHLA NTTLSGNPAV R 641
    Length:641
    Mass (Da):73,004
    Last modified:August 1, 1998 - v1
    Checksum:i19DA691A9C4B0ED3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF053626
    , AF053622, AF053623, AF053624, AF053625 Genomic DNA. Translation: AAC26201.1.
    AF027156 mRNA. Translation: AAC26169.1.
    AF053621
    , AF053619, AF053620, AF053615, AF053616, AF053617, AF053618 Genomic DNA. Translation: AAC26200.1.
    AL157902, AL358072 Genomic DNA. Translation: CAI22315.1.
    AL358072, AL157902 Genomic DNA. Translation: CAH71079.1.
    BC063300 mRNA. Translation: AAH63300.1.
    CCDSiCCDS895.1.
    RefSeqiNP_006690.1. NM_006699.3.
    UniGeneiHs.435938.
    Hs.602811.

    Genome annotation databases

    EnsembliENST00000356554; ENSP00000348959; ENSG00000198162.
    GeneIDi10905.
    KEGGihsa:10905.
    UCSCiuc001ehd.1. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF053626
    , AF053622 , AF053623 , AF053624 , AF053625 Genomic DNA. Translation: AAC26201.1 .
    AF027156 mRNA. Translation: AAC26169.1 .
    AF053621
    , AF053619 , AF053620 , AF053615 , AF053616 , AF053617 , AF053618 Genomic DNA. Translation: AAC26200.1 .
    AL157902 , AL358072 Genomic DNA. Translation: CAI22315.1 .
    AL358072 , AL157902 Genomic DNA. Translation: CAH71079.1 .
    BC063300 mRNA. Translation: AAH63300.1 .
    CCDSi CCDS895.1.
    RefSeqi NP_006690.1. NM_006699.3.
    UniGenei Hs.435938.
    Hs.602811.

    3D structure databases

    ProteinModelPortali O60476.
    SMRi O60476. Positions 156-627.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116111. 2 interactions.
    IntActi O60476. 4 interactions.
    MINTi MINT-1184386.
    STRINGi 9606.ENSP00000348959.

    Protein family/group databases

    CAZyi GH47. Glycoside Hydrolase Family 47.

    PTM databases

    PhosphoSitei O60476.

    Proteomic databases

    MaxQBi O60476.
    PaxDbi O60476.
    PRIDEi O60476.

    Protocols and materials databases

    DNASUi 10905.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356554 ; ENSP00000348959 ; ENSG00000198162 .
    GeneIDi 10905.
    KEGGi hsa:10905.
    UCSCi uc001ehd.1. human.

    Organism-specific databases

    CTDi 10905.
    GeneCardsi GC01P117910.
    HGNCi HGNC:6822. MAN1A2.
    HPAi HPA034559.
    MIMi 604345. gene.
    neXtProti NX_O60476.
    PharmGKBi PA30571.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG300315.
    HOGENOMi HOG000181988.
    HOVERGENi HBG052389.
    InParanoidi O60476.
    KOi K01230.
    OMAi DPEDNDI.
    OrthoDBi EOG7X0VH1.
    PhylomeDBi O60476.
    TreeFami TF313420.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_25396. Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2.

    Miscellaneous databases

    ChiTaRSi MAN1A2. human.
    GeneWikii MAN1A2.
    GenomeRNAii 10905.
    NextBioi 41419.
    PROi O60476.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60476.
    Bgeei O60476.
    CleanExi HS_MAN1A2.
    Genevestigatori O60476.

    Family and domain databases

    Gene3Di 1.50.10.50. 1 hit.
    InterProi IPR001382. Glyco_hydro_47.
    [Graphical view ]
    PANTHERi PTHR11742. PTHR11742. 1 hit.
    Pfami PF01532. Glyco_hydro_47. 1 hit.
    [Graphical view ]
    PRINTSi PR00747. GLYHDRLASE47.
    SUPFAMi SSF48225. SSF48225. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning, chromosomal mapping and tissue-specific expression of a novel human alpha-1,2-mannosidase gene involved in N-glycan maturation."
      Tremblay L.O., Campbell-Dyke N., Herscovics A.
      Glycobiology 8:585-595(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Brain and Placenta.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [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: Brain.
    4. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMA1A2_HUMAN
    AccessioniPrimary (citable) accession number: O60476
    Secondary accession number(s): Q9H510
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 127 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. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3