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Q9UKM7

- MA1B1_HUMAN

UniProt

Q9UKM7 - MA1B1_HUMAN

Protein

Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase

Gene

MAN1B1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (07 Mar 2006)
      Previous versions | rss
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    Functioni

    Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man9GlcNAc2 to produce Man8GlcNAc2, but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man5-6GlcNAc2.2 Publications

    Catalytic activityi

    Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.3 Publications

    Cofactori

    Calcium.

    Enzyme regulationi

    Inhibited by both 1-deoxymannojirimycin (dMNJ) and kifunensine.1 Publication

    Kineticsi

    1. KM=0.4 mM for Man9GlcNAc21 Publication

    pH dependencei

    Optimum pH is between 6.5 and 6.9.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei330 – 3301Proton donorCurated
    Active sitei463 – 4631Curated
    Active sitei599 – 5991Curated

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
    3. oligosaccharide metabolic process Source: ProtInc
    4. post-translational protein modification Source: Reactome
    5. protein folding Source: Reactome
    6. protein N-linked glycosylation Source: UniProtKB
    7. protein N-linked glycosylation via asparagine Source: Reactome

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    BRENDAi3.2.1.113. 2681.
    ReactomeiREACT_25091. ER Quality Control Compartment (ERQC).
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGH47. Glycoside Hydrolase Family 47.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase (EC:3.2.1.113)
    Alternative name(s):
    ER alpha-1,2-mannosidase
    ER mannosidase 1
    Short name:
    ERMan1
    Man9GlcNAc2-specific-processing alpha-mannosidase
    Mannosidase alpha class 1B member 1
    Gene namesi
    Name:MAN1B1
    ORF Names:UNQ747/PRO1477
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:6823. MAN1B1.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Single-pass type II membrane protein 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. endoplasmic reticulum quality control compartment Source: Reactome
    4. integral component of membrane Source: UniProtKB
    5. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Mental retardation, autosomal recessive 15 (MRT15) [MIM:614202]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti334 – 3341R → C in MRT15; results in about 1300-fold decrease in activity. 1 Publication
    VAR_066592
    Natural varianti397 – 3971E → K in MRT15; disrupts stable protein expression. 1 Publication
    VAR_066593

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi330 – 3301E → Q: About 44-fold reduction in K(cat), slight reduction in K(m), about 100-fold increase in binding affinity for Man(9)GlcnAc(2) but no change in binding affinity for the inhibitor, dMNJ. Even further greater reduction in K(cat) and increase in K(m); when associated with Q-599. 1 Publication
    Mutagenesisi463 – 4631D → N: Some reduction in K(cat) but no change in K(m), abolishes almost all binding to Man(9)GlcnAc(2) but reduced binding to the inhibitor dMNJ by about 73-fold. Further reduction in K(m) but slight increase in K(m); when associated with Q-599. 1 Publication
    Mutagenesisi524 – 5241H → A: About 4-fold reduction in K(cat). 1 Publication
    Mutagenesisi599 – 5991E → Q: Very significant reduction in K(cat), 4-fold weaker binding affinity for Man(9)GlcnAc(2) but about 1000-fold reduction in binding affinity for the inhibitor, dMNJ. Significant reductions in K(cat) and slight increase in K(m); when associated with E-330 or N-463. 1 Publication

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi614202. phenotype.
    Orphaneti88616. Autosomal recessive nonsyndromic intellectual disability.
    PharmGKBiPA30572.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 699699Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidasePRO_0000210314Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi527 ↔ 5561 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiQ9UKM7.
    PaxDbiQ9UKM7.
    PRIDEiQ9UKM7.

    PTM databases

    PhosphoSiteiQ9UKM7.

    Expressioni

    Tissue specificityi

    Widely expressed.2 Publications

    Gene expression databases

    ArrayExpressiQ9UKM7.
    BgeeiQ9UKM7.
    CleanExiHS_MAN1B1.
    GenevestigatoriQ9UKM7.

    Organism-specific databases

    HPAiHPA051516.

    Interactioni

    Protein-protein interaction databases

    BioGridi116414. 4 interactions.
    IntActiQ9UKM7. 2 interactions.
    MINTiMINT-6610355.
    STRINGi9606.ENSP00000360645.

    Structurei

    Secondary structure

    1
    699
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi244 – 2463
    Helixi248 – 26720
    Beta strandi271 – 2755
    Turni276 – 2794
    Beta strandi280 – 2823
    Beta strandi284 – 2874
    Helixi289 – 30012
    Helixi304 – 31714
    Beta strandi325 – 3273
    Helixi328 – 34619
    Helixi349 – 36214
    Helixi363 – 3664
    Beta strandi368 – 3703
    Beta strandi375 – 3784
    Turni379 – 3813
    Beta strandi391 – 3944
    Helixi395 – 3995
    Helixi402 – 41211
    Helixi416 – 42914
    Beta strandi441 – 4444
    Turni445 – 4473
    Beta strandi450 – 4523
    Turni460 – 4623
    Helixi463 – 47513
    Helixi481 – 49717
    Beta strandi499 – 5013
    Turni503 – 5053
    Beta strandi508 – 5103
    Beta strandi512 – 5143
    Beta strandi517 – 5193
    Beta strandi521 – 5233
    Helixi524 – 5274
    Helixi528 – 53811
    Helixi543 – 56119
    Beta strandi563 – 5664
    Beta strandi570 – 5734
    Beta strandi584 – 5863
    Helixi589 – 5913
    Helixi599 – 61113
    Helixi615 – 63016
    Helixi659 – 6624
    Helixi664 – 6729
    Turni676 – 6794
    Turni681 – 6833
    Beta strandi684 – 6863
    Beta strandi692 – 6943

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FMIX-ray1.90A243-697[»]
    1FO2X-ray2.38A243-699[»]
    1FO3X-ray1.75A243-699[»]
    1X9DX-ray1.41A172-699[»]
    ProteinModelPortaliQ9UKM7.
    SMRiQ9UKM7. Positions 243-697.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UKM7.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 8484CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini106 – 699594LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei85 – 10521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi39 – 457Poly-Pro

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 47 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG300315.
    HOGENOMiHOG000181987.
    HOVERGENiHBG052389.
    KOiK01230.
    OMAiVHFNLHA.
    OrthoDBiEOG7ZGX2S.
    PhylomeDBiQ9UKM7.
    TreeFamiTF354274.

    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.

    Q9UKM7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAACEGRRSG ALGSSQSDFL TPPVGGAPWA VATTVVMYPP PPPPPHRDFI    50
    SVTLSFGENY DNSKSWRRRS CWRKWKQLSR LQRNMILFLL AFLLFCGLLF 100
    YINLADHWKA LAFRLEEEQK MRPEIAGLKP ANPPVLPAPQ KADTDPENLP 150
    EISSQKTQRH IQRGPPHLQI RPPSQDLKDG TQEEATKRQE APVDPRPEGD 200
    PQRTVISWRG AVIEPEQGTE LPSRRAEVPT KPPLPPARTQ GTPVHLNYRQ 250
    KGVIDVFLHA WKGYRKFAWG HDELKPVSRS FSEWFGLGLT LIDALDTMWI 300
    LGLRKEFEEA RKWVSKKLHF EKDVDVNLFE STIRILGGLL SAYHLSGDSL 350
    FLRKAEDFGN RLMPAFRTPS KIPYSDVNIG TGVAHPPRWT SDSTVAEVTS 400
    IQLEFRELSR LTGDKKFQEA VEKVTQHIHG LSGKKDGLVP MFINTHSGLF 450
    THLGVFTLGA RADSYYEYLL KQWIQGGKQE TQLLEDYVEA IEGVRTHLLR 500
    HSEPSKLTFV GELAHGRFSA KMDHLVCFLP GTLALGVYHG LPASHMELAQ 550
    ELMETCYQMN RQMETGLSPE IVHFNLYPQP GRRDVEVKPA DRHNLLRPET 600
    VESLFYLYRV TGDRKYQDWG WEILQSFSRF TRVPSGGYSS INNVQDPQKP 650
    EPRDKMESFF LGETLKYLFL LFSDDPNLLS LDAYVFNTEA HPLPIWTPA 699
    Length:699
    Mass (Da):79,580
    Last modified:March 7, 2006 - v2
    Checksum:iB8BF3BE333D90261
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti204 – 2041T → A in AAD45504. (PubMed:10409699)Curated
    Sequence conflicti223 – 2231S → P in AAD45504. (PubMed:10409699)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti59 – 591N → S.4 Publications
    Corresponds to variant rs968733 [ dbSNP | Ensembl ].
    VAR_055841
    Natural varianti334 – 3341R → C in MRT15; results in about 1300-fold decrease in activity. 1 Publication
    VAR_066592
    Natural varianti397 – 3971E → K in MRT15; disrupts stable protein expression. 1 Publication
    VAR_066593

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF148509 mRNA. Translation: AAF03215.1.
    AF145732 mRNA. Translation: AAD45504.1.
    AY358465 mRNA. Translation: AAQ88830.1.
    AL929554, AL807752 Genomic DNA. Translation: CAH72887.1.
    AL807752, AL929554 Genomic DNA. Translation: CAI12781.1.
    BC002953 mRNA. Translation: AAH02953.1.
    BC006079 mRNA. Translation: AAH06079.1.
    CCDSiCCDS7029.1.
    RefSeqiNP_057303.2. NM_016219.4.
    UniGeneiHs.279881.

    Genome annotation databases

    EnsembliENST00000371589; ENSP00000360645; ENSG00000177239.
    GeneIDi11253.
    KEGGihsa:11253.
    UCSCiuc004cld.3. human.

    Polymorphism databases

    DMDMi93195043.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF148509 mRNA. Translation: AAF03215.1 .
    AF145732 mRNA. Translation: AAD45504.1 .
    AY358465 mRNA. Translation: AAQ88830.1 .
    AL929554 , AL807752 Genomic DNA. Translation: CAH72887.1 .
    AL807752 , AL929554 Genomic DNA. Translation: CAI12781.1 .
    BC002953 mRNA. Translation: AAH02953.1 .
    BC006079 mRNA. Translation: AAH06079.1 .
    CCDSi CCDS7029.1.
    RefSeqi NP_057303.2. NM_016219.4.
    UniGenei Hs.279881.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FMI X-ray 1.90 A 243-697 [» ]
    1FO2 X-ray 2.38 A 243-699 [» ]
    1FO3 X-ray 1.75 A 243-699 [» ]
    1X9D X-ray 1.41 A 172-699 [» ]
    ProteinModelPortali Q9UKM7.
    SMRi Q9UKM7. Positions 243-697.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116414. 4 interactions.
    IntActi Q9UKM7. 2 interactions.
    MINTi MINT-6610355.
    STRINGi 9606.ENSP00000360645.

    Chemistry

    BindingDBi Q9UKM7.
    ChEMBLi CHEMBL2308.

    Protein family/group databases

    CAZyi GH47. Glycoside Hydrolase Family 47.

    PTM databases

    PhosphoSitei Q9UKM7.

    Polymorphism databases

    DMDMi 93195043.

    Proteomic databases

    MaxQBi Q9UKM7.
    PaxDbi Q9UKM7.
    PRIDEi Q9UKM7.

    Protocols and materials databases

    DNASUi 11253.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371589 ; ENSP00000360645 ; ENSG00000177239 .
    GeneIDi 11253.
    KEGGi hsa:11253.
    UCSCi uc004cld.3. human.

    Organism-specific databases

    CTDi 11253.
    GeneCardsi GC09P139981.
    H-InvDB HIX0035043.
    HGNCi HGNC:6823. MAN1B1.
    HPAi HPA051516.
    MIMi 604346. gene.
    614202. phenotype.
    neXtProti NX_Q9UKM7.
    Orphaneti 88616. Autosomal recessive nonsyndromic intellectual disability.
    PharmGKBi PA30572.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG300315.
    HOGENOMi HOG000181987.
    HOVERGENi HBG052389.
    KOi K01230.
    OMAi VHFNLHA.
    OrthoDBi EOG7ZGX2S.
    PhylomeDBi Q9UKM7.
    TreeFami TF354274.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BRENDAi 3.2.1.113. 2681.
    Reactomei REACT_25091. ER Quality Control Compartment (ERQC).

    Miscellaneous databases

    EvolutionaryTracei Q9UKM7.
    GeneWikii MAN1B1.
    GenomeRNAii 11253.
    NextBioi 42822.
    PROi Q9UKM7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UKM7.
    Bgeei Q9UKM7.
    CleanExi HS_MAN1B1.
    Genevestigatori Q9UKM7.

    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. "Cloning and expression of a specific human alpha1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis."
      Tremblay L.O., Herscovics A.
      Glycobiology 9:1073-1078(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, VARIANT SER-59.
      Tissue: Fetal brain, Liver, Placenta and Testis.
    2. "Identification, expression, and characterization of a cDNA encoding human endoplasmic reticulum mannosidase I, the enzyme that catalyzes the first mannose trimming step in mammalian Asn-linked oligosaccharide biosynthesis."
      Gonzalez D.S., Karaveg K., Vandersall-Nairn A.S., Lal A., Moremen K.W.
      J. Biol. Chem. 274:21375-21386(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-699, TISSUE SPECIFICITY, ENZYME ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION, VARIANT SER-59.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-59.
    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], VARIANT SER-59.
      Tissue: Lung and Placenta.
    6. "The specificity of the yeast and human class I ER alpha 1,2-mannosidases involved in ER quality control is not as strict previously reported."
      Herscovics A., Romero P.A., Tremblay L.O.
      Glycobiology 12:14G-15G(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
    7. "Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation."
      Avezov E., Frenkel Z., Ehrlich M., Herscovics A., Lederkremer G.Z.
      Mol. Biol. Cell 19:216-225(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Structural basis for catalysis and inhibition of N-glycan processing class I alpha 1,2-mannosidases."
      Vallee F., Karaveg K., Herscovics A., Moremen K.W., Howell P.L.
      J. Biol. Chem. 275:41287-41298(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 243-699, DISULFIDE BOND.
    9. "Mechanism of class 1 (glycosylhydrolase family 47) {alpha}-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control."
      Karaveg K., Siriwardena A., Tempel W., Liu Z.J., Glushka J., Wang B.C., Moremen K.W.
      J. Biol. Chem. 280:16197-16207(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) OF 172-699 IN COMPLEX WITH A THIO-DISACCHARIDE SUBSTRATE ANALOG, ENZYME ACTIVITY, MUTAGENESIS OF GLU-330; ASP-463; HIS-524 AND GLU-599.
    10. Cited for: VARIANTS MRT15 CYS-334 AND LYS-397, CHARACTERIZATION OF VARIANTS MRT15 CYS-334 AND LYS-397.

    Entry informationi

    Entry nameiMA1B1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKM7
    Secondary accession number(s): Q5VSG3, Q9BRS9, Q9Y5K7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 142 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

    Caution

    It is uncertain whether Met-1 or Met-37 is the initiator.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

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