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Q13724

- MOGS_HUMAN

UniProt

Q13724 - MOGS_HUMAN

Protein

Mannosyl-oligosaccharide glucosidase

Gene

MOGS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 5 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Cleaves the distal alpha 1,2-linked glucose residue from the Glc3Man9GlcNAc2 oligosaccharide precursor in a highly specific manner.

    Catalytic activityi

    Exohydrolysis of the non-reducing terminal glucose residues in the mannosyl-oligosaccharide Glc3Man9GlcNAc2.

    Pathwayi

    GO - Molecular functioni

    1. glucosidase activity Source: ProtInc
    2. mannosyl-oligosaccharide glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. oligosaccharide metabolic process Source: InterPro
    3. post-translational protein modification Source: Reactome
    4. protein folding Source: Reactome
    5. protein N-linked glycosylation Source: ProtInc
    6. protein N-linked glycosylation via asparagine Source: Reactome

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    ReactomeiREACT_23878. N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
    UniPathwayiUPA00280.

    Protein family/group databases

    CAZyiGH63. Glycoside Hydrolase Family 63.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mannosyl-oligosaccharide glucosidase (EC:3.2.1.106)
    Alternative name(s):
    Processing A-glucosidase I
    Gene namesi
    Name:MOGS
    Synonyms:GCS1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:24862. MOGS.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: ProtInc
    2. endoplasmic reticulum membrane Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. integral component of membrane Source: UniProtKB-KW
    5. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Type IIb congenital disorder of glycosylation (CDGIIb) [MIM:606056]: Characterized by marked generalized hypotonia and hypomotility of the neonate, dysmorphic features, including a prominent occiput, short palpebral fissures, retrognathia, high arched palate, generalized edema, and hypoplastic genitalia. Symptoms of the infant included hepatomegaly, hypoventilation, feeding problems and seizures. The clinical course was progressive and the infant did not survive more than a few months.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti486 – 4861R → T in CDGIIb; loss of activity. 1 Publication
    VAR_018966
    Natural varianti652 – 6521F → L in CDGIIb; loss of activity. 1 Publication
    VAR_018967

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi606056. phenotype.
    Orphaneti79330. GCS1-CDG.
    PharmGKBiPA164723075.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 837837Mannosyl-oligosaccharide glucosidasePRO_0000057710Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi657 – 6571N-linked (GlcNAc...)

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ13724.
    PaxDbiQ13724.
    PeptideAtlasiQ13724.
    PRIDEiQ13724.

    PTM databases

    PhosphoSiteiQ13724.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13724.
    BgeeiQ13724.
    GenevestigatoriQ13724.

    Organism-specific databases

    HPAiHPA011969.

    Interactioni

    Protein-protein interaction databases

    BioGridi113599. 16 interactions.
    IntActiQ13724. 7 interactions.
    MINTiMINT-1414631.
    STRINGi9606.ENSP00000233616.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13724.
    SMRiQ13724. Positions 94-830.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3838CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini60 – 837778LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei39 – 5921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni76 – 13762Required for endoplasmic reticulum targetingBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi3 – 97Endoplasmic reticulum targeting

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 63 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG305138.
    HOGENOMiHOG000201473.
    InParanoidiQ13724.
    KOiK01228.
    OMAiWKAPLYT.
    OrthoDBiEOG7XSTD6.
    PhylomeDBiQ13724.
    TreeFamiTF300749.

    Family and domain databases

    InterProiIPR008928. 6-hairpin_glycosidase-like.
    IPR004888. Glycoside_hydrolase_63.
    [Graphical view]
    PANTHERiPTHR10412:SF1. PTHR10412:SF1. 1 hit.
    PfamiPF03200. Glyco_hydro_63. 1 hit.
    [Graphical view]
    SUPFAMiSSF48208. SSF48208. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13724-1) [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

    MARGERRRRA VPAEGVRTAE RAARGGPGRR DGRGGGPRST AGGVALAVVV    50
    LSLALGMSGR WVLAWYRARR AVTLHSAPPV LPADSSSPAV APDLFWGTYR 100
    PHVYFGMKTR SPKPLLTGLM WAQQGTTPGT PKLRHTCEQG DGVGPYGWEF 150
    HDGLSFGRQH IQDGALRLTT EFVKRPGGQH GGDWSWRVTV EPQDSGTSAL 200
    PLVSLFFYVV TDGKEVLLPE VGAKGQLKFI SGHTSELGDF RFTLLPPTSP 250
    GDTAPKYGSY NVFWTSNPGL PLLTEMVKSR LNSWFQHRPP GAPPERYLGL 300
    PGSLKWEDRG PSGQGQGQFL IQQVTLKIPI SIEFVFESGS AQAGGNQALP 350
    RLAGSLLTQA LESHAEGFRE RFEKTFQLKE KGLSSGEQVL GQAALSGLLG 400
    GIGYFYGQGL VLPDIGVEGS EQKVDPALFP PVPLFTAVPS RSFFPRGFLW 450
    DEGFHQLVVQ RWDPSLTREA LGHWLGLLNA DGWIGREQIL GDEARARVPP 500
    EFLVQRAVHA NPPTLLLPVA HMLEVGDPDD LAFLRKALPR LHAWFSWLHQ 550
    SQAGPLPLSY RWRGRDPALP TLLNPKTLPS GLDDYPRASH PSVTERHLDL 600
    RCWVALGARV LTRLAEHLGE AEVAAELGPL AASLEAAESL DELHWAPELG 650
    VFADFGNHTK AVQLKPRPPQ GLVRVVGRPQ PQLQYVDALG YVSLFPLLLR 700
    LLDPTSSRLG PLLDILADSR HLWSPFGLRS LAASSSFYGQ RNSEHDPPYW 750
    RGAVWLNVNY LALGALHHYG HLEGPHQARA AKLHGELRAN VVGNVWRQYQ 800
    ATGFLWEQYS DRDGRGMGCR PFHGWTSLVL LAMAEDY 837
    Length:837
    Mass (Da):91,918
    Last modified:October 17, 2006 - v5
    Checksum:i11C5B09301B50DEE
    GO
    Isoform 2 (identifier: Q13724-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-106: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:731
    Mass (Da):80,703
    Checksum:iB9B38429664731E6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti330 – 3301I → F in CAA60683. (PubMed:7635146)Curated
    Sequence conflicti389 – 3891V → A in CAA60683. (PubMed:7635146)Curated
    Sequence conflicti605 – 6051A → G in CAA60683. (PubMed:7635146)Curated
    Sequence conflicti818 – 8181Missing in CAA60683. (PubMed:7635146)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti222 – 2221G → R.
    Corresponds to variant rs3213671 [ dbSNP | Ensembl ].
    VAR_049233
    Natural varianti236 – 2361E → Q.1 Publication
    Corresponds to variant rs1063587 [ dbSNP | Ensembl ].
    VAR_019361
    Natural varianti239 – 2391D → N.1 Publication
    Corresponds to variant rs1063588 [ dbSNP | Ensembl ].
    VAR_019362
    Natural varianti293 – 2931P → S.1 Publication
    Corresponds to variant rs2268416 [ dbSNP | Ensembl ].
    VAR_049234
    Natural varianti486 – 4861R → T in CDGIIb; loss of activity. 1 Publication
    VAR_018966
    Natural varianti495 – 4951R → P.
    Corresponds to variant rs34075781 [ dbSNP | Ensembl ].
    VAR_049235
    Natural varianti652 – 6521F → L in CDGIIb; loss of activity. 1 Publication
    VAR_018967
    Natural varianti785 – 7851G → S.
    Corresponds to variant rs35533773 [ dbSNP | Ensembl ].
    VAR_049236

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 106106Missing in isoform 2. CuratedVSP_046921Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X87237 mRNA. Translation: CAA60683.1.
    AJ422288 Genomic DNA. Translation: CAD19636.1.
    AK292553 mRNA. Translation: BAF85242.1.
    AC005041 Genomic DNA. No translation available.
    CH471053 Genomic DNA. Translation: EAW99653.1.
    BC117252 mRNA. Translation: AAI17253.1.
    BC117250 mRNA. Translation: AAI17251.1.
    CCDSiCCDS42700.1. [Q13724-1]
    CCDS54370.1. [Q13724-2]
    PIRiS66258.
    RefSeqiNP_001139630.1. NM_001146158.1. [Q13724-2]
    NP_006293.2. NM_006302.2. [Q13724-1]
    UniGeneiHs.516119.

    Genome annotation databases

    EnsembliENST00000233616; ENSP00000233616; ENSG00000115275. [Q13724-1]
    ENST00000452063; ENSP00000388201; ENSG00000115275. [Q13724-2]
    GeneIDi7841.
    KEGGihsa:7841.
    UCSCiuc010ffh.3. human. [Q13724-1]

    Polymorphism databases

    DMDMi116242490.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X87237 mRNA. Translation: CAA60683.1 .
    AJ422288 Genomic DNA. Translation: CAD19636.1 .
    AK292553 mRNA. Translation: BAF85242.1 .
    AC005041 Genomic DNA. No translation available.
    CH471053 Genomic DNA. Translation: EAW99653.1 .
    BC117252 mRNA. Translation: AAI17253.1 .
    BC117250 mRNA. Translation: AAI17251.1 .
    CCDSi CCDS42700.1. [Q13724-1 ]
    CCDS54370.1. [Q13724-2 ]
    PIRi S66258.
    RefSeqi NP_001139630.1. NM_001146158.1. [Q13724-2 ]
    NP_006293.2. NM_006302.2. [Q13724-1 ]
    UniGenei Hs.516119.

    3D structure databases

    ProteinModelPortali Q13724.
    SMRi Q13724. Positions 94-830.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113599. 16 interactions.
    IntActi Q13724. 7 interactions.
    MINTi MINT-1414631.
    STRINGi 9606.ENSP00000233616.

    Chemistry

    ChEMBLi CHEMBL4684.

    Protein family/group databases

    CAZyi GH63. Glycoside Hydrolase Family 63.

    PTM databases

    PhosphoSitei Q13724.

    Polymorphism databases

    DMDMi 116242490.

    Proteomic databases

    MaxQBi Q13724.
    PaxDbi Q13724.
    PeptideAtlasi Q13724.
    PRIDEi Q13724.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000233616 ; ENSP00000233616 ; ENSG00000115275 . [Q13724-1 ]
    ENST00000452063 ; ENSP00000388201 ; ENSG00000115275 . [Q13724-2 ]
    GeneIDi 7841.
    KEGGi hsa:7841.
    UCSCi uc010ffh.3. human. [Q13724-1 ]

    Organism-specific databases

    CTDi 7841.
    GeneCardsi GC02M074688.
    GeneReviewsi MOGS.
    H-InvDB HIX0002184.
    HGNCi HGNC:24862. MOGS.
    HPAi HPA011969.
    MIMi 601336. gene.
    606056. phenotype.
    neXtProti NX_Q13724.
    Orphaneti 79330. GCS1-CDG.
    PharmGKBi PA164723075.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG305138.
    HOGENOMi HOG000201473.
    InParanoidi Q13724.
    KOi K01228.
    OMAi WKAPLYT.
    OrthoDBi EOG7XSTD6.
    PhylomeDBi Q13724.
    TreeFami TF300749.

    Enzyme and pathway databases

    UniPathwayi UPA00280 .
    Reactomei REACT_23878. N-glycan trimming in the ER and Calnexin/Calreticulin cycle.

    Miscellaneous databases

    ChiTaRSi MOGS. human.
    GeneWikii GCS1.
    GenomeRNAii 7841.
    NextBioi 30249.
    PROi Q13724.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13724.
    Bgeei Q13724.
    Genevestigatori Q13724.

    Family and domain databases

    InterProi IPR008928. 6-hairpin_glycosidase-like.
    IPR004888. Glycoside_hydrolase_63.
    [Graphical view ]
    PANTHERi PTHR10412:SF1. PTHR10412:SF1. 1 hit.
    Pfami PF03200. Glyco_hydro_63. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48208. SSF48208. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of glucosidase I from human hippocampus."
      Kalz-Fueller B., Bieberich E., Bause E.
      Eur. J. Biochem. 231:344-351(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLN-236; ASN-239 AND SER-293.
      Tissue: Hippocampus.
    2. Erratum
      Kalz-Fueller B., Bieberich E., Bause E.
      Eur. J. Biochem. 249:912-912(1997)
    3. Voelker C.
      Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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: Testis.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Brain.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: VARIANTS CDGIIB THR-486 AND LEU-652.
    10. "Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb)."
      Voelker C., De Praeter C.M., Hardt B., Breuer W., Kalz-Fueller B., Van Coster R.N., Bause E.
      Glycobiology 12:473-483(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS CDGIIB THR-486 AND LEU-652.

    Entry informationi

    Entry nameiMOGS_HUMAN
    AccessioniPrimary (citable) accession number: Q13724
    Secondary accession number(s): A8K938
    , F5H6D0, Q17RN9, Q8TCT5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 134 of the entry and version 5 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 2
      Human chromosome 2: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3