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                "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.",
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                "protein_xref_pubmed",
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                "",
                "Crystal structure of mammalian acid sphingomyelinase.",
                "Nature communications",
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                "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.",
                "Nature biotechnology",
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                "Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD",
                "protein_xref_pubmed",
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                "",
                "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.",
                "Nature biotechnology",
                "2009 Apr",
                "Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD",
                "protein_xref_pubmed",
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                "",
                "Characterization of a transneuronal cytokine family Cbln--regulation of secretion by heteromeric assembly.",
                "The European journal of neuroscience",
                "2007 Feb",
                "Iijima T, Miura E, Matsuda K, Kamekawa Y, Watanabe M, Yuzaki M",
                "protein_xref_pubmed",
                "17331201",
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                "",
                "Glycosylation analysis and protein structure determination of murine fetal antigen 1 (mFA1)--the circulating gene product of the delta-like protein (dlk), preadipocyte factor 1 (Pref-1) and stromal-cell-derived protein 1 (SCP-1) cDNAs.",
                "European journal of biochemistry",
                "1997 Mar 1",
                "Krogh TN, Bachmann E, Teisner B, Skjodt K, Hojrup P",
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                "",
                "High throughput quantitative glycomics and glycoform-focused proteomics of murine dermis and epidermis.",
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                "2005 Dec",
                "Uematsu R, Furukawa J, Nakagawa H, Shinohara Y, Deguchi K, Monde K, Nishimura S",
                "protein_xref_pubmed",
                "16170054",
                "protein_xref_uniprotkb_gly",
                "P18242"
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                "",
                "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.",
                "Nature biotechnology",
                "2009 Apr",
                "Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD",
                "protein_xref_pubmed",
                "19349973",
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                "",
                "De novo sulfur SAD phasing of the lysosomal 66.3 kDa protein from mouse.",
                "Acta crystallographica. Section D, Biological crystallography",
                "2009 Mar",
                "Lakomek K, Dickmanns A, Mueller U, Kollmann K, Deuschl F, Berndt A, Lubke T, Ficner R",
                "protein_xref_pubmed",
                "19237744",
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                "",
                "Molecular characterization of the hypothetical 66.3-kDa protein in mouse: lysosomal targeting, glycosylation, processing and tissue distribution.",
                "FEBS letters",
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                "Deuschl F, Kollmann K, von Figura K, Lubke T",
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                "",
                "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.",
                "Nature biotechnology",
                "2009 Apr",
                "Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD",
                "protein_xref_pubmed",
                "19349973",
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                "",
                "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.",
                "Nature biotechnology",
                "2009 Apr",
                "Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD",
                "protein_xref_pubmed",
                "19349973",
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                "",
                "Proteome-wide characterization of N-glycosylation events by diagonal chromatography.",
                "Journal of proteome research",
                "2006 Sep",
                "Ghesquiere B, Van Damme J, Martens L, Vandekerckhove J, Gevaert K",
                "protein_xref_pubmed",
                "16944957",
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                "",
                "The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members of the contactin family of neural recognition molecules.",
                "Proceedings of the National Academy of Sciences of the United States of America",
                "2010 Feb 9",
                "Bouyain S, Watkins DJ",
                "protein_xref_pubmed",
                "20133774",
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                "Q69Z26"
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                "",
                "Biosynthesis and expression of a disintegrin-like and metalloproteinase domain with thrombospondin-1 repeats-15: a novel versican-cleaving proteoglycanase.",
                "The Journal of biological chemistry",
                "2013 Dec 27",
                "Dancevic CM, Fraser FW, Smith AD, Stupka N, Ward AC, McCulloch DR",
                "protein_xref_pubmed",
                "24220035",
                "protein_xref_uniprotkb_gly",
                "P59384"
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                "",
                "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.",
                "Nature biotechnology",
                "2009 Apr",
                "Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD",
                "protein_xref_pubmed",
                "19349973",
                "protein_xref_uniprotkb_gly",
                "Q07113"
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                "",
                "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation.",
                "Molecular & cellular proteomics : MCP",
                "2009 Nov",
                "Gundry RL, Raginski K, Tarasova Y, Tchernyshyov I, Bausch-Fluck D, Elliott ST, Boheler KR, Van Eyk JE, Wollscheid B",
                "protein_xref_pubmed",
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                "",
                "Endoplasmic reticulum stress and N-glycosylation modulate expression of WFS1 protein.",
                "Biochemical and biophysical research communications",
                "2004 Dec 3",
                "Yamaguchi S, Ishihara H, Tamura A, Yamada T, Takahashi R, Takei D, Katagiri H, Oka Y",
                "protein_xref_pubmed",
                "15522226",
                "protein_xref_uniprotkb_gly",
                "P56695"
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            [
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                "",
                "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.",
                "Nature biotechnology",
                "2009 Apr",
                "Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD",
                "protein_xref_pubmed",
                "19349973",
                "protein_xref_uniprotkb_gly",
                "Q99MR3"
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            [
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                "",
                "Structure of a receptor-binding fragment of reelin and mutational analysis reveal a recognition mechanism similar to endocytic receptors.",
                "Proceedings of the National Academy of Sciences of the United States of America",
                "2007 Jun 12",
                "Yasui N, Nogi T, Kitao T, Nakano Y, Hattori M, Takagi J",
                "protein_xref_pubmed",
                "17548821",
                "protein_xref_uniprotkb_gly",
                "Q60841"
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                "",
                "O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry.",
                "Molecular &amp; cellular proteomics : MCP",
                "2006 May",
                "Vosseller K, Trinidad JC, Chalkley RJ, Specht CG, Thalhammer A, Lynn AJ, Snedecor JO, Guan S, Medzihradszky KF, Maltby DA, Schoepfer R, Burlingame AL",
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                "O88737"
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                "",
                "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.",
                "Nature biotechnology",
                "2009 Apr",
                "Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD",
                "protein_xref_pubmed",
                "19349973",
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                "",
                "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.",
                "Nature biotechnology",
                "2009 Apr",
                "Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD",
                "protein_xref_pubmed",
                "19349973",
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                "",
                "Identification of the glycosaminoglycan-attachment site of mouse invariant-chain proteoglycan core protein by site-directed mutagenesis.",
                "Proceedings of the National Academy of Sciences of the United States of America",
                "1988 Mar",
                "Miller J, Hatch JA, Simonis S, Cullen SE",
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                "3422739",
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                "",
                "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.",
                "Nature biotechnology",
                "2009 Apr",
                "Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD",
                "protein_xref_pubmed",
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                "",
                "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.",
                "Nature biotechnology",
                "2009 Apr",
                "Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD",
                "protein_xref_pubmed",
                "19349973",
                "protein_xref_uniprotkb_gly",
                "O09126"
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            [
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                "",
                "Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides.",
                "Journal of proteome research",
                "2007 Mar",
                "Bernhard OK, Kapp EA, Simpson RJ",
                "protein_xref_pubmed",
                "17330941",
                "protein_xref_uniprotkb_gly",
                "P01898"
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                "",
                "Role of glycosylation in the organic anion transporter OAT1.",
                "The Journal of biological chemistry",
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                "Tanaka K, Xu W, Zhou F, You G",
                "protein_xref_pubmed",
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                "Modification of N-glycosylation modulates the secretion and lipolytic function of apoptosis inhibitor of macrophage (AIM).",
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                "Mori M, Kimura H, Iwamura Y, Arai S, Miyazaki T",
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                "23236605",
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                "",
                "Proteome-wide characterization of N-glycosylation events by diagonal chromatography.",
                "Journal of proteome research",
                "2006 Sep",
                "Ghesquiere B, Van Damme J, Martens L, Vandekerckhove J, Gevaert K",
                "protein_xref_pubmed",
                "16944957",
                "protein_xref_uniprotkb_gly",
                "O70362"
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                "",
                "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation.",
                "Molecular & cellular proteomics : MCP",
                "2009 Nov",
                "Gundry RL, Raginski K, Tarasova Y, Tchernyshyov I, Bausch-Fluck D, Elliott ST, Boheler KR, Van Eyk JE, Wollscheid B",
                "protein_xref_pubmed",
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                "Q9R0E1-1",
                "",
                "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.",
                "Nature biotechnology",
                "2009 Apr",
                "Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD",
                "protein_xref_pubmed",
                "19349973",
                "protein_xref_uniprotkb_gly",
                "Q9R0E1"
            ],
            [
                "Q8BWC0-1",
                "",
                "The two-pore channel TPCN2 mediates NAADP-dependent Ca(2+)-release from lysosomal stores.",
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                "protein_xref_pubmed",
                "19557428",
                "protein_xref_uniprotkb_gly",
                "Q8BWC0"
            ],
            [
                "Q9WV91-1",
                "",
                "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.",
                "Nature biotechnology",
                "2009 Apr",
                "Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD",
                "protein_xref_pubmed",
                "19349973",
                "protein_xref_uniprotkb_gly",
                "Q9WV91"
            ],
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                "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation.",
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                "2009 Nov",
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                "protein_xref_uniprotkb_gly",
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                "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation.",
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                "2009 Nov",
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                "protein_xref_pubmed",
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        ]
    },
    "readme": "Name\n   - Mouse Proteoform Glycosylation Citations (UniProtKB)\n\nVersion\n   - 1.11.2\n\nCreated on\n  - 2021-06-03T16:33:45.288361\n\nModified on\n   - 2022-01-20T16:08:16.713145\n\nCreated by\n   - Jeet Vora [jeetvora@gwu.edu], Karina Martinez [karinamartinez@gwu.edu], Amanda Bell [amandab2140@gwu.edu], Jonathon Keeney [keeneyjg@gwu.edu], Millicent Quartey [mquartey@email.gwu.edu]\n\nAuthors\n   - Not Applicable []\n\nChecksum\n   - \n\nExecution Domain\n   Scripts\n\n   Software Prerequisites\n\nI/O Domain\n   Output Subdomain\n      Name: mouse_proteoform_citations_glycosylation_uniprotkb.csv\n      URI: http://data.glygen.org/ln2wwwdata/reviewed/mouse_proteoform_citations_glycosylation_uniprotkb.csv\n      Name: mouse_proteoform_citations_glycosylation_uniprotkb.stat.csv\n      URI: http://data.glygen.org/ln2wwwdata/reviewed/mouse_proteoform_citations_glycosylation_uniprotkb.stat.csv\n\nFields\n      Name: \"uniprotkb_canonical_ac\"\n     Description: \"\"\n      Unique Values: \"16\"\n      Name: \"motif_start\"\n     Description: \"\"\n      Unique Values: \"23\"\n      Name: \"filter_flags\"\n     Description: \"Filter tags/flags assigned to the mutation entries that have passed the mutation filter criteria\"\n      Unique Values: \"19\"\n      Name: \"sift_prediction\"\n     Description: \"The SIFT qualitative prediction is derived from this score such that substitutions with a score < 0.05 are called 'deleterious' and all others are called 'tolerated\"\n      Unique Values: \"3\"\n      Name: \"somatic_status\"\n     Description: \"The status of the variant whether it is germline (somatic status =0) or somatic (somatic status =1) variant\"\n      Unique Values: \"1\"\n      Name: \"chr_pos\"\n     Description: \"Chromosome Position of a gene\"\n      Unique Values: \"19\"\n      Name: \"chr_id\"\n     Description: \"\"\n      Unique Values: \"10\"\n      Name: \"dbsnp_id\"\n     Description: \"\"A reference SNP ID number\"\n      Unique Values: \"19\"\n      Name: \"evidence_ECO:0000313\"\n     Description: \"A type of evidence that is imported information used in an automatic assertion\"\n      Unique Values: \"1\"\n      Name: \"xref_id\"\n     Description: \"ID of the X-ref\"\n      Unique Values: \"19\"\n      Name: \"mim_id\"\n     Description: \"Disease ID from the OMIM database\"\n      Unique Values: \"1\"\n      Name: \"description\"\n     Description: \"\"\n      Unique Values: \"1\"\n      Name: \"begin_aa_pos\"\n     Description: \"Start position of the amino acid in the sequence of a protein in UniProtKB\"\n      Unique Values: \"18\"\n      Name: \"cytogenic_band\"\n     Description: \"One of the subregions of a chromosome visible microscopically after special staining\"\n      Unique Values: \"14\"\n      Name: \"aa_pos\"\n     Description: \"Position of the amino acid in canonical sequence of protein in the UniProtKB database\"\n      Unique Values: \"18\"\n      Name: \"ref_aa\"\n     Description: \"Reference amino acid residue\"\n      Unique Values: \"9\"\n      Name: \"sift_score\"\n     Description: \"SIFT predicts whether an amino acid substitution is likely to affect protein function based on sequence homology and the physico-chemical similarity between the alternate amino acids. The data we provide for each amino acid substitution is a score and a qualitative prediction (either 'tolerated' or 'deleterious'). The score is the normalized probability that the amino acid change is tolerated so scores nearer zero are more likely to be deleterious. The qualitative prediction is derived from this score such that substitutions with a score < 0.05 are called 'deleterious' and all others are called 'tolerated\"\n      Unique Values: \"10\"\n      Name: \"alt_motif\"\n     Description: \"Altered motif\"\n      Unique Values: \"24\"\n      Name: \"disease_xrefs\"\n     Description: \"\"\n      Unique Values: \"1\"\n      Name: \"polyphen_score\"\n     Description: \"The score assigned to a amino acid substitution by a tool called as PolyPhen (=Polymorphism Phenotyping)  which predicts possible impact of an amino acid substitution on the structure and function of a human protein using straightforward physical and comparative considerations. The PolyPhen score ranges from 0.0 (tolerated) to 1.0 (deleterious). Variants with scores of 0.0 are predicted to be benign. Values closer to 1.0 are more confidently predicted to be deleterious\"\n      Unique Values: \"1\"\n      Name: \"polyphen_prediction\"\n     Description: \"\"The PolyPhen prediction values are - greater than 0.908 - \"\"Probably Damaging\"\"; greater than 0.446 and less than or equal to 0.908 - \"\"Possibly Damaging\"\"; less than or equal to 0.446 - \"\"Benign\"\"\"\n      Unique Values: \"1\"\n      Name: \"is_known_glycoprotein\"\n     Description: \"Yes or no flag to denote if a protein is experimentally proven glycoprotein\"\n      Unique Values: \"1\"\n      Name: \"alt_nt\"\n     Description: \"Alternative nucleotide\"\n      Unique Values: \"1\"\n      Name: \"protein_name\"\n     Description: \"Protein name in the UniProtKB\"\n      Unique Values: \"16\"\n      Name: \"disease_evidence_ECO:0000313\"\n     Description: \"The evidence that could be a PMID or a ClinVar ID that associates disease with the variant\"\n      Unique Values: \"1\"\n      Name: \"effect\"\n     Description: \"The effect on glycosylation or N-sequon due to variation at site of glycosylated amino acid.\"\n      Unique Values: \"3\"\n      Name: \"end_aa_pos\"\n     Description: \"End position of the amino acid in the sequence of a protein in UniProtKB\"\n      Unique Values: \"18\"\n      Name: \"mutation_type\"\n     Description: \"Denotes whether mutation was reported with reference to amino acid or nucleotide\"\n      Unique Values: \"1\"\n      Name: \"disease_description\"\n     Description: \"The disease description and/or definition \"\n      Unique Values: \"1\"\n      Name: \"do_id\"\n     Description: \"Disease Ontology identifier\"\n      Unique Values: \"1\"\n      Name: \"evidence_ECO:0000269\"\n     Description: \"A type of experimental evidence that is used in a manual assertion. Usually the values are PMIDs\"\n      Unique Values: \"1\"\n      Name: \"ref_nt\"\n     Description: \"Reference nucleotide\"\n      Unique Values: \"4\"\n      Name: \"disease\"\n     Description: \"The disease name for the cell line\"\n      Unique Values: \"1\"\n      Name: \"alt_aa\"\n     Description: \"Altered amino acid residue\"\n      Unique Values: \"10\"\n      Name: \"cosmic_id\"\n     Description: \"Legacy mutation identifier (COSM) in Catalogue of Somatic Mutations in Cancer (COSMIC) represents existing COSM mutation identifiers. This identifier remains the same between different assemblies (GRCh37 and GRCh38). All the COSM ids at the same genomic location have been collapsed into one representative COSM id. These ids are maintained to help track existing mutations\"\n      Unique Values: \"1\"\n      Name: \"ref_motif\"\n     Description: \"Reference motif\"\n      Unique Values: \"20\"\n      Name: \"xref_key\"\n     Description: \"Source key associated to the  xref_id\"\n      Unique Values: \"2\"\n      Name: \"minor_allelic_frequency\"\n     Description: \"\"\n      Unique Values: \"1\"\n      Name: \"gene_name\"\n     Description: \"\"Official gene name/symbol assigned to the gene. Human gene name/symbol are approved by the HUGO Gene Nomenclature Committee (HGNC) and mouse gene name are approved by the Mouse Genome Informatics (MGI)\"\n      Unique Values: \"17\"\n      Name: \"disease_evidence_ECO:0000269\"\n     Description: \"The PMID evidence for the association of the disease with the variant.\"\n      Unique Values: \"1\"",
    "downloadurl": "/ln2data/releases/data/v-1.11.2/reviewed/mouse_proteoform_citations_glycosylation_uniprotkb.csv"
}
