{ "bcoid": "GLY_000318", "title": "Rat Protein PTM Annotation (UniProtKB)", "description": "The Rat Protein PTM Annotation (UniProtKB) dataset contains rat [taxid:10116] PTM annotations for UniProtKB ...", "filename": "rat_protein_ptm_annotation_uniprotkb.csv", "filetype": "csv", "categories": { "species": "Rattus norvegicus", "molecule": "Protein", "tags": "PTM annotation", "file_type": "csv", "status": "Reviewed", "scope": "internal" }, "minitable": { "content": [ [ "P30349-1...", "protein_xref..." ], [ "P30349-1...", "protein_xref..." ] ], "headers": [ "uniprotkb_ca...", "xref_key..." ], "colwidth": [ "40%", "20%" ] }, "sampledata": { "type": "table", "data": [ [ { "type": "string", "label": "uniprotkb_canonical_ac" }, { "type": "string", "label": "xref_key" }, { "type": "string", "label": "xref_id" }, { "type": "string", "label": "eco_id" }, { "type": "string", "label": "ptm_annotation" } ], [ "P30349-1", "protein_xref_uniprotkb", "P30349", "ECO_0000250", "Phosphorylation at Ser-416 inhibits leukotriene-A4 hydrolase activity." ], [ "P30349-1", "protein_xref_pubmed", "P09960", "ECO_0000250", "Phosphorylation at Ser-416 inhibits leukotriene-A4 hydrolase activity." ], [ "Q6MG56-1", "protein_xref_uniprotkb", "Q6MG56", "", "N-glycosylated." ], [ "Q6MG56-1", "protein_xref_pubmed", "", "", "N-glycosylated." ], [ "Q5XIH0-1", "protein_xref_uniprotkb", "Q5XIH0", "", "Phosphorylated at Ser-60, Ser-68 and Ser-75; the major sites of phosphorylation. Nuclear accumulation correlates with a concomitant dephosphorylation. Phosphorylation may attenuate its RNA polymerase III-repressive function (By similarity)." ], [ "Q5XIH0-1", "protein_xref_pubmed", "", "", "Phosphorylated at Ser-60, Ser-68 and Ser-75; the major sites of phosphorylation. Nuclear accumulation correlates with a concomitant dephosphorylation. Phosphorylation may attenuate its RNA polymerase III-repressive function (By similarity)." ], [ "Q5XIH0-1", "protein_xref_uniprotkb", "Q5XIH0", "", "Sumoylated with SUMO1 and SUMO2, mainly on Lys-35. Desumoylated by SENP1. SUMOylation promotes the ability of MAF1 to repress transcription and suppress colony formation (By similarity)." ], [ "Q5XIH0-1", "protein_xref_pubmed", "", "", "Sumoylated with SUMO1 and SUMO2, mainly on Lys-35. Desumoylated by SENP1. SUMOylation promotes the ability of MAF1 to repress transcription and suppress colony formation (By similarity)." ], [ "Q6MG53-1", "protein_xref_uniprotkb", "Q6MG53", "", "N-glycosylated." ], [ "Q6MG53-1", "protein_xref_pubmed", "", "", "N-glycosylated." ], [ "Q6MG59-1", "protein_xref_uniprotkb", "Q6MG59", "ECO_0000250", "May be O-glycosylated." ], [ "Q6MG59-1", "protein_xref_pubmed", "O95866", "ECO_0000250", "May be O-glycosylated." ], [ "Q6MG59-1", "protein_xref_uniprotkb", "Q6MG59", "ECO_0000250", "Phosphorylated." ], [ "Q6MG59-1", "protein_xref_pubmed", "D7PDD4", "ECO_0000250", "Phosphorylated." ], [ "Q6MG59-1", "protein_xref_uniprotkb", "Q6MG59", "ECO_0000250", "N-glycosylated." ], [ "Q6MG59-1", "protein_xref_pubmed", "O95866", "ECO_0000250", "N-glycosylated." ], [ "Q6MG59-1", "protein_xref_pubmed", "D7PDD4", "ECO_0000250", "N-glycosylated." ], [ "Q9WUD9-1", "protein_xref_uniprotkb", "Q9WUD9", "", "Ubiquitinated in response to CDK5-mediated phosphorylation. Ubiquitination mediated by CBLC requires SRC autophosphorylation at Tyr-419 and may lead to lysosomal degradation (By similarity)." ], [ "Q9WUD9-1", "protein_xref_pubmed", "", "", "Ubiquitinated in response to CDK5-mediated phosphorylation. Ubiquitination mediated by CBLC requires SRC autophosphorylation at Tyr-419 and may lead to lysosomal degradation (By similarity)." ], [ "Q9WUD9-1", "protein_xref_uniprotkb", "Q9WUD9", "", "Myristoylated at Gly-2, and this is essential for targeting to membranes." ], [ "Q9WUD9-1", "protein_xref_pubmed", "", "", "Myristoylated at Gly-2, and this is essential for targeting to membranes." ], [ "Q9WUD9-1", "protein_xref_uniprotkb", "Q9WUD9", "", "S-nitrosylation is important for activation of its kinase activity." ], [ "Q9WUD9-1", "protein_xref_pubmed", "", "", "S-nitrosylation is important for activation of its kinase activity." ], [ "Q9WUD9-1", "protein_xref_uniprotkb", "Q9WUD9", "ECO_0000250", "Dephosphorylated at Tyr-530 by PTPRJ. Phosphorylated on Tyr-530 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src (By similarity). Dephosphorylated by PTPRJ at Tyr-419. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-530, the SH3 domain engaged with the SH2-kinase linker, and Tyr-419 dephosphorylated. Dephosphorylation of Tyr-530 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-530, Tyr-419 can then become autophosphorylated, resulting in SRX activation. Phosphorylation of Tyr-530 by CSK allows this interaction to reform, resulting in SRC inactivation. CDK5-mediated phosphorylation at Ser-75 targets SRC to ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. Phosphorylated by PTK2/FAK1; this enhances kinase activity (By similarity). Phosphorylated by PTK2B/PYK2; this enhances kinase activity. Upon activation of IL6ST by IL6, Tyr-419 is phosphorylated and Tyr-530 dephosphorylated (By similarity)." ], [ "Q9WUD9-1", "protein_xref_pubmed", "P12931", "ECO_0000250", "Dephosphorylated at Tyr-530 by PTPRJ. Phosphorylated on Tyr-530 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src (By similarity). Dephosphorylated by PTPRJ at Tyr-419. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-530, the SH3 domain engaged with the SH2-kinase linker, and Tyr-419 dephosphorylated. Dephosphorylation of Tyr-530 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-530, Tyr-419 can then become autophosphorylated, resulting in SRX activation. Phosphorylation of Tyr-530 by CSK allows this interaction to reform, resulting in SRC inactivation. CDK5-mediated phosphorylation at Ser-75 targets SRC to ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. Phosphorylated by PTK2/FAK1; this enhances kinase activity (By similarity). Phosphorylated by PTK2B/PYK2; this enhances kinase activity. Upon activation of IL6ST by IL6, Tyr-419 is phosphorylated and Tyr-530 dephosphorylated (By similarity)." ], [ "Q9WUD9-1", "protein_xref_uniprotkb", "Q9WUD9", "ECO_0000269", "Dephosphorylated at Tyr-530 by PTPRJ. Phosphorylated on Tyr-530 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src (By similarity). Dephosphorylated by PTPRJ at Tyr-419. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-530, the SH3 domain engaged with the SH2-kinase linker, and Tyr-419 dephosphorylated. Dephosphorylation of Tyr-530 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-530, Tyr-419 can then become autophosphorylated, resulting in SRX activation. Phosphorylation of Tyr-530 by CSK allows this interaction to reform, resulting in SRC inactivation. CDK5-mediated phosphorylation at Ser-75 targets SRC to ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. Phosphorylated by PTK2/FAK1; this enhances kinase activity (By similarity). Phosphorylated by PTK2B/PYK2; this enhances kinase activity. Upon activation of IL6ST by IL6, Tyr-419 is phosphorylated and Tyr-530 dephosphorylated (By similarity)." ], [ "Q9WUD9-1", "protein_xref_pubmed", "8849729", "ECO_0000269", "Dephosphorylated at Tyr-530 by PTPRJ. Phosphorylated on Tyr-530 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src (By similarity). Dephosphorylated by PTPRJ at Tyr-419. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-530, the SH3 domain engaged with the SH2-kinase linker, and Tyr-419 dephosphorylated. Dephosphorylation of Tyr-530 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-530, Tyr-419 can then become autophosphorylated, resulting in SRX activation. Phosphorylation of Tyr-530 by CSK allows this interaction to reform, resulting in SRC inactivation. CDK5-mediated phosphorylation at Ser-75 targets SRC to ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. Phosphorylated by PTK2/FAK1; this enhances kinase activity (By similarity). Phosphorylated by PTK2B/PYK2; this enhances kinase activity. Upon activation of IL6ST by IL6, Tyr-419 is phosphorylated and Tyr-530 dephosphorylated (By similarity)." ], [ "Q9WUD9-1", "protein_xref_pubmed", "15735685", "ECO_0000269", "Dephosphorylated at Tyr-530 by PTPRJ. Phosphorylated on Tyr-530 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src (By similarity). Dephosphorylated by PTPRJ at Tyr-419. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-530, the SH3 domain engaged with the SH2-kinase linker, and Tyr-419 dephosphorylated. Dephosphorylation of Tyr-530 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-530, Tyr-419 can then become autophosphorylated, resulting in SRX activation. Phosphorylation of Tyr-530 by CSK allows this interaction to reform, resulting in SRC inactivation. CDK5-mediated phosphorylation at Ser-75 targets SRC to ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. Phosphorylated by PTK2/FAK1; this enhances kinase activity (By similarity). Phosphorylated by PTK2B/PYK2; this enhances kinase activity. Upon activation of IL6ST by IL6, Tyr-419 is phosphorylated and Tyr-530 dephosphorylated (By similarity)." ], [ "Q8R553-1", "protein_xref_uniprotkb", "Q8R553", "", "Proteolytically processed under normal cellular conditions. A primary zeta-cleavage generates a large extracellular (soluble) N-terminal domain (sAlc) and a short C-terminal transmembrane fragment (CTF1). A secondary cleavage catalyzed by gamma-secretase within the transmembrane domain releases the beta-Alc-beta chain in the extracellular milieu and produces an intracellular fragment (AlcICD). This processing is strongly suppressed in the tripartite complex formed with APBA2 and APP, which seems to prevent the association with gamma-secretase (By similarity)." ], [ "Q8R553-1", "protein_xref_pubmed", "", "", "Proteolytically processed under normal cellular conditions. A primary zeta-cleavage generates a large extracellular (soluble) N-terminal domain (sAlc) and a short C-terminal transmembrane fragment (CTF1). A secondary cleavage catalyzed by gamma-secretase within the transmembrane domain releases the beta-Alc-beta chain in the extracellular milieu and produces an intracellular fragment (AlcICD). This processing is strongly suppressed in the tripartite complex formed with APBA2 and APP, which seems to prevent the association with gamma-secretase (By similarity)." ], [ "Q9WUD2-1", "protein_xref_uniprotkb", "Q9WUD2", "ECO_0000269", "Phosphorylated by PKA." ], [ "Q9WUD2-1", "protein_xref_pubmed", "15249591", "ECO_0000269", "Phosphorylated by PKA." ], [ "Q9WUD2-1", "protein_xref_uniprotkb", "Q9WUD2", "ECO_0000269", "N-glycosylated." ], [ "Q9WUD2-1", "protein_xref_pubmed", "14622291", "ECO_0000269", "N-glycosylated." ], [ "Q07969-1", "protein_xref_uniprotkb", "Q07969", "ECO_0000250", "Ubiquitinated at Lys-469 and Lys-472. Ubiquitination is induced by fatty acids such as oleic acid and leads to degradation by the proteasome (PubMed:21610069). Ubiquitination and degradation are inhibited by insulin which blocks the effect of fatty acids (By similarity)." ], [ "Q07969-1", "protein_xref_pubmed", "Q08857", "ECO_0000250", "Ubiquitinated at Lys-469 and Lys-472. Ubiquitination is induced by fatty acids such as oleic acid and leads to degradation by the proteasome (PubMed:21610069). Ubiquitination and degradation are inhibited by insulin which blocks the effect of fatty acids (By similarity)." ], [ "Q07969-1", "protein_xref_uniprotkb", "Q07969", "ECO_0000269", "Ubiquitinated at Lys-469 and Lys-472. Ubiquitination is induced by fatty acids such as oleic acid and leads to degradation by the proteasome (PubMed:21610069). Ubiquitination and degradation are inhibited by insulin which blocks the effect of fatty acids (By similarity)." ], [ "Q07969-1", "protein_xref_pubmed", "21610069", "ECO_0000269", "Ubiquitinated at Lys-469 and Lys-472. Ubiquitination is induced by fatty acids such as oleic acid and leads to degradation by the proteasome (PubMed:21610069). Ubiquitination and degradation are inhibited by insulin which blocks the effect of fatty acids (By similarity)." ], [ "Q07969-1", "protein_xref_pubmed", "P16671", "ECO_0000250", "Ubiquitinated at Lys-469 and Lys-472. Ubiquitination is induced by fatty acids such as oleic acid and leads to degradation by the proteasome (PubMed:21610069). Ubiquitination and degradation are inhibited by insulin which blocks the effect of fatty acids (By similarity)." ], [ "Q8VHI8-1", "protein_xref_uniprotkb", "Q8VHI8", "ECO_0000250", "Polyubiquitinated. 'Lys-63'-linked polyubiquitination by RNF185 increases the interaction with the autophagy receptor SQSTM1. Undergoes 'Lys-29'- and 'Lys-63'-linked polyubiquitination by RNF186 that may regulate BNIP1 localization to the mitochondrion." ], [ "Q8VHI8-1", "protein_xref_pubmed", "Q12981", "ECO_0000250", "Polyubiquitinated. 'Lys-63'-linked polyubiquitination by RNF185 increases the interaction with the autophagy receptor SQSTM1. Undergoes 'Lys-29'- and 'Lys-63'-linked polyubiquitination by RNF186 that may regulate BNIP1 localization to the mitochondrion." ], [ "A0A096MJY4-1", "protein_xref_uniprotkb", "A0A096MJY4", "", "Phosphorylated on Ser-59; which enhances DNA binding activity. Phosphorylated on Ser-396; which is required for Lys-391 sumoylation and inhibits transcriptional activity." ], [ "A0A096MJY4-1", "protein_xref_pubmed", "", "", "Phosphorylated on Ser-59; which enhances DNA binding activity. Phosphorylated on Ser-396; which is required for Lys-391 sumoylation and inhibits transcriptional activity." ], [ "A0A096MJY4-1", "protein_xref_uniprotkb", "A0A096MJY4", "", "Proteolytically cleaved in cerebellar granule neurons on several sites by caspase 3 and caspase 7 following neurotoxicity. Preferentially cleaves the CDK5-mediated hyperphosphorylated form which leads to neuron apoptosis and transcriptional inactivation." ], [ "A0A096MJY4-1", "protein_xref_pubmed", "", "", "Proteolytically cleaved in cerebellar granule neurons on several sites by caspase 3 and caspase 7 following neurotoxicity. Preferentially cleaves the CDK5-mediated hyperphosphorylated form which leads to neuron apoptosis and transcriptional inactivation." ], [ "A0A096MJY4-1", "protein_xref_uniprotkb", "A0A096MJY4", "", "Acetylated by p300 on several sites in diffentiating myocytes. Acetylation on Lys-4 increases DNA binding and transactivation." ], [ "A0A096MJY4-1", "protein_xref_pubmed", "", "", "Acetylated by p300 on several sites in diffentiating myocytes. Acetylation on Lys-4 increases DNA binding and transactivation." ], [ "A0A096MJY4-1", "protein_xref_uniprotkb", "A0A096MJY4", "", "Sumoylated on Lys-391 with SUMO2 but not SUMO1; which represses transcriptional activity." ], [ "A0A096MJY4-1", "protein_xref_pubmed", "", "", "Sumoylated on Lys-391 with SUMO2 but not SUMO1; which represses transcriptional activity." ], [ "O55043-1", "protein_xref_uniprotkb", "O55043", "", "Phosphorylated on Ser-516 by CaMK1; enhancement of GEF activity and downstream activation of RAC1. Phosphorylated by PTK2/FAK1; this promotes interaction with RAC1 (By similarity)." ], [ "O55043-1", "protein_xref_pubmed", "", "", "Phosphorylated on Ser-516 by CaMK1; enhancement of GEF activity and downstream activation of RAC1. Phosphorylated by PTK2/FAK1; this promotes interaction with RAC1 (By similarity)." ], [ "P20646-1", "protein_xref_uniprotkb", "P20646", "ECO_0000269", "N-glycosylated." ], [ "P20646-1", "protein_xref_pubmed", "8334986", "ECO_0000269", "N-glycosylated." ], [ "P20646-1", "protein_xref_pubmed", "8407898", "ECO_0000269", "N-glycosylated." ], [ "P56574-1", "protein_xref_uniprotkb", "P56574", "", "Acetylation at Lys-413 dramatically reduces catalytic activity. Deacetylated by SIRT3 (By similarity)." ], [ "P56574-1", "protein_xref_pubmed", "", "", "Acetylation at Lys-413 dramatically reduces catalytic activity. Deacetylated by SIRT3 (By similarity)." ], [ "P48965-1", "protein_xref_uniprotkb", "P48965", "", "Phosphorylated by CHEK1 on Ser-76, Ser-124, Ser-178, Ser-283, Ser-296 and Thr-508 during checkpoint mediated cell cycle arrest. Also phosphorylated by CHEK2 on Ser-124, Ser-283, and Ser-296 during checkpoint mediated cell cycle arrest. Phosphorylation on Ser-178 and Thr-508 creates binding sites for YWHAE/14-3-3 epsilon which inhibits CDC25A. Phosphorylation on Ser-76, Ser-124, Ser-178, Ser-283 and Ser-296 may also promote ubiquitin-dependent proteolysis of CDC25A by the SCF complex. Phosphorylation of CDC25A at Ser-76 by CHEK1 primes it for subsequent phosphorylation at Ser-79, Ser-82 and Ser-88 by NEK11. Phosphorylation by NEK11 is required for BTRC-mediated polyubiquitination and degradation. Phosphorylation by PIM1 leads to an increase in phosphatase activity. Phosphorylated by PLK3 following DNA damage, leading to promote its ubiquitination and degradation (By similarity)." ], [ "P48965-1", "protein_xref_pubmed", "", "", "Phosphorylated by CHEK1 on Ser-76, Ser-124, Ser-178, Ser-283, Ser-296 and Thr-508 during checkpoint mediated cell cycle arrest. Also phosphorylated by CHEK2 on Ser-124, Ser-283, and Ser-296 during checkpoint mediated cell cycle arrest. Phosphorylation on Ser-178 and Thr-508 creates binding sites for YWHAE/14-3-3 epsilon which inhibits CDC25A. Phosphorylation on Ser-76, Ser-124, Ser-178, Ser-283 and Ser-296 may also promote ubiquitin-dependent proteolysis of CDC25A by the SCF complex. Phosphorylation of CDC25A at Ser-76 by CHEK1 primes it for subsequent phosphorylation at Ser-79, Ser-82 and Ser-88 by NEK11. Phosphorylation by NEK11 is required for BTRC-mediated polyubiquitination and degradation. Phosphorylation by PIM1 leads to an increase in phosphatase activity. Phosphorylated by PLK3 following DNA damage, leading to promote its ubiquitination and degradation (By similarity)." ], [ "P48965-1", "protein_xref_uniprotkb", "P48965", "", "Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex that contains FZR1/CDH1 during G1 phase leading to its degradation by the proteasome. Ubiquitinated by a SCF complex containing BTRC and FBXW11 during S phase leading to its degradation by the proteasome. Deubiquitination by USP17L2/DUB3 leads to its stabilization (By similarity)." ], [ "P48965-1", "protein_xref_pubmed", "", "", "Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex that contains FZR1/CDH1 during G1 phase leading to its degradation by the proteasome. Ubiquitinated by a SCF complex containing BTRC and FBXW11 during S phase leading to its degradation by the proteasome. Deubiquitination by USP17L2/DUB3 leads to its stabilization (By similarity)." ], [ "P48966-1", "protein_xref_uniprotkb", "P48966", "", "Phosphorylated by BRSK1 in vitro. Phosphorylated by CHEK1, which inhibits the activity of this protein. Phosphorylation at Ser-349 by AURKA might locally participate in the control of the onset of mitosis. Phosphorylation by MELK at Ser-166 promotes localization to the centrosome and the spindle poles during mitosis. Phosphorylation at Ser-319 and Ser-370 by MAPK14 is required for binding to 14-3-3 proteins (By similarity)." ], [ "P48966-1", "protein_xref_pubmed", "", "", "Phosphorylated by BRSK1 in vitro. Phosphorylated by CHEK1, which inhibits the activity of this protein. Phosphorylation at Ser-349 by AURKA might locally participate in the control of the onset of mitosis. Phosphorylation by MELK at Ser-166 promotes localization to the centrosome and the spindle poles during mitosis. Phosphorylation at Ser-319 and Ser-370 by MAPK14 is required for binding to 14-3-3 proteins (By similarity)." ], [ "P48961-1", "protein_xref_uniprotkb", "P48961", "", "Polyubiquitinated by the SCF(FBXL2) complex, leading to proteasomal degradation." ], [ "P48961-1", "protein_xref_pubmed", "", "", "Polyubiquitinated by the SCF(FBXL2) complex, leading to proteasomal degradation." ], [ "O35158-1", "protein_xref_uniprotkb", "O35158", "ECO_0000269", "N-glycosylated." ], [ "O35158-1", "protein_xref_pubmed", "9214393", "ECO_0000269", "N-glycosylated." ], [ "Q6P7Q4-1", "protein_xref_uniprotkb", "Q6P7Q4", "", "Glutathionylation at Cys-139 inhibits enzyme activity." ], [ "Q6P7Q4-1", "protein_xref_pubmed", "", "", "Glutathionylation at Cys-139 inhibits enzyme activity." ], [ "Q6P7Q4-1", "protein_xref_uniprotkb", "Q6P7Q4", "", "Phosphorylated at Thr-107 in the presence of CaMK2. However, this is a consensus site for phosphorylation by CK2 so phosphorylation may be mediated by CK2 rather than CaMK2. Phosphorylation is induced by TNF and suppresses the TNF-induced transcriptional activity of NF-kappa-B (By similarity)." ], [ "Q6P7Q4-1", "protein_xref_pubmed", "", "", "Phosphorylated at Thr-107 in the presence of CaMK2. However, this is a consensus site for phosphorylation by CK2 so phosphorylation may be mediated by CK2 rather than CaMK2. Phosphorylation is induced by TNF and suppresses the TNF-induced transcriptional activity of NF-kappa-B (By similarity)." ], [ "Q6P7Q4-1", "protein_xref_uniprotkb", "Q6P7Q4", "", "Exists in a nitric oxide (NO)-modified form. The exact nature of the modification is unknown, but it suppresses the TNF-induced transcriptional activity of NF-kappa-B (By similarity)." ], [ "Q6P7Q4-1", "protein_xref_pubmed", "", "", "Exists in a nitric oxide (NO)-modified form. The exact nature of the modification is unknown, but it suppresses the TNF-induced transcriptional activity of NF-kappa-B (By similarity)." ], [ "Q6MG58-1", "protein_xref_uniprotkb", "Q6MG58", "", "O-glycosylated." ], [ "Q6MG58-1", "protein_xref_pubmed", "", "", "O-glycosylated." ], [ "P43219-1", "protein_xref_uniprotkb", "P43219", "", "N-glycosylation is required for cell surface expression and lengthens receptor half-life by preventing degradation in the ER." ], [ "P43219-1", "protein_xref_pubmed", "", "", "N-glycosylation is required for cell surface expression and lengthens receptor half-life by preventing degradation in the ER." ], [ "Q8CF82-1", "protein_xref_uniprotkb", "Q8CF82", "", "N-glycosylated." ], [ "Q8CF82-1", "protein_xref_pubmed", "", "", "N-glycosylated." ], [ "P62804-1", "protein_xref_uniprotkb", "P62804", "ECO_0000250", "Butyrylation of histones marks active promoters and competes with histone acetylation." ], [ "P62804-1", "protein_xref_pubmed", "P62806", "ECO_0000250", "Butyrylation of histones marks active promoters and competes with histone acetylation." ], [ "P62804-1", "protein_xref_uniprotkb", "P62804", "ECO_0000250", "Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac) and Lys-13 (H4K12ac). Demethylation is performed by JMJD6. Symmetric dimethylation on Arg-4 (H4R3me2s) by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage (By similarity)." ], [ "P62804-1", "protein_xref_pubmed", "P62805", "ECO_0000250", "Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac) and Lys-13 (H4K12ac). Demethylation is performed by JMJD6. Symmetric dimethylation on Arg-4 (H4R3me2s) by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage (By similarity)." ], [ "P62804-1", "protein_xref_uniprotkb", "P62804", "ECO_0000250", "Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes." ], [ "P62804-1", "protein_xref_pubmed", "P62805", "ECO_0000250", "Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes." ] ] }, "readme": "Name\n - Rat Protein PTM Annotation (UniProtKB)\n\nVersion\n - 1.8.25\n\nCreated on\n - 2019-11-30T14:07:14.445471\n\nModified on\n - 2020-04-10T12:14:03.498068\n\nCreated by\n - Jeet Vora [jeetvora@gwu.edu], Rahi Navelkar [rsn13@gwu.edu], Robel Kahsay [rykahsay@gwu.edu], Xavier Holmes [xavierh@email.gwu.edu]\n\nAuthors\n - Maria Martin [martin@ebi.ac.uk], Preethi Vasudev [pvasudev@ebi.ac.uk]\n\nChecksum\n - \n\nUsability Domain\n - The Rat Protein PTM Annotation (UniProtKB) dataset contains rat [taxid:10116] PTM annotations for UniProtKB canonical accessions. The annotation is the curated statements of mainly about glycosylation and phosphorylation. The dataset is derived form 2019-09 UniprotKB release. If you use this dataset please give proper attribution to UniProtKB and GlyGen\n\nDescription Domain\n Keywords\n - ptm annotation\n - glycosylation\n - phosphorylation\n\n Pipeline Steps\n - Step-1: The script extracts the ptm annotation strings from the triplestore for the UniProtKB canonical sequnces asnd extracts as a dataset in a csv format\n\nExecution Domain\n Scripts - https://github.com/GW-HIVE/glygen-backend-integration/blob/master/pipeline/integrator/make-protein-dataset.py\n\n\n Software Prerequisites\n Name: Python\n Version: 2.7.5\n URI: https://www.python.org/download/releases/2.7.5/\n\nI/O Domain\n Input Subdomain\n Name: uniprot-proteome-rattus-norvegicus.nt\n URI: https://data.glygen.org/ln2data/releases/data/v-1.8.25/reviewed/uniprot-proteome-rattus-norvegicus.nt\n Name: rat_protein_masterlist.csv\n URI: https://data.glygen.org/ln2data/releases/data/v-1.8.25/reviewed/rat_protein_masterlist.csv\n Output Subdomain\n Name: rat_protein_ptm_annotation_uniprotkb.csv\n URI: http://data.glygen.org/ln2data/releases/data/v-1.8.25/reviewed/rat_protein_ptm_annotation_uniprotkb.csv\n Name: rat_protein_ptm_annotation_uniprotkb.stat.csv\n URI: http://data.glygen.org/ln2data/releases/data/v-1.8.25/reviewed/rat_protein_ptm_annotation_uniprotkb.stat.csv\n\nFields\n Name: \"src_xref_key\"\n Description: \"Source Xref key\"\n Unique Values: \"1\"\n Name: \"xref_id\"\n Description: \"ID of the X-ref\"\n Unique Values: \"119\"\n Name: \"title\"\n Description: \"Title of the published article in the journal\"\n Unique Values: \"119\"\n Name: \"src_xref_id\"\n Description: \"Source X-ref ID\"\n Unique Values: \"120\"\n Name: \"journal_name\"\n Description: \"The name of the journal in which the article is published\"\n Unique Values: \"49\"\n Name: \"authors\"\n Description: \"NA\"\n Unique Values: \"118\"\n Name: \"publication_date\"\n Description: \"Contains the full date on which the issue of the journal was published. Sourced from MEDLINE/PubMed data element(fields) description.\"\n Unique Values: \"117\"\n Name: \"glytoucan_ac\"\n Description: \"Unique accession assigned to the registered glycan structure in GlyTouCan database\"\n Unique Values: \"115\"\n Name: \"xref_key\"\n Description: \"Source key associated to the xref_id\"\n Unique Values: \"1\"", "downloadurl": "/ln2data/releases/data/v-1.8.25/reviewed/rat_protein_ptm_annotation_uniprotkb.csv" }