{ "bcoid": "GLY_000035", "title": "Human Protein Citations (UniProtKB)", "description": "The Human Protein Citations dataset contains publication information for human [taxid:9606] UniProtKB ...", "filename": "human_protein_citations_uniprotkb.csv", "filetype": "csv", "categories": { "species": "Homo sapiens", "molecule": "Protein", "tags": "Protein Citations", "file_type": "csv", "status": "Reviewed", "scope": "internal" }, "minitable": { "content": [ [ "P30613-1...", "Hematologica..." ], [ "P30613-1...", "Hematologica..." ] ], "headers": [ "uniprotkb_ca...", "title..." ], "colwidth": [ "40%", "20%" ] }, "sampledata": { "type": "table", "data": [ [ { "type": "string", "label": "uniprotkb_canonical_ac" }, { "type": "string", "label": "title" }, { "type": "string", "label": "journal_name" }, { "type": "string", "label": "publication_date" }, { "type": "string", "label": "authors" }, { "type": "string", "label": "xref_key" }, { "type": "string", "label": "xref_id" }, { "type": "string", "label": "src_xref_key" }, { "type": "string", "label": "src_xref_id" } ], [ "P30613-1", "Hematologically important mutations: red cell pyruvate kinase (2nd update).", "Blood Cells Mol. Dis.", "1998", "Bianchi P., Zanella A., Baronciani L.", "protein_xref_pubmed", "10087985", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "Hematologically important mutations: red cell pyruvate kinase (third update).", "Blood Cells Mol. Dis.", "2000", "Bianchi P., Zanella A.", "protein_xref_pubmed", "10772876", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "Molecular characterization of the PK-LR gene in sixteen pyruvate kinase-deficient patients.", "Br. J. Haematol.", "2001", "Bianchi P., Fermo E., Vercellati C., Zanella A., Baronciani L., Cotton F., Zappa M., Boschetti C., Iurlo A.", "protein_xref_pubmed", "11328279", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia.", "J. Biol. Chem.", "2002", "Wang C., Bianchi P., Chiarelli L.R., Galizzi A., Mattevi A., Valentini G., Zanella A., Abraham D.J., Dolzan M., Fortin R.", "protein_xref_pubmed", "11960989", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "Structural analysis of human pyruvate kinase L-gene and identification of the promoter activity in erythroid cells.", "Biochem. Biophys. Res. Commun.", "1992", "Fujii H., Kanno H., Miwa S.", "protein_xref_pubmed", "1445295", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "Identical point mutations of the R-type pyruvate kinase (PK) cDNA found in unrelated PK variants associated with hereditary hemolytic anemia.", "Blood", "1992", "Fujii H., Kanno H., Miwa S., Hirono A., Omine M.", "protein_xref_pubmed", "1536957", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "cDNA cloning of human R-type pyruvate kinase and identification of a single amino acid substitution (Thr384-->Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia.", "Proc. Natl. Acad. Sci. U.S.A.", "1991", "Fujii H., Kanno H., Miwa S., Hirono A.", "protein_xref_pubmed", "1896471", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "Fifteen novel mutations in PKLR associated with pyruvate kinase (PK) deficiency: structural implications of amino acid substitutions in PK.", "Hum. Mutat.", "2009", "Huizinga E.G., Hadders M.A., van Solinge W.W., van Wijk R., van Oirschot B.A., van Wesel A.C.W.", "protein_xref_pubmed", "19085939", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "Point mutations in the L-type pyruvate kinase gene of two children with hemolytic anemia caused by pyruvate kinase deficiency.", "Blood", "1991", "Winkler H., Neubauer B., Hofferbert S., Lakomek M., Schroter W., Parke M.", "protein_xref_pubmed", "2018831", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "Exome sequencing and unrelated findings in the context of complex disease research: ethical and clinical implications.", "Discov. Med.", "2011", "Lin Y., Liu Y., Tian L., Wang J., Wang W., Wei Z., Zhang P., Lyon G.J., Hakonarson H., Johnson W.E., Wang K., Jiang T., Moore B., Yandell M., Glessner J.T., Xing J., van Solinge W.W., Reimherr F., Bodily P.M., Clement M., Elia J., Robison R.J., Van Wijk R.", "protein_xref_pubmed", "21794208", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "Human liver type pyruvate kinase: complete amino acid sequence and the expression in mammalian cells.", "Proc. Natl. Acad. Sci. U.S.A.", "1988", "Nagata S., Tani K., Fujii H., Miwa S.", "protein_xref_pubmed", "3126495", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "Human liver type pyruvate kinase: cDNA cloning and chromosomal assignment.", "Biochem. Biophys. Res. Commun.", "1987", "Tanaka T., Yoshida M.C., Tani K., Fujii H., Miwa S., Noguchi T., Toyoshima K., Tsutsumi H., Sukegawa J.", "protein_xref_pubmed", "3566732", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "Molecular study of pyruvate kinase deficient patients with hereditary nonspherocytic hemolytic anemia.", "J. Clin. Invest.", "1995", "Beutler E., Baronciani L.", "protein_xref_pubmed", "7706479", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "Molecular abnormality of erythrocyte pyruvate kinase deficiency in the Amish.", "Blood", "1994", "Fujii H., Kanno H., Miwa S., Ballas S.K., Bowman H.S.", "protein_xref_pubmed", "8161798", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "Mutations in the pyruvate kinase L gene in patients with hereditary hemolytic anemia.", "Blood", "1994", "Nuernberg P., Reis A., Brabec V., Jacobasch G., Lenzner C., Sakalova A., Thiele B.-J.", "protein_xref_pubmed", "8180378", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "Molecular basis of impaired pyruvate kinase isozyme conversion in erythroid cells: a single amino acid substitution near the active site and decreased mRNA content of the R-type PK.", "Biochem. Biophys. Res. Commun.", "1993", "Fujii H., Kanno H., Miwa S., Tsujino G.", "protein_xref_pubmed", "8476433", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "Low substrate affinity of pyruvate kinase variant (PK Sapporo) caused by a single amino acid substitution (426 Arg-->Gln) associated with hereditary hemolytic anemia.", "Blood", "1993", "Fujii H., Kanno H., Miwa S.", "protein_xref_pubmed", "8481523", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia.", "Proc. Natl. Acad. Sci. U.S.A.", "1993", "Beutler E., Baronciani L.", "protein_xref_pubmed", "8483951", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "Mutations in pyruvate kinase.", "Hum. Mutat.", "1996", "Beutler E., Baronciani L.", "protein_xref_pubmed", "8664896", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "Hematologically important mutations: red cell pyruvate kinase.", "Blood Cells Mol. Dis.", "1996", "Bianchi P., Zanella A., Baronciani L.", "protein_xref_pubmed", "8807089", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "Hematologically important mutations: red cell pyruvate kinase (1st update).", "Blood Cells Mol. Dis.", "1996", "Bianchi P., Zanella A., Baronciani L.", "protein_xref_pubmed", "9075576", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "G-to-T transition at cDNA nt 110 (K37Q) in the PKLR (pyruvate kinase) gene is the molecular basis of a case of hereditary increase of red blood cell ATP.", "Hum. Mutat.", "1997", "Beutler E., Roos D., van Zwieten R., Westwood B.", "protein_xref_pubmed", "9090535", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "Novel mutations and structural implications in R-type pyruvate kinase-deficient patients from Southern Italy.", "Hum. Mutat.", "1998", "Alfinito F., Ferraro F., Rotoli B., Salvatore F., Zagari A., Vitale D., Pastore L., Calise R.M., Frisso G., della Morte R.", "protein_xref_pubmed", "9482576", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "Molecular characterization of the PK-LR gene in pyruvate kinase deficient Spanish patients.", "Br. J. Haematol.", "1998", "Alvarez R., Morey M., Vives Corrons J.L., Remacha A., Bureo E., Carrera A., Cortes T., Estella J., Nomdedeu B., Perez Lungmus G., Pujades A., Sanchez J.M., Zarza R.", "protein_xref_pubmed", "9827908", "protein_xref_uniprotkb", "P30613" ], [ "P30613-1", "A new sickle cell disease phenotype associating Hb S trait, severe pyruvate kinase deficiency (PK Conakry), and an alpha-2 globin gene variant (Hb Conakry).", "Br. J. Haematol.", "1998", "Wajcman H., Cohen-Solal M., Bardakdjian-Michau J., Galacteros F., Kister J., Poyart C., Prehu C., Prome D., Bachir D., Valentin C.", "protein_xref_pubmed", "9886305", "protein_xref_uniprotkb", "P30613" ], [ "P23919-1", "Lysine acetylation targets protein complexes and co-regulates major cellular functions.", "Science", "2009", "Choudhary C., Gnad F., Kumar C., Mann M., Nielsen M.L., Olsen J.V., Rehman M., Walther T.C.", "protein_xref_pubmed", "19608861", "protein_xref_uniprotkb", "P23919" ], [ "P23919-1", "Structures of human thymidylate kinase in complex with prodrugs: implications for the structure-based design of novel compounds.", "Biochemistry", "2003", "Konrad M., Meier C., Lavie A., Ostermann N., Monnerjahn C., Segura-Pena D., Veit T.", "protein_xref_pubmed", "12614151", "protein_xref_uniprotkb", "P23919" ], [ "P23919-1", "Molecular cloning and expression of the human deoxythymidylate kinase gene in yeast.", "Nucleic Acids Res.", "1991", "Sclafani R.A., Su J.Y.", "protein_xref_pubmed", "2017365", "protein_xref_uniprotkb", "P23919" ], [ "P23919-1", "Human dTMP kinase: gene expression and enzymatic activity coinciding with cell cycle progression and cell growth.", "DNA Cell Biol.", "1994", "Li C., Tang A., Zhang S.Q., Drisco B., Huang S.H., Jong A., Seeger R.", "protein_xref_pubmed", "8024690", "protein_xref_uniprotkb", "P23919" ], [ "Q8NHX4-1", "Molecular cloning for testis spermatogenesis cell apoptosis related gene TSARG1 and Mtsarg1 and expression analysis for Mtsarg1 gene.", "Yi Chuan Xue Bao", "2003", "Liu G., Li L.Y., Lu G.X., Xing X.W., Fu J.J., Liu S.F.", "protein_xref_pubmed", "12812072", "protein_xref_uniprotkb", "Q8NHX4" ], [ "Q8NHX9-1", "Two newly identified genetic determinants of pigmentation in Europeans.", "Nat. Genet.", "2008", "Gudbjartsson D.F., Jakobsdottir M., Kiemeney L.A., Kong A., Rafnar T., Stacey S.N., Stefansson K., Steinberg S., Sulem P., Thorleifsson G., Thorsteinsdottir U., Gudjonsson S.A., Tucker M.A., Palsson S., Goldstein A.M., Aben K.K., Benediktsdottir K.R., Vermeulen S.H., Helgason A., Gulcher J., Olafsson J.H., Palsson A., Ragnarsson R., Sigurgeirsson B., Thorisdottir K.", "protein_xref_pubmed", "18488028", "protein_xref_uniprotkb", "Q8NHX9" ], [ "Q8NHX9-1", "NAADP mobilizes calcium from acidic organelles through two-pore channels.", "Nature", "2009", "Lin Y., Ma J., Pan Z., Tang J., Wang C., Zhu Y., Cheng X., Hao X., Lin P., Xiao R., Rietdorf K., Zhu M.X., Ruas M., Evans A.M., Parrington J., Galione A., Arredouani A., Calcraft P.J., Chuang K.T., Teboul L., Wyatt C.N.", "protein_xref_pubmed", "19387438", "protein_xref_uniprotkb", "Q8NHX9" ], [ "Q8NHX9-1", "Essential requirement for two-pore channel 1 in NAADP-mediated calcium signaling.", "J. Cell Biol.", "2009", "Gao X., Cai X., Patel S., Brailoiu E., Brailoiu G.C., Dun N.J., Churamani D., Marchant J.S., Boulware M.J., Hooper R., Schrlau M.G.", "protein_xref_pubmed", "19620632", "protein_xref_uniprotkb", "Q8NHX9" ], [ "Q8NHX9-1", "Leucine-rich repeat kinase 2 regulates autophagy through a calcium-dependent pathway involving NAADP.", "Hum. Mol. Genet.", "2012", "Zhang L., Patel S., Woodman P.G., Churchill G.C., Bloor-Young D., Churamani D., Gomez-Suaga P., Hilfiker S., Luzon-Toro B.", "protein_xref_pubmed", "22012985", "protein_xref_uniprotkb", "Q8NHX9" ], [ "Q8NHX9-1", "Hax-1 identified as a two-pore channel (TPC)-binding protein.", "FEBS Lett.", "2013", "Lai F.A., Galione A., Lam A.K., Zissimopoulos S.", "protein_xref_pubmed", "24188827", "protein_xref_uniprotkb", "Q8NHX9" ], [ "Q8NHX9-1", "Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV.", "Nat. Commun.", "2020", "Chen J., Chen X., Li P., Liu Y., Wang J., Chen T., Hu J., Hu K., Guo L., Jin Q., Lei X., Guo R., Qian Z., Ren L., Ou X., Xiang Z., Mi D., Mu Z.", "protein_xref_pubmed", "32221306", "protein_xref_uniprotkb", "Q8NHX9" ], [ "Q9C0H2-1", "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.", "Cell", "2006", "Blagoev B., Gnad F., Kumar C., Macek B., Mann M., Mortensen P., Olsen J.V.", "protein_xref_pubmed", "17081983", "protein_xref_uniprotkb", "Q9C0H2" ], [ "Q9C0H2-1", "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.", "J. Proteome Res.", "2008", "Cantin G.T., Lee J.-D., Lu B., Park S.K., Xu T., Yates J.R. III, Yi W., Yates J.R., Lee J.D.", "protein_xref_pubmed", "18220336", "protein_xref_uniprotkb", "Q9C0H2" ], [ "Q9C0H2-1", "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.", "J. Proteome Res.", "2009", "Chen R., Han G., Jiang X., Sun D., Wang F., Wang L., Ye M., Zou H.", "protein_xref_pubmed", "19159218", "protein_xref_uniprotkb", "Q9C0H2" ], [ "Q9C0H2-1", "A novel human Cl(-) channel family related to Drosophila flightless locus.", "J. Biol. Chem.", "2004", "Suzuki M., Mizuno A.", "protein_xref_pubmed", "15010458", "protein_xref_uniprotkb", "Q9C0H2" ], [ "Q9C0H5-1", "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.", "Mol. Cell", "2008", "Bairlein M., Daub H., Gnad F., Greff Z., Keri G., Korner R., Mann M., Olsen J.V., Oppermann F.S., Stemmann O.", "protein_xref_pubmed", "18691976", "protein_xref_uniprotkb", "Q9C0H5" ], [ "Q9C0H6-1", "Identification and characterization of KLHL4, a novel human homologue of the Drosophila Kelch gene that maps within the X-linked cleft palate and ankyloglossia (CPX) critical region.", "Genomics", "2001", "Moore G.E., Ross M.T., Stanier P., Arnason A., Bjornsson A., Braybrook C., Howell G., Warry G.", "protein_xref_pubmed", "11401425", "protein_xref_uniprotkb", "Q9C0H6" ], [ "Q9C0H9-5", "p140Cap protein suppresses tumour cell properties, regulating Csk and Src kinase activity.", "EMBO J.", "2007", "Silengo L., Tarone G., Turco E., Aramu S., Cabodi S., Cavallo F., Damiano L., Defilippi P., Di Stefano P., Forni G., Piva R., Praduroux A., Tordella L.", "protein_xref_pubmed", "17525734", "protein_xref_uniprotkb", "Q9C0H9" ], [ "Q9C0H9-5", "p130Cas-associated protein (p140Cap) as a new tyrosine-phosphorylated protein involved in cell spreading.", "Mol. Biol. Cell", "2004", "Silengo L., Tarone G., Turco E., Cabodi S., Defilippi P., Di Stefano P., Giuffrida M.G., Bergatto E., Erba E.B., Margaria V.", "protein_xref_pubmed", "14657239", "protein_xref_uniprotkb", "Q9C0H9" ], [ "Q9C0H9-5", "SNIP/p140Cap mRNA expression is an unfavourable prognostic factor in breast cancer and is not expressed in normal breast tissue.", "Br. J. Cancer", "2008", "Kennedy S., Clynes M., Crown J., Doolan P., Mehta J.P., O'Driscoll L., Rani S.", "protein_xref_pubmed", "18475297", "protein_xref_uniprotkb", "Q9C0H9" ], [ "Q9C0H9-5", "Characterization of a multidomain adaptor protein, p140Cap, as part of a pre-synaptic complex.", "J. Neurochem.", "2008", "Ito H., Morishita R., Usuda N., Nagata K., Sudo K., Asano T., Iwamoto I., Defilippi P., Di Stefano P., Atsuzawa K., Semba R., Takei S.", "protein_xref_pubmed", "18662323", "protein_xref_uniprotkb", "Q9C0H9" ], [ "Q9C0H9-5", "Dynamic microtubules regulate dendritic spine morphology and synaptic plasticity.", "Neuron", "2009", "Grigoriev I., Akhmanova A., Gouveia S.M., Hoogenraad C.C., Demmers J., Kapitein L.C., Wulf P.S., Jaworski J., Camera P., Defilippi P., Di Stefano P., Dortland B.R., Spangler S.A., Krugers H.", "protein_xref_pubmed", "19146815", "protein_xref_uniprotkb", "Q9C0H9" ], [ "Q96J65-1", "Two new genes from the human ATP-binding cassette transporter superfamily, ABCC11 and ABCC12, tandemly duplicated on chromosome 16q12.", "Gene", "2001", "Allikmets R., Arnould I., Dean M., Prades C., Rosier M., Hutchinson A., Schuetz J.D., Tammur J., Adachi M., Ptacek L.J., Rzhetsky A., Swoboda K.J.", "protein_xref_pubmed", "11483364", "protein_xref_uniprotkb", "Q96J65" ], [ "Q96J65-1", "Multiple splicing variants of two new human ATP-binding cassette transporters, ABCC11 and ABCC12.", "Biochem. Biophys. Res. Commun.", "2001", "Shimizu H., Ishikawa T., Takayanagi S., Yabuuchi H.", "protein_xref_pubmed", "11688999", "protein_xref_uniprotkb", "Q96J65" ], [ "Q96J65-1", "MRP9, an unusual truncated member of the ABC transporter superfamily, is highly expressed in breast cancer.", "Proc. Natl. Acad. Sci. U.S.A.", "2002", "Lee S., Kumar V., Bera T.K., Lee B., Pastan I., Iavarone C.", "protein_xref_pubmed", "12011458", "protein_xref_uniprotkb", "Q96J65" ], [ "Q96J65-1", "Multidrug resistance-associated protein 9 (ABCC12) is present in mouse and boar sperm.", "Biochem. J.", "2007", "Ishikawa T., Borst P., Scheffer G.L., Ono N., Oomen L., Neefjes J.J., Boerke A., Brocks L., De Haas M., De Rooij D.G., Gadella B.M., Groothuis T.A., Van Deemter E., Van de Wetering K., Van der Heijden I.", "protein_xref_pubmed", "17472575", "protein_xref_uniprotkb", "Q96J65" ], [ "Q8NC06-1", "Widespread Expansion of Protein Interaction Capabilities by Alternative Splicing.", "Cell", "2016", "Yang X., Yi S., Tam S., Yang F., Vidal M., Richardson A., Xia Y., Zhong Q., Hill D.E., Sun S., Calderwood M.A., Ghamsari L., Hao T., Iakoucheva L.M., Kang S., Roth F.P., Salehi-Ashtiani K., Chen A., Aloy P., Tan G., Andrews B., Murray R., Boone C., Costanzo M., Zhou X.J., Balcha D., Begg B.E., Charloteaux B., Coulombe-Huntington J., Duran-Frigola M., MacWilliams A., Pevzner S.J., Rodriguez M.D., Sahni N., Shen Y.A., Sheynkman G.M., Spirohn K., Trigg S.A.", "protein_xref_pubmed", "26871637", "protein_xref_uniprotkb", "K7EM05" ], [ "P40424-1", "Analysis of PBX1 as a candidate gene for type 2 diabetes mellitus in Pima Indians.", "Biochim. Biophys. Acta", "2001", "Bogardus C., Prochazka M., Wolford J.K., Thameem F.", "protein_xref_pubmed", "11267683", "protein_xref_uniprotkb", "P40424" ], [ "P40424-1", "The t(1;19)(q23;p13) results in consistent fusion of E2A and PBX1 coding sequences in acute lymphoblastic leukemias.", "Blood", "1991", "Cleary M.L., Crist W.M., Hunger S.P., Galili N., Carroll A.J., Link M.P.", "protein_xref_pubmed", "1671560", "protein_xref_uniprotkb", "P40424" ], [ "P40424-1", "A new homeobox gene contributes the DNA binding domain of the t(1;19) translocation protein in pre-B ALL.", "Cell", "1990", "Baltimore D., Kamps M.P., Sun X.-H., Murre C.", "protein_xref_pubmed", "1967983", "protein_xref_uniprotkb", "P40424" ], [ "P40424-1", "PBX1 haploinsufficiency leads to syndromic congenital anomalies of the kidney and urinary tract (CAKUT) in humans.", "J. Med. Genet.", "2017", "Breton J., Dieterich K., Jouk P.S., Odent S., Digilio M.C., Harbuz R., Ray P.F., Coutton C., Vieville G., Apostolou A., Mackenroth L., Vogel I., Fokstuen S., Satre V., Bidart M., Le Tanno P., Devillard F., Bosson C., Jaillard S., Pisanti M.A., Bernardini L., Amblard F., Beddow R., Bena F., Christensen R., Guebre-Egziabher F., Hackmann K., Novelli A., Poke G., Sartelet H.", "protein_xref_pubmed", "28270404", "protein_xref_uniprotkb", "P40424" ], [ "P40424-1", "Targeted exome sequencing identifies PBX1 as involved in monogenic congenital anomalies of the kidney and urinary tract.", "J. Am. Soc. Nephrol.", "2017", "Salomon R., Antignac C., Gonzales M., Roume J., Nitschke P., Schaefer E., Bras M., Gaillard D., Saunier S., Henry C., Jeanpierre C., Martinovic J., Bole-Feysot C., Jeanpierre M., Heidet L., Alibeu O., Novo R., Pietrement C., Fourrage C., Tores F., Moriniere V., Humbert C., Malan V., De Tomasi L., Reilly M.L.", "protein_xref_pubmed", "28566479", "protein_xref_uniprotkb", "P40424" ], [ "P40424-1", "Pbx1 is converted into a transcriptional activator upon acquiring the N-terminal region of E2A in pre-B-cell acute lymphoblastoid leukemia.", "Proc. Natl. Acad. Sci. U.S.A.", "1993", "Voorhoeve P.M., van Dijk M.A., Murre C.", "protein_xref_pubmed", "8327485", "protein_xref_uniprotkb", "P40424" ], [ "P40424-1", "Structure of a HoxB1-Pbx1 heterodimer bound to DNA: role of the hexapeptide and a fourth homeodomain helix in complex formation.", "Cell", "1999", "Cleary M.L., Wolberger C., Piper D.E., Batchelor A.H., Chang C.-P.", "protein_xref_pubmed", "10052460", "protein_xref_uniprotkb", "P40424" ], [ "P40424-1", "Cooperative transcriptional activation by Klf4, Meis2, and Pbx1.", "Mol. Cell. Biol.", "2011", "Wotton D., Bjerke G.A., Hyman-Walsh C.", "protein_xref_pubmed", "21746878", "protein_xref_uniprotkb", "P40424" ], [ "P40424-1", "Homeodomain proteins MEIS1 and PBXs regulate the lineage-specific transcription of the platelet factor 4 gene.", "Blood", "2003", "Doi T., Sato T., Matsuura E., Okada Y., Nagai R., Minami T., Morita I.", "protein_xref_pubmed", "12609849", "protein_xref_uniprotkb", "P40424" ], [ "P40424-1", "MEIS proteins as partners of the TLX1/HOX11 oncoprotein.", "Leuk. Res.", "2010", "Kees U.R., Ford J., Greene W.K., D'Souza D., Gottardo N.G., Milech N., Watt P.M.", "protein_xref_pubmed", "19559479", "protein_xref_uniprotkb", "P40424" ], [ "P40424-1", "An autoinhibitory effect of the homothorax domain of Meis2.", "FEBS J.", "2010", "Wotton D., Bjerke G.A., Hyman-Walsh C.", "protein_xref_pubmed", "20553494", "protein_xref_uniprotkb", "P40424" ], [ "P40424-1", "FOXC1 transcriptional regulatory activity is impaired by PBX1 in a filamin A-mediated manner.", "Mol. Cell. Biol.", "2005", "O'Neill M.A., Walter M.A., Coca-Prados M., Berry F.B.", "protein_xref_pubmed", "15684392", "protein_xref_uniprotkb", "P40424" ], [ "P40424-1", "Functional cloning and characterization of a novel nonhomeodomain protein that inhibits the binding of PBX1-HOX complexes to DNA.", "J. Biol. Chem.", "2000", "Humphries R.K., Largman C., Montpetit B., Shen W.-F., Abramovich C., Imren S., Pineault N.", "protein_xref_pubmed", "10825160", "protein_xref_uniprotkb", "P40424" ], [ "P40424-1", "PBX2 and PBX3, new homeobox genes with extensive homology to the human proto-oncogene PBX1.", "Mol. Cell. Biol.", "1991", "Cleary M.L., Galili N., Monica K., Nourse J., Saltman D.", "protein_xref_pubmed", "1682799", "protein_xref_uniprotkb", "P40424" ], [ "P40424-1", "Fusion with E2A converts the Pbx1 homeodomain protein into a constitutive transcriptional activator in human leukemias carrying the t(1;19) translocation.", "Mol. Cell. Biol.", "1994", "Lu Q., Kamps M.P., Wright D.D.", "protein_xref_pubmed", "7910944", "protein_xref_uniprotkb", "P40424" ], [ "P40424-1", "PBX1 and MEIS1 up-regulate SOX3 gene expression by direct interaction with a consensus binding site within the basal promoter region.", "Biochem. J.", "2009", "Stevanovic M., Mojsin M.", "protein_xref_pubmed", "19799567", "protein_xref_uniprotkb", "P40424" ], [ "P40424-1", "Both Pbx1 and E2A-Pbx1 bind the DNA motif ATCAATCAA cooperatively with the products of multiple murine Hox genes, some of which are themselves oncogenes.", "Mol. Cell. Biol.", "1995", "Lu Q., Kamps M.P., Wright D.D., Knoepfler P.S., Scheele J.", "protein_xref_pubmed", "7791786", "protein_xref_uniprotkb", "P40424" ], [ "P40424-1", "The highest affinity DNA element bound by Pbx complexes in t(1;19) leukemic cells fails to mediate cooperative DNA-binding or cooperative transactivation by E2a-Pbx1 and class I Hox proteins - evidence for selective targetting of E2a-Pbx1 to a subset of Pbx-recognition elements.", "Oncogene", "1997", "Kamps M.P., Knoepfler P.S.", "protein_xref_pubmed", "9191052", "protein_xref_uniprotkb", "P40424" ], [ "P40424-1", "Gain-of-function MN1 truncation variants cause a recognizable syndrome with craniofacial and brain abnormalities.", "Am. J. Hum. Genet.", "2020", "Hirose T., Miyatake S., Takahashi H., Abe R., Suzuki H., Sasaki K., Kimura Y., Akiyama T., Isidor B., Kato M., Matsumoto N., Miyake N., Nakamura K., Hiraki Y., Mizuguchi T., Ogata K., Shiina M., Mitsuhashi S., Koshimizu E., Takata A., Hamanaka K., Obo K., Tomizawa S.I.", "protein_xref_pubmed", "31839203", "protein_xref_uniprotkb", "P40424" ], [ "P40425-1", "The novel gene G17, located in the human major histocompatibility complex, encodes PBX2, a homeodomain-containing protein.", "Genomics", "1995", "Aguado B., Campbell R.D.", "protein_xref_pubmed", "7759099", "protein_xref_uniprotkb", "P40425" ], [ "P40425-1", "Three genes in the human MHC class III region near the junction with the class II: gene for receptor of advanced glycosylation end products, PBX2 homeobox gene and a notch homolog, human counterpart of mouse mammary tumor gene int-3.", "Genomics", "1994", "Takahashi E., Inoko H., Ando A., Matsumoto K., Fukagawa T., Sugaya K., Mita K., Ikemura T.", "protein_xref_pubmed", "7835890", "protein_xref_uniprotkb", "P40425" ], [ "P40425-1", "Homeodomain proteins MEIS1 and PBXs regulate the lineage-specific transcription of the platelet factor 4 gene.", "Blood", "2003", "Doi T., Sato T., Matsuura E., Okada Y., Nagai R., Minami T., Morita I.", "protein_xref_pubmed", "12609849", "protein_xref_uniprotkb", "P40425" ], [ "P40425-1", "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.", "Science", "2007", "Bakalarski C.E., Ballif B.A., Elledge S.J., Gygi S.P., Hurov K.E., Lerenthal Y., Luo J., Matsuoka S., McDonald E.R. III, Shiloh Y., Smogorzewska A., Solimini N., Zhao Z., McDonald E.R.", "protein_xref_pubmed", "17525332", "protein_xref_uniprotkb", "P40425" ], [ "P40425-1", "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.", "J. Proteome Res.", "2008", "Cantin G.T., Lee J.-D., Lu B., Park S.K., Xu T., Yates J.R. III, Yi W., Yates J.R., Lee J.D.", "protein_xref_pubmed", "18220336", "protein_xref_uniprotkb", "P40425" ], [ "P40425-1", "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse.", "Genome Res.", "2003", "Aguado B., Hood L., Madan A., Qin S., Rowen L., Xie T., Ahearn M.E., Campbell R.D.", "protein_xref_pubmed", "14656967", "protein_xref_uniprotkb", "P40425" ], [ "P40425-1", "Functional cloning and characterization of a novel nonhomeodomain protein that inhibits the binding of PBX1-HOX complexes to DNA.", "J. Biol. Chem.", "2000", "Humphries R.K., Largman C., Montpetit B., Shen W.-F., Abramovich C., Imren S., Pineault N.", "protein_xref_pubmed", "10825160", "protein_xref_uniprotkb", "P40425" ], [ "P40425-1", "PBX2 and PBX3, new homeobox genes with extensive homology to the human proto-oncogene PBX1.", "Mol. Cell. Biol.", "1991", "Cleary M.L., Galili N., Monica K., Nourse J., Saltman D.", "protein_xref_pubmed", "1682799", "protein_xref_uniprotkb", "P40425" ], [ "P40425-1", "Fusion with E2A converts the Pbx1 homeodomain protein into a constitutive transcriptional activator in human leukemias carrying the t(1;19) translocation.", "Mol. Cell. Biol.", "1994", "Lu Q., Kamps M.P., Wright D.D.", "protein_xref_pubmed", "7910944", "protein_xref_uniprotkb", "P40425" ], [ "P40426-1", "Functional cloning and characterization of a novel nonhomeodomain protein that inhibits the binding of PBX1-HOX complexes to DNA.", "J. Biol. Chem.", "2000", "Humphries R.K., Largman C., Montpetit B., Shen W.-F., Abramovich C., Imren S., Pineault N.", "protein_xref_pubmed", "10825160", "protein_xref_uniprotkb", "P40426" ], [ "P40426-1", "Novel alternative PBX3 isoforms in leukemia cells with distinct interaction specificities.", "Genes Chromosomes Cancer", "2001", "Kees U.R., Milech N., Watt P.M.", "protein_xref_pubmed", "11579467", "protein_xref_uniprotkb", "P40426" ], [ "P40426-1", "PBX2 and PBX3, new homeobox genes with extensive homology to the human proto-oncogene PBX1.", "Mol. Cell. Biol.", "1991", "Cleary M.L., Galili N., Monica K., Nourse J., Saltman D.", "protein_xref_pubmed", "1682799", "protein_xref_uniprotkb", "P40426" ], [ "P40426-1", "Fusion with E2A converts the Pbx1 homeodomain protein into a constitutive transcriptional activator in human leukemias carrying the t(1;19) translocation.", "Mol. Cell. Biol.", "1994", "Lu Q., Kamps M.P., Wright D.D.", "protein_xref_pubmed", "7910944", "protein_xref_uniprotkb", "P40426" ] ] }, "readme": "Name\n - Human Protein Citations (UniProtKB)\n\nVersion\n - 1.11.2\n\nCreated on\n - 2019-01-23T17:21:05.902655\n\nModified on\n - 2020-04-10T11:27:33.124175\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], Karina Martinez [karinamartinez@gwu.edu], Amanda Bell [amandab2140@gwu.edu], Jonathon Keeney [keeneyjg@gwu.edu], Millicent Quartey [mquartey@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 Human Protein Citations dataset contains publication information for human [taxid:9606] UniProtKB accessions that includes PMID, journal name, date and author and title. Publications of large scale studies, and high frequency publications pertaining to genome sequencing, cDNA, chromosomes have been filtered out as per https://data.glygen.org/ln2wwwdata/compiled/human_protein_blacklisted_pmids_uniprotkb.csv. The dataset is derived from 2019-09 UniProt release. If you use this dataset please provide proper attribution to EMBL-EBI-UniProtKB and GlyGen\n\nDescription Domain\n Keywords\n - publications\n - PMID\n - journal\n - citations\n - authors\n - UniProtKB\n - PubMed\n\n Pipeline Steps\n - Step-1: The script loads the UniProtKB publication data from the triplestore containing triples from nt file to retrieve the publication information associated with the UniProtKB accession and maps it to the UniProtKB canonical accessions. The script also filters out publications of large scale studies, and high frequency publications pertaining to DNA sequencing, cDNA, chromosomes using blacklisted PMIDs file.\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-homo-sapiens.nt\n URI: https://data.glygen.org/ln2wwwdata/source/uniprot-proteome-homo-sapiens.nt\n Name: human_protein_blacklisted_pmids_uniprotkb.csv\n URI: https://data.glygen.org/ln2wwwdata/compiled/human_protein_blacklisted_pmids_uniprotkb.csv\n Name: human_protein_masterlist.csv\n URI: https://data.glygen.org/ln2wwwdata/reviewed/human_protein_masterlist.csv\n Output Subdomain\n Name: human_protein_citations_uniprotkb.csv\n URI: http://data.glygen.org/ln2wwwdata/reviewed/human_protein_citations_uniprotkb.csv\n Name: human_protein_citations_uniprotkb.stat.csv\n URI: http://data.glygen.org/ln2wwwdata/reviewed/human_protein_citations_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/human_protein_citations_uniprotkb.csv" }