UniProtKB - P61244 (MAX_HUMAN)
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- BLAST>sp|P61244|MAX_HUMAN Protein max OS=Homo sapiens OX=9606 GN=MAX PE=1 SV=1 MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASR AQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQTNYPSSDN SLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS
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Protein
Protein max
Gene
MAX
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC:MAX complex is a transcriptional activator, whereas the MAD:MAX complex is a repressor. May repress transcription via the recruitment of a chromatin remodeling complex containing H3 'Lys-9' histone methyltransferase activity. Represses MYC transcriptional activity from E-box elements.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.22"Functional and in silico assessment of MAX variants of unknown significance."
Comino-Mendez I., Leandro-Garcia L.J., Montoya G., Inglada-Perez L., de Cubas A.A., Curras-Freixes M., Tysoe C., Izatt L., Leton R., Gomez-Grana A., Mancikova V., Apellaniz-Ruiz M., Mannelli M., Schiavi F., Favier J., Gimenez-Roqueplo A.P., Timmers H.J., Roncador G. , Garcia J.F., Rodriguez-Antona C., Robledo M., Cascon A.
J. Mol. Med. 93:1247-1255(2015) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS PCC LEU-9; ASN-23; TRP-25; 33-ARG--SER-160 DEL; CYS-35; TRP-60; SER-71; VAL-74; PRO-90; PRO-94; PRO-102 AND PRO-102, CHARACTERIZATION OF VARIANTS PCC LEU-9; ASN-23; TRP-25; 33-ARG--SER-160 DEL; CYS-35; TRP-60; SER-71; VAL-74; PRO-90; PRO-94 AND PRO-102, FUNCTION, VARIANTS THR-114 AND LEU-142, CHARACTERIZATION OF VARIANTS THR-114 AND LEU-142.
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- DNA binding Source: CAFA <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- DNA binding transcription factor activity Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- E-box binding Source: CAFA <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- protein-containing complex binding Source: Ensembl
- protein heterodimerization activity Source: Ensembl
- protein homodimerization activity Source: CAFA <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: NTNU_SB
- transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- transcription coactivator activity Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- transcription coregulator activity Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- cellular response to peptide hormone stimulus Source: Ensembl
- cellular response to starvation Source: Ensembl
- G1/S transition of mitotic cell cycle Source: Reactome
- negative regulation of G0 to G1 transition Source: Reactome
- negative regulation of transcription by RNA polymerase II Source: NTNU_SB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- neuron apoptotic process Source: Ensembl
- protein-containing complex assembly Source: Ensembl
- response to axon injury Source: Ensembl
- response to insulin Source: Ensembl
- retina development in camera-type eye Source: Ensembl
- transcription by RNA polymerase II Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Activator, DNA-binding, Repressor |
| Biological process | Transcription, Transcription regulation |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1362277 Transcription of E2F targets under negative control by DREAM complex R-HSA-69202 Cyclin E associated events during G1/S transition R-HSA-69656 Cyclin A:Cdk2-associated events at S phase entry R-HSA-8953750 Transcriptional Regulation by E2F6 |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P61244 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P61244 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Protein maxCuratedAlternative name(s): Class D basic helix-loop-helix protein 4 Short name: bHLHd4 Myc-associated factor XImported <p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000125952.18 |
Human Gene Nomenclature Database More...HGNCi | HGNC:6913 MAX |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 154950 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P61244 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Nucleus
- MLL1 complex Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- nuclear chromatin Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- nucleoplasm Source: Reactome
- nucleus Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- PML body Source: Ensembl
- RNA polymerase II transcription factor complex Source: NTNU_SB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Other locations
- cytoplasm Source: Ensembl
- dendrite Source: UniProtKB-SubCell
- protein-DNA complex Source: CAFA <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cell projection, Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Pheochromocytoma (PCC)3 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.18"Exome sequencing identifies MAX mutations as a cause of hereditary pheochromocytoma."
Comino-Mendez I., Gracia-Aznarez F.J., Schiavi F., Landa I., Leandro-Garcia L.J., Leton R., Honrado E., Ramos-Medina R., Caronia D., Pita G., Gomez-Grana A., de Cubas A.A., Inglada-Perez L., Maliszewska A., Taschin E., Bobisse S., Pica G., Loli P. , Hernandez-Lavado R., Diaz J.A., Gomez-Morales M., Gonzalez-Neira A., Roncador G., Rodriguez-Antona C., Benitez J., Mannelli M., Opocher G., Robledo M., Cascon A.
Nat. Genet. 43:663-667(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN PCC, VARIANTS PCC ASN-23; 33-ARG--SER-160 DEL; 75-ARG--SER-160 DEL AND PRO-94, VARIANT LEU-142. - Ref.21"MAX mutations cause hereditary and sporadic pheochromocytoma and paraganglioma."
Burnichon N., Cascon A., Schiavi F., Morales N.P., Comino-Mendez I., Abermil N., Inglada-Perez L., de Cubas A.A., Amar L., Barontini M., de Quiros S.B., Bertherat J., Bignon Y.J., Blok M.J., Bobisse S., Borrego S., Castellano M., Chanson P. , Chiara M.D., Corssmit E.P., Giacche M., de Krijger R.R., Ercolino T., Girerd X., Gomez-Garcia E.B., Gomez-Grana A., Guilhem I., Hes F.J., Honrado E., Korpershoek E., Lenders J.W., Leton R., Mensenkamp A.R., Merlo A., Mori L., Murat A., Pierre P., Plouin P.F., Prodanov T., Quesada-Charneco M., Qin N., Rapizzi E., Raymond V., Reisch N., Roncador G., Ruiz-Ferrer M., Schillo F., Stegmann A.P., Suarez C., Taschin E., Timmers H.J., Tops C.M., Urioste M., Beuschlein F., Pacak K., Mannelli M., Dahia P.L., Opocher G., Eisenhofer G., Gimenez-Roqueplo A.P., Robledo M.
Clin. Cancer Res. 18:2828-2837(2012) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS PCC LEU-9; TRP-25; 33-ARG--SER-160 DEL; CYS-35; 47-ARG--SER-52 DEL; TRP-60; SER-71; VAL-74; 75-ARG--SER-160 DEL; 82-GLN--SER-160 DEL; PRO-90 AND PRO-102. - Ref.22"Functional and in silico assessment of MAX variants of unknown significance."
Comino-Mendez I., Leandro-Garcia L.J., Montoya G., Inglada-Perez L., de Cubas A.A., Curras-Freixes M., Tysoe C., Izatt L., Leton R., Gomez-Grana A., Mancikova V., Apellaniz-Ruiz M., Mannelli M., Schiavi F., Favier J., Gimenez-Roqueplo A.P., Timmers H.J., Roncador G. , Garcia J.F., Rodriguez-Antona C., Robledo M., Cascon A.
J. Mol. Med. 93:1247-1255(2015) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS PCC LEU-9; ASN-23; TRP-25; 33-ARG--SER-160 DEL; CYS-35; TRP-60; SER-71; VAL-74; PRO-90; PRO-94; PRO-102 AND PRO-102, CHARACTERIZATION OF VARIANTS PCC LEU-9; ASN-23; TRP-25; 33-ARG--SER-160 DEL; CYS-35; TRP-60; SER-71; VAL-74; PRO-90; PRO-94 AND PRO-102, FUNCTION, VARIANTS THR-114 AND LEU-142, CHARACTERIZATION OF VARIANTS THR-114 AND LEU-142.
Ref.18
"Exome sequencing identifies MAX mutations as a cause of hereditary pheochromocytoma."
Comino-Mendez I., Gracia-Aznarez F.J., Schiavi F., Landa I., Leandro-Garcia L.J., Leton R., Honrado E., Ramos-Medina R., Caronia D., Pita G., Gomez-Grana A., de Cubas A.A., Inglada-Perez L., Maliszewska A., Taschin E., Bobisse S., Pica G., Loli P. , Hernandez-Lavado R., Diaz J.A., Gomez-Morales M., Gonzalez-Neira A., Roncador G., Rodriguez-Antona C., Benitez J., Mannelli M., Opocher G., Robledo M., Cascon A.
Nat. Genet. 43:663-667(2011) [PubMed] [Europe PMC] [Abstract]
Comino-Mendez I., Gracia-Aznarez F.J., Schiavi F., Landa I., Leandro-Garcia L.J., Leton R., Honrado E., Ramos-Medina R., Caronia D., Pita G., Gomez-Grana A., de Cubas A.A., Inglada-Perez L., Maliszewska A., Taschin E., Bobisse S., Pica G., Loli P. , Hernandez-Lavado R., Diaz J.A., Gomez-Morales M., Gonzalez-Neira A., Roncador G., Rodriguez-Antona C., Benitez J., Mannelli M., Opocher G., Robledo M., Cascon A.
Nat. Genet. 43:663-667(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PCC, VARIANTS PCC ASN-23; 33-ARG--SER-160 DEL; 75-ARG--SER-160 DEL AND PRO-94, VARIANT LEU-142.
Ref.21
"MAX mutations cause hereditary and sporadic pheochromocytoma and paraganglioma."
Burnichon N., Cascon A., Schiavi F., Morales N.P., Comino-Mendez I., Abermil N., Inglada-Perez L., de Cubas A.A., Amar L., Barontini M., de Quiros S.B., Bertherat J., Bignon Y.J., Blok M.J., Bobisse S., Borrego S., Castellano M., Chanson P. , Chiara M.D., Corssmit E.P., Giacche M., de Krijger R.R., Ercolino T., Girerd X., Gomez-Garcia E.B., Gomez-Grana A., Guilhem I., Hes F.J., Honrado E., Korpershoek E., Lenders J.W., Leton R., Mensenkamp A.R., Merlo A., Mori L., Murat A., Pierre P., Plouin P.F., Prodanov T., Quesada-Charneco M., Qin N., Rapizzi E., Raymond V., Reisch N., Roncador G., Ruiz-Ferrer M., Schillo F., Stegmann A.P., Suarez C., Taschin E., Timmers H.J., Tops C.M., Urioste M., Beuschlein F., Pacak K., Mannelli M., Dahia P.L., Opocher G., Eisenhofer G., Gimenez-Roqueplo A.P., Robledo M.
Clin. Cancer Res. 18:2828-2837(2012) [PubMed] [Europe PMC] [Abstract]
Burnichon N., Cascon A., Schiavi F., Morales N.P., Comino-Mendez I., Abermil N., Inglada-Perez L., de Cubas A.A., Amar L., Barontini M., de Quiros S.B., Bertherat J., Bignon Y.J., Blok M.J., Bobisse S., Borrego S., Castellano M., Chanson P. , Chiara M.D., Corssmit E.P., Giacche M., de Krijger R.R., Ercolino T., Girerd X., Gomez-Garcia E.B., Gomez-Grana A., Guilhem I., Hes F.J., Honrado E., Korpershoek E., Lenders J.W., Leton R., Mensenkamp A.R., Merlo A., Mori L., Murat A., Pierre P., Plouin P.F., Prodanov T., Quesada-Charneco M., Qin N., Rapizzi E., Raymond V., Reisch N., Roncador G., Ruiz-Ferrer M., Schillo F., Stegmann A.P., Suarez C., Taschin E., Timmers H.J., Tops C.M., Urioste M., Beuschlein F., Pacak K., Mannelli M., Dahia P.L., Opocher G., Eisenhofer G., Gimenez-Roqueplo A.P., Robledo M.
Clin. Cancer Res. 18:2828-2837(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PCC LEU-9; TRP-25; 33-ARG--SER-160 DEL; CYS-35; 47-ARG--SER-52 DEL; TRP-60; SER-71; VAL-74; 75-ARG--SER-160 DEL; 82-GLN--SER-160 DEL; PRO-90 AND PRO-102.
Ref.22
"Functional and in silico assessment of MAX variants of unknown significance."
Comino-Mendez I., Leandro-Garcia L.J., Montoya G., Inglada-Perez L., de Cubas A.A., Curras-Freixes M., Tysoe C., Izatt L., Leton R., Gomez-Grana A., Mancikova V., Apellaniz-Ruiz M., Mannelli M., Schiavi F., Favier J., Gimenez-Roqueplo A.P., Timmers H.J., Roncador G. , Garcia J.F., Rodriguez-Antona C., Robledo M., Cascon A.
J. Mol. Med. 93:1247-1255(2015) [PubMed] [Europe PMC] [Abstract]
Comino-Mendez I., Leandro-Garcia L.J., Montoya G., Inglada-Perez L., de Cubas A.A., Curras-Freixes M., Tysoe C., Izatt L., Leton R., Gomez-Grana A., Mancikova V., Apellaniz-Ruiz M., Mannelli M., Schiavi F., Favier J., Gimenez-Roqueplo A.P., Timmers H.J., Roncador G. , Garcia J.F., Rodriguez-Antona C., Robledo M., Cascon A.
J. Mol. Med. 93:1247-1255(2015) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PCC LEU-9; ASN-23; TRP-25; 33-ARG--SER-160 DEL; CYS-35; TRP-60; SER-71; VAL-74; PRO-90; PRO-94; PRO-102 AND PRO-102, CHARACTERIZATION OF VARIANTS PCC LEU-9; ASN-23; TRP-25; 33-ARG--SER-160 DEL; CYS-35; TRP-60; SER-71; VAL-74; PRO-90; PRO-94 AND PRO-102, FUNCTION, VARIANTS THR-114 AND LEU-142, CHARACTERIZATION OF VARIANTS THR-114 AND LEU-142.
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA catecholamine-producing tumor of chromaffin tissue of the adrenal medulla or sympathetic paraganglia. The cardinal symptom, reflecting the increased secretion of epinephrine and norepinephrine, is hypertension, which may be persistent or intermittent.
See also OMIM:171300| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079347 | 9 | V → L in PCC; does not repress MYC transcriptional activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079348 | 23 | D → N in PCC; unknown pathological significance; does not affect MYC transcriptional activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079349 | 25 | R → W in PCC; does not repress MYC transcriptional activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079350 | 33 – 160 | Missing in PCC; does not repress MYC transcriptional activity. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 128 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079351 | 35 | R → C in PCC; does not repress MYC transcriptional activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079352 | 47 – 52 | Missing in PCC; unknown pathological significance; somatic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 6 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079353 | 60 | R → W in PCC; does not repress MYC transcriptional activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079354 | 71 | I → S in PCC; does not repress MYC transcriptional activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079355 | 74 | M → V in PCC; does not repress MYC transcriptional activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079356 | 75 – 160 | Missing in PCC; unknown pathological significance. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 86 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079357 | 82 – 160 | Missing in PCC; unknown pathological significance. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 79 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079358 | 90 | R → P in PCC; does not repress MYC transcriptional activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079359 | 94 | L → P in PCC; does not repress MYC transcriptional activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079360 | 102 | L → P in PCC; does not repress MYC transcriptional activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 66 | K → Q: Kept nuclear localization. Loss of nuclear localization; when associated with Q-153 and Q-154. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 66 | K → R: Loss of acetylation, kept nuclear localization; when associated with R-153 and R-154. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 153 | K → Q: Loss of nuclear localization; when associated with Q-66 and Q-154. Kept nuclear localization; when associated with Q-154. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 153 | K → R: Loss of acetylation, kept nuclear localization; when associated with R-66 and R-154. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 154 | K → Q: Loss of nuclear localization; when associated with Q-66 and Q-153. Kept nuclear localization; when associated with Q-153. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 154 | K → R: Loss of acetylation, kept nuclear localization; when associated with R-66 and R-153. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Diseasei
Disease mutationOrganism-specific databases
DisGeNET More...DisGeNETi | 4149 |
GeneReviews a resource of expert-authored, peer-reviewed disease descriptions. More...GeneReviewsi | MAX |
MalaCards human disease database More...MalaCardsi | MAX |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 171300 phenotype |
Open Targets More...OpenTargetsi | ENSG00000125952 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 29072 Hereditary pheochromocytoma-paraganglioma |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA30656 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1250363 |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 47117704 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
|---|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | RemovedCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||||
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000127269 | 2 – 160 | Protein maxAdd BLAST | 159 | ||
| Isoform 2 (identifier: P61244-2) | |||||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | RemovedCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||||
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
|---|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2 | N-acetylserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 11 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 66 | N6-acetyllysine1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 107 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 153 | N6-acetyllysine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 154 | N6-acetyllysine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | ||
| Isoform 2 (identifier: P61244-2) | |||||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2 | N-acetylserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 11 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Reversible lysine acetylation might regulate the nuclear-cytoplasmic shuttling of specific Max complexes.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.13"Max is acetylated by p300 at several nuclear localization residues."
Faiola F., Wu Y.-T., Pan S., Zhang K., Farina A., Martinez E.
Biochem. J. 403:397-407(2007) [PubMed] [Europe PMC] [Abstract]Cited for: ACETYLATION AT LYS-66; LYS-153 AND LYS-154, MUTAGENESIS OF LYS-66; LYS-153 AND LYS-154.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P61244 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P61244 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P61244 |
PeptideAtlas More...PeptideAtlasi | P61244 |
PRoteomics IDEntifications database More...PRIDEi | P61244 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 57281 57282 [P61244-2] 57283 [P61244-3] 57284 [P61244-4] 57285 [P61244-5] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P61244 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P61244 |
Miscellaneous databases
CutDB - Proteolytic event database More...PMAP-CutDBi | P61244 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
High levels found in the brain, heart and lung while lower levels are seen in the liver, kidney and skeletal muscle.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000125952 |
CleanEx database of gene expression profiles More...CleanExi | HS_MAX |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P61244 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P61244 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB000328 HPA003474 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MYC or MAD. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with SPAG9. The heterodimer MYC:MAX interacts with ABI1; the interaction may enhance MYC:MAX transcriptional activity.2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.8"A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells."
Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.
Science 296:1132-1136(2002) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MGA; EUHMTASE1; BAT8; CBX3; RING1; RNF2; MBLR; L3MBTL2 AND YAF2. - Ref.10"Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| BANP | Q8N9N5 | 3 | EBI-751711,EBI-744695 | |
| E2F6 | O75461 | 4 | EBI-751711,EBI-749694 | |
| EEF1D | P29692 | 2 | EBI-751711,EBI-358607 | |
| EPAS1 | Q99814 | 2 | EBI-751711,EBI-447470 | |
| FOXK2 | Q01167 | 4 | EBI-751711,EBI-2509991 | |
| FTH1 | P02794 | 2 | EBI-751711,EBI-713259 | |
| GABBR1 | Q9UBS5 | 3 | EBI-751711,EBI-724156 | |
| H2AFY | O75367 | 2 | EBI-751711,EBI-2868511 | |
| L3MBTL2 | Q969R5 | 5 | EBI-751711,EBI-739909 | |
| LIG3 | P49916 | 2 | EBI-751711,EBI-1753381 | |
| MECP2 | P51608 | 2 | EBI-751711,EBI-1189067 | |
| MGA | Q8IWI9 | 4 | EBI-751711,EBI-2815196 | |
| MXD1 | Q05195 | 3 | EBI-751711,EBI-8833637 | |
| MXI1 | P50539 | 6 | EBI-751711,EBI-752241 | |
| MYC | P01106 | 37 | EBI-751711,EBI-447544 | |
| MYCN | P04198 | 10 | EBI-751711,EBI-878369 | |
| PLEKHF2 | Q9H8W4 | 3 | EBI-751711,EBI-742388 | |
| TFAP2A | P05549 | 2 | EBI-751711,EBI-347351 | |
| TFDP1 | Q14186 | 4 | EBI-751711,EBI-749713 | |
| UNC45A | Q9H3U1 | 3 | EBI-10218525,EBI-1048763 | |
| VRK3 | Q8IV63 | 2 | EBI-751711,EBI-1058605 | |
| XRCC1 | P18887 | 2 | EBI-751711,EBI-947466 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- protein heterodimerization activity Source: Ensembl
- protein homodimerization activity Source: CAFA <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 110319, 151 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-104 Transcriptional repressor Mad-Max complex CPX-91 Transcriptional activator Myc-Max complex |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P61244 |
Database of interacting proteins More...DIPi | DIP-28145N |
Protein interaction database and analysis system More...IntActi | P61244, 129 interactors |
Molecular INTeraction database More...MINTi | P61244 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000351490 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P61244 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 5 – 9 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 24 – 47 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 24 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 51 – 53 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 60 – 100 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 41 |
3D structure databases
Database of protein disorder More...DisProti | DP00084 DP01097 |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P61244 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P61244 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P61244 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 23 – 74 | bHLHPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 52 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 81 – 102 | Leucine-zipperAdd BLAST | 22 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 152 – 156 | Nuclear localization signal | 5 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the MAX family.Curated
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG2483 Eukaryota ENOG4111V1C LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00530000064011 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000293257 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG008542 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P61244 |
KEGG Orthology (KO) More...KOi | K04453 |
Identification of Orthologs from Complete Genome Data More...OMAi | RHTSTAN |
Database of Orthologous Groups More...OrthoDBi | EOG091G1312 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P61244 |
TreeFam database of animal gene trees More...TreeFami | TF318841 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00083 HLH, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 4.10.280.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR011598 bHLH_dom IPR036638 HLH_DNA-bd_sf IPR037933 MAX |
The PANTHER Classification System More...PANTHERi | PTHR10328 PTHR10328, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00010 HLH, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00353 HLH, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF47459 SSF47459, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50888 BHLH, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (6)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 6 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P61244-1) [UniParc]FASTAAdd to basketAdded to basketShow »
Also known as: Long
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.
10 20 30 40 50
MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV
60 70 80 90 100
PSLQGEKASR AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR
110 120 130 140 150
ALEKARSSAQ LQTNYPSSDN SLYTNAKGST ISAFDGGSDS SSESEPEEPQ
160
SRKKLRMEAS
Length:160
Mass (Da):18,275
Last modified:May 10, 2004 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iEB10F3137727A56F
Isoform 2 (identifier: P61244-2) [UniParc] [UniParc]FASTAAdd to basketAdded to basketShow »
Also known as: Short
The sequence of this isoform differs from the canonical sequence as follows:
13-21: Missing.
10 20 30 40 50
MSDNDDIEVE SDADKRAHHN ALERKRRDHI KDSFHSLRDS VPSLQGEKAS
60 70 80 90 100
RAQILDKATE YIQYMRRKNH THQQDIDDLK RQNALLEQQV RALEKARSSA
110 120 130 140 150
QLQTNYPSSD NSLYTNAKGS TISAFDGGSD SSSESEPEEP QSRKKLRMEA
S
Length:151
Mass (Da):17,202
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iCB69F6F5F39793FA
Isoform 3 (identifier: P61244-3) [UniParc] [UniParc]FASTAAdd to basketAdded to basket
Also known as: Delta-Max
The sequence of this isoform differs from the canonical sequence as follows:
99-160: VRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS → GESES
10 20 30 40 50
MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV
60 70 80 90 100
PSLQGEKASR AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQGE
SES
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »Length:103
Mass (Da):12,099
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i49DC1A0441FFA301
Isoform 4 (identifier: P61244-4) [UniParc]FASTAAdd to basketAdded to basketShow »
The sequence of this isoform differs from the canonical sequence as follows:
99-160: VRALEKARSS...SRKKLRMEAS → GEHPSSWGSW...VRASHGVCAQ
10 20 30 40 50
MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV
60 70 80 90 100
PSLQGEKASR AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQGE
110 120 130
HPSSWGSWPC CAPARSGFGT WACRVRASHG VCAQ
Length:134
Mass (Da):15,395
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iA2FFD0B98CF93275
Isoform 5 (identifier: P61244-5) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
58-160: ASRAQILDKA...SRKKLRMEAS → LYFLFWKLCT...QVHKKKECKI
10 20 30 40 50
MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV
60 70 80 90
PSLQGEKLYF LFWKLCTPVL HRQSLMQKCH TFISSYQVHK KKECKI
Note: No experimental confirmation available.
Show »Length:96
Mass (Da):11,455
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iD380F721DCF2D6C8
Isoform 6 (identifier: P61244-6) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
58-160: ASRAQILDKA...SRKKLRMEAS → GTKMKLTLPPVFPYEHLPFPTVFCHG
10 20 30 40 50
MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV
60 70 80
PSLQGEKGTK MKLTLPPVFP YEHLPFPTVF CHG
Note: No experimental confirmation available.
Show »Length:83
Mass (Da):9,599
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iFE0E966237003D47
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079347 | 9 | V → L in PCC; does not repress MYC transcriptional activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079348 | 23 | D → N in PCC; unknown pathological significance; does not affect MYC transcriptional activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079349 | 25 | R → W in PCC; does not repress MYC transcriptional activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079350 | 33 – 160 | Missing in PCC; does not repress MYC transcriptional activity. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 128 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079351 | 35 | R → C in PCC; does not repress MYC transcriptional activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079352 | 47 – 52 | Missing in PCC; unknown pathological significance; somatic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 6 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079353 | 60 | R → W in PCC; does not repress MYC transcriptional activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079354 | 71 | I → S in PCC; does not repress MYC transcriptional activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079355 | 74 | M → V in PCC; does not repress MYC transcriptional activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079356 | 75 – 160 | Missing in PCC; unknown pathological significance. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 86 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079357 | 82 – 160 | Missing in PCC; unknown pathological significance. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 79 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079358 | 90 | R → P in PCC; does not repress MYC transcriptional activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079359 | 94 | L → P in PCC; does not repress MYC transcriptional activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079360 | 102 | L → P in PCC; does not repress MYC transcriptional activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079361 | 114 | N → T Polymorphism; does not affect MYC transcriptional activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079362 | 142 | S → L Polymorphism; does not affect MYC transcriptional activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_002117 | 13 – 21 | Missing in isoform 2. 3 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 9 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_043430 | 58 – 160 | ASRAQ…RMEAS → LYFLFWKLCTPVLHRQSLMQ KCHTFISSYQVHKKKECKI in isoform 5. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 103 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_047661 | 58 – 160 | ASRAQ…RMEAS → GTKMKLTLPPVFPYEHLPFP TVFCHG in isoform 6. CuratedAdd BLAST | 103 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_002118 | 99 – 160 | VRALE…RMEAS → GESES in isoform 3. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 62 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_043183 | 99 – 160 | VRALE…RMEAS → GEHPSSWGSWPCCAPARSGF GTWACRVRASHGVCAQ in isoform 4. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 62 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | M64240 mRNA Translation: AAA36200.1 M64240 mRNA Translation: AAA36201.1 X66867 Genomic DNA Translation: CAA47337.1 X66867 Genomic DNA Translation: CAA47338.1 X66867 Genomic DNA Translation: CAA47339.1 X60287 mRNA Translation: CAA42827.1 AK290130 mRNA Translation: BAF82819.1 AK290929 mRNA Translation: BAF83618.1 AK292189 mRNA Translation: BAF84878.1 AK292630 mRNA Translation: BAF85319.1 AL139022 Genomic DNA No translation available. CH471061 Genomic DNA Translation: EAW80899.1 CH471061 Genomic DNA Translation: EAW80901.1 CH471061 Genomic DNA Translation: EAW80903.1 CH471061 Genomic DNA Translation: EAW80904.1 BC003525 mRNA Translation: AAH03525.1 BC004516 mRNA Translation: AAH04516.1 BC013669 mRNA Translation: AAH13669.1 BC027924 mRNA Translation: AAH27924.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS41965.1 [P61244-3] CCDS9770.1 [P61244-6] CCDS9771.1 CCDS9772.1 [P61244-2] CCDS9774.1 [P61244-5] |
Protein sequence database of the Protein Information Resource More...PIRi | A38431 A42611 B38431 S33118 |
NCBI Reference Sequences More...RefSeqi | NP_001257997.1, NM_001271068.1 NP_002373.3, NM_002382.4 [P61244-1] NP_660087.1, NM_145112.2 [P61244-2] NP_660088.1, NM_145113.2 [P61244-3] NP_660089.1, NM_145114.2 [P61244-5] NP_932061.1, NM_197957.3 [P61244-6] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.285354 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000246163; ENSP00000246163; ENSG00000125952 [P61244-5] ENST00000284165; ENSP00000284165; ENSG00000125952 [P61244-4] ENST00000341653; ENSP00000342482; ENSG00000125952 [P61244-6] ENST00000358402; ENSP00000351175; ENSG00000125952 [P61244-2] ENST00000358664; ENSP00000351490; ENSG00000125952 [P61244-1] ENST00000394606; ENSP00000378104; ENSG00000125952 [P61244-3] ENST00000553928; ENSP00000451907; ENSG00000125952 [P61244-3] ENST00000556979; ENSP00000452378; ENSG00000125952 [P61244-3] ENST00000618858; ENSP00000480127; ENSG00000125952 [P61244-3] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 4149 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:4149 |
UCSC genome browser More...UCSCi | uc001xic.3 human |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P61244 | Protein max | 160 | |||
| MAX isoform 7 | 160 | ||||
| MYC associated factor X | 160 | ||||
| MYC associated factor X | 160 | ||||
| MAX isoform 7 | 160 | ||||
| +21 | |||||
| P61244-2 | MAX isoform 2 | 151 | |||
| MYC associated factor X | 151 | ||||
| MYC associated factor X | 151 | ||||
| Protein max | 151 | ||||
| MYC associated factor X | 151 | ||||
| +17 | |||||
| P61244-3 | MYC associated factor X, isoform CRA_d | 103 | |||
| MAX isoform 13 | 103 | ||||
| MAX isoform 13 | 103 | ||||
| MYC associated factor X | 103 | ||||
| MYC associated factor X | 103 | ||||
| +8 | |||||
| P61244-4 | MAX isoform 6 | 134 | |||
| MAX isoform 6 | 134 | ||||
| P61244-6 | MAX isoform 1 | 83 | |||
| MYC associated factor X | 71 | ||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P61244 | Protein max | 160 | |||
| MAX isoform 7 | 160 | ||||
| MYC associated factor X | 160 | ||||
| MYC associated factor X | 160 | ||||
| MAX isoform 7 | 160 | ||||
| +70 | |||||
| P61244-2 | UPI00072E2770 | 185 | |||
| MYC associated factor X | 162 | ||||
| UPI0005F376C8 | 160 | ||||
| UPI0004422F13 | 160 | ||||
| MYC associated factor X | 160 | ||||
| +65 | |||||
| P61244-3 | MAX protein | 94 | |||
| Protein max isoform c | 94 | ||||
| MAX isoform 14 | 94 | ||||
| MAX isoform 14 | 94 | ||||
| UPI000980993F | 116 | ||||
| +23 | |||||
| P61244-4 | Protein max | 125 | |||
| MAX isoform 16 | 125 | ||||
| MAX isoform 16 | 125 | ||||
| MYC associated factor X | 135 | ||||
| UPI000A3430D8 | 115 | ||||
| +3 | |||||
| P61244-5 | MYC associated factor X | 104 | |||
| MYC associated factor X | 104 | ||||
| MYC associated factor X | 97 | ||||
| MAX isoform 17 | 96 | ||||
| MYC associated factor X | 96 | ||||
| +13 | |||||
| P61244-6 | MAX isoform 1 | 83 | |||
| MYC associated factor X | 71 | ||||
| MYC associated factor X | 83 | ||||
| MAX isoform 1 | 83 | ||||
| MYC associated factor X | 83 | ||||
| +10 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P61244 | Protein max | 160 | |||
| MAX isoform 7 | 160 | ||||
| MYC associated factor X | 160 | ||||
| MYC associated factor X | 160 | ||||
| MAX isoform 7 | 160 | ||||
| +123 | |||||
| P61244-2 | UPI00072E2770 | 185 | |||
| MYC associated factor X | 162 | ||||
| MYC associated factor X | 160 | ||||
| UPI0005F376C8 | 160 | ||||
| UPI0002C63DC2 | 160 | ||||
| +307 | |||||
| P61244-3 | MAX protein | 94 | |||
| Protein max isoform c | 94 | ||||
| MAX isoform 14 | 94 | ||||
| MAX isoform 14 | 94 | ||||
| UPI000980993F | 116 | ||||
| +35 | |||||
| P61244-4 | MAX protein | 94 | |||
| Protein max isoform c | 94 | ||||
| MAX isoform 14 | 94 | ||||
| MAX isoform 14 | 94 | ||||
| UPI000980993F | 116 | ||||
| +35 | |||||
| P61244-5 | MYC associated factor X | 104 | |||
| MYC associated factor X | 104 | ||||
| MYC associated factor X | 97 | ||||
| MAX isoform 17 | 96 | ||||
| MYC associated factor X | 96 | ||||
| +22 | |||||
| P61244-6 | MAX isoform 1 | 83 | |||
| MYC associated factor X | 71 | ||||
| MYC associated factor X | 83 | ||||
| MYC associated factor X | 83 | ||||
| MYC associated factor X | 83 | ||||
| +16 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | M64240 mRNA Translation: AAA36200.1 M64240 mRNA Translation: AAA36201.1 X66867 Genomic DNA Translation: CAA47337.1 X66867 Genomic DNA Translation: CAA47338.1 X66867 Genomic DNA Translation: CAA47339.1 X60287 mRNA Translation: CAA42827.1 AK290130 mRNA Translation: BAF82819.1 AK290929 mRNA Translation: BAF83618.1 AK292189 mRNA Translation: BAF84878.1 AK292630 mRNA Translation: BAF85319.1 AL139022 Genomic DNA No translation available. CH471061 Genomic DNA Translation: EAW80899.1 CH471061 Genomic DNA Translation: EAW80901.1 CH471061 Genomic DNA Translation: EAW80903.1 CH471061 Genomic DNA Translation: EAW80904.1 BC003525 mRNA Translation: AAH03525.1 BC004516 mRNA Translation: AAH04516.1 BC013669 mRNA Translation: AAH13669.1 BC027924 mRNA Translation: AAH27924.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS41965.1 [P61244-3] CCDS9770.1 [P61244-6] CCDS9771.1 CCDS9772.1 [P61244-2] CCDS9774.1 [P61244-5] |
Protein sequence database of the Protein Information Resource More...PIRi | A38431 A42611 B38431 S33118 |
NCBI Reference Sequences More...RefSeqi | NP_001257997.1, NM_001271068.1 NP_002373.3, NM_002382.4 [P61244-1] NP_660087.1, NM_145112.2 [P61244-2] NP_660088.1, NM_145113.2 [P61244-3] NP_660089.1, NM_145114.2 [P61244-5] NP_932061.1, NM_197957.3 [P61244-6] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.285354 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1AN2 | X-ray | 2.90 | A | 22-107 | [»] | |
| 1HLO | X-ray | 2.80 | A/B | 4-92 | [»] | |
| 1NKP | X-ray | 1.80 | B/E | 23-102 | [»] | |
| 1NLW | X-ray | 2.00 | B/E | 24-99 | [»] | |
| 1R05 | NMR | - | A/B | 22-103 | [»] | |
| 5EYO | X-ray | 2.39 | A/C | 22-107 | [»] | |
Database of protein disorder More...DisProti | DP00084 DP01097 | |||||
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P61244 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P61244 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 110319, 151 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-104 Transcriptional repressor Mad-Max complex CPX-91 Transcriptional activator Myc-Max complex |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P61244 |
Database of interacting proteins More...DIPi | DIP-28145N |
Protein interaction database and analysis system More...IntActi | P61244, 129 interactors |
Molecular INTeraction database More...MINTi | P61244 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000351490 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P61244 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1250363 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P61244 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P61244 |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 47117704 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P61244 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P61244 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P61244 |
PeptideAtlas More...PeptideAtlasi | P61244 |
PRoteomics IDEntifications database More...PRIDEi | P61244 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 57281 57282 [P61244-2] 57283 [P61244-3] 57284 [P61244-4] 57285 [P61244-5] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 4149 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000246163; ENSP00000246163; ENSG00000125952 [P61244-5] ENST00000284165; ENSP00000284165; ENSG00000125952 [P61244-4] ENST00000341653; ENSP00000342482; ENSG00000125952 [P61244-6] ENST00000358402; ENSP00000351175; ENSG00000125952 [P61244-2] ENST00000358664; ENSP00000351490; ENSG00000125952 [P61244-1] ENST00000394606; ENSP00000378104; ENSG00000125952 [P61244-3] ENST00000553928; ENSP00000451907; ENSG00000125952 [P61244-3] ENST00000556979; ENSP00000452378; ENSG00000125952 [P61244-3] ENST00000618858; ENSP00000480127; ENSG00000125952 [P61244-3] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 4149 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:4149 |
UCSC genome browser More...UCSCi | uc001xic.3 human |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 4149 |
DisGeNET More...DisGeNETi | 4149 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000125952.18 |
GeneCards: human genes, protein and diseases More...GeneCardsi | MAX |
GeneReviews a resource of expert-authored, peer-reviewed disease descriptions. More...GeneReviewsi | MAX |
Human Gene Nomenclature Database More...HGNCi | HGNC:6913 MAX |
Human Protein Atlas More...HPAi | CAB000328 HPA003474 |
MalaCards human disease database More...MalaCardsi | MAX |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 154950 gene 171300 phenotype |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P61244 |
Open Targets More...OpenTargetsi | ENSG00000125952 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 29072 Hereditary pheochromocytoma-paraganglioma |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA30656 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG2483 Eukaryota ENOG4111V1C LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00530000064011 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000293257 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG008542 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P61244 |
KEGG Orthology (KO) More...KOi | K04453 |
Identification of Orthologs from Complete Genome Data More...OMAi | RHTSTAN |
Database of Orthologous Groups More...OrthoDBi | EOG091G1312 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P61244 |
TreeFam database of animal gene trees More...TreeFami | TF318841 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1362277 Transcription of E2F targets under negative control by DREAM complex R-HSA-69202 Cyclin E associated events during G1/S transition R-HSA-69656 Cyclin A:Cdk2-associated events at S phase entry R-HSA-8953750 Transcriptional Regulation by E2F6 |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P61244 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P61244 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | MAX human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P61244 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | MAX_(gene) |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 4149 |
CutDB - Proteolytic event database More...PMAP-CutDBi | P61244 |
Protein Ontology More...PROi | PR:P61244 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000125952 |
CleanEx database of gene expression profiles More...CleanExi | HS_MAX |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P61244 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P61244 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd00083 HLH, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 4.10.280.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR011598 bHLH_dom IPR036638 HLH_DNA-bd_sf IPR037933 MAX |
The PANTHER Classification System More...PANTHERi | PTHR10328 PTHR10328, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00010 HLH, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00353 HLH, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF47459 SSF47459, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50888 BHLH, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | MAX_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P61244Primary (citable) accession number: P61244 Secondary accession number(s): A6NH73 , A8K265, A8K4G4, A8K824, P25912, P52163, Q14803, Q96CY8 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 10, 2004 |
| Last sequence update: | May 10, 2004 | |
| Last modified: | July 18, 2018 | |
| This is version 171 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any 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. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 14
Human chromosome 14: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
