UniProtKB - Q04637 (IF4G1_HUMAN)
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- BLAST>sp|Q04637|IF4G1_HUMAN Eukaryotic translation initiation factor 4 gamma 1 OS=Homo sapiens OX=9606 GN=EIF4G1 PE=1 SV=4 MNKAPQSTGPPPAPSPGLPQPAFPPGQTAPVVFSTPQATQMNTPSQPRQHFYPSRAQPPS SAASRVQSAAPARPGPAAHVYPAGSQVMMIPSQISYPASQGAYYIPGQGRSTYVVPTQQY PVQPGAPGFYPGASPTEFGTYAGAYYPAQGVQQFPTGVAPTPVLMNQPPQIAPKRERKTI RIRDPNQGGKDITEEIMSGARTASTPTPPQTGGGLEPQANGETPQVAVIVRPDDRSQGAI IADRPGLPGPEHSPSESQPSSPSPTPSPSPVLEPGSEPNLAVLSIPGDTMTTIQMSVEES TPISRETGEPYRLSPEPTPLAEPILEVEVTLSKPVPESEFSSSPLQAPTPLASHTVEIHE PNGMVPSEDLEPEVESSPELAPPPACPSESPVPIAPTAQPEELLNGAPSPPAVDLSPVSE PEEQAKEVTASMAPPTIPSATPATAPSATSPAQEEEMEEEEEEEEGEAGEAGEAESEKGG EELLPPESTPIPANLSQNLEAAAATQVAVSVPKRRRKIKELNKKEAVGDLLDAFKEANPA VPEVENQPPAGSNPGPESEGSGVPPRPEEADETWDSKEDKIHNAENIQPGEQKYEYKSDQ WKPLNLEEKKRYDREFLLGFQFIFASMQKPEGLPHISDVVLDKANKTPLRPLDPTRLQGI NCGPDFTPSFANLGRTTLSTRGPPRGGPGGELPRGPAGLGPRRSQQGPRKEPRKIIATVL MTEDIKLNKAEKAWKPSSKRTAADKDRGEEDADGSKTQDLFRRVRSILNKLTPQMFQQLM KQVTQLAIDTEERLKGVIDLIFEKAISEPNFSVAYANMCRCLMALKVPTTEKPTVTVNFR KLLLNRCQKEFEKDKDDDEVFEKKQKEMDEAATAEERGRLKEELEEARDIARRRSLGNIK FIGELFKLKMLTEAIMHDCVVKLLKNHDEESLECLCRLLTTIGKDLDFEKAKPRMDQYFN QMEKIIKEKKTSSRIRFMLQDVLDLRGSNWVPRRGDQGPKTIDQIHKEAEMEEHREHIKV QQLMAKGSDKRRGGPPGPPISRGLPLVDDGGWNTVPISKGSRPIDTSRLTKITKPGSIDS NNQLFAPGGRLSWGKGSSGGSGAKPSDAASEAARPATSTLNRFSALQQAVPTESTDNRRV VQRSSLSRERGEKAGDRGDRLERSERGGDRGDRLDRARTPATKRSFSKEVEERSRERPSQ PEGLRKAASLTEDRDRGRDAVKREAALPPVSPLKAALSEEELEKKSKAIIEEYLHLNDMK EAVQCVQELASPSLLFIFVRHGVESTLERSAIAREHMGQLLHQLLCAGHLSTAQYYQGLY EILELAEDMEIDIPHVWLYLAELVTPILQEGGVPMGELFREITKPLRPLGKAASLLLEIL GLLCKSMGPKKVGTLWREAGLSWKEFLPEGQDIGAFVAEQKVEYTLGEESEAPGQRALPS EELNRQLEKLLKEGSSNQRVFDWIEANLSEQQIVSNTLVRALMTAVCYSAIIFETPLRVD VAVLKARAKLLQKYLCDEQKELQALYALQALVVTLEQPPNLLRMFFDALYDEDVVKEDAF YSWESSKDPAEQQGKGVALKSVTAFFKWLREAEEESDHN
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Protein
Eukaryotic translation initiation factor 4 gamma 1
Gene
EIF4G1
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
Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome.
<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
- ATP binding Source: ParkinsonsUK-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
- eukaryotic initiation factor 4E binding Source: AgBase <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
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- mRNA binding Source: ParkinsonsUK-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
- protein-containing complex scaffold activity Source: ParkinsonsUK-UCL <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
- RNA binding Source: UniProtKBInferred from high throughput direct assayi
- translation factor activity, RNA binding Source: ParkinsonsUK-UCL <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
- translation initiation factor activity Source: UniProtKB <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
- translation initiation factor binding Source: ParkinsonsUK-UCL <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
- behavioral fear response Source: Ensembl
- cap-dependent translational initiation Source: ParkinsonsUK-UCL <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
- cellular macromolecule biosynthetic process Source: ParkinsonsUK-UCL <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
- cellular response to nutrient levels Source: ParkinsonsUK-UCL <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
- developmental process Source: ParkinsonsUK-UCL <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
- energy homeostasis Source: ParkinsonsUK-UCL <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
- mitochondrion organization Source: ParkinsonsUK-UCL <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
- negative regulation of autophagy Source: ParkinsonsUK-UCL <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
- negative regulation of neuron death Source: ParkinsonsUK-UCL <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
- negative regulation of peptidyl-threonine phosphorylation Source: ParkinsonsUK-UCL <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
- nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
- positive regulation of cell death Source: ParkinsonsUK-UCL <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
- positive regulation of cell growth Source: ParkinsonsUK-UCL <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
- positive regulation of cell proliferation Source: ParkinsonsUK-UCL <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
- positive regulation of cellular protein metabolic process Source: ParkinsonsUK-UCL <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
- positive regulation of eukaryotic translation initiation factor 4F complex assembly Source: ParkinsonsUK-UCL <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
- positive regulation of G1/S transition of mitotic cell cycle Source: ParkinsonsUK-UCL <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
- positive regulation of miRNA mediated inhibition of translation Source: ParkinsonsUK-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
- positive regulation of mRNA cap binding Source: ParkinsonsUK-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
- positive regulation of neuron differentiation Source: Ensembl
- positive regulation of peptidyl-serine phosphorylation Source: ParkinsonsUK-UCL <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
- regulation of cellular response to stress Source: ParkinsonsUK-UCL <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
- regulation of gene silencing by miRNA Source: ParkinsonsUK-UCL <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
- regulation of mRNA stability Source: Reactome
- regulation of polysome binding Source: ParkinsonsUK-UCL <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
- regulation of presynapse assembly Source: ParkinsonsUK-UCL <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
- regulation of translational initiation Source: UniProtKB <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
- translation Source: ParkinsonsUK-UCL <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
- translational initiation Source: ParkinsonsUK-UCL <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
- viral process Source: UniProtKB-KW
<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 | Initiation factor, RNA-binding, Translational shunt |
| Biological process | Host-virus interaction, Protein biosynthesis, Translation regulation |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1169408 ISG15 antiviral mechanism R-HSA-156827 L13a-mediated translational silencing of Ceruloplasmin expression R-HSA-166208 mTORC1-mediated signalling R-HSA-429947 Deadenylation of mRNA R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA R-HSA-72649 Translation initiation complex formation R-HSA-72662 Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S R-HSA-72702 Ribosomal scanning and start codon recognition R-HSA-72706 GTP hydrolysis and joining of the 60S ribosomal subunit R-HSA-9010553 Regulation of expression of SLITs and ROBOs R-HSA-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) R-HSA-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q04637 |
Protein family/group databases
MoonProt database of moonlighting proteins More...MoonProti | Q04637 |
<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: Eukaryotic translation initiation factor 4 gamma 1Short name: eIF-4-gamma 1 Short name: eIF-4G 1 Short name: eIF-4G1 Alternative name(s): p220 |
| <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 | Name:EIF4G1 Synonyms:EIF4F, EIF4G, EIF4GI |
| <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:ENSG00000114867.19 |
Human Gene Nomenclature Database More...HGNCi | HGNC:3296 EIF4G1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 600495 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q04637 |
<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
Cytosol
- cytosol Source: HPA
Nucleus
- nucleus Source: ParkinsonsUK-UCL <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
Other locations
- cytoplasm Source: AgBase <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
- eukaryotic translation initiation factor 4F complex Source: ParkinsonsUK-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
- membrane Source: UniProtKBInferred from high throughput direct assayi
- polysome Source: ParkinsonsUK-UCL <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>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
Parkinson disease 18 (PARK18)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.51"Translation initiator EIF4G1 mutations in familial Parkinson disease."
Chartier-Harlin M.C., Dachsel J.C., Vilarino-Guell C., Lincoln S.J., Lepretre F., Hulihan M.M., Kachergus J., Milnerwood A.J., Tapia L., Song M.S., Le Rhun E., Mutez E., Larvor L., Duflot A., Vanbesien-Mailliot C., Kreisler A., Ross O.A., Nishioka K. , Soto-Ortolaza A.I., Cobb S.A., Melrose H.L., Behrouz B., Keeling B.H., Bacon J.A., Hentati E., Williams L., Yanagiya A., Sonenberg N., Lockhart P.J., Zubair A.C., Uitti R.J., Aasly J.O., Krygowska-Wajs A., Opala G., Wszolek Z.K., Frigerio R., Maraganore D.M., Gosal D., Lynch T., Hutchinson M., Bentivoglio A.R., Valente E.M., Nichols W.C., Pankratz N., Foroud T., Gibson R.A., Hentati F., Dickson D.W., Destee A., Farrer M.J.
Am. J. Hum. Genet. 89:398-406(2011) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS PARK18 VAL-502 AND HIS-1205, VARIANTS SER-71; ALA-161; CYS-311; VAL-432; 466-GLY--ALA-468 DEL; CYS-686; VAL-806; SER-829; ARG-1164; TRP-1197; ALA-1229; PRO-1233 AND SER-1257.
Ref.51
"Translation initiator EIF4G1 mutations in familial Parkinson disease."
Chartier-Harlin M.C., Dachsel J.C., Vilarino-Guell C., Lincoln S.J., Lepretre F., Hulihan M.M., Kachergus J., Milnerwood A.J., Tapia L., Song M.S., Le Rhun E., Mutez E., Larvor L., Duflot A., Vanbesien-Mailliot C., Kreisler A., Ross O.A., Nishioka K. , Soto-Ortolaza A.I., Cobb S.A., Melrose H.L., Behrouz B., Keeling B.H., Bacon J.A., Hentati E., Williams L., Yanagiya A., Sonenberg N., Lockhart P.J., Zubair A.C., Uitti R.J., Aasly J.O., Krygowska-Wajs A., Opala G., Wszolek Z.K., Frigerio R., Maraganore D.M., Gosal D., Lynch T., Hutchinson M., Bentivoglio A.R., Valente E.M., Nichols W.C., Pankratz N., Foroud T., Gibson R.A., Hentati F., Dickson D.W., Destee A., Farrer M.J.
Am. J. Hum. Genet. 89:398-406(2011) [PubMed] [Europe PMC] [Abstract]
Chartier-Harlin M.C., Dachsel J.C., Vilarino-Guell C., Lincoln S.J., Lepretre F., Hulihan M.M., Kachergus J., Milnerwood A.J., Tapia L., Song M.S., Le Rhun E., Mutez E., Larvor L., Duflot A., Vanbesien-Mailliot C., Kreisler A., Ross O.A., Nishioka K. , Soto-Ortolaza A.I., Cobb S.A., Melrose H.L., Behrouz B., Keeling B.H., Bacon J.A., Hentati E., Williams L., Yanagiya A., Sonenberg N., Lockhart P.J., Zubair A.C., Uitti R.J., Aasly J.O., Krygowska-Wajs A., Opala G., Wszolek Z.K., Frigerio R., Maraganore D.M., Gosal D., Lynch T., Hutchinson M., Bentivoglio A.R., Valente E.M., Nichols W.C., Pankratz N., Foroud T., Gibson R.A., Hentati F., Dickson D.W., Destee A., Farrer M.J.
Am. J. Hum. Genet. 89:398-406(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PARK18 VAL-502 AND HIS-1205, VARIANTS SER-71; ALA-161; CYS-311; VAL-432; 466-GLY--ALA-468 DEL; CYS-686; VAL-806; SER-829; ARG-1164; TRP-1197; ALA-1229; PRO-1233 AND SER-1257.
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant, late-onset form of Parkinson disease. Parkinson disease is a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain.
See also OMIM:614251| 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_066573 | 502 | A → V in PARK18. 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_066579 | 1205 | R → H in PARK18. 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 |
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 | 174 – 178 | KRERK → AAAAA: Loss of PABPC1 binding; when associated with 184-AAAA-187. 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
| 5 | |
| <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 | 180 | I → A: Loss of PABPC1 binding. 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 | 182 | I → A: Loss of PABPC1 binding. 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 | 184 – 187 | DPNQ → AAAA: Loss of PABPC1 binding; when associated with 174-AAAAA-178. | 4 | |
| <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 | 192 | I → A: Loss of PABPC1 binding. 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 | 196 | I → A: Loss of PABPC1 binding. 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 | 612 | Y → A or F: Abolishes binding to EIF4E. 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 | 617 – 618 | LL → AA: Abolishes binding to EIF4E. 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
| 2 | |
| <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 | 682 | G → A, V, W, R or E: Reduced cleavage by protease 2A from human rhinovirus 2. 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 | 768 | L → A: Abolishes binding to EIF4A; when associated with A-770 and A-775. 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 | 771 | L → A: Abolishes binding to EIF4A; when associated with A-767 and A-775. 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 | 776 | F → A: Abolishes binding to EIF4A; when associated with A-767 and A-770. 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 | 842 – 843 | LL → AA: Abolishes binding to EIF4A; when associated with A-850 and K-851. 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
| 2 | |
| <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 | 851 – 852 | FE → AK: Abolishes binding to EIF4A; when associated with A-841 and A-842. 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
| 2 | |
| <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 | 896 | L → A: Abolishes binding to EIF4A; when associated with A-92 and A-95. 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 | 902 | I → A: Abolishes binding to EIF4A; when associated with A-895 and A-95. 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 | 905 | L → A: Abolishes binding to EIF4A; when associated with A-895 and A-92. 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 | 974 | R → A: Abolishes binding to EIF4A; when associated with A-976. 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 | 977 | F → A: Abolishes binding to EIF4A; when associated with A-973. 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 | 985 | L → A: Slightly reduced binding to EIF4A; when associated with A-989. 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 | 990 | W → A: Slightly reduced binding to EIF4A; when associated with A-984. 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 mutation, Neurodegeneration, Parkinson disease, ParkinsonismOrganism-specific databases
DisGeNET More...DisGeNETi | 1981 |
MalaCards human disease database More...MalaCardsi | EIF4G1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 614251 phenotype |
Open Targets More...OpenTargetsi | ENSG00000114867 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 2828 Young adult-onset Parkinsonism |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA27722 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | EIF4G1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 294862538 |
<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 ‘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_0000007786 | 1 – 1599 | Eukaryotic translation initiation factor 4 gamma 1Add BLAST | 1599 | ||
| Isoform C (identifier: Q04637-4) | |||||
| <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 | Removed | ||||
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 | 15 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 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 | 73 | Omega-N-methylarginineCombined 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 | 110 | Omega-N-methylarginineCombined 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 | 207 | PhosphothreonineCombined 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 | 223 | PhosphothreonineCombined 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 | 314 | 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 | 602 | N6-acetyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 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 | 647 | PhosphothreonineCombined 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 | 685 | Omega-N-methylarginineCombined 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 | 694 | Omega-N-methylarginineCombined 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 | 1028 | 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 | 1032 | Omega-N-methylarginineCombined 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 | 1042 | Omega-N-methylarginineCombined 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 | 1077 | 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 | 1092 | 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 | 1095 | N6-acetyllysineCombined 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 | 1145 | 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 | 1147 | 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 | 1185 | Phosphoserine; by PKC/PRKCACombined 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>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 | 1187 | 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 | 1194 | 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 | 1209 | 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 | 1211 | PhosphothreonineCombined 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 | 1231 | 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 | 1238 | 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 | 1596 | 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 | ||
| Isoform C (identifier: Q04637-4) | |||||
| <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-acetylmethionine | 1 | ||
| Isoform 7 (identifier: Q04637-7) | |||||
| <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 | 489 | Omega-N-methylarginine | 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 | 498 | Omega-N-methylarginine | 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 | 509 | Phosphoserine | 1 | ||
| Isoform 8 (identifier: Q04637-8) | |||||
| <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 | 685 | Omega-N-methylarginine | 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 | 694 | Omega-N-methylarginine | 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 | 705 | Phosphoserine | 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
Phosphorylated at multiple sites in vivo. Phosphorylation at Ser-1185 by PRKCA induces binding to MKNK1.1 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.39"Phosphorylation of eukaryotic translation initiation factor 4G1 (eIF4G1) by protein kinase C{alpha} regulates eIF4G1 binding to Mnk1."
Dobrikov M., Dobrikova E., Shveygert M., Gromeier M.
Mol. Cell. Biol. 31:2947-2959(2011) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT SER-1185.
Following infection by certain enteroviruses, rhinoviruses and aphthoviruses, EIF4G1 is cleaved by the viral protease 2A, or the leader protease in the case of aphthoviruses. This shuts down the capped cellular mRNA transcription.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.13"Mapping the cleavage site in protein synthesis initiation factor eIF-4 gamma of the 2A proteases from human Coxsackievirus and rhinovirus."
Lamphear B.J., Yan R., Yang F., Waters D., Liebig H.-D., Klump H., Kuechler E., Skern T., Rhoads R.E.
J. Biol. Chem. 268:19200-19203(1993) [PubMed] [Europe PMC] [Abstract]Cited for: CLEAVAGE BY RHINOVIRUS AND COXSACKIEVIRUS PROTEASE. - Ref.17"Poliovirus 2A proteinase cleaves directly the eIF-4G subunit of eIF-4F complex."
Ventoso I., MacMillan S.E., Hershey J.W., Carrasco L.
FEBS Lett. 435:79-83(1998) [PubMed] [Europe PMC] [Abstract]Cited for: CLEAVAGE BY POLIOVIRUS. - Ref.22"Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A in vitro."
Glaser W., Skern T.
FEBS Lett. 480:151-155(2000) [PubMed] [Europe PMC] [Abstract]Cited for: CLEAVAGE BY FMDV AND HRV-2.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 674 – 675 | Cleavage; by foot-and-mouth disease virus leader protease | 2 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 681 – 682 | Cleavage; by enterovirus/rhinovirus protease 2A | 2 |
<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, Methylation, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q04637 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q04637 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q04637 |
PeptideAtlas More...PeptideAtlasi | Q04637 |
PRoteomics IDEntifications database More...PRIDEi | Q04637 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 58250 58251 [Q04637-3] 58252 [Q04637-4] 58253 [Q04637-5] 58254 [Q04637-6] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q04637 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q04637 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q04637 |
Miscellaneous databases
CutDB - Proteolytic event database More...PMAP-CutDBi | Q04637 |
<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
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000114867 |
CleanEx database of gene expression profiles More...CleanExi | HS_EIF4G1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q04637 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q04637 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB014774 HPA028487 HPA043866 |
<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
eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E (cap-binding) and EIF4G1/EIF4G3. Interacts with eIF3, mutually exclusive with EIF4A1 or EIFA2, EIF4E and through its N-terminus with PAPBC1. Interacts through its C-terminus with the serine/threonine kinases MKNK1, and with MKNK2. Appears to act as a scaffold protein, holding these enzymes in place to phosphorylate EIF4E. Non-phosphorylated EIF4EBP1 competes with EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation. EIF4G1/EIF4G3 interacts with PABPC1 to bring about circularization of the mRNA. Rapamycin can attenuate insulin stimulation mediated by FKBPs. Interacts with EIF4E3. Interacts with CIRBP and MIF4GD. Interacts with RBM4. Interacts with HNRNPD/AUF1; the interaction requires RNA.15 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.2"A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation."
Imataka H., Gradi A., Sonenberg N.
EMBO J. 17:7480-7489(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), INTERACTION WITH PABPC1. - Ref.9"Rotavirus RNA binding protein NSP3, interacts with eIF-4GI and evicts the poly(A) binding protein from eIF4F."
Piron M., Vende P., Cohen J., Poncet D.
EMBO J. 17:5811-5821(1998) [PubMed] [Europe PMC] [Abstract] - Ref.10"Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A."
Imataka H., Sonenberg N.
Mol. Cell. Biol. 17:6940-6947(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-1599 (ISOFORM 8), INTERACTION WITH EIF4A, VARIANTS ALA-161 AND VAL-432, MUTAGENESIS OF LEU-768; LEU-771; PHE-776; 842-LEU-LEU-843; 851-PHE-GLU-852; LEU-896; ILE-902; LEU-905; ARG-974; PHE-977; LEU-985 AND TRP-990. - Ref.11"The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins."
Mader S., Lee H., Pause A., Sonenberg N.
Mol. Cell. Biol. 15:4990-4997(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 605-721, INTERACTION WITH EIF4E, MUTAGENESIS OF TYR-612 AND 617-LEU-LEU-618. - Ref.14"Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function."
Pause A., Belsham G.J., Gingras A.-C., Donze O., Lin T.-A., Lawrence J.C. Jr., Sonenberg N.
Nature 371:762-767(1994) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH EIF4E. - Ref.15"Repression of cap-dependent translation by 4E-binding protein 1: competition with p220 for binding to eukaryotic initiation factor-4E."
Haghighat A., Mader S., Pause A., Sonenberg N.
EMBO J. 14:5701-5709(1995) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH EIF4E AND EIF4EBP1. - Ref.19"Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E."
Pyronnet S., Imataka H., Gingras A.-C., Fukunaga R., Hunter T., Sonenberg N.
EMBO J. 18:270-279(1999) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH MKNK1. - Ref.20"Interaction of eIF4G with poly(A)-binding protein stimulates translation and is critical for Xenopus oocyte maturation."
Wakiyama M., Imataka H., Sonenberg N.
Curr. Biol. 10:1147-1150(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PABPC1, MUTAGENESIS OF 174-LYS--LYS-178 AND 184-ASP--GLN-197. - Ref.21"Multiple portions of poly(A)-binding protein stimulate translation in vivo."
Gray N.K., Coller J.M., Dickson K.S., Wickens M.
EMBO J. 19:4723-4733(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PABPC1. - Ref.23"The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a eukaryotic initiation factor 4E kinase with high levels of basal activity in mammalian cells."
Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.
Mol. Cell. Biol. 21:743-754(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH MKNK2. - Ref.27"Post-transcriptional regulation of thioredoxin by the stress inducible heterogeneous ribonucleoprotein A18."
Yang R., Weber D.J., Carrier F.
Nucleic Acids Res. 34:1224-1236(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CIRBP. - Ref.29"Cell stress modulates the function of splicing regulatory protein RBM4 in translation control."
Lin J.C., Hsu M., Tarn W.Y.
Proc. Natl. Acad. Sci. U.S.A. 104:2235-2240(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RBM4. - Ref.32"SLIP1, a factor required for activation of histone mRNA translation by the stem-loop binding protein."
Cakmakci N.G., Lerner R.S., Wagner E.J., Zheng L., Marzluff W.F.
Mol. Cell. Biol. 28:1182-1194(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH MIF4GD. - Ref.48"Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization."
Groft C.M., Burley S.K.
Mol. Cell 9:1273-1283(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 172-199 IN COMPLEX WITH ROTAVIRAL NSP3, INTERACTION WITH PABPC1, MUTAGENESIS OF ILE-180; ILE-182; ILE-192 AND ILE-196.
(Microbial infection) Interacts with rotavirus A NSP3; in this interaction, NSP3 takes the place of PABPC1 thereby inducing shutoff of host protein synthesis.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.31"Nuclear localization of cytoplasmic poly(A)-binding protein upon rotavirus infection involves the interaction of NSP3 with eIF4G and RoXaN."
Harb M., Becker M.M., Vitour D., Baron C.H., Vende P., Brown S.C., Bolte S., Arold S.T., Poncet D.
J. Virol. 82:11283-11293(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ROTAVIRUS A NSP3 (MICROBIAL INFECTION).
(Microbial infection) Interacts with human adenovirus 5 protein 100K; this interaction promotes translational shunt in presence of polysomes containing viral tripartite leader mRNAs.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.24"Tethering of eIF4G to adenoviral mRNAs by viral 100k protein drives ribosome shunting."
Xi Q., Cuesta R., Schneider R.J.
Genes Dev. 18:1997-2009(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HADV5 100K PROTEIN (MICROBIAL INFECTION).
<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 |
|---|---|---|---|---|
| itself | 2 | EBI-73711,EBI-73711 | ||
| DDX3X | O00571 | 3 | EBI-73711,EBI-353779 | |
| EIF3J | O75822 | 2 | EBI-73711,EBI-366647 | |
| EIF4A1 | P60842 | 15 | EBI-73711,EBI-73449 | |
| EIF4A2 | Q14240 | 4 | EBI-73711,EBI-73473 | |
| EIF4E | P06730 | 9 | EBI-73711,EBI-73440 | |
| HNRNPD | Q14103-4 | 3 | EBI-73711,EBI-432545 | |
| MKNK1 | Q9BUB5 | 2 | EBI-73711,EBI-73837 | |
| PABPC1 | P11940 | 6 | EBI-73711,EBI-81531 | |
| RBM4 | Q9BWF3-1 | 4 | EBI-73711,EBI-15621561 | |
| UL54 | Q9J0X9 | 3 | EBI-73711,EBI-7967856 | From Human herpesvirus 1. |
| ZC3H7B | Q9UGR2 | 3 | EBI-73711,EBI-948845 |
<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
- eukaryotic initiation factor 4E binding Source: AgBase <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
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein-containing complex scaffold activity Source: ParkinsonsUK-UCL <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
- translation initiation factor binding Source: ParkinsonsUK-UCL <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
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 108296, 104 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q04637 |
Database of interacting proteins More...DIPi | DIP-1161N |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | Q04637 |
Protein interaction database and analysis system More...IntActi | Q04637, 80 interactors |
Molecular INTeraction database More...MINTi | Q04637 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000338020 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q04637 |
<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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 181 – 183 | 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 | 185 – 187 | 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 | 193 – 197 | 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 | 614 – 618 | 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 hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 619 – 622 | 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 | 4 | |
| <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 | 624 – 627 | 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 | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 637 – 639 | 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 | 1234 – 1256 | 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 | 23 | |
| <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 | 1259 – 1267 | 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 | 9 | |
| <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 | 1272 – 1274 | 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 | 1275 – 1286 | 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 | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 1287 – 1289 | 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 | 1291 – 1306 | 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 | 16 | |
| <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 | 1312 – 1329 | 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 | 18 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 1330 – 1332 | 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 | 1336 – 1344 | 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 | 9 | |
| <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 | 1345 – 1348 | 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 | 4 | |
| <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 | 1355 – 1362 | 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 | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 1363 – 1365 | 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 | 1366 – 1369 | 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 | 4 | |
| <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 | 1372 – 1387 | 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 | 16 | |
| <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 | 1389 – 1398 | 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 | 10 | |
| <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 | 1403 – 1405 | 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 | 1413 – 1419 | 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 | 7 | |
| <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 | 1423 – 1425 | 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 | 1439 – 1452 | 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 | 14 | |
| <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 | 1457 – 1467 | 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 | 11 | |
| <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 | 1470 – 1473 | 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 | 4 | |
| <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 | 1476 – 1489 | 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 | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 1494 – 1496 | 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 | 1501 – 1514 | 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 | 14 | |
| <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 | 1518 – 1534 | 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 | 17 | |
| <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 | 1541 – 1551 | 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 | 11 | |
| <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 | 1557 – 1563 | 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 | 7 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q04637 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q04637 |
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 | Q04637 |
<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 | 565 – 792 | MIF4GPROSITE-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 | 228 | |
| <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 | 1241 – 1363 | MIPROSITE-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 | 123 | |
| <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 | 1433 – 1599 | W2PROSITE-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 | 167 |
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 | 172 – 200 | PABPC1-bindingAdd BLAST | 29 | |
| <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 | 607 – 618 | EIF4E-bindingAdd BLAST | 12 | |
| <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 | 682 – 1085 | eIF3/EIF4A-bindingAdd BLAST | 404 | |
| <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 | 1450 – 1599 | EIF4A-bindingAdd BLAST | 150 | |
| <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 | 1585 – 1599 | Necessary but not sufficient for MKNK1-bindingAdd BLAST | 15 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 454 – 467 | Poly-GluAdd BLAST | 14 | |
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 501 – 504 | Poly-Ala | 4 |
<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 eukaryotic initiation factor 4G family.Curated
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0401 Eukaryota ENOG410XS4P LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00530000063038 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000231658 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG052083 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q04637 |
KEGG Orthology (KO) More...KOi | K03260 |
Identification of Orthologs from Complete Genome Data More...OMAi | EMNKAPQ |
Database of Orthologous Groups More...OrthoDBi | EOG091G03ZW |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q04637 |
TreeFam database of animal gene trees More...TreeFami | TF101527 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.25.40.180, 3 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR016024 ARM-type_fold IPR037584 EIF4G1 IPR003891 Initiation_fac_eIF4g_MI IPR016021 MIF4-like_sf IPR003890 MIF4G-like_typ-3 IPR003307 W2_domain |
The PANTHER Classification System More...PANTHERi | PTHR23253:SF10 PTHR23253:SF10, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF02847 MA3, 1 hit PF02854 MIF4G, 1 hit PF02020 W2, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00515 eIF5C, 1 hit SM00544 MA3, 1 hit SM00543 MIF4G, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF48371 SSF48371, 3 hits |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51366 MI, 1 hit PS51363 W2, 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 (8)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 8 <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 and alternative initiation. AlignAdd to basketAdded to basket
Isoform A (identifier: Q04637-1) [UniParc]FASTAAdd to basketAdded to basketShow »
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
MNKAPQSTGP PPAPSPGLPQ PAFPPGQTAP VVFSTPQATQ MNTPSQPRQH
60 70 80 90 100
FYPSRAQPPS SAASRVQSAA PARPGPAAHV YPAGSQVMMI PSQISYPASQ
110 120 130 140 150
GAYYIPGQGR STYVVPTQQY PVQPGAPGFY PGASPTEFGT YAGAYYPAQG
160 170 180 190 200
VQQFPTGVAP TPVLMNQPPQ IAPKRERKTI RIRDPNQGGK DITEEIMSGA
210 220 230 240 250
RTASTPTPPQ TGGGLEPQAN GETPQVAVIV RPDDRSQGAI IADRPGLPGP
260 270 280 290 300
EHSPSESQPS SPSPTPSPSP VLEPGSEPNL AVLSIPGDTM TTIQMSVEES
310 320 330 340 350
TPISRETGEP YRLSPEPTPL AEPILEVEVT LSKPVPESEF SSSPLQAPTP
360 370 380 390 400
LASHTVEIHE PNGMVPSEDL EPEVESSPEL APPPACPSES PVPIAPTAQP
410 420 430 440 450
EELLNGAPSP PAVDLSPVSE PEEQAKEVTA SMAPPTIPSA TPATAPSATS
460 470 480 490 500
PAQEEEMEEE EEEEEGEAGE AGEAESEKGG EELLPPESTP IPANLSQNLE
510 520 530 540 550
AAAATQVAVS VPKRRRKIKE LNKKEAVGDL LDAFKEANPA VPEVENQPPA
560 570 580 590 600
GSNPGPESEG SGVPPRPEEA DETWDSKEDK IHNAENIQPG EQKYEYKSDQ
610 620 630 640 650
WKPLNLEEKK RYDREFLLGF QFIFASMQKP EGLPHISDVV LDKANKTPLR
660 670 680 690 700
PLDPTRLQGI NCGPDFTPSF ANLGRTTLST RGPPRGGPGG ELPRGPAGLG
710 720 730 740 750
PRRSQQGPRK EPRKIIATVL MTEDIKLNKA EKAWKPSSKR TAADKDRGEE
760 770 780 790 800
DADGSKTQDL FRRVRSILNK LTPQMFQQLM KQVTQLAIDT EERLKGVIDL
810 820 830 840 850
IFEKAISEPN FSVAYANMCR CLMALKVPTT EKPTVTVNFR KLLLNRCQKE
860 870 880 890 900
FEKDKDDDEV FEKKQKEMDE AATAEERGRL KEELEEARDI ARRRSLGNIK
910 920 930 940 950
FIGELFKLKM LTEAIMHDCV VKLLKNHDEE SLECLCRLLT TIGKDLDFEK
960 970 980 990 1000
AKPRMDQYFN QMEKIIKEKK TSSRIRFMLQ DVLDLRGSNW VPRRGDQGPK
1010 1020 1030 1040 1050
TIDQIHKEAE MEEHREHIKV QQLMAKGSDK RRGGPPGPPI SRGLPLVDDG
1060 1070 1080 1090 1100
GWNTVPISKG SRPIDTSRLT KITKPGSIDS NNQLFAPGGR LSWGKGSSGG
1110 1120 1130 1140 1150
SGAKPSDAAS EAARPATSTL NRFSALQQAV PTESTDNRRV VQRSSLSRER
1160 1170 1180 1190 1200
GEKAGDRGDR LERSERGGDR GDRLDRARTP ATKRSFSKEV EERSRERPSQ
1210 1220 1230 1240 1250
PEGLRKAASL TEDRDRGRDA VKREAALPPV SPLKAALSEE ELEKKSKAII
1260 1270 1280 1290 1300
EEYLHLNDMK EAVQCVQELA SPSLLFIFVR HGVESTLERS AIAREHMGQL
1310 1320 1330 1340 1350
LHQLLCAGHL STAQYYQGLY EILELAEDME IDIPHVWLYL AELVTPILQE
1360 1370 1380 1390 1400
GGVPMGELFR EITKPLRPLG KAASLLLEIL GLLCKSMGPK KVGTLWREAG
1410 1420 1430 1440 1450
LSWKEFLPEG QDIGAFVAEQ KVEYTLGEES EAPGQRALPS EELNRQLEKL
1460 1470 1480 1490 1500
LKEGSSNQRV FDWIEANLSE QQIVSNTLVR ALMTAVCYSA IIFETPLRVD
1510 1520 1530 1540 1550
VAVLKARAKL LQKYLCDEQK ELQALYALQA LVVTLEQPPN LLRMFFDALY
1560 1570 1580 1590
DEDVVKEDAF YSWESSKDPA EQQGKGVALK SVTAFFKWLR EAEEESDHN
Length:1,599
Mass (Da):175,491
Last modified:April 20, 2010 - v4
<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:i324088B60863DA34
Isoform B (identifier: Q04637-3) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-40: Missing.
10 20 30 40 50
MNTPSQPRQH FYPSRAQPPS SAASRVQSAA PARPGPAAHV YPAGSQVMMI
60 70 80 90 100
PSQISYPASQ GAYYIPGQGR STYVVPTQQY PVQPGAPGFY PGASPTEFGT
110 120 130 140 150
YAGAYYPAQG VQQFPTGVAP TPVLMNQPPQ IAPKRERKTI RIRDPNQGGK
160 170 180 190 200
DITEEIMSGA RTASTPTPPQ TGGGLEPQAN GETPQVAVIV RPDDRSQGAI
210 220 230 240 250
IADRPGLPGP EHSPSESQPS SPSPTPSPSP VLEPGSEPNL AVLSIPGDTM
260 270 280 290 300
TTIQMSVEES TPISRETGEP YRLSPEPTPL AEPILEVEVT LSKPVPESEF
310 320 330 340 350
SSSPLQAPTP LASHTVEIHE PNGMVPSEDL EPEVESSPEL APPPACPSES
360 370 380 390 400
PVPIAPTAQP EELLNGAPSP PAVDLSPVSE PEEQAKEVTA SMAPPTIPSA
410 420 430 440 450
TPATAPSATS PAQEEEMEEE EEEEEGEAGE AGEAESEKGG EELLPPESTP
460 470 480 490 500
IPANLSQNLE AAAATQVAVS VPKRRRKIKE LNKKEAVGDL LDAFKEANPA
510 520 530 540 550
VPEVENQPPA GSNPGPESEG SGVPPRPEEA DETWDSKEDK IHNAENIQPG
560 570 580 590 600
EQKYEYKSDQ WKPLNLEEKK RYDREFLLGF QFIFASMQKP EGLPHISDVV
610 620 630 640 650
LDKANKTPLR PLDPTRLQGI NCGPDFTPSF ANLGRTTLST RGPPRGGPGG
660 670 680 690 700
ELPRGPAGLG PRRSQQGPRK EPRKIIATVL MTEDIKLNKA EKAWKPSSKR
710 720 730 740 750
TAADKDRGEE DADGSKTQDL FRRVRSILNK LTPQMFQQLM KQVTQLAIDT
760 770 780 790 800
EERLKGVIDL IFEKAISEPN FSVAYANMCR CLMALKVPTT EKPTVTVNFR
810 820 830 840 850
KLLLNRCQKE FEKDKDDDEV FEKKQKEMDE AATAEERGRL KEELEEARDI
860 870 880 890 900
ARRRSLGNIK FIGELFKLKM LTEAIMHDCV VKLLKNHDEE SLECLCRLLT
910 920 930 940 950
TIGKDLDFEK AKPRMDQYFN QMEKIIKEKK TSSRIRFMLQ DVLDLRGSNW
960 970 980 990 1000
VPRRGDQGPK TIDQIHKEAE MEEHREHIKV QQLMAKGSDK RRGGPPGPPI
1010 1020 1030 1040 1050
SRGLPLVDDG GWNTVPISKG SRPIDTSRLT KITKPGSIDS NNQLFAPGGR
1060 1070 1080 1090 1100
LSWGKGSSGG SGAKPSDAAS EAARPATSTL NRFSALQQAV PTESTDNRRV
1110 1120 1130 1140 1150
VQRSSLSRER GEKAGDRGDR LERSERGGDR GDRLDRARTP ATKRSFSKEV
1160 1170 1180 1190 1200
EERSRERPSQ PEGLRKAASL TEDRDRGRDA VKREAALPPV SPLKAALSEE
1210 1220 1230 1240 1250
ELEKKSKAII EEYLHLNDMK EAVQCVQELA SPSLLFIFVR HGVESTLERS
1260 1270 1280 1290 1300
AIAREHMGQL LHQLLCAGHL STAQYYQGLY EILELAEDME IDIPHVWLYL
1310 1320 1330 1340 1350
AELVTPILQE GGVPMGELFR EITKPLRPLG KAASLLLEIL GLLCKSMGPK
1360 1370 1380 1390 1400
KVGTLWREAG LSWKEFLPEG QDIGAFVAEQ KVEYTLGEES EAPGQRALPS
1410 1420 1430 1440 1450
EELNRQLEKL LKEGSSNQRV FDWIEANLSE QQIVSNTLVR ALMTAVCYSA
1460 1470 1480 1490 1500
IIFETPLRVD VAVLKARAKL LQKYLCDEQK ELQALYALQA LVVTLEQPPN
1510 1520 1530 1540 1550
LLRMFFDALY DEDVVKEDAF YSWESSKDPA EQQGKGVALK SVTAFFKWLR
EAEEESDHN
Note: Produced by alternative initiation at Met-41 of isoform A.
Show »Length:1,559
Mass (Da):171,514
<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:i22F62E219E629C0E
Isoform C (identifier: Q04637-4) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-87: Missing.
10 20 30 40 50
MMIPSQISYP ASQGAYYIPG QGRSTYVVPT QQYPVQPGAP GFYPGASPTE
60 70 80 90 100
FGTYAGAYYP AQGVQQFPTG VAPTPVLMNQ PPQIAPKRER KTIRIRDPNQ
110 120 130 140 150
GGKDITEEIM SGARTASTPT PPQTGGGLEP QANGETPQVA VIVRPDDRSQ
160 170 180 190 200
GAIIADRPGL PGPEHSPSES QPSSPSPTPS PSPVLEPGSE PNLAVLSIPG
210 220 230 240 250
DTMTTIQMSV EESTPISRET GEPYRLSPEP TPLAEPILEV EVTLSKPVPE
260 270 280 290 300
SEFSSSPLQA PTPLASHTVE IHEPNGMVPS EDLEPEVESS PELAPPPACP
310 320 330 340 350
SESPVPIAPT AQPEELLNGA PSPPAVDLSP VSEPEEQAKE VTASMAPPTI
360 370 380 390 400
PSATPATAPS ATSPAQEEEM EEEEEEEEGE AGEAGEAESE KGGEELLPPE
410 420 430 440 450
STPIPANLSQ NLEAAAATQV AVSVPKRRRK IKELNKKEAV GDLLDAFKEA
460 470 480 490 500
NPAVPEVENQ PPAGSNPGPE SEGSGVPPRP EEADETWDSK EDKIHNAENI
510 520 530 540 550
QPGEQKYEYK SDQWKPLNLE EKKRYDREFL LGFQFIFASM QKPEGLPHIS
560 570 580 590 600
DVVLDKANKT PLRPLDPTRL QGINCGPDFT PSFANLGRTT LSTRGPPRGG
610 620 630 640 650
PGGELPRGPA GLGPRRSQQG PRKEPRKIIA TVLMTEDIKL NKAEKAWKPS
660 670 680 690 700
SKRTAADKDR GEEDADGSKT QDLFRRVRSI LNKLTPQMFQ QLMKQVTQLA
710 720 730 740 750
IDTEERLKGV IDLIFEKAIS EPNFSVAYAN MCRCLMALKV PTTEKPTVTV
760 770 780 790 800
NFRKLLLNRC QKEFEKDKDD DEVFEKKQKE MDEAATAEER GRLKEELEEA
810 820 830 840 850
RDIARRRSLG NIKFIGELFK LKMLTEAIMH DCVVKLLKNH DEESLECLCR
860 870 880 890 900
LLTTIGKDLD FEKAKPRMDQ YFNQMEKIIK EKKTSSRIRF MLQDVLDLRG
910 920 930 940 950
SNWVPRRGDQ GPKTIDQIHK EAEMEEHREH IKVQQLMAKG SDKRRGGPPG
960 970 980 990 1000
PPISRGLPLV DDGGWNTVPI SKGSRPIDTS RLTKITKPGS IDSNNQLFAP
1010 1020 1030 1040 1050
GGRLSWGKGS SGGSGAKPSD AASEAARPAT STLNRFSALQ QAVPTESTDN
1060 1070 1080 1090 1100
RRVVQRSSLS RERGEKAGDR GDRLERSERG GDRGDRLDRA RTPATKRSFS
1110 1120 1130 1140 1150
KEVEERSRER PSQPEGLRKA ASLTEDRDRG RDAVKREAAL PPVSPLKAAL
1160 1170 1180 1190 1200
SEEELEKKSK AIIEEYLHLN DMKEAVQCVQ ELASPSLLFI FVRHGVESTL
1210 1220 1230 1240 1250
ERSAIAREHM GQLLHQLLCA GHLSTAQYYQ GLYEILELAE DMEIDIPHVW
1260 1270 1280 1290 1300
LYLAELVTPI LQEGGVPMGE LFREITKPLR PLGKAASLLL EILGLLCKSM
1310 1320 1330 1340 1350
GPKKVGTLWR EAGLSWKEFL PEGQDIGAFV AEQKVEYTLG EESEAPGQRA
1360 1370 1380 1390 1400
LPSEELNRQL EKLLKEGSSN QRVFDWIEAN LSEQQIVSNT LVRALMTAVC
1410 1420 1430 1440 1450
YSAIIFETPL RVDVAVLKAR AKLLQKYLCD EQKELQALYA LQALVVTLEQ
1460 1470 1480 1490 1500
PPNLLRMFFD ALYDEDVVKE DAFYSWESSK DPAEQQGKGV ALKSVTAFFK
1510
WLREAEEESD HN
Note: Produced by alternative initiation at Met-88 of isoform A.
Show »Length:1,512
Mass (Da):166,619
<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:i09DD6DC263462CB6
Isoform D (identifier: Q04637-5) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-164: Missing.
10 20 30 40 50
MNQPPQIAPK RERKTIRIRD PNQGGKDITE EIMSGARTAS TPTPPQTGGG
60 70 80 90 100
LEPQANGETP QVAVIVRPDD RSQGAIIADR PGLPGPEHSP SESQPSSPSP
110 120 130 140 150
TPSPSPVLEP GSEPNLAVLS IPGDTMTTIQ MSVEESTPIS RETGEPYRLS
160 170 180 190 200
PEPTPLAEPI LEVEVTLSKP VPESEFSSSP LQAPTPLASH TVEIHEPNGM
210 220 230 240 250
VPSEDLEPEV ESSPELAPPP ACPSESPVPI APTAQPEELL NGAPSPPAVD
260 270 280 290 300
LSPVSEPEEQ AKEVTASMAP PTIPSATPAT APSATSPAQE EEMEEEEEEE
310 320 330 340 350
EGEAGEAGEA ESEKGGEELL PPESTPIPAN LSQNLEAAAA TQVAVSVPKR
360 370 380 390 400
RRKIKELNKK EAVGDLLDAF KEANPAVPEV ENQPPAGSNP GPESEGSGVP
410 420 430 440 450
PRPEEADETW DSKEDKIHNA ENIQPGEQKY EYKSDQWKPL NLEEKKRYDR
460 470 480 490 500
EFLLGFQFIF ASMQKPEGLP HISDVVLDKA NKTPLRPLDP TRLQGINCGP
510 520 530 540 550
DFTPSFANLG RTTLSTRGPP RGGPGGELPR GPAGLGPRRS QQGPRKEPRK
560 570 580 590 600
IIATVLMTED IKLNKAEKAW KPSSKRTAAD KDRGEEDADG SKTQDLFRRV
610 620 630 640 650
RSILNKLTPQ MFQQLMKQVT QLAIDTEERL KGVIDLIFEK AISEPNFSVA
660 670 680 690 700
YANMCRCLMA LKVPTTEKPT VTVNFRKLLL NRCQKEFEKD KDDDEVFEKK
710 720 730 740 750
QKEMDEAATA EERGRLKEEL EEARDIARRR SLGNIKFIGE LFKLKMLTEA
760 770 780 790 800
IMHDCVVKLL KNHDEESLEC LCRLLTTIGK DLDFEKAKPR MDQYFNQMEK
810 820 830 840 850
IIKEKKTSSR IRFMLQDVLD LRGSNWVPRR GDQGPKTIDQ IHKEAEMEEH
860 870 880 890 900
REHIKVQQLM AKGSDKRRGG PPGPPISRGL PLVDDGGWNT VPISKGSRPI
910 920 930 940 950
DTSRLTKITK PGSIDSNNQL FAPGGRLSWG KGSSGGSGAK PSDAASEAAR
960 970 980 990 1000
PATSTLNRFS ALQQAVPTES TDNRRVVQRS SLSRERGEKA GDRGDRLERS
1010 1020 1030 1040 1050
ERGGDRGDRL DRARTPATKR SFSKEVEERS RERPSQPEGL RKAASLTEDR
1060 1070 1080 1090 1100
DRGRDAVKRE AALPPVSPLK AALSEEELEK KSKAIIEEYL HLNDMKEAVQ
1110 1120 1130 1140 1150
CVQELASPSL LFIFVRHGVE STLERSAIAR EHMGQLLHQL LCAGHLSTAQ
1160 1170 1180 1190 1200
YYQGLYEILE LAEDMEIDIP HVWLYLAELV TPILQEGGVP MGELFREITK
1210 1220 1230 1240 1250
PLRPLGKAAS LLLEILGLLC KSMGPKKVGT LWREAGLSWK EFLPEGQDIG
1260 1270 1280 1290 1300
AFVAEQKVEY TLGEESEAPG QRALPSEELN RQLEKLLKEG SSNQRVFDWI
1310 1320 1330 1340 1350
EANLSEQQIV SNTLVRALMT AVCYSAIIFE TPLRVDVAVL KARAKLLQKY
1360 1370 1380 1390 1400
LCDEQKELQA LYALQALVVT LEQPPNLLRM FFDALYDEDV VKEDAFYSWE
1410 1420 1430
SSKDPAEQQG KGVALKSVTA FFKWLREAEE ESDHN
Note: Produced by alternative initiation at Met-165 of isoform A.
Show »Length:1,435
Mass (Da):158,517
<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:i6F7E9DE4106E73B9
Isoform E (identifier: Q04637-6) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-196: Missing.
10 20 30 40 50
MSGARTASTP TPPQTGGGLE PQANGETPQV AVIVRPDDRS QGAIIADRPG
60 70 80 90 100
LPGPEHSPSE SQPSSPSPTP SPSPVLEPGS EPNLAVLSIP GDTMTTIQMS
110 120 130 140 150
VEESTPISRE TGEPYRLSPE PTPLAEPILE VEVTLSKPVP ESEFSSSPLQ
160 170 180 190 200
APTPLASHTV EIHEPNGMVP SEDLEPEVES SPELAPPPAC PSESPVPIAP
210 220 230 240 250
TAQPEELLNG APSPPAVDLS PVSEPEEQAK EVTASMAPPT IPSATPATAP
260 270 280 290 300
SATSPAQEEE MEEEEEEEEG EAGEAGEAES EKGGEELLPP ESTPIPANLS
310 320 330 340 350
QNLEAAAATQ VAVSVPKRRR KIKELNKKEA VGDLLDAFKE ANPAVPEVEN
360 370 380 390 400
QPPAGSNPGP ESEGSGVPPR PEEADETWDS KEDKIHNAEN IQPGEQKYEY
410 420 430 440 450
KSDQWKPLNL EEKKRYDREF LLGFQFIFAS MQKPEGLPHI SDVVLDKANK
460 470 480 490 500
TPLRPLDPTR LQGINCGPDF TPSFANLGRT TLSTRGPPRG GPGGELPRGP
510 520 530 540 550
AGLGPRRSQQ GPRKEPRKII ATVLMTEDIK LNKAEKAWKP SSKRTAADKD
560 570 580 590 600
RGEEDADGSK TQDLFRRVRS ILNKLTPQMF QQLMKQVTQL AIDTEERLKG
610 620 630 640 650
VIDLIFEKAI SEPNFSVAYA NMCRCLMALK VPTTEKPTVT VNFRKLLLNR
660 670 680 690 700
CQKEFEKDKD DDEVFEKKQK EMDEAATAEE RGRLKEELEE ARDIARRRSL
710 720 730 740 750
GNIKFIGELF KLKMLTEAIM HDCVVKLLKN HDEESLECLC RLLTTIGKDL
760 770 780 790 800
DFEKAKPRMD QYFNQMEKII KEKKTSSRIR FMLQDVLDLR GSNWVPRRGD
810 820 830 840 850
QGPKTIDQIH KEAEMEEHRE HIKVQQLMAK GSDKRRGGPP GPPISRGLPL
860 870 880 890 900
VDDGGWNTVP ISKGSRPIDT SRLTKITKPG SIDSNNQLFA PGGRLSWGKG
910 920 930 940 950
SSGGSGAKPS DAASEAARPA TSTLNRFSAL QQAVPTESTD NRRVVQRSSL
960 970 980 990 1000
SRERGEKAGD RGDRLERSER GGDRGDRLDR ARTPATKRSF SKEVEERSRE
1010 1020 1030 1040 1050
RPSQPEGLRK AASLTEDRDR GRDAVKREAA LPPVSPLKAA LSEEELEKKS
1060 1070 1080 1090 1100
KAIIEEYLHL NDMKEAVQCV QELASPSLLF IFVRHGVEST LERSAIAREH
1110 1120 1130 1140 1150
MGQLLHQLLC AGHLSTAQYY QGLYEILELA EDMEIDIPHV WLYLAELVTP
1160 1170 1180 1190 1200
ILQEGGVPMG ELFREITKPL RPLGKAASLL LEILGLLCKS MGPKKVGTLW
1210 1220 1230 1240 1250
REAGLSWKEF LPEGQDIGAF VAEQKVEYTL GEESEAPGQR ALPSEELNRQ
1260 1270 1280 1290 1300
LEKLLKEGSS NQRVFDWIEA NLSEQQIVSN TLVRALMTAV CYSAIIFETP
1310 1320 1330 1340 1350
LRVDVAVLKA RAKLLQKYLC DEQKELQALY ALQALVVTLE QPPNLLRMFF
1360 1370 1380 1390 1400
DALYDEDVVK EDAFYSWESS KDPAEQQGKG VALKSVTAFF KWLREAEEES
DHN
Note: Produced by alternative initiation at Met-197 of isoform A.
Show »Length:1,403
Mass (Da):154,805
<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:i3E93A66EE3DFDDA9
Isoform 7 (identifier: Q04637-7) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-196: Missing.
696-696: P → PQ
10 20 30 40 50
MSGARTASTP TPPQTGGGLE PQANGETPQV AVIVRPDDRS QGAIIADRPG
60 70 80 90 100
LPGPEHSPSE SQPSSPSPTP SPSPVLEPGS EPNLAVLSIP GDTMTTIQMS
110 120 130 140 150
VEESTPISRE TGEPYRLSPE PTPLAEPILE VEVTLSKPVP ESEFSSSPLQ
160 170 180 190 200
APTPLASHTV EIHEPNGMVP SEDLEPEVES SPELAPPPAC PSESPVPIAP
210 220 230 240 250
TAQPEELLNG APSPPAVDLS PVSEPEEQAK EVTASMAPPT IPSATPATAP
260 270 280 290 300
SATSPAQEEE MEEEEEEEEG EAGEAGEAES EKGGEELLPP ESTPIPANLS
310 320 330 340 350
QNLEAAAATQ VAVSVPKRRR KIKELNKKEA VGDLLDAFKE ANPAVPEVEN
360 370 380 390 400
QPPAGSNPGP ESEGSGVPPR PEEADETWDS KEDKIHNAEN IQPGEQKYEY
410 420 430 440 450
KSDQWKPLNL EEKKRYDREF LLGFQFIFAS MQKPEGLPHI SDVVLDKANK
460 470 480 490 500
TPLRPLDPTR LQGINCGPDF TPSFANLGRT TLSTRGPPRG GPGGELPRGP
510 520 530 540 550
QAGLGPRRSQ QGPRKEPRKI IATVLMTEDI KLNKAEKAWK PSSKRTAADK
560 570 580 590 600
DRGEEDADGS KTQDLFRRVR SILNKLTPQM FQQLMKQVTQ LAIDTEERLK
610 620 630 640 650
GVIDLIFEKA ISEPNFSVAY ANMCRCLMAL KVPTTEKPTV TVNFRKLLLN
660 670 680 690 700
RCQKEFEKDK DDDEVFEKKQ KEMDEAATAE ERGRLKEELE EARDIARRRS
710 720 730 740 750
LGNIKFIGEL FKLKMLTEAI MHDCVVKLLK NHDEESLECL CRLLTTIGKD
760 770 780 790 800
LDFEKAKPRM DQYFNQMEKI IKEKKTSSRI RFMLQDVLDL RGSNWVPRRG
810 820 830 840 850
DQGPKTIDQI HKEAEMEEHR EHIKVQQLMA KGSDKRRGGP PGPPISRGLP
860 870 880 890 900
LVDDGGWNTV PISKGSRPID TSRLTKITKP GSIDSNNQLF APGGRLSWGK
910 920 930 940 950
GSSGGSGAKP SDAASEAARP ATSTLNRFSA LQQAVPTEST DNRRVVQRSS
960 970 980 990 1000
LSRERGEKAG DRGDRLERSE RGGDRGDRLD RARTPATKRS FSKEVEERSR
1010 1020 1030 1040 1050
ERPSQPEGLR KAASLTEDRD RGRDAVKREA ALPPVSPLKA ALSEEELEKK
1060 1070 1080 1090 1100
SKAIIEEYLH LNDMKEAVQC VQELASPSLL FIFVRHGVES TLERSAIARE
1110 1120 1130 1140 1150
HMGQLLHQLL CAGHLSTAQY YQGLYEILEL AEDMEIDIPH VWLYLAELVT
1160 1170 1180 1190 1200
PILQEGGVPM GELFREITKP LRPLGKAASL LLEILGLLCK SMGPKKVGTL
1210 1220 1230 1240 1250
WREAGLSWKE FLPEGQDIGA FVAEQKVEYT LGEESEAPGQ RALPSEELNR
1260 1270 1280 1290 1300
QLEKLLKEGS SNQRVFDWIE ANLSEQQIVS NTLVRALMTA VCYSAIIFET
1310 1320 1330 1340 1350
PLRVDVAVLK ARAKLLQKYL CDEQKELQAL YALQALVVTL EQPPNLLRMF
1360 1370 1380 1390 1400
FDALYDEDVV KEDAFYSWES SKDPAEQQGK GVALKSVTAF FKWLREAEEE
SDHN
Note: Produced by alternative splicing.
Show »Length:1,404
Mass (Da):154,933
<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:iE2CE3C54B5BB0A50
Isoform 8 (identifier: Q04637-8) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
696-696: P → PQ
10 20 30 40 50
MNKAPQSTGP PPAPSPGLPQ PAFPPGQTAP VVFSTPQATQ MNTPSQPRQH
60 70 80 90 100
FYPSRAQPPS SAASRVQSAA PARPGPAAHV YPAGSQVMMI PSQISYPASQ
110 120 130 140 150
GAYYIPGQGR STYVVPTQQY PVQPGAPGFY PGASPTEFGT YAGAYYPAQG
160 170 180 190 200
VQQFPTGVAP TPVLMNQPPQ IAPKRERKTI RIRDPNQGGK DITEEIMSGA
210 220 230 240 250
RTASTPTPPQ TGGGLEPQAN GETPQVAVIV RPDDRSQGAI IADRPGLPGP
260 270 280 290 300
EHSPSESQPS SPSPTPSPSP VLEPGSEPNL AVLSIPGDTM TTIQMSVEES
310 320 330 340 350
TPISRETGEP YRLSPEPTPL AEPILEVEVT LSKPVPESEF SSSPLQAPTP
360 370 380 390 400
LASHTVEIHE PNGMVPSEDL EPEVESSPEL APPPACPSES PVPIAPTAQP
410 420 430 440 450
EELLNGAPSP PAVDLSPVSE PEEQAKEVTA SMAPPTIPSA TPATAPSATS
460 470 480 490 500
PAQEEEMEEE EEEEEGEAGE AGEAESEKGG EELLPPESTP IPANLSQNLE
510 520 530 540 550
AAAATQVAVS VPKRRRKIKE LNKKEAVGDL LDAFKEANPA VPEVENQPPA
560 570 580 590 600
GSNPGPESEG SGVPPRPEEA DETWDSKEDK IHNAENIQPG EQKYEYKSDQ
610 620 630 640 650
WKPLNLEEKK RYDREFLLGF QFIFASMQKP EGLPHISDVV LDKANKTPLR
660 670 680 690 700
PLDPTRLQGI NCGPDFTPSF ANLGRTTLST RGPPRGGPGG ELPRGPQAGL
710 720 730 740 750
GPRRSQQGPR KEPRKIIATV LMTEDIKLNK AEKAWKPSSK RTAADKDRGE
760 770 780 790 800
EDADGSKTQD LFRRVRSILN KLTPQMFQQL MKQVTQLAID TEERLKGVID
810 820 830 840 850
LIFEKAISEP NFSVAYANMC RCLMALKVPT TEKPTVTVNF RKLLLNRCQK
860 870 880 890 900
EFEKDKDDDE VFEKKQKEMD EAATAEERGR LKEELEEARD IARRRSLGNI
910 920 930 940 950
KFIGELFKLK MLTEAIMHDC VVKLLKNHDE ESLECLCRLL TTIGKDLDFE
960 970 980 990 1000
KAKPRMDQYF NQMEKIIKEK KTSSRIRFML QDVLDLRGSN WVPRRGDQGP
1010 1020 1030 1040 1050
KTIDQIHKEA EMEEHREHIK VQQLMAKGSD KRRGGPPGPP ISRGLPLVDD
1060 1070 1080 1090 1100
GGWNTVPISK GSRPIDTSRL TKITKPGSID SNNQLFAPGG RLSWGKGSSG
1110 1120 1130 1140 1150
GSGAKPSDAA SEAARPATST LNRFSALQQA VPTESTDNRR VVQRSSLSRE
1160 1170 1180 1190 1200
RGEKAGDRGD RLERSERGGD RGDRLDRART PATKRSFSKE VEERSRERPS
1210 1220 1230 1240 1250
QPEGLRKAAS LTEDRDRGRD AVKREAALPP VSPLKAALSE EELEKKSKAI
1260 1270 1280 1290 1300
IEEYLHLNDM KEAVQCVQEL ASPSLLFIFV RHGVESTLER SAIAREHMGQ
1310 1320 1330 1340 1350
LLHQLLCAGH LSTAQYYQGL YEILELAEDM EIDIPHVWLY LAELVTPILQ
1360 1370 1380 1390 1400
EGGVPMGELF REITKPLRPL GKAASLLLEI LGLLCKSMGP KKVGTLWREA
1410 1420 1430 1440 1450
GLSWKEFLPE GQDIGAFVAE QKVEYTLGEE SEAPGQRALP SEELNRQLEK
1460 1470 1480 1490 1500
LLKEGSSNQR VFDWIEANLS EQQIVSNTLV RALMTAVCYS AIIFETPLRV
1510 1520 1530 1540 1550
DVAVLKARAK LLQKYLCDEQ KELQALYALQ ALVVTLEQPP NLLRMFFDAL
1560 1570 1580 1590 1600
YDEDVVKEDA FYSWESSKDP AEQQGKGVAL KSVTAFFKWL REAEEESDHN
Note: Produced by alternative splicing.
Show »Length:1,600
Mass (Da):175,619
<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:i2B32EF7A6D50B657
Isoform 9 (identifier: Q04637-9) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
48-48: R → RQGGFRSL
10 20 30 40 50
MNKAPQSTGP PPAPSPGLPQ PAFPPGQTAP VVFSTPQATQ MNTPSQPRQG
60 70 80 90 100
GFRSLQHFYP SRAQPPSSAA SRVQSAAPAR PGPAAHVYPA GSQVMMIPSQ
110 120 130 140 150
ISYPASQGAY YIPGQGRSTY VVPTQQYPVQ PGAPGFYPGA SPTEFGTYAG
160 170 180 190 200
AYYPAQGVQQ FPTGVAPTPV LMNQPPQIAP KRERKTIRIR DPNQGGKDIT
210 220 230 240 250
EEIMSGARTA STPTPPQTGG GLEPQANGET PQVAVIVRPD DRSQGAIIAD
260 270 280 290 300
RPGLPGPEHS PSESQPSSPS PTPSPSPVLE PGSEPNLAVL SIPGDTMTTI
310 320 330 340 350
QMSVEESTPI SRETGEPYRL SPEPTPLAEP ILEVEVTLSK PVPESEFSSS
360 370 380 390 400
PLQAPTPLAS HTVEIHEPNG MVPSEDLEPE VESSPELAPP PACPSESPVP
410 420 430 440 450
IAPTAQPEEL LNGAPSPPAV DLSPVSEPEE QAKEVTASMA PPTIPSATPA
460 470 480 490 500
TAPSATSPAQ EEEMEEEEEE EEGEAGEAGE AESEKGGEEL LPPESTPIPA
510 520 530 540 550
NLSQNLEAAA ATQVAVSVPK RRRKIKELNK KEAVGDLLDA FKEANPAVPE
560 570 580 590 600
VENQPPAGSN PGPESEGSGV PPRPEEADET WDSKEDKIHN AENIQPGEQK
610 620 630 640 650
YEYKSDQWKP LNLEEKKRYD REFLLGFQFI FASMQKPEGL PHISDVVLDK
660 670 680 690 700
ANKTPLRPLD PTRLQGINCG PDFTPSFANL GRTTLSTRGP PRGGPGGELP
710 720 730 740 750
RGPAGLGPRR SQQGPRKEPR KIIATVLMTE DIKLNKAEKA WKPSSKRTAA
760 770 780 790 800
DKDRGEEDAD GSKTQDLFRR VRSILNKLTP QMFQQLMKQV TQLAIDTEER
810 820 830 840 850
LKGVIDLIFE KAISEPNFSV AYANMCRCLM ALKVPTTEKP TVTVNFRKLL
860 870 880 890 900
LNRCQKEFEK DKDDDEVFEK KQKEMDEAAT AEERGRLKEE LEEARDIARR
910 920 930 940 950
RSLGNIKFIG ELFKLKMLTE AIMHDCVVKL LKNHDEESLE CLCRLLTTIG
960 970 980 990 1000
KDLDFEKAKP RMDQYFNQME KIIKEKKTSS RIRFMLQDVL DLRGSNWVPR
1010 1020 1030 1040 1050
RGDQGPKTID QIHKEAEMEE HREHIKVQQL MAKGSDKRRG GPPGPPISRG
1060 1070 1080 1090 1100
LPLVDDGGWN TVPISKGSRP IDTSRLTKIT KPGSIDSNNQ LFAPGGRLSW
1110 1120 1130 1140 1150
GKGSSGGSGA KPSDAASEAA RPATSTLNRF SALQQAVPTE STDNRRVVQR
1160 1170 1180 1190 1200
SSLSRERGEK AGDRGDRLER SERGGDRGDR LDRARTPATK RSFSKEVEER
1210 1220 1230 1240 1250
SRERPSQPEG LRKAASLTED RDRGRDAVKR EAALPPVSPL KAALSEEELE
1260 1270 1280 1290 1300
KKSKAIIEEY LHLNDMKEAV QCVQELASPS LLFIFVRHGV ESTLERSAIA
1310 1320 1330 1340 1350
REHMGQLLHQ LLCAGHLSTA QYYQGLYEIL ELAEDMEIDI PHVWLYLAEL
1360 1370 1380 1390 1400
VTPILQEGGV PMGELFREIT KPLRPLGKAA SLLLEILGLL CKSMGPKKVG
1410 1420 1430 1440 1450
TLWREAGLSW KEFLPEGQDI GAFVAEQKVE YTLGEESEAP GQRALPSEEL
1460 1470 1480 1490 1500
NRQLEKLLKE GSSNQRVFDW IEANLSEQQI VSNTLVRALM TAVCYSAIIF
1510 1520 1530 1540 1550
ETPLRVDVAV LKARAKLLQK YLCDEQKELQ ALYALQALVV TLEQPPNLLR
1560 1570 1580 1590 1600
MFFDALYDED VVKEDAFYSW ESSKDPAEQQ GKGVALKSVT AFFKWLREAE
EESDHN
Note: Produced by alternative splicing. Gene prediction based on EST data.
Show »Length:1,606
Mass (Da):176,237
<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:iE4464821E0BA5FF6
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
The sequence AAC78444 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAC82471 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA02185 differs from that shown. Reason: Frameshift at several positions.Curated
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 30 | P → R in AAC78443 (PubMed:9755181).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 138 | F → L in AAL92872 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 138 | F → L in AAM69365 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 149 | Q → R in AAL92872 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 149 | Q → R in AAM69365 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 214 | G → S in BAA02185 (PubMed:1429670).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 462 | E → D in BAA02185 (PubMed:1429670).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 468 | A → V in BAA02185 (PubMed:1429670).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 474 | A → G in BAA02185 (PubMed:1429670).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 479 | G → R in BAA02185 (PubMed:1429670).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 604 | L → P in BAA02185 (PubMed:1429670).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 604 | L → P in AAL92872 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 604 | L → P in AAM69365 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 604 | L → P in AAC82471 (PubMed:9372926).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 625 – 626 | AS → CQ in BAA02185 (PubMed:1429670).Curated | 2 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 693 | P → A in BAA02185 (PubMed:1429670).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 696 | P → A in BAA02185 (PubMed:1429670).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 764 | V → W in BAA02185 (PubMed:1429670).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 878 | G → E in BAA02185 (PubMed:1429670).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 894 | R → C in BAA02185 (PubMed:1429670).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1104 | K → Q in BAA02185 (PubMed:1429670).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1121 | N → I in BAA02185 (PubMed:1429670).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1185 | S → T in BAA02185 (PubMed:1429670).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1384 | C → Y in CAI46013 (PubMed:17974005).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1472 | Missing in BAA02185 (PubMed:1429670).Curated | 1 |
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_066571 | 71 | P → S1 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_061147 | 161 | T → A5 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_079031 | 201 | R → H Found in a patient with Rett syndrome-like phenotype; 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
| 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_055704 | 311 | Y → C1 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_063040 | 432 | M → VCombined 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>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_066572 | 466 – 468 | Missing 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
| 3 | |
| <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_066573 | 502 | A → V in PARK18. 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_066574 | 686 | G → C Found in patients with Parkinson disease; 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
| 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_036117 | 696 | P → L in a colorectal cancer sample; 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
| 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_066575 | 806 | I → V1 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_066576 | 829 | T → S1 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_066577 | 1164 | S → R Found in a patient with Parkinson disease; 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
| 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_066578 | 1197 | R → W Found in a patient with Parkinson disease; 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
| 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_066579 | 1205 | R → H in PARK18. 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_061148 | 1229 | P → A1 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_055705 | 1233 | L → P1 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_066580 | 1257 | N → S1 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 |
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_018723 | 1 – 196 | Missing in isoform E and isoform 7. 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
| 196 | |
| <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_018722 | 1 – 164 | Missing in isoform D. CuratedAdd BLAST | 164 | |
| <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_018721 | 1 – 87 | Missing in isoform C. 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
| 87 | |
| <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_018720 | 1 – 40 | Missing in isoform B. 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
| 40 | |
| <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_047396 | 48 | R → RQGGFRSL in isoform 9. Curated | 1 | |
| <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_047397 | 696 | P → PQ in isoform 7 and isoform 8. 4 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
| 1 |
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 | D12686 mRNA Translation: BAA02185.1 Frameshift. AY082886 mRNA Translation: AAL92872.1 AF281070 mRNA Translation: AAM69365.1 AK131407 mRNA Translation: BAD18554.1 Sequence problems. BX647812 mRNA Translation: CAI46013.1 AC078797 Genomic DNA No translation available. CH471052 Genomic DNA Translation: EAW78257.1 CH471052 Genomic DNA Translation: EAW78259.1 CH471052 Genomic DNA Translation: EAW78262.1 CH471052 Genomic DNA Translation: EAW78263.1 CH471052 Genomic DNA Translation: EAW78264.1 CH471052 Genomic DNA Translation: EAW78265.1 CH471052 Genomic DNA Translation: EAW78266.1 CH471052 Genomic DNA Translation: EAW78267.1 AF002816 mRNA Translation: AAC78443.1 AF004836 Genomic DNA Translation: AAC78444.1 Different initiation. AF104913 mRNA Translation: AAC82471.1 Different initiation. AJ001046 mRNA Translation: CAA04500.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS3259.1 [Q04637-1] CCDS3260.1 [Q04637-4] CCDS3261.1 [Q04637-5] CCDS46970.2 [Q04637-7] CCDS54687.1 [Q04637-9] CCDS54688.1 [Q04637-8] CCDS77866.1 [Q04637-3] |
Protein sequence database of the Protein Information Resource More...PIRi | A44453 |
NCBI Reference Sequences More...RefSeqi | NP_004944.3, NM_004953.4 [Q04637-7] NP_886553.3, NM_182917.4 NP_937884.1, NM_198241.2 NP_937885.1, NM_198242.2 [Q04637-5] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.433750 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000342981; ENSP00000343450; ENSG00000114867 [Q04637-8] ENST00000346169; ENSP00000316879; ENSG00000114867 [Q04637-1] ENST00000350481; ENSP00000317600; ENSG00000114867 [Q04637-5] ENST00000352767; ENSP00000338020; ENSG00000114867 [Q04637-9] ENST00000382330; ENSP00000371767; ENSG00000114867 [Q04637-9] ENST00000392537; ENSP00000376320; ENSG00000114867 [Q04637-4] ENST00000414031; ENSP00000391935; ENSG00000114867 [Q04637-3] ENST00000424196; ENSP00000416255; ENSG00000114867 [Q04637-9] ENST00000434061; ENSP00000411826; ENSG00000114867 [Q04637-7] ENST00000435046; ENSP00000404754; ENSG00000114867 [Q04637-6] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 1981 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:1981 |
UCSC genome browser More...UCSCi | uc003fnp.4 human [Q04637-1] |
<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 - Coding sequence diversityi
Alternative initiation, 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 | |
|---|---|---|---|---|---|
| Q04637 | UPI000CEAC6C5 | 1875 | |||
| Eukaryotic translation initiation factor 4 gamma 1 | 1629 | ||||
| Eukaryotic translation initiation factor 4 gamma 1 | 1627 | ||||
| UPI000737D909 | 1619 | ||||
| UPI00070445DC | 1618 | ||||
| +478 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q04637 | UPI000CEAC6C5 | 1875 | |||
| Eukaryotic translation initiation factor 4 gamma 1 | 1629 | ||||
| Eukaryotic translation initiation factor 4 gamma 1 | 1627 | ||||
| UPI000737D909 | 1619 | ||||
| UPI00070445DC | 1618 | ||||
| +513 | |||||
<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 | D12686 mRNA Translation: BAA02185.1 Frameshift. AY082886 mRNA Translation: AAL92872.1 AF281070 mRNA Translation: AAM69365.1 AK131407 mRNA Translation: BAD18554.1 Sequence problems. BX647812 mRNA Translation: CAI46013.1 AC078797 Genomic DNA No translation available. CH471052 Genomic DNA Translation: EAW78257.1 CH471052 Genomic DNA Translation: EAW78259.1 CH471052 Genomic DNA Translation: EAW78262.1 CH471052 Genomic DNA Translation: EAW78263.1 CH471052 Genomic DNA Translation: EAW78264.1 CH471052 Genomic DNA Translation: EAW78265.1 CH471052 Genomic DNA Translation: EAW78266.1 CH471052 Genomic DNA Translation: EAW78267.1 AF002816 mRNA Translation: AAC78443.1 AF004836 Genomic DNA Translation: AAC78444.1 Different initiation. AF104913 mRNA Translation: AAC82471.1 Different initiation. AJ001046 mRNA Translation: CAA04500.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS3259.1 [Q04637-1] CCDS3260.1 [Q04637-4] CCDS3261.1 [Q04637-5] CCDS46970.2 [Q04637-7] CCDS54687.1 [Q04637-9] CCDS54688.1 [Q04637-8] CCDS77866.1 [Q04637-3] |
Protein sequence database of the Protein Information Resource More...PIRi | A44453 |
NCBI Reference Sequences More...RefSeqi | NP_004944.3, NM_004953.4 [Q04637-7] NP_886553.3, NM_182917.4 NP_937884.1, NM_198241.2 NP_937885.1, NM_198242.2 [Q04637-5] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.433750 |
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 |
| 1LJ2 | X-ray | 2.38 | C/D | 172-199 | [»] | |
| 1UG3 | X-ray | 2.24 | A/B | 1233-1571 | [»] | |
| 2W97 | X-ray | 2.29 | E/F | 609-622 | [»] | |
| 4AZA | X-ray | 2.16 | B/D | 609-620 | [»] | |
| 4F02 | X-ray | 2.00 | C/F | 178-203 | [»] | |
| 5EHC | X-ray | 2.40 | B | 609-622 | [»] | |
| 5EI3 | X-ray | 1.71 | B | 609-622 | [»] | |
| 5EIR | X-ray | 2.69 | B | 609-622 | [»] | |
| 5T46 | X-ray | 1.53 | B/D | 592-653 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q04637 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q04637 | |||||
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 | 108296, 104 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q04637 |
Database of interacting proteins More...DIPi | DIP-1161N |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | Q04637 |
Protein interaction database and analysis system More...IntActi | Q04637, 80 interactors |
Molecular INTeraction database More...MINTi | Q04637 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000338020 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q04637 |
Protein family/group databases
MoonProt database of moonlighting proteins More...MoonProti | Q04637 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q04637 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q04637 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q04637 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | EIF4G1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 294862538 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q04637 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q04637 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q04637 |
PeptideAtlas More...PeptideAtlasi | Q04637 |
PRoteomics IDEntifications database More...PRIDEi | Q04637 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 58250 58251 [Q04637-3] 58252 [Q04637-4] 58253 [Q04637-5] 58254 [Q04637-6] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 1981 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000342981; ENSP00000343450; ENSG00000114867 [Q04637-8] ENST00000346169; ENSP00000316879; ENSG00000114867 [Q04637-1] ENST00000350481; ENSP00000317600; ENSG00000114867 [Q04637-5] ENST00000352767; ENSP00000338020; ENSG00000114867 [Q04637-9] ENST00000382330; ENSP00000371767; ENSG00000114867 [Q04637-9] ENST00000392537; ENSP00000376320; ENSG00000114867 [Q04637-4] ENST00000414031; ENSP00000391935; ENSG00000114867 [Q04637-3] ENST00000424196; ENSP00000416255; ENSG00000114867 [Q04637-9] ENST00000434061; ENSP00000411826; ENSG00000114867 [Q04637-7] ENST00000435046; ENSP00000404754; ENSG00000114867 [Q04637-6] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 1981 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:1981 |
UCSC genome browser More...UCSCi | uc003fnp.4 human [Q04637-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 1981 |
DisGeNET More...DisGeNETi | 1981 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000114867.19 |
GeneCards: human genes, protein and diseases More...GeneCardsi | EIF4G1 |
Human Gene Nomenclature Database More...HGNCi | HGNC:3296 EIF4G1 |
Human Protein Atlas More...HPAi | CAB014774 HPA028487 HPA043866 |
MalaCards human disease database More...MalaCardsi | EIF4G1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 600495 gene 614251 phenotype |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q04637 |
Open Targets More...OpenTargetsi | ENSG00000114867 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 2828 Young adult-onset Parkinsonism |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA27722 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0401 Eukaryota ENOG410XS4P LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00530000063038 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000231658 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG052083 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q04637 |
KEGG Orthology (KO) More...KOi | K03260 |
Identification of Orthologs from Complete Genome Data More...OMAi | EMNKAPQ |
Database of Orthologous Groups More...OrthoDBi | EOG091G03ZW |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q04637 |
TreeFam database of animal gene trees More...TreeFami | TF101527 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1169408 ISG15 antiviral mechanism R-HSA-156827 L13a-mediated translational silencing of Ceruloplasmin expression R-HSA-166208 mTORC1-mediated signalling R-HSA-429947 Deadenylation of mRNA R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA R-HSA-72649 Translation initiation complex formation R-HSA-72662 Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S R-HSA-72702 Ribosomal scanning and start codon recognition R-HSA-72706 GTP hydrolysis and joining of the 60S ribosomal subunit R-HSA-9010553 Regulation of expression of SLITs and ROBOs R-HSA-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) R-HSA-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q04637 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | EIF4G1 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q04637 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | Eukaryotic_translation_initiation_factor_4_gamma |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 1981 |
CutDB - Proteolytic event database More...PMAP-CutDBi | Q04637 |
Protein Ontology More...PROi | PR:Q04637 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000114867 |
CleanEx database of gene expression profiles More...CleanExi | HS_EIF4G1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q04637 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q04637 HS |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.25.40.180, 3 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR016024 ARM-type_fold IPR037584 EIF4G1 IPR003891 Initiation_fac_eIF4g_MI IPR016021 MIF4-like_sf IPR003890 MIF4G-like_typ-3 IPR003307 W2_domain |
The PANTHER Classification System More...PANTHERi | PTHR23253:SF10 PTHR23253:SF10, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF02847 MA3, 1 hit PF02854 MIF4G, 1 hit PF02020 W2, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00515 eIF5C, 1 hit SM00544 MA3, 1 hit SM00543 MIF4G, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF48371 SSF48371, 3 hits |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51366 MI, 1 hit PS51363 W2, 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 | IF4G1_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 | Q04637Primary (citable) accession number: Q04637 Secondary accession number(s): D3DNT2 , D3DNT4, D3DNT5, E9PFM1, G5E9S1, O43177, O95066, Q5HYG0, Q6ZN21, Q8N102 | |
| <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: | February 1, 1995 |
| Last sequence update: | April 20, 2010 | |
| Last modified: | July 18, 2018 | |
| This is version 207 of the entry and version 4 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 3
Human chromosome 3: 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
