UniProtKB - O14776 (TCRG1_HUMAN)
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- BLAST>sp|O14776|TCRG1_HUMAN Transcription elongation regulator 1 OS=Homo sapiens OX=9606 GN=TCERG1 PE=1 SV=2 MAERGGDGGESERFNPGELRMAQQQALRFRGPAPPPNAVMRGPPPLMRPPPPFGMMRGPP PPPRPPFGRPPFDPNMPPMPPPGGIPPPMGPPHLQRPPFMPPPMSSMPPPPGMMFPPGMP PVTAPGTPALPPTEEIWVENKTPDGKVYYYNARTRESAWTKPDGVKVIQQSELTPMLAAQ AQVQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQ AQVQAQVQAQVQAQAVGASTPTTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPT TQDQTPSSAVSVATPTVSVSTPAPTATPVQTVPQPHPQTLPPAVPHSVPQPTTAIPAFPP VMVPPFRVPLPGMPIPLPGVAMMQIVSCPYVKTVATTKTGVLPGMAPPIVPMIHPQVAIA ASPATLAGATAVSEWTEYKTADGKTYYYNNRTLESTWEKPQELKEKEKLEEKIKEPIKEP SEEPLPMETEEEDPKEEPIKEIKEEPKEEEMTEEEKAAQKAKPVATAPIPGTPWCVVWTG DERVFFYNPTTRLSMWDRPDDLIGRADVDKIIQEPPHKKGMEELKKLRHPTPTMLSIQKW QFSMSAIKEEQELMEEINEDEPVKAKKRKRDDNKDIDSEKEAAMEAEIKAARERAIVPLE ARMKQFKDMLLERGVSAFSTWEKELHKIVFDPRYLLLNPKERKQVFDQYVKTRAEEERRE KKNKIMQAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAA RKKEKEDSKTRGEKIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLF KQYIEKIAKNLDSEKEKELERQARIEASLREREREVQKARSEQTKEIDREREQHKREEAI QNFKALLSDMVRSSDVSWSDTRRTLRKDHRWESGSLLEREEKEKLFNEHIEALTKKKREH FRQLLDETSAITLTSTWKEVKKIIKEDPRCIKFSSSDRKKQREFEEYIRDKYITAKADFR TLLKETKFITYRSKKLIQESDQHLKDVEKILQNDKRYLVLDCVPEERRKLIVAYVDDLDR RGPPPPPTASEPTRRSTK
- Align
Transcription elongation regulator 1
TCERG1
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
<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.1"CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription."
Sune C., Hayashi T., Liu Y., Lane W.S., Young R.A., Garcia-Blanco M.A.
Mol. Cell. Biol. 17:6029-6039(1997) [PubMed] [Europe PMC] [Abstract] - Ref.5"The transcription elongation factor CA150 interacts with RNA polymerase II and the pre-mRNA splicing factor SF1."
Goldstrohm A.C., Albrecht T.R., Sune C., Bedford M.T., Garcia-Blanco M.A.
Mol. Cell. Biol. 21:7617-7628(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, MUTAGENESIS OF 148-TYR--TYR-150; 446-TYR--TYR-448 AND 545-PHE--TYR-547, INTERACTION WITH RNA POLYMERASE II AND SF1.
<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
- 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
- proline-rich region binding Source: Ensembl
- RNA binding Source: UniProtKBInferred from high throughput direct assayi
- RNA polymerase II repressing transcription factor binding Source: BHF-UCL <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
- RNA polymerase II transcription corepressor activity Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- transcription coactivator activity Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
<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
- negative regulation of transcription by RNA polymerase II Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- transcription by RNA polymerase II Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Activator, Repressor |
| Biological process | Transcription, Transcription regulation |
Enzyme and pathway databases
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | O14776 |
<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: Transcription elongation regulator 1Alternative name(s): TATA box-binding protein-associated factor 2S Transcription factor CA150 |
| <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:TCERG1 Synonyms:CA150, TAF2S |
| <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:ENSG00000113649.11 |
Human Gene Nomenclature Database More...HGNCi | HGNC:15630 TCERG1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 605409 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_O14776 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Nucleus
- Nucleus 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.1"CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription."
Sune C., Hayashi T., Liu Y., Lane W.S., Young R.A., Garcia-Blanco M.A.
Mol. Cell. Biol. 17:6029-6039(1997) [PubMed] [Europe PMC] [Abstract] - Ref.4"Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II."
Carty S.M., Goldstrohm A.C., Sune C., Garcia-Blanco M.A., Greenleaf A.L.
Proc. Natl. Acad. Sci. U.S.A. 97:9015-9020(2000) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RNA POLYMERASE II. - Ref.7"FF domains of CA150 bind transcription and splicing factors through multiple weak interactions."
Smith M.J., Kulkarni S., Pawson T.
Mol. Cell. Biol. 24:9274-9285(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HTATSF1, SUBCELLULAR LOCATION.
- Nucleus 3 Publications
Nucleus
- nucleoplasm Source: HPA
- nucleus Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
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 | 148 – 150 | YYY → AAA: Reduces repression of transcription by 35%. Reduces repression of transcription by 63%; when associated with 446-AAA-448. 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 <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 | 446 – 448 | YYY → AAA: Loss of interaction with SF1. Reduces repression of transcription by 35%. Reduces repression of transcription by 63%; when associated with 148-AAA-150. 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 <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 | 545 – 547 | FFY → AAA: No effect. 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 |
Organism-specific databases
DisGeNET More...DisGeNETi | 10915 |
Open Targets More...OpenTargetsi | ENSG00000113649 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA38007 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | TCERG1 |
<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_0000076063 | 1 – 1098 | Transcription elongation regulator 1Add BLAST | 1098 |
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 | 11 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 20 | 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 | 28 | Asymmetric dimethylarginineCombined 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 | 30 | Asymmetric dimethylarginineCombined 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 | 41 | Asymmetric dimethylarginineCombined 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 | 48 | Asymmetric dimethylarginineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 503 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)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
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 507 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)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
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 608 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)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
| ||
| <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 | 638 | 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 | 834 | 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 | 933 | 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>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
Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | O14776 |
MaxQB - The MaxQuant DataBase More...MaxQBi | O14776 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | O14776 |
PeptideAtlas More...PeptideAtlasi | O14776 |
PRoteomics IDEntifications database More...PRIDEi | O14776 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 48229 48230 [O14776-2] |
PTM databases
CarbonylDB database of protein carbonylation sites More...CarbonylDBi | O14776 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | O14776 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | O14776 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | O14776 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<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.6"The Gln-Ala repeat transcriptional activator CA150 interacts with huntingtin: neuropathologic and genetic evidence for a role in Huntington's disease pathogenesis."
Holbert S., Denghien I., Kiechle T., Rosenblatt A., Wellington C., Hayden M.R., Margolis R.L., Ross C.A., Dausset J., Ferrante R.J., Neri C.
Proc. Natl. Acad. Sci. U.S.A. 98:1811-1816(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HD, INDUCTION, TISSUE SPECIFICITY.
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
<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.6"The Gln-Ala repeat transcriptional activator CA150 interacts with huntingtin: neuropathologic and genetic evidence for a role in Huntington's disease pathogenesis."
Holbert S., Denghien I., Kiechle T., Rosenblatt A., Wellington C., Hayden M.R., Margolis R.L., Ross C.A., Dausset J., Ferrante R.J., Neri C.
Proc. Natl. Acad. Sci. U.S.A. 98:1811-1816(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HD, INDUCTION, TISSUE SPECIFICITY.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000113649 |
CleanEx database of gene expression profiles More...CleanExi | HS_TCERG1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | O14776 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | O14776 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA064854 HPA069752 HPA069808 |
<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
<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.1"CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription."
Sune C., Hayashi T., Liu Y., Lane W.S., Young R.A., Garcia-Blanco M.A.
Mol. Cell. Biol. 17:6029-6039(1997) [PubMed] [Europe PMC] [Abstract] - Ref.4"Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II."
Carty S.M., Goldstrohm A.C., Sune C., Garcia-Blanco M.A., Greenleaf A.L.
Proc. Natl. Acad. Sci. U.S.A. 97:9015-9020(2000) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RNA POLYMERASE II. - Ref.5"The transcription elongation factor CA150 interacts with RNA polymerase II and the pre-mRNA splicing factor SF1."
Goldstrohm A.C., Albrecht T.R., Sune C., Bedford M.T., Garcia-Blanco M.A.
Mol. Cell. Biol. 21:7617-7628(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, MUTAGENESIS OF 148-TYR--TYR-150; 446-TYR--TYR-448 AND 545-PHE--TYR-547, INTERACTION WITH RNA POLYMERASE II AND SF1. - Ref.6"The Gln-Ala repeat transcriptional activator CA150 interacts with huntingtin: neuropathologic and genetic evidence for a role in Huntington's disease pathogenesis."
Holbert S., Denghien I., Kiechle T., Rosenblatt A., Wellington C., Hayden M.R., Margolis R.L., Ross C.A., Dausset J., Ferrante R.J., Neri C.
Proc. Natl. Acad. Sci. U.S.A. 98:1811-1816(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HD, INDUCTION, TISSUE SPECIFICITY. - Ref.7"FF domains of CA150 bind transcription and splicing factors through multiple weak interactions."
Smith M.J., Kulkarni S., Pawson T.
Mol. Cell. Biol. 24:9274-9285(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HTATSF1, SUBCELLULAR LOCATION.
<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 | 4 | EBI-473271,EBI-473271 | ||
| BARD1 | Q99728 | 2 | EBI-473271,EBI-473181 | |
| HTT | P42858 | 9 | EBI-473271,EBI-466029 |
<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
- 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
- proline-rich region binding Source: Ensembl
- RNA polymerase II repressing transcription factor binding Source: BHF-UCL <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-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 116120, 84 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | O14776 |
Database of interacting proteins More...DIPi | DIP-32504N |
Protein interaction database and analysis system More...IntActi | O14776, 19 interactors |
Molecular INTeraction database More...MINTi | O14776 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000296702 |
<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
| 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 | 103 – 105 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 435 – 440 | 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 | 6 | |
| <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 | 441 – 443 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 444 – 449 | 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 | 6 | |
| <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 | 450 – 453 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 454 – 458 | 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 | 461 – 463 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 523 – 528 | 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 | 6 | |
| <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 | 530 – 533 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 535 – 542 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 544 – 548 | 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 | 549 – 552 | 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 | 560 – 564 | 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 | 567 – 573 | 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 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 | 576 – 578 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 652 – 656 | 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 | 661 – 663 | 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 | 669 – 672 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 677 – 679 | 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 | 681 – 689 | 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 | 692 – 696 | 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 | 705 – 710 | 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 | 6 | |
| <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 | 713 – 720 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 721 – 723 | 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 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 | 726 – 728 | 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 | 747 – 752 | 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 | 6 | |
| <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 | 758 – 762 | 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 | 773 – 780 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 783 – 786 | 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 | 798 – 804 | 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 | 814 – 821 | 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 | 825 – 827 | 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 | 833 – 840 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 888 – 890 | 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 | 895 – 910 | 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 | 918 – 925 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 929 – 934 | 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 | 6 | |
| <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 | 939 – 966 | 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 | 28 | |
| <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 | 977 – 984 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 988 – 991 | 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 | 997 – 1025 | 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 | 29 | |
| <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 | 1033 – 1039 | 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 | 1042 – 1051 | 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 | 1055 – 1058 | 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 | 1059 – 1062 | 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 | 1064 – 1076 | 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 | 13 |
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 |
| 2DK7 | NMR | - | A | 520-579 | [»] | |
| 2DOD | NMR | - | A | 651-719 | [»] | |
| 2DOE | NMR | - | A | 784-853 | [»] | |
| 2DOF | NMR | - | A | 888-959 | [»] | |
| 2E71 | NMR | - | A | 717-786 | [»] | |
| 2KIQ | NMR | - | A | 724-782 | [»] | |
| 2KIS | NMR | - | A | 659-724 | [»] | |
| 2MW9 | NMR | - | A | 428-464 | [»] | |
| 2MWA | NMR | - | A | 428-464 | [»] | |
| 2MWB | NMR | - | A | 428-464 | [»] | |
| 2MWD | NMR | - | A | 433-460 | [»] | |
| 2MWE | NMR | - | A | 433-460 | [»] | |
| 2MWF | NMR | - | A | 433-464 | [»] | |
| 2N4R | NMR | - | A | 428-464 | [»] | |
| 2N4S | NMR | - | A | 428-464 | [»] | |
| 2N4T | NMR | - | A | 428-464 | [»] | |
| 2N4U | NMR | - | A | 428-464 | [»] | |
| 2N4V | NMR | - | A | 428-464 | [»] | |
| 2N4W | NMR | - | A | 428-464 | [»] | |
| 2NNT | NMR | - | A/B/C/D | 428-464 | [»] | |
| 3HFH | X-ray | 2.70 | A/B | 661-845 | [»] | |
| 3Q1I | X-ray | 1.40 | E | 99-107 | [»] | |
| 4FQG | X-ray | 2.00 | A/B | 895-1081 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | O14776 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | O14776 | |||||
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 | O14776 |
<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 | 131 – 164 | WW 1PROSITE-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 | 34 | |
| <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 | 429 – 462 | WW 2PROSITE-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 | 34 | |
| <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 | 528 – 561 | WW 3PROSITE-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 | 34 | |
| <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 | 659 – 712 | FF 1Add BLAST | 54 | |
| <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 | 725 – 779 | FF 2Add BLAST | 55 | |
| <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 | 791 – 846 | FF 3Add BLAST | 56 | |
| <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 | 896 – 952 | FF 4Add BLAST | 57 | |
| <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 | 954 – 1010 | FF 5Add BLAST | 57 | |
| <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 | 1012 – 1077 | FF 6Add BLAST | 66 |
Coiled coil
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili | 184 – 244 | Sequence analysisAdd BLAST | 61 | |
| <p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili | 606 – 655 | Sequence analysisAdd BLAST | 50 | |
| <p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili | 844 – 906 | Sequence analysisAdd BLAST | 63 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 626 – 630 | Nuclear localization signalSequence analysis | 5 |
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 | 32 – 132 | Pro-richAdd BLAST | 101 | |
| <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 | 169 – 258 | Ala/Gln-richAdd BLAST | 90 | |
| <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 | 260 – 331 | Thr-richAdd BLAST | 72 | |
| <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 | 328 – 378 | Pro-richAdd BLAST | 51 | |
| <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 – 515 | Glu-richAdd BLAST | 62 | |
| <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 | 1083 – 1087 | Poly-Pro | 5 |
<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
<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 - Domaini
Coiled coil, RepeatPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0155 Eukaryota ENOG410XPZW LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00920000149021 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000008544 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG062908 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | O14776 |
KEGG Orthology (KO) More...KOi | K12824 |
Identification of Orthologs from Complete Genome Data More...OMAi | PAEEIWV |
Database of Orthologous Groups More...OrthoDBi | EOG091G0I5O |
Database for complete collections of gene phylogenies More...PhylomeDBi | O14776 |
TreeFam database of animal gene trees More...TreeFami | TF317748 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00201 WW, 3 hits |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.10.440, 6 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR002713 FF_domain IPR036517 FF_domain_sf IPR001202 WW_dom IPR036020 WW_dom_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF01846 FF, 6 hits PF00397 WW, 2 hits |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00441 FF, 6 hits SM00456 WW, 3 hits |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51045 SSF51045, 3 hits SSF81698 SSF81698, 5 hits |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51676 FF, 6 hits PS01159 WW_DOMAIN_1, 1 hit PS50020 WW_DOMAIN_2, 3 hits |
<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 (2)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.
This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
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
MAERGGDGGE SERFNPGELR MAQQQALRFR GPAPPPNAVM RGPPPLMRPP
60 70 80 90 100
PPFGMMRGPP PPPRPPFGRP PFDPNMPPMP PPGGIPPPMG PPHLQRPPFM
110 120 130 140 150
PPPMSSMPPP PGMMFPPGMP PVTAPGTPAL PPTEEIWVEN KTPDGKVYYY
160 170 180 190 200
NARTRESAWT KPDGVKVIQQ SELTPMLAAQ AQVQAQAQAQ AQAQAQAQAQ
210 220 230 240 250
AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQVQAQVQAQ
260 270 280 290 300
VQAQAVGAST PTTSSPAPAV STSTSSSTPS STTSTTTTAT SVAQTVSTPT
310 320 330 340 350
TQDQTPSSAV SVATPTVSVS TPAPTATPVQ TVPQPHPQTL PPAVPHSVPQ
360 370 380 390 400
PTTAIPAFPP VMVPPFRVPL PGMPIPLPGV AMMQIVSCPY VKTVATTKTG
410 420 430 440 450
VLPGMAPPIV PMIHPQVAIA ASPATLAGAT AVSEWTEYKT ADGKTYYYNN
460 470 480 490 500
RTLESTWEKP QELKEKEKLE EKIKEPIKEP SEEPLPMETE EEDPKEEPIK
510 520 530 540 550
EIKEEPKEEE MTEEEKAAQK AKPVATAPIP GTPWCVVWTG DERVFFYNPT
560 570 580 590 600
TRLSMWDRPD DLIGRADVDK IIQEPPHKKG MEELKKLRHP TPTMLSIQKW
610 620 630 640 650
QFSMSAIKEE QELMEEINED EPVKAKKRKR DDNKDIDSEK EAAMEAEIKA
660 670 680 690 700
ARERAIVPLE ARMKQFKDML LERGVSAFST WEKELHKIVF DPRYLLLNPK
710 720 730 740 750
ERKQVFDQYV KTRAEEERRE KKNKIMQAKE DFKKMMEEAK FNPRATFSEF
760 770 780 790 800
AAKHAKDSRF KAIEKMKDRE ALFNEFVAAA RKKEKEDSKT RGEKIKSDFF
810 820 830 840 850
ELLSNHHLDS QSRWSKVKDK VESDPRYKAV DSSSMREDLF KQYIEKIAKN
860 870 880 890 900
LDSEKEKELE RQARIEASLR EREREVQKAR SEQTKEIDRE REQHKREEAI
910 920 930 940 950
QNFKALLSDM VRSSDVSWSD TRRTLRKDHR WESGSLLERE EKEKLFNEHI
960 970 980 990 1000
EALTKKKREH FRQLLDETSA ITLTSTWKEV KKIIKEDPRC IKFSSSDRKK
1010 1020 1030 1040 1050
QREFEEYIRD KYITAKADFR TLLKETKFIT YRSKKLIQES DQHLKDVEKI
1060 1070 1080 1090
LQNDKRYLVL DCVPEERRKL IVAYVDDLDR RGPPPPPTAS EPTRRSTK
The sequence of this isoform differs from the canonical sequence as follows:
379-399: Missing.
10 20 30 40 50
MAERGGDGGE SERFNPGELR MAQQQALRFR GPAPPPNAVM RGPPPLMRPP
60 70 80 90 100
PPFGMMRGPP PPPRPPFGRP PFDPNMPPMP PPGGIPPPMG PPHLQRPPFM
110 120 130 140 150
PPPMSSMPPP PGMMFPPGMP PVTAPGTPAL PPTEEIWVEN KTPDGKVYYY
160 170 180 190 200
NARTRESAWT KPDGVKVIQQ SELTPMLAAQ AQVQAQAQAQ AQAQAQAQAQ
210 220 230 240 250
AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQVQAQVQAQ
260 270 280 290 300
VQAQAVGAST PTTSSPAPAV STSTSSSTPS STTSTTTTAT SVAQTVSTPT
310 320 330 340 350
TQDQTPSSAV SVATPTVSVS TPAPTATPVQ TVPQPHPQTL PPAVPHSVPQ
360 370 380 390 400
PTTAIPAFPP VMVPPFRVPL PGMPIPLPGV LPGMAPPIVP MIHPQVAIAA
410 420 430 440 450
SPATLAGATA VSEWTEYKTA DGKTYYYNNR TLESTWEKPQ ELKEKEKLEE
460 470 480 490 500
KIKEPIKEPS EEPLPMETEE EDPKEEPIKE IKEEPKEEEM TEEEKAAQKA
510 520 530 540 550
KPVATAPIPG TPWCVVWTGD ERVFFYNPTT RLSMWDRPDD LIGRADVDKI
560 570 580 590 600
IQEPPHKKGM EELKKLRHPT PTMLSIQKWQ FSMSAIKEEQ ELMEEINEDE
610 620 630 640 650
PVKAKKRKRD DNKDIDSEKE AAMEAEIKAA RERAIVPLEA RMKQFKDMLL
660 670 680 690 700
ERGVSAFSTW EKELHKIVFD PRYLLLNPKE RKQVFDQYVK TRAEEERREK
710 720 730 740 750
KNKIMQAKED FKKMMEEAKF NPRATFSEFA AKHAKDSRFK AIEKMKDREA
760 770 780 790 800
LFNEFVAAAR KKEKEDSKTR GEKIKSDFFE LLSNHHLDSQ SRWSKVKDKV
810 820 830 840 850
ESDPRYKAVD SSSMREDLFK QYIEKIAKNL DSEKEKELER QARIEASLRE
860 870 880 890 900
REREVQKARS EQTKEIDRER EQHKREEAIQ NFKALLSDMV RSSDVSWSDT
910 920 930 940 950
RRTLRKDHRW ESGSLLEREE KEKLFNEHIE ALTKKKREHF RQLLDETSAI
960 970 980 990 1000
TLTSTWKEVK KIIKEDPRCI KFSSSDRKKQ REFEEYIRDK YITAKADFRT
1010 1020 1030 1040 1050
LLKETKFITY RSKKLIQESD QHLKDVEKIL QNDKRYLVLD CVPEERRKLI
1060 1070
VAYVDDLDRR GPPPPPTASE PTRRSTK
<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
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 | 324 | P → R in AAB80727 (PubMed:9315662).Curated | 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_026933 | 379 – 399 | Missing in isoform 2. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 21 |
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 | AF017789 mRNA Translation: AAB80727.1 AB209910 mRNA Translation: BAD93147.1 Different initiation. BC111727 mRNA Translation: AAI11728.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS4282.1 [O14776-1] CCDS43379.1 [O14776-2] |
Protein sequence database of the Protein Information Resource More...PIRi | T08599 |
NCBI Reference Sequences More...RefSeqi | NP_001035095.1, NM_001040006.1 [O14776-2] NP_006697.2, NM_006706.3 [O14776-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.443465 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000296702; ENSP00000296702; ENSG00000113649 [O14776-1] ENST00000394421; ENSP00000377943; ENSG00000113649 [O14776-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 10915 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:10915 |
UCSC genome browser More...UCSCi | uc003lob.4 human [O14776-1] |
<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 splicing<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 | |
|---|---|---|---|---|---|
| O14776 | Transcription elongation regulator 1 | 1098 | |||
| Transcription elongation regulator 1 | 1098 | ||||
| UPI000A1BA212 | 1147 | ||||
| UPI00005A01BC | 455 | ||||
| UPI00042C41ED | 1131 | ||||
| +56 | |||||
| O14776-2 | Transcription elongation regulator 1 | 1077 | |||
| UPI00093EC085 | 1138 | ||||
| UPI0007194AD1 | 1099 | ||||
| UPI000A33EFD8 | 1095 | ||||
| transcription elongation regulator 1 isoform X5 | 1091 | ||||
| +52 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| O14776 | Transcription elongation regulator 1 | 1098 | |||
| Transcription elongation regulator 1 | 1098 | ||||
| UPI000A1BA212 | 1147 | ||||
| UPI00005A01BC | 455 | ||||
| UPI00042C41ED | 1131 | ||||
| +303 | |||||
| O14776-2 | Transcription elongation regulator 1 | 938 | |||
| UPI00046C0D29 | 1079 | ||||
| UPI000CEF7E67 | 1065 | ||||
| UPI00093B266E | 1024 | ||||
| transcription elongation regulator 1 isoform X2 | 1024 | ||||
| +272 | |||||
<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 | AF017789 mRNA Translation: AAB80727.1 AB209910 mRNA Translation: BAD93147.1 Different initiation. BC111727 mRNA Translation: AAI11728.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS4282.1 [O14776-1] CCDS43379.1 [O14776-2] |
Protein sequence database of the Protein Information Resource More...PIRi | T08599 |
NCBI Reference Sequences More...RefSeqi | NP_001035095.1, NM_001040006.1 [O14776-2] NP_006697.2, NM_006706.3 [O14776-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.443465 |
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 |
| 2DK7 | NMR | - | A | 520-579 | [»] | |
| 2DOD | NMR | - | A | 651-719 | [»] | |
| 2DOE | NMR | - | A | 784-853 | [»] | |
| 2DOF | NMR | - | A | 888-959 | [»] | |
| 2E71 | NMR | - | A | 717-786 | [»] | |
| 2KIQ | NMR | - | A | 724-782 | [»] | |
| 2KIS | NMR | - | A | 659-724 | [»] | |
| 2MW9 | NMR | - | A | 428-464 | [»] | |
| 2MWA | NMR | - | A | 428-464 | [»] | |
| 2MWB | NMR | - | A | 428-464 | [»] | |
| 2MWD | NMR | - | A | 433-460 | [»] | |
| 2MWE | NMR | - | A | 433-460 | [»] | |
| 2MWF | NMR | - | A | 433-464 | [»] | |
| 2N4R | NMR | - | A | 428-464 | [»] | |
| 2N4S | NMR | - | A | 428-464 | [»] | |
| 2N4T | NMR | - | A | 428-464 | [»] | |
| 2N4U | NMR | - | A | 428-464 | [»] | |
| 2N4V | NMR | - | A | 428-464 | [»] | |
| 2N4W | NMR | - | A | 428-464 | [»] | |
| 2NNT | NMR | - | A/B/C/D | 428-464 | [»] | |
| 3HFH | X-ray | 2.70 | A/B | 661-845 | [»] | |
| 3Q1I | X-ray | 1.40 | E | 99-107 | [»] | |
| 4FQG | X-ray | 2.00 | A/B | 895-1081 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | O14776 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | O14776 | |||||
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 | 116120, 84 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | O14776 |
Database of interacting proteins More...DIPi | DIP-32504N |
Protein interaction database and analysis system More...IntActi | O14776, 19 interactors |
Molecular INTeraction database More...MINTi | O14776 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000296702 |
PTM databases
CarbonylDB database of protein carbonylation sites More...CarbonylDBi | O14776 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | O14776 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | O14776 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | O14776 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | TCERG1 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | O14776 |
MaxQB - The MaxQuant DataBase More...MaxQBi | O14776 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | O14776 |
PeptideAtlas More...PeptideAtlasi | O14776 |
PRoteomics IDEntifications database More...PRIDEi | O14776 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 48229 48230 [O14776-2] |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000296702; ENSP00000296702; ENSG00000113649 [O14776-1] ENST00000394421; ENSP00000377943; ENSG00000113649 [O14776-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 10915 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:10915 |
UCSC genome browser More...UCSCi | uc003lob.4 human [O14776-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 10915 |
DisGeNET More...DisGeNETi | 10915 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000113649.11 |
GeneCards: human genes, protein and diseases More...GeneCardsi | TCERG1 |
Human Gene Nomenclature Database More...HGNCi | HGNC:15630 TCERG1 |
Human Protein Atlas More...HPAi | HPA064854 HPA069752 HPA069808 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 605409 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_O14776 |
Open Targets More...OpenTargetsi | ENSG00000113649 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA38007 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0155 Eukaryota ENOG410XPZW LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00920000149021 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000008544 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG062908 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | O14776 |
KEGG Orthology (KO) More...KOi | K12824 |
Identification of Orthologs from Complete Genome Data More...OMAi | PAEEIWV |
Database of Orthologous Groups More...OrthoDBi | EOG091G0I5O |
Database for complete collections of gene phylogenies More...PhylomeDBi | O14776 |
TreeFam database of animal gene trees More...TreeFami | TF317748 |
Enzyme and pathway databases
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | O14776 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | TCERG1 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | O14776 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | Transcription_elongation_regulator_1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 10915 |
Protein Ontology More...PROi | PR:O14776 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000113649 |
CleanEx database of gene expression profiles More...CleanExi | HS_TCERG1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | O14776 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | O14776 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd00201 WW, 3 hits |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.10.440, 6 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR002713 FF_domain IPR036517 FF_domain_sf IPR001202 WW_dom IPR036020 WW_dom_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF01846 FF, 6 hits PF00397 WW, 2 hits |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00441 FF, 6 hits SM00456 WW, 3 hits |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51045 SSF51045, 3 hits SSF81698 SSF81698, 5 hits |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51676 FF, 6 hits PS01159 WW_DOMAIN_1, 1 hit PS50020 WW_DOMAIN_2, 3 hits |
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 | TCRG1_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 | O14776Primary (citable) accession number: O14776 Secondary accession number(s): Q2NKN2, Q59EA1 | |
| <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: | September 27, 2004 |
| Last sequence update: | July 24, 2007 | |
| Last modified: | June 20, 2018 | |
| This is version 166 of the entry and version 2 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, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 5
Human chromosome 5: entries, gene names and cross-references to MIM - 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
