UniProtKB - Q8TAD8 (SNIP1_HUMAN)
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- BLAST>sp|Q8TAD8|SNIP1_HUMAN Smad nuclear-interacting protein 1 OS=Homo sapiens OX=9606 GN=SNIP1 PE=1 SV=1 MKAVKSERERGSRRRHRDGDVVLPAGVVVKQERLSPEVAPPAHRRPDHSGGSPSPPTSEP ARSGHRGNRARGVSRSPPKKKNKASGRRSKSPRSKRNRSPHHSTVKVKQEREDHPRRGRE DRQHREPSEQEHRRARNSDRDRHRGHSHQRRTSNERPGSGQGQGRDRDTQNLQAQEEERE FYNARRREHRQRNDVGGGGSESQELVPRPGGNNKEKEVPAKEKPSFELSGALLEDTNTFR GVVIKYSEPPEARIPKKRWRLYPFKNDEVLPVMYIHRQSAYLLGRHRRIADIPIDHPSCS KQHAVFQYRLVEYTRADGTVGRRVKPYIIDLGSGNGTFLNNKRIEPQRYYELKEKDVLKF GFSSREYVLLHESSDTSEIDRKDDEDEEEEEEVSDS
- Align
Smad nuclear-interacting protein 1
SNIP1
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.4"SNIP1 inhibits NF-kappa B signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators."
Kim R.H., Flanders K.C., Birkey Reffey S., Anderson L.A., Duckett C.S., Perkins N.D., Roberts A.B.
J. Biol. Chem. 276:46297-46304(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH CREBBP AND EP300. - Ref.6"The FHA domain protein SNIP1 is a regulator of the cell cycle and cyclin D1 expression."
Roche K.C., Wiechens N., Owen-Hughes T., Perkins N.D.
Oncogene 23:8185-8195(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH SMARCA4. - Ref.9"Regulation of cyclin D1 RNA stability by SNIP1."
Bracken C.P., Wall S.J., Barre B., Panov K.I., Ajuh P.M., Perkins N.D.
Cancer Res. 68:7621-7628(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN THE SNARP COMPLEX. - Ref.10"The FHA domain proteins DAWDLE in Arabidopsis and SNIP1 in humans act in small RNA biogenesis."
Yu B., Bi L., Zheng B., Ji L., Chevalier D., Agarwal M., Ramachandran V., Li W., Lagrange T., Walker J.C., Chen X.
Proc. Natl. Acad. Sci. U.S.A. 105:10073-10078(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH DROSHA.
<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
- mRNA binding Source: GO_Central
- RNA binding Source: UniProtKBInferred from high throughput direct assayi
<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
- I-kappaB kinase/NF-kappaB signaling Source: Ensembl
- production of miRNAs involved in gene silencing by miRNA 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
- regulation of transcription, DNA-templated Source: Ensembl
<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
| Biological process | RNA-mediated gene silencing |
Enzyme and pathway databases
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q8TAD8 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q8TAD8 |
Protein family/group databases
MoonDB Database of extreme multifunctional and moonlighting proteins More...MoonDBi | Q8TAD8 Predicted |
<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: Smad nuclear-interacting protein 1Alternative name(s): FHA domain-containing protein SNIP1 |
| <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:SNIP1 |
| <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:ENSG00000163877.9 |
Human Gene Nomenclature Database More...HGNCi | HGNC:30587 SNIP1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 608241 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q8TAD8 |
<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 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.1"A novel Smad nuclear interacting protein, SNIP1, suppresses p300-dependent TGF-beta signal transduction."
Kim R.H., Wang D., Tsang M., Martin J., Huff C., de Caestecker M.P., Parks T.W., Meng X., Lechleider R.J., Wang T., Roberts A.B.
Genes Dev. 14:1605-1616(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SMAD4 AND CREBBP/EP300, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
- Nucleus 1 Publication
Cytosol
- cytosol Source: HPA
Nucleus
- nucleoplasm Source: HPA
- nucleus Source: GO_Central
<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
<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
Psychomotor retardation, epilepsy, and craniofacial dysmorphism (PMRED)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.23"Genetic mapping and exome sequencing identify variants associated with five novel diseases."
Puffenberger E.G., Jinks R.N., Sougnez C., Cibulskis K., Willert R.A., Achilly N.P., Cassidy R.P., Fiorentini C.J., Heiken K.F., Lawrence J.J., Mahoney M.H., Miller C.J., Nair D.T., Politi K.A., Worcester K.N., Setton R.A., Dipiazza R., Sherman E.A. , Eastman J.T., Francklyn C., Robey-Bond S., Rider N.L., Gabriel S., Morton D.H., Strauss K.A.
PLoS ONE 7:E28936-E28936(2012) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT PMRED GLY-366.
Puffenberger E.G., Jinks R.N., Sougnez C., Cibulskis K., Willert R.A., Achilly N.P., Cassidy R.P., Fiorentini C.J., Heiken K.F., Lawrence J.J., Mahoney M.H., Miller C.J., Nair D.T., Politi K.A., Worcester K.N., Setton R.A., Dipiazza R., Sherman E.A. , Eastman J.T., Francklyn C., Robey-Bond S., Rider N.L., Gabriel S., Morton D.H., Strauss K.A.
PLoS ONE 7:E28936-E28936(2012) [PubMed] [Europe PMC] [Abstract]
| 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_067542 | 366 | E → G in PMRED. 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 | 30 | K → R: Abolishes sumoylation. 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, EpilepsyOrganism-specific databases
DisGeNET More...DisGeNETi | 79753 |
MalaCards human disease database More...MalaCardsi | SNIP1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 614501 phenotype |
Open Targets More...OpenTargetsi | ENSG00000163877 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA142670893 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | SNIP1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 48428655 |
<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_0000072009 | 1 – 396 | Smad nuclear-interacting protein 1Add BLAST | 396 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section 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 | 30 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate | ||
| <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 | 30 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined 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 | 30 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined 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 | 35 | 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 | 49 | 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 | 52 | 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 | 54 | 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 | 57 | 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 | 58 | 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 | 99 | 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 <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 | 108 | 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 | 153 | 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 | 202 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes 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 | 223 | 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 | 394 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<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, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q8TAD8 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q8TAD8 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q8TAD8 |
PeptideAtlas More...PeptideAtlasi | Q8TAD8 |
PRoteomics IDEntifications database More...PRIDEi | Q8TAD8 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 73865 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q8TAD8 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q8TAD8 |
<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.1"A novel Smad nuclear interacting protein, SNIP1, suppresses p300-dependent TGF-beta signal transduction."
Kim R.H., Wang D., Tsang M., Martin J., Huff C., de Caestecker M.P., Parks T.W., Meng X., Lechleider R.J., Wang T., Roberts A.B.
Genes Dev. 14:1605-1616(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SMAD4 AND CREBBP/EP300, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000163877 |
CleanEx database of gene expression profiles More...CleanExi | HS_SNIP1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q8TAD8 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q8TAD8 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA036896 |
<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"A novel Smad nuclear interacting protein, SNIP1, suppresses p300-dependent TGF-beta signal transduction."
Kim R.H., Wang D., Tsang M., Martin J., Huff C., de Caestecker M.P., Parks T.W., Meng X., Lechleider R.J., Wang T., Roberts A.B.
Genes Dev. 14:1605-1616(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SMAD4 AND CREBBP/EP300, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.4"SNIP1 inhibits NF-kappa B signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators."
Kim R.H., Flanders K.C., Birkey Reffey S., Anderson L.A., Duckett C.S., Perkins N.D., Roberts A.B.
J. Biol. Chem. 276:46297-46304(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH CREBBP AND EP300. - Ref.5"A novel link between the proteasome pathway and the signal transduction pathway of the bone morphogenetic proteins (BMPs)."
Lin Y., Martin J., Gruendler C., Farley J., Meng X., Li B.-Y., Lechleider R., Huff C., Kim R.H., Grasser W.A., Paralkar V., Wang T.
BMC Cell Biol. 3:15-15(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH THE SMAD1/OAZ1/PSMB4 COMPLEX, DEGRADATION BY THE PROTEASOME. - Ref.6"The FHA domain protein SNIP1 is a regulator of the cell cycle and cyclin D1 expression."
Roche K.C., Wiechens N., Owen-Hughes T., Perkins N.D.
Oncogene 23:8185-8195(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH SMARCA4. - Ref.9"Regulation of cyclin D1 RNA stability by SNIP1."
Bracken C.P., Wall S.J., Barre B., Panov K.I., Ajuh P.M., Perkins N.D.
Cancer Res. 68:7621-7628(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN THE SNARP COMPLEX. - Ref.10"The FHA domain proteins DAWDLE in Arabidopsis and SNIP1 in humans act in small RNA biogenesis."
Yu B., Bi L., Zheng B., Ji L., Chevalier D., Agarwal M., Ramachandran V., Li W., Lagrange T., Walker J.C., Chen X.
Proc. Natl. Acad. Sci. U.S.A. 105:10073-10078(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH DROSHA.
<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 |
|---|---|---|---|---|
| CLK2 | P49760 | 8 | EBI-749336,EBI-750020 | |
| IK | Q13123 | 2 | EBI-749336,EBI-713456 | |
| KRTAP10-6 | P60371 | 4 | EBI-749336,EBI-12012928 | |
| MFAP1 | P55081 | 3 | EBI-749336,EBI-1048159 | |
| MYC | P01106 | 9 | EBI-749336,EBI-447544 | |
| SNW1 | Q13573 | 7 | EBI-749336,EBI-632715 | |
| SRPK2 | P78362 | 3 | EBI-749336,EBI-593303 | |
| TNIP1 | Q15025 | 3 | EBI-749336,EBI-357849 | |
| TSPYL2 | Q9H2G4 | 4 | EBI-749336,EBI-947459 | |
| ZBTB9 | Q96C00 | 4 | EBI-749336,EBI-395708 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 122864, 75 interactors |
Database of interacting proteins More...DIPi | DIP-38956N |
Protein interaction database and analysis system More...IntActi | Q8TAD8, 57 interactors |
Molecular INTeraction database More...MINTi | Q8TAD8 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000296215 |
<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
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q8TAD8 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q8TAD8 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<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 | 281 – 344 | FHAPROSITE-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 | 64 |
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 | 165 – 196 | Sequence analysisAdd BLAST | 32 |
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 | 62 – 192 | Arg-richAdd BLAST | 131 | |
| <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 | 385 – 392 | Poly-Glu | 8 |
<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 coilPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1882 Eukaryota ENOG4111F4H LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00730000110659 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000264922 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG056615 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q8TAD8 |
KEGG Orthology (KO) More...KOi | K13108 |
Identification of Orthologs from Complete Genome Data More...OMAi | LKYHEPA |
Database of Orthologous Groups More...OrthoDBi | EOG091G0M70 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q8TAD8 |
TreeFam database of animal gene trees More...TreeFami | TF312797 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00060 FHA, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000253 FHA_dom IPR008984 SMAD_FHA_dom_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF00498 FHA, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00240 FHA, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF49879 SSF49879, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50006 FHA_DOMAIN, 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>Sequencei
<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.
10 20 30 40 50
MKAVKSERER GSRRRHRDGD VVLPAGVVVK QERLSPEVAP PAHRRPDHSG
60 70 80 90 100
GSPSPPTSEP ARSGHRGNRA RGVSRSPPKK KNKASGRRSK SPRSKRNRSP
110 120 130 140 150
HHSTVKVKQE REDHPRRGRE DRQHREPSEQ EHRRARNSDR DRHRGHSHQR
160 170 180 190 200
RTSNERPGSG QGQGRDRDTQ NLQAQEEERE FYNARRREHR QRNDVGGGGS
210 220 230 240 250
ESQELVPRPG GNNKEKEVPA KEKPSFELSG ALLEDTNTFR GVVIKYSEPP
260 270 280 290 300
EARIPKKRWR LYPFKNDEVL PVMYIHRQSA YLLGRHRRIA DIPIDHPSCS
310 320 330 340 350
KQHAVFQYRL VEYTRADGTV GRRVKPYIID LGSGNGTFLN NKRIEPQRYY
360 370 380 390
ELKEKDVLKF GFSSREYVLL HESSDTSEID RKDDEDEEEE EEVSDS
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 | 181 | F → S in BAB55241 (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 | 364 | S → I in BAB14134 (PubMed:14702039).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_067542 | 366 | E → G in PMRED. 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 |
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 | AY081909 mRNA Translation: AAL91140.1 AK022615 mRNA Translation: BAB14134.1 AK027622 mRNA Translation: BAB55241.1 BC027040 mRNA Translation: AAH27040.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS419.1 |
NCBI Reference Sequences More...RefSeqi | NP_078976.2, NM_024700.3 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.47232 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000296215; ENSP00000296215; ENSG00000163877 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 79753 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:79753 |
UCSC genome browser More...UCSCi | uc001cbi.5 human |
<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 | |
|---|---|---|---|---|---|
| Q8TAD8 | Smad nuclear interacting protein 1 | 396 | |||
| Smad nuclear interacting protein 1 | 402 | ||||
| Smad nuclear interacting protein 1 | 397 | ||||
| UPI0004D0A868 | 397 | ||||
| SNIP1 isoform 1 | 396 | ||||
| +27 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q8TAD8 | Smad nuclear interacting protein 1 | 396 | |||
| Smad nuclear interacting protein 1 | 402 | ||||
| Smad nuclear interacting protein 1 | 397 | ||||
| UPI0004D0A868 | 397 | ||||
| UPI000C29B075 | 396 | ||||
| +112 | |||||
<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 | AY081909 mRNA Translation: AAL91140.1 AK022615 mRNA Translation: BAB14134.1 AK027622 mRNA Translation: BAB55241.1 BC027040 mRNA Translation: AAH27040.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS419.1 |
NCBI Reference Sequences More...RefSeqi | NP_078976.2, NM_024700.3 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.47232 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q8TAD8 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q8TAD8 |
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 | 122864, 75 interactors |
Database of interacting proteins More...DIPi | DIP-38956N |
Protein interaction database and analysis system More...IntActi | Q8TAD8, 57 interactors |
Molecular INTeraction database More...MINTi | Q8TAD8 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000296215 |
Protein family/group databases
MoonDB Database of extreme multifunctional and moonlighting proteins More...MoonDBi | Q8TAD8 Predicted |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q8TAD8 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q8TAD8 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | SNIP1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 48428655 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q8TAD8 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q8TAD8 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q8TAD8 |
PeptideAtlas More...PeptideAtlasi | Q8TAD8 |
PRoteomics IDEntifications database More...PRIDEi | Q8TAD8 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 73865 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 79753 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000296215; ENSP00000296215; ENSG00000163877 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 79753 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:79753 |
UCSC genome browser More...UCSCi | uc001cbi.5 human |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 79753 |
DisGeNET More...DisGeNETi | 79753 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000163877.9 |
GeneCards: human genes, protein and diseases More...GeneCardsi | SNIP1 |
Human Gene Nomenclature Database More...HGNCi | HGNC:30587 SNIP1 |
Human Protein Atlas More...HPAi | HPA036896 |
MalaCards human disease database More...MalaCardsi | SNIP1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 608241 gene 614501 phenotype |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q8TAD8 |
Open Targets More...OpenTargetsi | ENSG00000163877 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA142670893 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1882 Eukaryota ENOG4111F4H LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00730000110659 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000264922 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG056615 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q8TAD8 |
KEGG Orthology (KO) More...KOi | K13108 |
Identification of Orthologs from Complete Genome Data More...OMAi | LKYHEPA |
Database of Orthologous Groups More...OrthoDBi | EOG091G0M70 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q8TAD8 |
TreeFam database of animal gene trees More...TreeFami | TF312797 |
Enzyme and pathway databases
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q8TAD8 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q8TAD8 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | SNIP1 human |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | SNIP1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 79753 |
Protein Ontology More...PROi | PR:Q8TAD8 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000163877 |
CleanEx database of gene expression profiles More...CleanExi | HS_SNIP1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q8TAD8 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q8TAD8 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd00060 FHA, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000253 FHA_dom IPR008984 SMAD_FHA_dom_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF00498 FHA, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00240 FHA, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF49879 SSF49879, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50006 FHA_DOMAIN, 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 | SNIP1_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 | Q8TAD8Primary (citable) accession number: Q8TAD8 Secondary accession number(s): Q96SP9, Q9H9T7 | |
| <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: | June 7, 2004 |
| Last sequence update: | June 1, 2002 | |
| Last modified: | June 20, 2018 | |
| This is version 144 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
Complete proteome, Reference proteomeDocuments
- Human chromosome 1
Human chromosome 1: 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
