UniProtKB - Q15642 (CIP4_HUMAN)
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- BLAST>sp|Q15642|CIP4_HUMAN Cdc42-interacting protein 4 OS=Homo sapiens OX=9606 GN=TRIP10 PE=1 SV=3 MDWGTELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRPAK DDPESKFSQQQSFVQILQEVNDFAGQRELVAENLSVRVCLELTKYSQEMKQERKMHFQEG RRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQDINATKADVEKAKQQAHLRS HMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELE VVPIIAKCLEGMKVAANAVDPKNDSHVLIELHKSGFARPGDVEFEDFSQPMNRAPSDSSL GTPSDGRPELRGPGRSRTKRWPFGKKNKPRPPPLSPLGGPVPSALPNGPPSPRSGRDPLA ILSEISKSVKPRLASFRSLRGSRGTVVTEDFSHLPPEQQRKRLQQQLEERSRELQKEVDQ REALKKMKDVYEKTPQMGDPASLEPQIAETLSNIERLKLEVQKYEAWLAEAESRVLSNRG DSLSRHARPPDPPASAPPDSSSNSASQDTKESSEEPPSEESQDTPIYTEFDEDFEEEPTS PIGHCVAIYHFEGSSEGTISMAEGEDLSLMEEDKGDGWTRVRRKEGGEGYVPTSYLRVTL N
- Align
Cdc42-interacting protein 4
TRIP10
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.15"Microtubule-dependent formation of podosomal adhesion structures in primary human macrophages."
Linder S., Huefner K., Wintergerst U., Aepfelbacher M.
J. Cell Sci. 113:4165-4176(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.21"Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins."
Itoh T., Erdmann K.S., Roux A., Habermann B., Werner H., De Camilli P.
Dev. Cell 9:791-804(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH DNM1 AND WASL, SUBCELLULAR LOCATION. - Ref.23"Regulation of FasL expression: a SH3 domain containing protein family involved in the lysosomal association of FasL."
Qian J., Chen W., Lettau M., Podda G., Zoernig M., Kabelitz D., Janssen O.
Cell. Signal. 18:1327-1337(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH FASLG, SUBCELLULAR LOCATION.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 166 | Mediates end-to-end attachment of dimers | 1 |
<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
- GTPase activator activity Source: Reactome
- 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
- lipid binding Source: UniProtKB-KW
<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
- actin cytoskeleton organization Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- cell communication Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- endocytosis Source: UniProtKB-KW
- membrane organization Source: Reactome
- regulation of small GTPase mediated signal transduction Source: Reactome
- signal transduction 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
| Biological process | Endocytosis |
| Ligand | Lipid-binding |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-194840 Rho GTPase cycle R-HSA-8856828 Clathrin-mediated endocytosis |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q15642 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q15642 |
<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: Cdc42-interacting protein 4Alternative name(s): Protein Felic Salt tolerant protein Short name: hSTP Thyroid receptor-interacting protein 10 Short name: TR-interacting protein 10 Short name: TRIP-10 |
| <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:TRIP10 Synonyms:CIP4, STOT, STP |
| <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:ENSG00000125733.17 |
Human Gene Nomenclature Database More...HGNCi | HGNC:12304 TRIP10 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 604504 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q15642 |
<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
Lysosome
Cytoskeleton
Plasma membrane
Golgi apparatus
Other locations
Note: Translocates to the plasma membrane in response to insulin stimulation, and this may require active RHOQ (By similarity). Localizes to cortical regions coincident with F-actin, to lysosomes and to sites of phagocytosis in macrophages. Also localizes to the Golgi, and this requires AKAP9.By similarity
Other locations
Cytoskeleton
- cytoskeleton Source: UniProtKB-SubCell
Cytosol
- cytosol Source: Reactome
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Golgi apparatus
- Golgi apparatus Source: UniProtKB-SubCell
Lysosome
- lysosome Source: UniProtKB-SubCell
Nucleus
- nucleoplasm Source: HPA
Plasma Membrane
- phagocytic cup Source: UniProtKB-SubCell
Other locations
- cell cortex Source: UniProtKB-SubCell
- cell projection Source: UniProtKB-KW
- cytoplasm Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- intracellular membrane-bounded organelle Source: HPA
- perinuclear region of cytoplasm Source: UniProtKB-SubCell
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Golgi apparatus, Lysosome, Membrane<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 | 454 | I → S: Abrogates interaction with CDC42. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 468 | L → S: Impairs interaction with CDC42. 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 |
Organism-specific databases
DisGeNET More...DisGeNETi | 9322 |
Open Targets More...OpenTargetsi | ENSG00000125733 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA36983 |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 118572632 |
<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_0000089766 | 1 – 601 | Cdc42-interacting protein 4Add BLAST | 601 |
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 | 296 | 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 | 298 | 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 | 299 | 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 | 335 | 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 | 351 | 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 | 482 | 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>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.3"Splicing variant of Cdc42 interacting protein-4 disrupts beta-catenin-mediated cell-cell adhesion: expression and function in renal cell carcinoma."
Tsuji E., Tsuji Y., Fujiwara T., Ogata S., Tsukamoto K., Saku K.
Biochem. Biophys. Res. Commun. 339:1083-1088(2006) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), INTERACTION WITH CTNNB1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYROSINE RESIDUES. - Ref.18"Felic (CIP4b), a novel binding partner with the Src kinase Lyn and Cdc42, localizes to the phagocytic cup."
Dombrosky-Ferlan P., Grishin A., Botelho R.J., Sampson M., Wang L., Rudert W.A., Grinstein S., Corey S.J.
Blood 101:2804-2809(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CDC42; LYN AND SRC, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT TYROSINE RESIDUES. - Ref.20"AKAP350 interaction with cdc42 interacting protein 4 at the Golgi apparatus."
Larocca M.C., Shanks R.A., Tian L., Nelson D.L., Stewart D.M., Goldenring J.R.
Mol. Biol. Cell 15:2771-2781(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH AKAP9, SUBCELLULAR LOCATION, PHOSPHORYLATION.
<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
PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q15642 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q15642 |
PeptideAtlas More...PeptideAtlasi | Q15642 |
PRoteomics IDEntifications database More...PRIDEi | Q15642 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 60675 60676 [Q15642-2] 60677 [Q15642-3] 60678 [Q15642-4] 60679 [Q15642-5] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q15642 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q15642 |
<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 Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton."
Aspenstroem P.
Curr. Biol. 7:479-487(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH CDC42, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.2"Identification and genetic analysis of human and mouse activated Cdc42 interacting protein-4 isoforms."
Wang L., Rudert W.A., Grishin A., Dombrosky-Ferlan P., Sullivan K., Deng X., Whitcomb D., Corey S.J.
Biochem. Biophys. Res. Commun. 293:1426-1430(2002) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY, INDUCTION. - Ref.13"Molecular cloning and chromosomal localization of human salt-tolerant protein."
Tsuji E., Tsuji Y.
Genetica 108:259-262(2000) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY. - Ref.18"Felic (CIP4b), a novel binding partner with the Src kinase Lyn and Cdc42, localizes to the phagocytic cup."
Dombrosky-Ferlan P., Grishin A., Botelho R.J., Sampson M., Wang L., Rudert W.A., Grinstein S., Corey S.J.
Blood 101:2804-2809(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CDC42; LYN AND SRC, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT TYROSINE RESIDUES. - Ref.19"Cdc42-interacting protein 4 binds to huntingtin: neuropathologic and biological evidence for a role in Huntington's disease."
Holbert S., Dedeoglu A., Humbert S., Saudou F., Ferrante R.J., Neri C.
Proc. Natl. Acad. Sci. U.S.A. 100:2712-2717(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HD, SUBCELLULAR LOCATION, 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.2"Identification and genetic analysis of human and mouse activated Cdc42 interacting protein-4 isoforms."
Wang L., Rudert W.A., Grishin A., Dombrosky-Ferlan P., Sullivan K., Deng X., Whitcomb D., Corey S.J.
Biochem. Biophys. Res. Commun. 293:1426-1430(2002) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY, INDUCTION. - Ref.16"Altered gene expression pattern in cultured human breast cancer cells treated with hepatocyte growth factor/scatter factor in the setting of DNA damage."
Yuan R.-Q., Fan S., Achary M., Stewart D.M., Goldberg I.D., Rosen E.M.
Cancer Res. 61:8022-8031(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000125733 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q15642 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q15642 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA041934 HPA072625 HPA073886 |
<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 Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton."
Aspenstroem P.
Curr. Biol. 7:479-487(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH CDC42, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.3"Splicing variant of Cdc42 interacting protein-4 disrupts beta-catenin-mediated cell-cell adhesion: expression and function in renal cell carcinoma."
Tsuji E., Tsuji Y., Fujiwara T., Ogata S., Tsukamoto K., Saku K.
Biochem. Biophys. Res. Commun. 339:1083-1088(2006) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), INTERACTION WITH CTNNB1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYROSINE RESIDUES. - Ref.14"Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules."
Tian L., Nelson D.L., Stewart D.M.
J. Biol. Chem. 275:7854-7861(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CDC42; MICROTUBULES AND WAS, SUBCELLULAR LOCATION, MUTAGENESIS OF ILE-454 AND LEU-468. - Ref.17"Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1."
Richnau N., Aspenstroem P.
J. Biol. Chem. 276:35060-35070(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ARHGAP17, SUBCELLULAR LOCATION. - Ref.18"Felic (CIP4b), a novel binding partner with the Src kinase Lyn and Cdc42, localizes to the phagocytic cup."
Dombrosky-Ferlan P., Grishin A., Botelho R.J., Sampson M., Wang L., Rudert W.A., Grinstein S., Corey S.J.
Blood 101:2804-2809(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CDC42; LYN AND SRC, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT TYROSINE RESIDUES. - Ref.19"Cdc42-interacting protein 4 binds to huntingtin: neuropathologic and biological evidence for a role in Huntington's disease."
Holbert S., Dedeoglu A., Humbert S., Saudou F., Ferrante R.J., Neri C.
Proc. Natl. Acad. Sci. U.S.A. 100:2712-2717(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HD, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.20"AKAP350 interaction with cdc42 interacting protein 4 at the Golgi apparatus."
Larocca M.C., Shanks R.A., Tian L., Nelson D.L., Stewart D.M., Goldenring J.R.
Mol. Biol. Cell 15:2771-2781(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH AKAP9, SUBCELLULAR LOCATION, PHOSPHORYLATION. - Ref.21"Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins."
Itoh T., Erdmann K.S., Roux A., Habermann B., Werner H., De Camilli P.
Dev. Cell 9:791-804(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH DNM1 AND WASL, SUBCELLULAR LOCATION. - Ref.23"Regulation of FasL expression: a SH3 domain containing protein family involved in the lysosomal association of FasL."
Qian J., Chen W., Lettau M., Podda G., Zoernig M., Kabelitz D., Janssen O.
Cell. Signal. 18:1327-1337(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH FASLG, SUBCELLULAR LOCATION. - Ref.24"The diaphanous-related formin DAAM1 collaborates with the Rho GTPases RhoA and Cdc42, CIP4 and Src in regulating cell morphogenesis and actin dynamics."
Aspenstroem P., Richnau N., Johansson A.-S.
Exp. Cell Res. 312:2180-2194(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH DAAM1; DIAPH1 AND DIAPH2, SUBCELLULAR LOCATION. - Ref.33"Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis."
Shimada A., Niwa H., Tsujita K., Suetsugu S., Nitta K., Hanawa-Suetsugu K., Akasaka R., Nishino Y., Toyama M., Chen L., Liu Z.-J., Wang B.C., Yamamoto M., Terada T., Miyazawa A., Tanaka A., Sugano S., Shirouzu M. , Nagayama K., Takenawa T., Yokoyama S.
Cell 129:761-772(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 10-303, DOMAIN F-BAR, COILED-COIL DOMAIN, SUBUNIT.
<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-739936,EBI-739936 | ||
| APP1 | P53933 | 3 | EBI-6550597,EBI-28798 | From Saccharomyces cerevisiae (strain ATCC 204508 / S288c). |
| ARHGAP12 | Q1RLN5 | 3 | EBI-739936,EBI-3959665 | |
| ARHGAP17 | Q68EM7 | 3 | EBI-739936,EBI-1642807 | |
| ARHGAP44 | Q17R89-2 | 3 | EBI-739936,EBI-10238335 | |
| CDC42 | P60953 | 2 | EBI-739936,EBI-81752 | |
| DAAM1 | Q9Y4D1 | 2 | EBI-6550597,EBI-2817289 | |
| FASLG | P48023 | 4 | EBI-739936,EBI-495538 | |
| Inpp5d | P97573 | 2 | EBI-16191375,EBI-8008869 | From Rattus norvegicus. |
| LYN | P07948 | 2 | EBI-739936,EBI-79452 | |
| RHOJ | Q9H4E5 | 3 | EBI-739936,EBI-6285694 | |
| SH3BP1 | Q9Y3L3 | 3 | EBI-739936,EBI-346869 | |
| SMARCE1 | Q969G3 | 4 | EBI-6550597,EBI-455078 | |
| TINF2 | Q9BSI4 | 2 | EBI-739936,EBI-717399 | |
| WASF1 | Q92558 | 3 | EBI-739936,EBI-1548747 |
<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
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 114733, 52 interactors |
Database of interacting proteins More...DIPi | DIP-39840N |
Protein interaction database and analysis system More...IntActi | Q15642, 46 interactors |
Molecular INTeraction database More...MINTi | Q15642 |
<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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 10 – 53 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 44 | |
| <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 | 68 – 97 | 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 | 30 | |
| <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 | 99 – 160 | 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 | 62 | |
| <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 | 166 – 206 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 41 | |
| <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 | 208 – 258 | 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 | 51 | |
| <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 | 261 – 271 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 273 – 275 | 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 | 391 – 394 | 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 | 396 – 421 | 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 | 26 | |
| <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 | 423 – 433 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 435 – 437 | 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 | 440 – 442 | 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 | 444 – 477 | 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 | 34 | |
| <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 – 549 | 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 | 566 – 571 | 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 | 574 – 576 | 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 | 578 – 582 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 584 – 586 | 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 | 588 – 592 | 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 | 593 – 595 | 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 | 596 – 598 | 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 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q15642 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q15642 |
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 | Q15642 |
<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 | 1 – 264 | F-BARPROSITE-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 | 264 | |
| <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 | 393 – 470 | REM-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 | 78 | |
| <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 | 540 – 601 | SH3PROSITE-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 | 62 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 1 – 117 | Required for podosome formation and interaction with AKAP9 and microtubules1 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
| 117 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 1 – 117 | Required for translocation to the plasma membrane in response to insulinBy similarityAdd BLAST | 117 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 293 – 601 | Interaction with PDE6GBy similarityAdd BLAST | 309 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 293 – 537 | Interaction with CDC42Add BLAST | 245 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 471 – 601 | Required for interaction with FASLG and localization to lysosomes1 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
| 131 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 487 – 541 | Interaction with DNM2 and WASLBy similarityAdd BLAST | 55 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 529 – 601 | Interaction with DNM1 and WASL1 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
| 73 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 538 – 601 | Required for podosome formationAdd BLAST | 64 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 544 – 601 | Interaction with WAS1 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
| 58 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 546 – 601 | Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH22 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
| 56 |
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 | 67 – 259 | Add BLAST | 193 | |
| <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 | 388 – 481 | Add BLAST | 94 |
<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>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.33"Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis."
Shimada A., Niwa H., Tsujita K., Suetsugu S., Nitta K., Hanawa-Suetsugu K., Akasaka R., Nishino Y., Toyama M., Chen L., Liu Z.-J., Wang B.C., Yamamoto M., Terada T., Miyazawa A., Tanaka A., Sugano S., Shirouzu M. , Nagayama K., Takenawa T., Yokoyama S.
Cell 129:761-772(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 10-303, DOMAIN F-BAR, COILED-COIL DOMAIN, SUBUNIT.
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<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, SH3 domainPhylogenomic databases
Ensembl GeneTree More...GeneTreei | ENSGT00510000046403 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG002489 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q15642 |
KEGG Orthology (KO) More...KOi | K07196 |
Identification of Orthologs from Complete Genome Data More...OMAi | MNRAPSD |
Database of Orthologous Groups More...OrthoDBi | EOG091G038P |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q15642 |
TreeFam database of animal gene trees More...TreeFami | TF351162 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.20.1270.60, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR027267 AH/BAR_dom_sf IPR028498 CIP4 IPR031160 F_BAR IPR001060 FCH_dom IPR036028 SH3-like_dom_sf IPR001452 SH3_domain |
The PANTHER Classification System More...PANTHERi | PTHR43990:SF2 PTHR43990:SF2, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00611 FCH, 1 hit PF00018 SH3_1, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00055 FCH, 1 hit SM00326 SH3, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF103657 SSF103657, 1 hit SSF50044 SSF50044, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51741 F_BAR, 1 hit PS51860 REM_1, 1 hit PS50002 SH3, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (5)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 5 <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
MDWGTELWDQ FEVLERHTQW GLDLLDRYVK FVKERTEVEQ AYAKQLRSLV
60 70 80 90 100
KKYLPKRPAK DDPESKFSQQ QSFVQILQEV NDFAGQRELV AENLSVRVCL
110 120 130 140 150
ELTKYSQEMK QERKMHFQEG RRAQQQLENG FKQLENSKRK FERDCREAEK
160 170 180 190 200
AAQTAERLDQ DINATKADVE KAKQQAHLRS HMAEESKNEY AAQLQRFNRD
210 220 230 240 250
QAHFYFSQMP QIFDKLQDMD ERRATRLGAG YGLLSEAELE VVPIIAKCLE
260 270 280 290 300
GMKVAANAVD PKNDSHVLIE LHKSGFARPG DVEFEDFSQP MNRAPSDSSL
310 320 330 340 350
GTPSDGRPEL RGPGRSRTKR WPFGKKNKPR PPPLSPLGGP VPSALPNGPP
360 370 380 390 400
SPRSGRDPLA ILSEISKSVK PRLASFRSLR GSRGTVVTED FSHLPPEQQR
410 420 430 440 450
KRLQQQLEER SRELQKEVDQ REALKKMKDV YEKTPQMGDP ASLEPQIAET
460 470 480 490 500
LSNIERLKLE VQKYEAWLAE AESRVLSNRG DSLSRHARPP DPPASAPPDS
510 520 530 540 550
SSNSASQDTK ESSEEPPSEE SQDTPIYTEF DEDFEEEPTS PIGHCVAIYH
560 570 580 590 600
FEGSSEGTIS MAEGEDLSLM EEDKGDGWTR VRRKEGGEGY VPTSYLRVTL
N
The sequence of this isoform differs from the canonical sequence as follows:
329-384: Missing.
10 20 30 40 50
MDWGTELWDQ FEVLERHTQW GLDLLDRYVK FVKERTEVEQ AYAKQLRSLV
60 70 80 90 100
KKYLPKRPAK DDPESKFSQQ QSFVQILQEV NDFAGQRELV AENLSVRVCL
110 120 130 140 150
ELTKYSQEMK QERKMHFQEG RRAQQQLENG FKQLENSKRK FERDCREAEK
160 170 180 190 200
AAQTAERLDQ DINATKADVE KAKQQAHLRS HMAEESKNEY AAQLQRFNRD
210 220 230 240 250
QAHFYFSQMP QIFDKLQDMD ERRATRLGAG YGLLSEAELE VVPIIAKCLE
260 270 280 290 300
GMKVAANAVD PKNDSHVLIE LHKSGFARPG DVEFEDFSQP MNRAPSDSSL
310 320 330 340 350
GTPSDGRPEL RGPGRSRTKR WPFGKKNKTV VTEDFSHLPP EQQRKRLQQQ
360 370 380 390 400
LEERSRELQK EVDQREALKK MKDVYEKTPQ MGDPASLEPQ IAETLSNIER
410 420 430 440 450
LKLEVQKYEA WLAEAESRVL SNRGDSLSRH ARPPDPPASA PPDSSSNSAS
460 470 480 490 500
QDTKESSEEP PSEESQDTPI YTEFDEDFEE EPTSPIGHCV AIYHFEGSSE
510 520 530 540
GTISMAEGED LSLMEEDKGD GWTRVRRKEG GEGYVPTSYL RVTLN
The sequence of this isoform differs from the canonical sequence as follows:
329-384: Missing.
553-601: GSSEGTISMA...PTSYLRVTLN → DLGPPPPPSQ...LTPWLRLRPV
10 20 30 40 50
MDWGTELWDQ FEVLERHTQW GLDLLDRYVK FVKERTEVEQ AYAKQLRSLV
60 70 80 90 100
KKYLPKRPAK DDPESKFSQQ QSFVQILQEV NDFAGQRELV AENLSVRVCL
110 120 130 140 150
ELTKYSQEMK QERKMHFQEG RRAQQQLENG FKQLENSKRK FERDCREAEK
160 170 180 190 200
AAQTAERLDQ DINATKADVE KAKQQAHLRS HMAEESKNEY AAQLQRFNRD
210 220 230 240 250
QAHFYFSQMP QIFDKLQDMD ERRATRLGAG YGLLSEAELE VVPIIAKCLE
260 270 280 290 300
GMKVAANAVD PKNDSHVLIE LHKSGFARPG DVEFEDFSQP MNRAPSDSSL
310 320 330 340 350
GTPSDGRPEL RGPGRSRTKR WPFGKKNKTV VTEDFSHLPP EQQRKRLQQQ
360 370 380 390 400
LEERSRELQK EVDQREALKK MKDVYEKTPQ MGDPASLEPQ IAETLSNIER
410 420 430 440 450
LKLEVQKYEA WLAEAESRVL SNRGDSLSRH ARPPDPPASA PPDSSSNSAS
460 470 480 490 500
QDTKESSEEP PSEESQDTPI YTEFDEDFEE EPTSPIGHCV AIYHFEDLGP
510 520 530 540 550
PPPPSQGPAR ALSLWPRVKT SVLWKKTKGT AGPGSGGKRE ARATCPPPTS
560 570 580 590
ESRSIEPCQR REEGGCRLLL LGHGGSQDLG TLFLTPWLRL RPV
The sequence of this isoform differs from the canonical sequence as follows:
329-384: Missing.
512-512: S → R
513-601: Missing.
10 20 30 40 50
MDWGTELWDQ FEVLERHTQW GLDLLDRYVK FVKERTEVEQ AYAKQLRSLV
60 70 80 90 100
KKYLPKRPAK DDPESKFSQQ QSFVQILQEV NDFAGQRELV AENLSVRVCL
110 120 130 140 150
ELTKYSQEMK QERKMHFQEG RRAQQQLENG FKQLENSKRK FERDCREAEK
160 170 180 190 200
AAQTAERLDQ DINATKADVE KAKQQAHLRS HMAEESKNEY AAQLQRFNRD
210 220 230 240 250
QAHFYFSQMP QIFDKLQDMD ERRATRLGAG YGLLSEAELE VVPIIAKCLE
260 270 280 290 300
GMKVAANAVD PKNDSHVLIE LHKSGFARPG DVEFEDFSQP MNRAPSDSSL
310 320 330 340 350
GTPSDGRPEL RGPGRSRTKR WPFGKKNKTV VTEDFSHLPP EQQRKRLQQQ
360 370 380 390 400
LEERSRELQK EVDQREALKK MKDVYEKTPQ MGDPASLEPQ IAETLSNIER
410 420 430 440 450
LKLEVQKYEA WLAEAESRVL SNRGDSLSRH ARPPDPPASA PPDSSSNSAS
QDTKER
The sequence of this isoform differs from the canonical sequence as follows:
330-341: RPPPLSPLGGPV → SRQPWDSGDRGF
342-601: Missing.
10 20 30 40 50
MDWGTELWDQ FEVLERHTQW GLDLLDRYVK FVKERTEVEQ AYAKQLRSLV
60 70 80 90 100
KKYLPKRPAK DDPESKFSQQ QSFVQILQEV NDFAGQRELV AENLSVRVCL
110 120 130 140 150
ELTKYSQEMK QERKMHFQEG RRAQQQLENG FKQLENSKRK FERDCREAEK
160 170 180 190 200
AAQTAERLDQ DINATKADVE KAKQQAHLRS HMAEESKNEY AAQLQRFNRD
210 220 230 240 250
QAHFYFSQMP QIFDKLQDMD ERRATRLGAG YGLLSEAELE VVPIIAKCLE
260 270 280 290 300
GMKVAANAVD PKNDSHVLIE LHKSGFARPG DVEFEDFSQP MNRAPSDSSL
310 320 330 340
GTPSDGRPEL RGPGRSRTKR WPFGKKNKPS RQPWDSGDRG F
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 | 158 | L → P in AAK77492 (PubMed:12054674).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 | 310 | L → P in AAK77492 (PubMed:12054674).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 | 419 | D → G in BAD96829 (Ref. 8) 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 | 440 | P → S in BAD96829 (Ref. 8) 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 | 473 | S → R in AAK77492 (PubMed:12054674).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 | 487 – 499 | ARPPD…SAPPD → KHPIICRLIHFSN in AAC41729 (Ref. 10) CuratedAdd BLAST | 13 | |
| <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 | 553 | G → W in CAG38751 (Ref. 5) 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_021716 | 329 – 384 | Missing in isoform 2, isoform 3 and isoform 4. 7 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
| 56 | |
| <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_021717 | 330 – 341 | RPPPL…LGGPV → SRQPWDSGDRGF in isoform 5. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 12 | |
| <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_021718 | 342 – 601 | Missing in isoform 5. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 260 | |
| <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_021719 | 512 | S → R in isoform 4. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_021720 | 513 – 601 | Missing in isoform 4. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 89 | |
| <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_021721 | 553 – 601 | GSSEG…RVTLN → DLGPPPPPSQGPARALSLWP RVKTSVLWKKTKGTAGPGSG GKREARATCPPPTSESRSIE PCQRREEGGCRLLLLGHGGS QDLGTLFLTPWLRLRPV in isoform 3. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 49 |
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 | AJ000414 mRNA Translation: CAA04062.1 AF380114 mRNA Translation: AAK77492.1 AY081141 mRNA Translation: AAL89588.1 AB072596 mRNA Translation: BAB88853.1 AF502289 mRNA Translation: AAM46851.1 CR536513 mRNA Translation: CAG38751.1 BT006698 mRNA Translation: AAP35344.1 BT020167 mRNA Translation: AAV38969.1 BT020171 mRNA Translation: AAV43773.1 AK223109 mRNA Translation: BAD96829.1 AK313296 mRNA Translation: BAG36103.1 AC008760 Genomic DNA No translation available. CH471139 Genomic DNA Translation: EAW69065.1 CH471139 Genomic DNA Translation: EAW69062.1 CH471139 Genomic DNA Translation: EAW69063.1 BC013002 mRNA Translation: AAH13002.1 L40379 mRNA Translation: AAC41729.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS12172.1 [Q15642-2] CCDS74271.1 [Q15642-1] CCDS74272.1 [Q15642-3] |
NCBI Reference Sequences More...RefSeqi | NP_001275891.1, NM_001288962.1 [Q15642-1] NP_001275892.1, NM_001288963.1 NP_004231.1, NM_004240.3 [Q15642-2] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.515094 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000313244; ENSP00000320117; ENSG00000125733 [Q15642-1] ENST00000313285; ENSP00000320493; ENSG00000125733 [Q15642-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 9322 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:9322 |
UCSC genome browser More...UCSCi | uc002mfr.5 human [Q15642-1] |
<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 | |
|---|---|---|---|---|---|
| Q15642 | UPI00059ABC23 | 689 | |||
| UPI0003AE06E5 | 634 | ||||
| UPI0008139AD9 | 620 | ||||
| UPI0004BDBABE | 619 | ||||
| UPI000C2FAB98 | 617 | ||||
| +98 | |||||
| Q15642-2 | Uncharacterized protein | 662 | |||
| TRIP10 isoform 10 (Fragment) | 84 | ||||
| TRIP10 isoform 10 (Fragment) | 84 | ||||
| Cdc42-interacting protein 4 (Fragment) | 83 | ||||
| cdc42-interacting protein 4 isoform X2 | 595 | ||||
| +37 | |||||
| Q15642-3 | Uncharacterized protein | 662 | |||
| TRIP10 isoform 10 (Fragment) | 84 | ||||
| TRIP10 isoform 10 (Fragment) | 84 | ||||
| Cdc42-interacting protein 4 (Fragment) | 83 | ||||
| cdc42-interacting protein 4 isoform X2 | 595 | ||||
| +37 | |||||
| Q15642-5 | Cdc42-interacting protein 4 | 343 | |||
| TRIP10 isoform 4 | 343 | ||||
| TRIP10 isoform 4 | 343 | ||||
| UPI0005F58AB3 | 341 | ||||
| UPI000387D319 | 334 | ||||
| +1 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q15642 | UPI00059ABC23 | 689 | |||
| UPI0003AE06E5 | 634 | ||||
| UPI0008139AD9 | 620 | ||||
| UPI0004BDBABE | 619 | ||||
| UPI000C2FAB98 | 617 | ||||
| +144 | |||||
| Q15642-4 | UPI00032B1322 | 548 | |||
| UPI000C2A5951 | 455 | ||||
| UPI00062A5B3F | 602 | ||||
| UPI00064ED1BA | 583 | ||||
| Uncharacterized protein | 524 | ||||
| +114 | |||||
| Q15642-5 | TRIP10 isoform 4 | 343 | |||
| Cdc42-interacting protein 4 | 343 | ||||
| TRIP10 isoform 4 | 343 | ||||
| UPI0005F58AB3 | 341 | ||||
| CIP4 | 329 | ||||
| +12 | |||||
<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 | AJ000414 mRNA Translation: CAA04062.1 AF380114 mRNA Translation: AAK77492.1 AY081141 mRNA Translation: AAL89588.1 AB072596 mRNA Translation: BAB88853.1 AF502289 mRNA Translation: AAM46851.1 CR536513 mRNA Translation: CAG38751.1 BT006698 mRNA Translation: AAP35344.1 BT020167 mRNA Translation: AAV38969.1 BT020171 mRNA Translation: AAV43773.1 AK223109 mRNA Translation: BAD96829.1 AK313296 mRNA Translation: BAG36103.1 AC008760 Genomic DNA No translation available. CH471139 Genomic DNA Translation: EAW69065.1 CH471139 Genomic DNA Translation: EAW69062.1 CH471139 Genomic DNA Translation: EAW69063.1 BC013002 mRNA Translation: AAH13002.1 L40379 mRNA Translation: AAC41729.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS12172.1 [Q15642-2] CCDS74271.1 [Q15642-1] CCDS74272.1 [Q15642-3] |
NCBI Reference Sequences More...RefSeqi | NP_001275891.1, NM_001288962.1 [Q15642-1] NP_001275892.1, NM_001288963.1 NP_004231.1, NM_004240.3 [Q15642-2] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.515094 |
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 |
| 2CT4 | NMR | - | A | 543-599 | [»] | |
| 2EFK | X-ray | 2.30 | A | 10-303 | [»] | |
| 2KE4 | NMR | - | A | 388-481 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q15642 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q15642 | |||||
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 | 114733, 52 interactors |
Database of interacting proteins More...DIPi | DIP-39840N |
Protein interaction database and analysis system More...IntActi | Q15642, 46 interactors |
Molecular INTeraction database More...MINTi | Q15642 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q15642 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q15642 |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 118572632 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q15642 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q15642 |
PeptideAtlas More...PeptideAtlasi | Q15642 |
PRoteomics IDEntifications database More...PRIDEi | Q15642 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 60675 60676 [Q15642-2] 60677 [Q15642-3] 60678 [Q15642-4] 60679 [Q15642-5] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 9322 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000313244; ENSP00000320117; ENSG00000125733 [Q15642-1] ENST00000313285; ENSP00000320493; ENSG00000125733 [Q15642-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 9322 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:9322 |
UCSC genome browser More...UCSCi | uc002mfr.5 human [Q15642-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 9322 |
DisGeNET More...DisGeNETi | 9322 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000125733.17 |
GeneCards: human genes, protein and diseases More...GeneCardsi | TRIP10 |
H-Invitational Database, human transcriptome db More...H-InvDBi | HIX0014704 |
Human Gene Nomenclature Database More...HGNCi | HGNC:12304 TRIP10 |
Human Protein Atlas More...HPAi | HPA041934 HPA072625 HPA073886 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 604504 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q15642 |
Open Targets More...OpenTargetsi | ENSG00000125733 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA36983 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
Ensembl GeneTree More...GeneTreei | ENSGT00510000046403 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG002489 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q15642 |
KEGG Orthology (KO) More...KOi | K07196 |
Identification of Orthologs from Complete Genome Data More...OMAi | MNRAPSD |
Database of Orthologous Groups More...OrthoDBi | EOG091G038P |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q15642 |
TreeFam database of animal gene trees More...TreeFami | TF351162 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-194840 Rho GTPase cycle R-HSA-8856828 Clathrin-mediated endocytosis |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q15642 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q15642 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | TRIP10 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q15642 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | TRIP10 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 9322 |
Protein Ontology More...PROi | PR:Q15642 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000125733 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q15642 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q15642 HS |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.20.1270.60, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR027267 AH/BAR_dom_sf IPR028498 CIP4 IPR031160 F_BAR IPR001060 FCH_dom IPR036028 SH3-like_dom_sf IPR001452 SH3_domain |
The PANTHER Classification System More...PANTHERi | PTHR43990:SF2 PTHR43990:SF2, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00611 FCH, 1 hit PF00018 SH3_1, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00055 FCH, 1 hit SM00326 SH3, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF103657 SSF103657, 1 hit SSF50044 SSF50044, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51741 F_BAR, 1 hit PS51860 REM_1, 1 hit PS50002 SH3, 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 | CIP4_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 | Q15642Primary (citable) accession number: Q15642 Secondary accession number(s): B2R8A6 , B7WP22, D6W645, O15184, Q53G22, Q5TZN1, Q6FI24, Q8NFL1, Q8TCY1, Q8TDX3, Q96RJ1 | |
| <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: | November 1, 1997 |
| Last sequence update: | November 28, 2006 | |
| Last modified: | July 18, 2018 | |
| This is version 181 of the entry and version 3 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 19
Human chromosome 19: 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 - SIMILARITY comments
Index of protein domains and families
