UniProtKB - P55735 (SEC13_HUMAN)
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- BLAST>sp|P55735|SEC13_HUMAN Protein SEC13 homolog OS=Homo sapiens OX=9606 GN=SEC13 PE=1 SV=3 MVSVINTVDTSHEDMIHDAQMDYYGTRLATCSSDRSVKIFDVRNGGQILIADLRGHEGPV WQVAWAHPMYGNILASCSYDRKVIIWREENGTWEKSHEHAGHDSSVNSVCWAPHDYGLIL ACGSSDGAISLLTYTGEGQWEVKKINNAHTIGCNAVSWAPAVVPGSLIDHPSGQKPNYIK RFASGGCDNLIKLWKEEEDGQWKEEQKLEAHSDWVRDVAWAPSIGLPTSTIASCSQDGRV FIWTCDDASSNTWSPKLLHKFNDVVWHVSWSITANILAVSGGDNKVTLWKESVDGQWVCI SDVNKGQGSVSASVTEGQQNEQ
- Align
Protein SEC13 homolog
SEC13
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.9"The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus."
Tang B.L., Peter F., Krijnse-Locker J., Low S.H., Griffiths G., Hong W.
Mol. Cell. Biol. 17:256-266(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
<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.19"Sestrins inhibit mTORC1 kinase activation through the GATOR complex."
Parmigiani A., Nourbakhsh A., Ding B., Wang W., Kim Y.C., Akopiants K., Guan K.L., Karin M., Budanov A.V.
Cell Rep. 9:1281-1291(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH SESN2. - Ref.20"A Tumor suppressor complex with GAP activity for the Rag GTPases that signal amino acid sufficiency to mTORC1."
Bar-Peled L., Chantranupong L., Cherniack A.D., Chen W.W., Ottina K.A., Grabiner B.C., Spear E.D., Carter S.L., Meyerson M., Sabatini D.M.
Science 340:1100-1106(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN GATOR COMPLEX, INTERACTION WITH RRAG PROTEINS. - Ref.23"Mechanism of arginine sensing by CASTOR1 upstream of mTORC1."
Saxton R.A., Chantranupong L., Knockenhauer K.E., Schwartz T.U., Sabatini D.M.
Nature 536:229-233(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.
<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
- structural molecule activity Source: InterPro
<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
- antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
- antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
- cargo loading into COPII-coated vesicle Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- COPII vesicle coating Source: Reactome
- intracellular protein transport 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
- mRNA transport Source: UniProtKB-KW
- positive regulation of TORC1 signaling Source: InterPro
- positive regulation of TOR signaling Source: SGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Biological process | ER-Golgi transport, mRNA transport, Protein transport, Translocation, Transport |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal R-HSA-204005 COPII-mediated vesicle transport R-HSA-2132295 MHC class II antigen presentation R-HSA-2467813 Separation of Sister Chromatids R-HSA-2500257 Resolution of Sister Chromatid Cohesion R-HSA-5663220 RHO GTPases Activate Formins R-HSA-68877 Mitotic Prometaphase R-HSA-983170 Antigen Presentation: Folding, assembly and peptide loading of class I MHC |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P55735 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P55735 |
Protein family/group databases
Transport Classification Database More...TCDBi | 1.I.1.1.3 the eukaryotic nuclear pore complex (e-npc) family |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Protein SEC13 homologCuratedAlternative name(s): GATOR complex protein SEC13Curated SEC13-like protein 1 SEC13-related protein |
| <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:SEC13 Synonyms:D3S1231E, SEC13L1, SEC13R |
| <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:ENSG00000157020.17 |
Human Gene Nomenclature Database More...HGNCi | HGNC:10697 SEC13 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 600152 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P55735 |
<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
- Lysosome membrane 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.24"KICSTOR recruits GATOR1 to the lysosome and is necessary for nutrients to regulate mTORC1."
Wolfson R.L., Chantranupong L., Wyant G.A., Gu X., Orozco J.M., Shen K., Condon K.J., Petri S., Kedir J., Scaria S.M., Abu-Remaileh M., Frankel W.N., Sabatini D.M.
Nature 543:438-442(2017) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION.
- Lysosome membrane 1 Publication
Nucleus
- nuclear pore complex 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"Sec13 shuttles between the nucleus and the cytoplasm and stably interacts with Nup96 at the nuclear pore complex."
Enninga J., Levay A., Fontoura B.M.
Mol. Cell. Biol. 23:7271-7284(2003) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NUP96. - Ref.25"Architecture of a coat for the nuclear pore membrane."
Hsia K.C., Stavropoulos P., Blobel G., Hoelz A.
Cell 131:1313-1326(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-316 IN COMPLEX WITH YEAST NUP145C, SUBUNIT, SUBCELLULAR LOCATION.
- nuclear pore complex 2 Publications
Endoplasmic reticulum
- Endoplasmic reticulum membrane 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.9"The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus."
Tang B.L., Peter F., Krijnse-Locker J., Low S.H., Griffiths G., Hong W.
Mol. Cell. Biol. 17:256-266(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
<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.9"The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus."
Tang B.L., Peter F., Krijnse-Locker J., Low S.H., Griffiths G., Hong W.
Mol. Cell. Biol. 17:256-266(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
<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.9"The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus."
Tang B.L., Peter F., Krijnse-Locker J., Low S.H., Griffiths G., Hong W.
Mol. Cell. Biol. 17:256-266(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
- Endoplasmic reticulum membrane 1 Publication
Other locations
- COPII-coated vesicle membrane 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.9"The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus."
Tang B.L., Peter F., Krijnse-Locker J., Low S.H., Griffiths G., Hong W.
Mol. Cell. Biol. 17:256-266(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
<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.9"The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus."
Tang B.L., Peter F., Krijnse-Locker J., Low S.H., Griffiths G., Hong W.
Mol. Cell. Biol. 17:256-266(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
<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.9"The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus."
Tang B.L., Peter F., Krijnse-Locker J., Low S.H., Griffiths G., Hong W.
Mol. Cell. Biol. 17:256-266(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
Note: In interphase, localizes at both sides of the NPC.1 Publication- COPII-coated vesicle membrane 1 Publication
- Ref.10"Sec13 shuttles between the nucleus and the cytoplasm and stably interacts with Nup96 at the nuclear pore complex."
Enninga J., Levay A., Fontoura B.M.
Mol. Cell. Biol. 23:7271-7284(2003) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NUP96.
<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
Cytosol
- cytosol Source: Reactome
Endoplasmic reticulum
- endoplasmic reticulum membrane Source: Reactome
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Golgi apparatus
- Golgi membrane Source: GOC
Lysosome
- lysosomal membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Nucleus
- nuclear envelope Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- nuclear pore outer ring Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- nucleoplasm Source: HPA
Other locations
- COPII vesicle coat Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ER to Golgi transport vesicle membrane Source: Reactome
- GATOR2 complex Source: SGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- intracellular membrane-bounded organelle Source: HPA
<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
Cytoplasmic vesicle, Endoplasmic reticulum, Lysosome, Membrane, Nuclear pore complex, 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
Organism-specific databases
DisGeNET More...DisGeNETi | 6396 |
Open Targets More...OpenTargetsi | ENSG00000157020 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA35620 |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 50403748 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | RemovedCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>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
| |||
| <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_0000051203 | 2 – 322 | Protein SEC13 homologAdd BLAST | 321 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2 | N-acetylvalineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 184 | 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 | 309 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P55735 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P55735 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P55735 |
PeptideAtlas More...PeptideAtlasi | P55735 |
PRoteomics IDEntifications database More...PRIDEi | P55735 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 56858 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P55735 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P55735 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P55735 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000157020 |
CleanEx database of gene expression profiles More...CleanExi | HS_SEC13 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P55735 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P55735 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA035292 HPA057943 |
<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.10"Sec13 shuttles between the nucleus and the cytoplasm and stably interacts with Nup96 at the nuclear pore complex."
Enninga J., Levay A., Fontoura B.M.
Mol. Cell. Biol. 23:7271-7284(2003) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NUP96. - Ref.11"Human Sec31B: a family of new mammalian orthologues of yeast Sec31p that associate with the COPII coat."
Stankewich M.C., Stabach P.R., Morrow J.S.
J. Cell Sci. 119:958-969(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SEC31B. - Ref.12"The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A."
Yamasaki A., Tani K., Yamamoto A., Kitamura N., Komada M.
Mol. Biol. Cell 17:4876-4887(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SEC31A. - Ref.18"The Sestrins interact with GATOR2 to negatively regulate the amino-acid-sensing pathway upstream of mTORC1."
Chantranupong L., Wolfson R.L., Orozco J.M., Saxton R.A., Scaria S.M., Bar-Peled L., Spooner E., Isasa M., Gygi S.P., Sabatini D.M.
Cell Rep. 9:1-8(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SESN1; SESN2 AND SESN3. - Ref.19"Sestrins inhibit mTORC1 kinase activation through the GATOR complex."
Parmigiani A., Nourbakhsh A., Ding B., Wang W., Kim Y.C., Akopiants K., Guan K.L., Karin M., Budanov A.V.
Cell Rep. 9:1281-1291(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH SESN2. - Ref.20"A Tumor suppressor complex with GAP activity for the Rag GTPases that signal amino acid sufficiency to mTORC1."
Bar-Peled L., Chantranupong L., Cherniack A.D., Chen W.W., Ottina K.A., Grabiner B.C., Spear E.D., Carter S.L., Meyerson M., Sabatini D.M.
Science 340:1100-1106(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN GATOR COMPLEX, INTERACTION WITH RRAG PROTEINS. - Ref.22"The CASTOR proteins are arginine sensors for the mTORC1 pathway."
Chantranupong L., Scaria S.M., Saxton R.A., Gygi M.P., Shen K., Wyant G.A., Wang T., Harper J.W., Gygi S.P., Sabatini D.M.
Cell 165:153-164(2016) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CASTOR2 AND CASTOR1. - Ref.25"Architecture of a coat for the nuclear pore membrane."
Hsia K.C., Stavropoulos P., Blobel G., Hoelz A.
Cell 131:1313-1326(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-316 IN COMPLEX WITH YEAST NUP145C, SUBUNIT, SUBCELLULAR LOCATION.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| itself | 3 | EBI-1046596,EBI-1046596 | ||
| NUP145 | P49687 | 15 | EBI-1046596,EBI-11730 | From Saccharomyces cerevisiae (strain ATCC 204508 / S288c). |
| SEC16B | E9PK14 | 4 | EBI-12235008,EBI-12372595 | |
| SEC16B | Q96JE7-2 | 5 | EBI-1046596,EBI-10215083 | |
| SEC31A | O94979-1 | 9 | EBI-10045850,EBI-15564399 | |
| SEH1L | Q96EE3 | 3 | EBI-1046596,EBI-922818 | |
| TRAF5 | O00463 | 3 | EBI-1046596,EBI-523498 |
<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 | 112296, 83 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P55735 |
Database of interacting proteins More...DIPi | DIP-39091N |
Protein interaction database and analysis system More...IntActi | P55735, 66 interactors |
Molecular INTeraction database More...MINTi | P55735 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000312122 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 16 – 21 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 23 – 25 | 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 | 27 – 32 | 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 | 35 – 43 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 46 – 54 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 60 – 65 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 68 – 70 | 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 | 74 – 78 | 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 | 83 – 86 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 89 – 91 | 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 | 95 – 99 | 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 | 108 – 111 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 114 – 116 | 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 | 120 – 123 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 125 – 127 | 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 | 129 – 134 | 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 | 136 – 138 | 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 | 140 – 142 | 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 | 148 – 151 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 181 – 183 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 193 – 196 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 202 – 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 | 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 | 215 – 219 | 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 | 230 – 235 | 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 | 239 – 244 | 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 | 246 – 249 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 257 – 260 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 265 – 270 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 272 – 274 | 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 | 277 – 284 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 286 – 291 | 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 | 297 – 302 | 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 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P55735 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P55735 |
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 | P55735 |
<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 ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 11 – 50 | WD 1Add BLAST | 40 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 55 – 96 | WD 2Add BLAST | 42 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 101 – 144 | WD 3Add BLAST | 44 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 148 – 204 | WD 4Add BLAST | 57 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 210 – 253 | WD 5Add BLAST | 44 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 260 – 299 | WD 6Add BLAST | 40 |
<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
Repeat, WD repeatPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1332 Eukaryota ENOG410XPFM LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00550000075049 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000216895 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG057343 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P55735 |
KEGG Orthology (KO) More...KOi | K14004 |
Identification of Orthologs from Complete Genome Data More...OMAi | REDNDRW |
Database of Orthologous Groups More...OrthoDBi | EOG091G0DTE |
Database for complete collections of gene phylogenies More...PhylomeDBi | P55735 |
TreeFam database of animal gene trees More...TreeFami | TF300815 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.130.10.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR037596 Sec13 IPR037363 Sec13/Seh1_fam IPR015943 WD40/YVTN_repeat-like_dom_sf IPR001680 WD40_repeat IPR017986 WD40_repeat_dom IPR036322 WD40_repeat_dom_sf |
The PANTHER Classification System More...PANTHERi | PTHR11024 PTHR11024, 1 hit PTHR11024:SF2 PTHR11024:SF2, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00400 WD40, 5 hits |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00320 WD40, 6 hits |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50978 SSF50978, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50082 WD_REPEATS_2, 3 hits PS50294 WD_REPEATS_REGION, 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 (4)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 4 <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
MVSVINTVDT SHEDMIHDAQ MDYYGTRLAT CSSDRSVKIF DVRNGGQILI
60 70 80 90 100
ADLRGHEGPV WQVAWAHPMY GNILASCSYD RKVIIWREEN GTWEKSHEHA
110 120 130 140 150
GHDSSVNSVC WAPHDYGLIL ACGSSDGAIS LLTYTGEGQW EVKKINNAHT
160 170 180 190 200
IGCNAVSWAP AVVPGSLIDH PSGQKPNYIK RFASGGCDNL IKLWKEEEDG
210 220 230 240 250
QWKEEQKLEA HSDWVRDVAW APSIGLPTST IASCSQDGRV FIWTCDDASS
260 270 280 290 300
NTWSPKLLHK FNDVVWHVSW SITANILAVS GGDNKVTLWK ESVDGQWVCI
310 320
SDVNKGQGSV SASVTEGQQN EQ
The sequence of this isoform differs from the canonical sequence as follows:
1-14: Missing.
10 20 30 40 50
MIHDAQMDYY GTRLATCSSD RSVKIFDVRN GGQILIADLR GHEGPVWQVA
60 70 80 90 100
WAHPMYGNIL ASCSYDRKVI IWREENGTWE KSHEHAGHDS SVNSVCWAPH
110 120 130 140 150
DYGLILACGS SDGAISLLTY TGEGQWEVKK INNAHTIGCN AVSWAPAVVP
160 170 180 190 200
GSLIDHPSGQ KPNYIKRFAS GGCDNLIKLW KEEEDGQWKE EQKLEAHSDW
210 220 230 240 250
VRDVAWAPSI GLPTSTIASC SQDGRVFIWT CDDASSNTWS PKLLHKFNDV
260 270 280 290 300
VWHVSWSITA NILAVSGGDN KVTLWKESVD GQWVCISDVN KGQGSVSASV
TEGQQNEQ
The sequence of this isoform differs from the canonical sequence as follows:
1-1: M → MREPVLTWCVPLELLCSHPLPLSAFLKSQVKLYTYRACAGKDEMGKM
10 20 30 40 50
MREPVLTWCV PLELLCSHPL PLSAFLKSQV KLYTYRACAG KDEMGKMVSV
60 70 80 90 100
INTVDTSHED MIHDAQMDYY GTRLATCSSD RSVKIFDVRN GGQILIADLR
110 120 130 140 150
GHEGPVWQVA WAHPMYGNIL ASCSYDRKVI IWREENGTWE KSHEHAGHDS
160 170 180 190 200
SVNSVCWAPH DYGLILACGS SDGAISLLTY TGEGQWEVKK INNAHTIGCN
210 220 230 240 250
AVSWAPAVVP GSLIDHPSGQ KPNYIKRFAS GGCDNLIKLW KEEEDGQWKE
260 270 280 290 300
EQKLEAHSDW VRDVAWAPSI GLPTSTIASC SQDGRVFIWT CDDASSNTWS
310 320 330 340 350
PKLLHKFNDV VWHVSWSITA NILAVSGGDN KVTLWKESVD GQWVCISDVN
360
KGQGSVSASV TEGQQNEQ
The sequence of this isoform differs from the canonical sequence as follows:
1-1: M → MGKM
10 20 30 40 50
MGKMVSVINT VDTSHEDMIH DAQMDYYGTR LATCSSDRSV KIFDVRNGGQ
60 70 80 90 100
ILIADLRGHE GPVWQVAWAH PMYGNILASC SYDRKVIIWR EENGTWEKSH
110 120 130 140 150
EHAGHDSSVN SVCWAPHDYG LILACGSSDG AISLLTYTGE GQWEVKKINN
160 170 180 190 200
AHTIGCNAVS WAPAVVPGSL IDHPSGQKPN YIKRFASGGC DNLIKLWKEE
210 220 230 240 250
EDGQWKEEQK LEAHSDWVRD VAWAPSIGLP TSTIASCSQD GRVFIWTCDD
260 270 280 290 300
ASSNTWSPKL LHKFNDVVWH VSWSITANIL AVSGGDNKVT LWKESVDGQW
310 320
VCISDVNKGQ GSVSASVTEG QQNEQ
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 | 51 | A → V in L09260 (PubMed:7987303).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_053413 | 172 | S → L. Corresponds to variant dbSNP:rs34078590Ensembl. | 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_046191 | 1 – 14 | Missing in isoform 2. 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
| 14 | |
| <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_054695 | 1 | M → MREPVLTWCVPLELLCSHPL PLSAFLKSQVKLYTYRACAG KDEMGKM 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
| 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_058966 | 1 | M → MGKM in isoform 4. | 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 | L09260 mRNA No translation available. AF052155 mRNA No translation available. AK301999 mRNA Translation: BAG63403.1 AC022384 Genomic DNA No translation available. BC002634 mRNA Translation: AAH02634.2 BC006167 mRNA Translation: AAH06167.1 BC091506 mRNA Translation: AAH91506.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS2599.1 [P55735-1] CCDS46751.1 [P55735-2] CCDS63540.1 [P55735-3] |
NCBI Reference Sequences More...RefSeqi | NP_001129498.1, NM_001136026.2 [P55735-3] NP_001129704.1, NM_001136232.2 [P55735-2] NP_109598.2, NM_030673.3 [P55735-4] NP_899195.1, NM_183352.2 [P55735-1] XP_005265436.1, XM_005265379.2 [P55735-4] XP_016862508.1, XM_017007019.1 [P55735-3] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.166924 Hs.672979 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000337354; ENSP00000336566; ENSG00000157020 [P55735-4] ENST00000350697; ENSP00000312122; ENSG00000157020 [P55735-1] ENST00000383801; ENSP00000373312; ENSG00000157020 [P55735-3] ENST00000397109; ENSP00000380298; ENSG00000157020 [P55735-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 6396 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:6396 |
UCSC genome browser More...UCSCi | uc003bvm.5 human [P55735-1] |
<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, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P55735 | UPI000181D1B4 | 316 | |||
| P55735-3 | 368 | ||||
| P55735-2 | 308 | ||||
| Protein SEC13 homolog (Fragment) | 24 | ||||
| P55735-4 | 325 | ||||
| +1 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P55735 | UPI000181D1B4 | 316 | |||
| Protein SEC13 like protein | 432 | ||||
| SEC13 homolog, nuclear pore and COPII coat complex component | 368 | ||||
| SEC13 homolog, nuclear pore and COPII coat complex component | 368 | ||||
| SEC13 homolog, nuclear pore and COPII coat complex component | 322 | ||||
| +46 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P55735 | UPI000181D1B4 | 316 | |||
| Protein SEC13 like protein | 432 | ||||
| SEC13 homolog, nuclear pore and COPII coat complex component | 368 | ||||
| SEC13 homolog, nuclear pore and COPII coat complex component | 322 | ||||
| SEC13 homolog, nuclear pore and COPII coat complex component | 308 | ||||
| +227 | |||||
<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 | L09260 mRNA No translation available. AF052155 mRNA No translation available. AK301999 mRNA Translation: BAG63403.1 AC022384 Genomic DNA No translation available. BC002634 mRNA Translation: AAH02634.2 BC006167 mRNA Translation: AAH06167.1 BC091506 mRNA Translation: AAH91506.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS2599.1 [P55735-1] CCDS46751.1 [P55735-2] CCDS63540.1 [P55735-3] |
NCBI Reference Sequences More...RefSeqi | NP_001129498.1, NM_001136026.2 [P55735-3] NP_001129704.1, NM_001136232.2 [P55735-2] NP_109598.2, NM_030673.3 [P55735-4] NP_899195.1, NM_183352.2 [P55735-1] XP_005265436.1, XM_005265379.2 [P55735-4] XP_016862508.1, XM_017007019.1 [P55735-3] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.166924 Hs.672979 |
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 |
| 3BG0 | X-ray | 3.15 | A/D/E/H | 1-316 | [»] | |
| 3BG1 | X-ray | 3.00 | A/D/E/H | 1-316 | [»] | |
| 5A9Q | electron microscopy | 23.00 | 6/F/O/X | 1-322 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P55735 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P55735 | |||||
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 | 112296, 83 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P55735 |
Database of interacting proteins More...DIPi | DIP-39091N |
Protein interaction database and analysis system More...IntActi | P55735, 66 interactors |
Molecular INTeraction database More...MINTi | P55735 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000312122 |
Protein family/group databases
Transport Classification Database More...TCDBi | 1.I.1.1.3 the eukaryotic nuclear pore complex (e-npc) family |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P55735 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P55735 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P55735 |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 50403748 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P55735 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P55735 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P55735 |
PeptideAtlas More...PeptideAtlasi | P55735 |
PRoteomics IDEntifications database More...PRIDEi | P55735 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 56858 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 6396 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000337354; ENSP00000336566; ENSG00000157020 [P55735-4] ENST00000350697; ENSP00000312122; ENSG00000157020 [P55735-1] ENST00000383801; ENSP00000373312; ENSG00000157020 [P55735-3] ENST00000397109; ENSP00000380298; ENSG00000157020 [P55735-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 6396 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:6396 |
UCSC genome browser More...UCSCi | uc003bvm.5 human [P55735-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 6396 |
DisGeNET More...DisGeNETi | 6396 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000157020.17 |
GeneCards: human genes, protein and diseases More...GeneCardsi | SEC13 |
Human Gene Nomenclature Database More...HGNCi | HGNC:10697 SEC13 |
Human Protein Atlas More...HPAi | HPA035292 HPA057943 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 600152 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P55735 |
Open Targets More...OpenTargetsi | ENSG00000157020 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA35620 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1332 Eukaryota ENOG410XPFM LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00550000075049 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000216895 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG057343 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P55735 |
KEGG Orthology (KO) More...KOi | K14004 |
Identification of Orthologs from Complete Genome Data More...OMAi | REDNDRW |
Database of Orthologous Groups More...OrthoDBi | EOG091G0DTE |
Database for complete collections of gene phylogenies More...PhylomeDBi | P55735 |
TreeFam database of animal gene trees More...TreeFami | TF300815 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal R-HSA-204005 COPII-mediated vesicle transport R-HSA-2132295 MHC class II antigen presentation R-HSA-2467813 Separation of Sister Chromatids R-HSA-2500257 Resolution of Sister Chromatid Cohesion R-HSA-5663220 RHO GTPases Activate Formins R-HSA-68877 Mitotic Prometaphase R-HSA-983170 Antigen Presentation: Folding, assembly and peptide loading of class I MHC |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P55735 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P55735 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | SEC13 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P55735 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | SEC13 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 6396 |
Protein Ontology More...PROi | PR:P55735 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000157020 |
CleanEx database of gene expression profiles More...CleanExi | HS_SEC13 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P55735 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P55735 HS |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.130.10.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR037596 Sec13 IPR037363 Sec13/Seh1_fam IPR015943 WD40/YVTN_repeat-like_dom_sf IPR001680 WD40_repeat IPR017986 WD40_repeat_dom IPR036322 WD40_repeat_dom_sf |
The PANTHER Classification System More...PANTHERi | PTHR11024 PTHR11024, 1 hit PTHR11024:SF2 PTHR11024:SF2, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00400 WD40, 5 hits |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00320 WD40, 6 hits |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50978 SSF50978, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50082 WD_REPEATS_2, 3 hits PS50294 WD_REPEATS_REGION, 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 | SEC13_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 | P55735Primary (citable) accession number: P55735 Secondary accession number(s): A8MV37 , B4DXJ1, Q5BJF0, Q9BRM6, Q9BUG7 | |
| <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: | January 23, 2007 | |
| 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, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 3
Human chromosome 3: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
