UniProtKB - Q01082 (SPTB2_HUMAN)
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- BLAST>sp|Q01082|SPTB2_HUMAN Spectrin beta chain, non-erythrocytic 1 OS=Homo sapiens OX=9606 GN=SPTBN1 PE=1 SV=2 MTTTVATDYDNIEIQQQYSDVNNRWDVDDWDNENSSARLFERSRIKALADEREAVQKKTF TKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKAL QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILRFQIQDISVETEDNKEKKSAKDALL LWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNL AEQHLGLTKLLDPEDISVDHPDEKSIITYVVTYYHYFSKMKALAVEGKRIGKVLDNAIET EKMIEKYESLASDLLEWIEQTIIILNNRKFANSLVGVQQQLQAFNTYRTVEKPPKFTEKG NLEVLLFTIQSKMRANNQKVYMPREGKLISDINKAWERLEKAEHERELALRNELIRQEKL EQLARRFDRKAAMRETWLSENQRLVSQDNFGFDLPAVEAATKKHEAIETDIAAYEERVQA VVAVARELEAENYHDIKRITARKDNVIRLWEYLLELLRARRQRLEMNLGLQKIFQEMLYI MDWMDEMKVLVLSQDYGKHLLGVEDLLQKHTLVEADIGIQAERVRGVNASAQKFATDGEG YKPCDPQVIRDRVAHMEFCYQELCQLAAERRARLEESRRLWKFFWEMAEEEGWIREKEKI LSSDDYGKDLTSVMRLLSKHRAFEDEMSGRSGHFEQAIKEGEDMIAEEHFGSEKIRERII YIREQWANLEQLSAIRKKRLEEASLLHQFQADADDIDAWMLDILKIVSSSDVGHDEYSTQ SLVKKHKDVAEEIANYRPTLDTLHEQASALPQEHAESPDVRGRLSGIEERYKEVAELTRL RKQALQDTLALYKMFSEADACELWIDEKEQWLNNMQIPEKLEDLEVIQHRFESLEPEMNN QASRVAVVNQIARQLMHSGHPSEKEIKAQQDKLNTRWSQFRELVDRKKDALLSALSIQNY HLECNETKSWIREKTKVIESTQDLGNDLAGVMALQRKLTGMERDLVAIEAKLSDLQKEAE KLESEHPDQAQAILSRLAEISDVWEEMKTTLKNREASLGEASKLQQFLRDLDDFQSWLSR TQTAIASEDMPNTLTEAEKLLTQHENIKNEIDNYEEDYQKMRDMGEMVTQGQTDAQYMFL RQRLQALDTGWNELHKMWENRQNLLSQSHAYQQFLRDTKQAEAFLNNQEYVLAHTEMPTT LEGAEAAIKKQEDFMTTMDANEEKINAVVETGRRLVSDGNINSDRIQEKVDSIDDRHRKN RETASELLMRLKDNRDLQKFLQDCQELSLWINEKMLTAQDMSYDEARNLHSKWLKHQAFM AELASNKEWLDKIEKEGMQLISEKPETEAVVKEKLTGLHKMWEVLESTTQTKAQRLFDAN KAELFTQSCADLDKWLHGLESQIQSDDYGKDLTSVNILLKKQQMLENQMEVRKKEIEELQ SQAQALSQEGKSTDEVDSKRLTVQTKFMELLEPLNERKHNLLASKEIHQFNRDVEDEILW VGERMPLATSTDHGHNLQTVQLLIKKNQTLQKEIQGHQPRIDDIFERSQNIVTDSSSLSA EAIRQRLADLKQLWGLLIEETEKRHRRLEEAHRAQQYYFDAAEAEAWMSEQELYMMSEEK AKDEQSAVSMLKKHQILEQAVEDYAETVHQLSKTSRALVADSHPESERISMRQSKVDKLY AGLKDLAEERRGKLDERHRLFQLNREVDDLEQWIAEREVVAGSHELGQDYEHVTMLQERF REFARDTGNIGQERVDTVNHLADELINSGHSDAATIAEWKDGLNEAWADLLELIDTRTQI LAASYELHKFYHDAKEIFGRIQDKHKKLPEELGRDQNTVETLQRMHTTFEHDIQALGTQV RQLQEDAARLQAAYAGDKADDIQKRENEVLEAWKSLLDACESRRVRLVDTGDKFRFFSMV RDLMLWMEDVIRQIEAQEKPRDVSSVELLMNNHQGIKAEIDARNDSFTTCIELGKSLLAR KHYASEEIKEKLLQLTEKRKEMIDKWEDRWEWLRLILEVHQFSRDASVAEAWLLGQEPYL SSREIGQSVDEVEKLIKRHEAFEKSAATWDERFSALERLTTLELLEVRRQQEEEERKRRP PSPEPSTKVSEEAESQQQWDTSKGEQVSQNGLPAEQGSPRMAETVDTSEMVNGATEQRTS SKESSPIPSPTSDRKAKTALPAQSAATLPARTQETPSAQMEGFLNRKHEWEAHNKKASSR SWHNVYCVINNQEMGFYKDAKTAASGIPYHSEVPVSLKEAVCEVALDYKKKKHVFKLRLN DGNEYLFQAKDDEEMNTWIQAISSAISSDKHEVSASTQSTPASSRAQTLPTSVVTITSES SPGKREKDKEKDKEKRFSLFGKKK
- Align
Spectrin beta chain, non-erythrocytic 1
SPTBN1
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>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
- actin binding 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
- ankyrin binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- cadherin binding Source: BHF-UCLInferred from high throughput direct assayi
- calmodulin binding Source: UniProtKB-KW
- GTPase binding Source: UniProtKB <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
- phospholipid binding Source: InterPro
- protein-containing complex binding Source: Ensembl
- Ras guanyl-nucleotide exchange factor activity Source: Reactome
- RNA binding Source: UniProtKBInferred from high throughput direct assayi
- structural constituent of cytoskeleton Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
<p>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 filament capping Source: UniProtKB-KW
- axon guidance Source: Reactome
- common-partner SMAD protein phosphorylation Source: Ensembl
- ER to Golgi vesicle-mediated transport Source: Reactome
- Golgi to plasma membrane protein transport Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- MAPK cascade Source: Reactome
- membrane assembly Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- mitotic cytokinesis Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- plasma membrane organization Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of interleukin-2 secretion Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of protein localization to plasma membrane Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- protein localization to plasma membrane Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- regulation of protein localization to plasma membrane Source: UniProtKB <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
- regulation of SMAD protein signal transduction Source: Ensembl
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Actin capping, Actin-binding, Calmodulin-binding |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-373753 Nephrin family interactions R-HSA-375165 NCAM signaling for neurite out-growth R-HSA-445095 Interaction between L1 and Ankyrins R-HSA-5673001 RAF/MAP kinase cascade R-HSA-6807878 COPI-mediated anterograde transport |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q01082 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q01082 |
<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: Spectrin beta chain, non-erythrocytic 1Alternative name(s): Beta-II spectrin Fodrin beta chain Spectrin, non-erythroid beta chain 1 |
| <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:SPTBN1 Synonyms:SPTB2 |
| <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:ENSG00000115306.15 |
Human Gene Nomenclature Database More...HGNCi | HGNC:11275 SPTBN1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 182790 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q01082 |
<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
Cytoskeleton
- cytoskeleton By similarity
Other locations
- M line By similarity
Note: Colocalizes with ANK2 in a distinct intracellular compartment of neonatal cardiomyocytes.By similarity
Plasma membrane
- Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Cytoskeleton
- cuticular plate Source: Ensembl
- spectrin 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
- spectrin-associated cytoskeleton Source: BHF-UCL <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
Cytosol
- cytosol Source: Reactome
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Nucleus
- nucleolus Source: HGNC <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
Plasma Membrane
- axolemma Source: BHF-UCL
Other locations
- cytoplasm Source: HGNC <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
- M band Source: UniProtKB-SubCell
- postsynaptic density Source: Ensembl
- protein-containing complex Source: Ensembl
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cell membrane, Cytoplasm, Cytoskeleton, 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
Organism-specific databases
DisGeNET More...DisGeNETi | 6711 |
Open Targets More...OpenTargetsi | ENSG00000115306 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA36104 |
Chemistry databases
Drug and drug target database More...DrugBanki | DB01373 Calcium |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | SPTBN1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 116242799 |
<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>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_0000073461 | 2 – 2364 | Spectrin beta chain, non-erythrocytic 1Add BLAST | 2363 |
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-acetylthreonineCombined 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 | 36 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 90 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 228 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 817 | 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 | 825 | 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 | 903 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1057 | 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 | 1076 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1079 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1237 | 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 | 1388 | 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 | 1447 | 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 | 1557 | 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 | 1805 | PhosphotyrosineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1815 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1913 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1989 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2102 | 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 | 2128 | 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 | 2138 | 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 | 2147 | PhosphothreonineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2148 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2159 | PhosphothreonineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2160 | 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 | 2161 | 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 | 2164 | 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 | 2165 | 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 | 2169 | 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 | 2171 | PhosphothreonineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2172 | 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 | 2184 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2187 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2195 | PhosphothreonineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2314 | 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 | 2319 | 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 | 2320 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 2324 | O-linked (GlcNAc) serineBy similarity | 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 | 2328 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2340 | 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 | 2341 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Isoform 2 (identifier: Q01082-3) | |||||
| <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 | 14 | 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, Glycoprotein, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q01082 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q01082 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q01082 |
PeptideAtlas More...PeptideAtlasi | Q01082 |
PRoteomics IDEntifications database More...PRIDEi | Q01082 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 57910 57911 [Q01082-2] 57912 [Q01082-3] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q01082 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q01082 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q01082 |
<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.2"A novel isoform of beta-spectrin II localizes to cerebellar Purkinje-cell bodies and interacts with neurofibromatosis type 2 gene product schwannomin."
Chen Y., Yu P., Lu D., Tagle D.A., Cai T.
J. Mol. Neurosci. 17:59-70(2001) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, VARIANT HIS-1411.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000115306 |
CleanEx database of gene expression profiles More...CleanExi | HS_SPTBN1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q01082 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q01082 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA012685 HPA013149 |
<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 which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
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.9"Ankyrin-B targets beta2-spectrin to an intracellular compartment in neonatal cardiomyocytes."
Mohler P.J., Yoon W., Bennett V.
J. Biol. Chem. 279:40185-40193(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ANK2. - Ref.25"A conserved sequence in CAMSAP1 (calmodulin regulated spectrin-associated protein 1) links its interaction with spectrin and calmodulin to neurite outgrowth."
King M.D., Phillips G.W., Bignone P.A., Hayes N.V., Pinder J.C., Baines A.J.
J. Neurochem. 128:391-402(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CAMSAP1.
<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 |
|---|---|---|---|---|
| DISC1 | Q9NRI5 | 3 | EBI-351561,EBI-529989 | |
| SPTA1 | P02549 | 3 | EBI-351561,EBI-375617 | |
| SPTAN1 | Q13813 | 7 | EBI-351561,EBI-351450 |
<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
- actin binding 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
- ankyrin binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- cadherin binding Source: BHF-UCLInferred from high throughput direct assayi
- calmodulin binding Source: UniProtKB-KW
- GTPase binding Source: UniProtKB <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
- Ras guanyl-nucleotide exchange factor activity Source: Reactome
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 112589, 143 interactors |
Database of interacting proteins More...DIPi | DIP-33182N |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | Q01082 |
Protein interaction database and analysis system More...IntActi | Q01082, 94 interactors |
Molecular INTeraction database More...MINTi | Q01082 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000349259 |
<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 | 174 – 186 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <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 | 187 – 189 | 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 | 196 – 199 | 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 | 200 – 202 | 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 | 206 – 215 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 217 – 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 | 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 | 222 – 224 | 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 | 230 – 245 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 253 – 256 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 263 – 277 | 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 | 15 | |
| <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 | 1697 – 1721 | 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 | 25 | |
| <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 | 1730 – 1767 | 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 | 38 | |
| <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 | 1773 – 1826 | 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 | 54 | |
| <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 | 1836 – 1852 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1854 – 1873 | 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 | 20 | |
| <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 | 1877 – 1935 | 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 | 59 | |
| <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 | 1943 – 1962 | 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 | 20 | |
| <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 | 1964 – 1979 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1985 – 2014 | 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 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q01082 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q01082 |
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 | Q01082 |
<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 | 54 – 158 | Calponin-homology (CH) 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 | 105 | |
| <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 | 173 – 278 | Calponin-homology (CH) 2PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 106 | |
| <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 | 303 – 411 | Spectrin 1Sequence analysisAdd BLAST | 109 | |
| <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 | 423 – 525 | Spectrin 2Sequence analysisAdd BLAST | 103 | |
| <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 | 530 – 636 | Spectrin 3Sequence analysisAdd BLAST | 107 | |
| <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 | 639 – 742 | Spectrin 4Sequence analysisAdd BLAST | 104 | |
| <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 | 745 – 847 | Spectrin 5Sequence analysisAdd BLAST | 103 | |
| <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 | 850 – 952 | Spectrin 6Sequence analysisAdd BLAST | 103 | |
| <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 | 957 – 1060 | Spectrin 7Sequence analysisAdd BLAST | 104 | |
| <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 | 1063 – 1166 | Spectrin 8Sequence analysisAdd BLAST | 104 | |
| <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 | 1170 – 1258 | Spectrin 9Sequence analysisAdd BLAST | 89 | |
| <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 | 1276 – 1376 | Spectrin 10Sequence analysisAdd BLAST | 101 | |
| <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 | 1381 – 1482 | Spectrin 11Sequence analysisAdd BLAST | 102 | |
| <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 | 1486 – 1590 | Spectrin 12Sequence analysisAdd BLAST | 105 | |
| <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 | 1592 – 1696 | Spectrin 13Sequence analysisAdd BLAST | 105 | |
| <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 | 1698 – 1801 | Spectrin 14Sequence analysisAdd BLAST | 104 | |
| <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 | 1805 – 1907 | Spectrin 15Sequence analysisAdd BLAST | 103 | |
| <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 | 1914 – 2014 | Spectrin 16Sequence analysisAdd BLAST | 101 | |
| <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 | 2018 – 2097 | Spectrin 17Sequence analysisAdd BLAST | 80 | |
| <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 | 2197 – 2307 | PHPROSITE-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 | 111 |
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 | 2 – 275 | Actin-bindingAdd BLAST | 274 | |
| <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 | 1563 – 2093 | Interaction with ANK21 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
| 531 | |
| <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 | 2149 – 2177 | Mediates interaction with CAMSAP11 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
| 29 |
<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
RepeatPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0035 Eukaryota COG5069 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118813 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG057912 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q01082 |
KEGG Orthology (KO) More...KOi | K06115 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q01082 |
TreeFam database of animal gene trees More...TreeFami | TF313446 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00014 CH, 2 hits |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.418.10, 2 hits 2.30.29.30, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001589 Actinin_actin-bd_CS IPR001715 CH-domain IPR036872 CH_dom_sf IPR011993 PH-like_dom_sf IPR001605 PH_dom-spectrin-type IPR001849 PH_domain IPR018159 Spectrin/alpha-actinin IPR016343 Spectrin_bsu IPR002017 Spectrin_repeat |
Pfam protein domain database More...Pfami | View protein in Pfam PF00307 CH, 2 hits PF00435 Spectrin, 17 hits |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF002297 Spectrin_beta_subunit, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00683 SPECTRINPH |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00033 CH, 2 hits SM00233 PH, 1 hit SM00150 SPEC, 17 hits |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF47576 SSF47576, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00019 ACTININ_1, 1 hit PS00020 ACTININ_2, 1 hit PS50021 CH, 2 hits PS50003 PH_DOMAIN, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)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 3 <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
MTTTVATDYD NIEIQQQYSD VNNRWDVDDW DNENSSARLF ERSRIKALAD
60 70 80 90 100
EREAVQKKTF TKWVNSHLAR VSCRITDLYT DLRDGRMLIK LLEVLSGERL
110 120 130 140 150
PKPTKGRMRI HCLENVDKAL QFLKEQRVHL ENMGSHDIVD GNHRLTLGLI
160 170 180 190 200
WTIILRFQIQ DISVETEDNK EKKSAKDALL LWCQMKTAGY PNVNIHNFTT
210 220 230 240 250
SWRDGMAFNA LIHKHRPDLI DFDKLKKSNA HYNLQNAFNL AEQHLGLTKL
260 270 280 290 300
LDPEDISVDH PDEKSIITYV VTYYHYFSKM KALAVEGKRI GKVLDNAIET
310 320 330 340 350
EKMIEKYESL ASDLLEWIEQ TIIILNNRKF ANSLVGVQQQ LQAFNTYRTV
360 370 380 390 400
EKPPKFTEKG NLEVLLFTIQ SKMRANNQKV YMPREGKLIS DINKAWERLE
410 420 430 440 450
KAEHERELAL RNELIRQEKL EQLARRFDRK AAMRETWLSE NQRLVSQDNF
460 470 480 490 500
GFDLPAVEAA TKKHEAIETD IAAYEERVQA VVAVARELEA ENYHDIKRIT
510 520 530 540 550
ARKDNVIRLW EYLLELLRAR RQRLEMNLGL QKIFQEMLYI MDWMDEMKVL
560 570 580 590 600
VLSQDYGKHL LGVEDLLQKH TLVEADIGIQ AERVRGVNAS AQKFATDGEG
610 620 630 640 650
YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE
660 670 680 690 700
EGWIREKEKI LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE
710 720 730 740 750
GEDMIAEEHF GSEKIRERII YIREQWANLE QLSAIRKKRL EEASLLHQFQ
760 770 780 790 800
ADADDIDAWM LDILKIVSSS DVGHDEYSTQ SLVKKHKDVA EEIANYRPTL
810 820 830 840 850
DTLHEQASAL PQEHAESPDV RGRLSGIEER YKEVAELTRL RKQALQDTLA
860 870 880 890 900
LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN
910 920 930 940 950
QASRVAVVNQ IARQLMHSGH PSEKEIKAQQ DKLNTRWSQF RELVDRKKDA
960 970 980 990 1000
LLSALSIQNY HLECNETKSW IREKTKVIES TQDLGNDLAG VMALQRKLTG
1010 1020 1030 1040 1050
MERDLVAIEA KLSDLQKEAE KLESEHPDQA QAILSRLAEI SDVWEEMKTT
1060 1070 1080 1090 1100
LKNREASLGE ASKLQQFLRD LDDFQSWLSR TQTAIASEDM PNTLTEAEKL
1110 1120 1130 1140 1150
LTQHENIKNE IDNYEEDYQK MRDMGEMVTQ GQTDAQYMFL RQRLQALDTG
1160 1170 1180 1190 1200
WNELHKMWEN RQNLLSQSHA YQQFLRDTKQ AEAFLNNQEY VLAHTEMPTT
1210 1220 1230 1240 1250
LEGAEAAIKK QEDFMTTMDA NEEKINAVVE TGRRLVSDGN INSDRIQEKV
1260 1270 1280 1290 1300
DSIDDRHRKN RETASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD
1310 1320 1330 1340 1350
MSYDEARNLH SKWLKHQAFM AELASNKEWL DKIEKEGMQL ISEKPETEAV
1360 1370 1380 1390 1400
VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN KAELFTQSCA DLDKWLHGLE
1410 1420 1430 1440 1450
SQIQSDDYGK DLTSVNILLK KQQMLENQME VRKKEIEELQ SQAQALSQEG
1460 1470 1480 1490 1500
KSTDEVDSKR LTVQTKFMEL LEPLNERKHN LLASKEIHQF NRDVEDEILW
1510 1520 1530 1540 1550
VGERMPLATS TDHGHNLQTV QLLIKKNQTL QKEIQGHQPR IDDIFERSQN
1560 1570 1580 1590 1600
IVTDSSSLSA EAIRQRLADL KQLWGLLIEE TEKRHRRLEE AHRAQQYYFD
1610 1620 1630 1640 1650
AAEAEAWMSE QELYMMSEEK AKDEQSAVSM LKKHQILEQA VEDYAETVHQ
1660 1670 1680 1690 1700
LSKTSRALVA DSHPESERIS MRQSKVDKLY AGLKDLAEER RGKLDERHRL
1710 1720 1730 1740 1750
FQLNREVDDL EQWIAEREVV AGSHELGQDY EHVTMLQERF REFARDTGNI
1760 1770 1780 1790 1800
GQERVDTVNH LADELINSGH SDAATIAEWK DGLNEAWADL LELIDTRTQI
1810 1820 1830 1840 1850
LAASYELHKF YHDAKEIFGR IQDKHKKLPE ELGRDQNTVE TLQRMHTTFE
1860 1870 1880 1890 1900
HDIQALGTQV RQLQEDAARL QAAYAGDKAD DIQKRENEVL EAWKSLLDAC
1910 1920 1930 1940 1950
ESRRVRLVDT GDKFRFFSMV RDLMLWMEDV IRQIEAQEKP RDVSSVELLM
1960 1970 1980 1990 2000
NNHQGIKAEI DARNDSFTTC IELGKSLLAR KHYASEEIKE KLLQLTEKRK
2010 2020 2030 2040 2050
EMIDKWEDRW EWLRLILEVH QFSRDASVAE AWLLGQEPYL SSREIGQSVD
2060 2070 2080 2090 2100
EVEKLIKRHE AFEKSAATWD ERFSALERLT TLELLEVRRQ QEEEERKRRP
2110 2120 2130 2140 2150
PSPEPSTKVS EEAESQQQWD TSKGEQVSQN GLPAEQGSPR MAETVDTSEM
2160 2170 2180 2190 2200
VNGATEQRTS SKESSPIPSP TSDRKAKTAL PAQSAATLPA RTQETPSAQM
2210 2220 2230 2240 2250
EGFLNRKHEW EAHNKKASSR SWHNVYCVIN NQEMGFYKDA KTAASGIPYH
2260 2270 2280 2290 2300
SEVPVSLKEA VCEVALDYKK KKHVFKLRLN DGNEYLFQAK DDEEMNTWIQ
2310 2320 2330 2340 2350
AISSAISSDK HEVSASTQST PASSRAQTLP TSVVTITSES SPGKREKDKE
2360
KDKEKRFSLF GKKK
The sequence of this isoform differs from the canonical sequence as follows:
2141-2168: MAETVDTSEMVNGATEQRTSSKESSPIP → VSYRSQTYQNYKNFNSRRTASDQPWSGL
2169-2364: Missing.
10 20 30 40 50
MTTTVATDYD NIEIQQQYSD VNNRWDVDDW DNENSSARLF ERSRIKALAD
60 70 80 90 100
EREAVQKKTF TKWVNSHLAR VSCRITDLYT DLRDGRMLIK LLEVLSGERL
110 120 130 140 150
PKPTKGRMRI HCLENVDKAL QFLKEQRVHL ENMGSHDIVD GNHRLTLGLI
160 170 180 190 200
WTIILRFQIQ DISVETEDNK EKKSAKDALL LWCQMKTAGY PNVNIHNFTT
210 220 230 240 250
SWRDGMAFNA LIHKHRPDLI DFDKLKKSNA HYNLQNAFNL AEQHLGLTKL
260 270 280 290 300
LDPEDISVDH PDEKSIITYV VTYYHYFSKM KALAVEGKRI GKVLDNAIET
310 320 330 340 350
EKMIEKYESL ASDLLEWIEQ TIIILNNRKF ANSLVGVQQQ LQAFNTYRTV
360 370 380 390 400
EKPPKFTEKG NLEVLLFTIQ SKMRANNQKV YMPREGKLIS DINKAWERLE
410 420 430 440 450
KAEHERELAL RNELIRQEKL EQLARRFDRK AAMRETWLSE NQRLVSQDNF
460 470 480 490 500
GFDLPAVEAA TKKHEAIETD IAAYEERVQA VVAVARELEA ENYHDIKRIT
510 520 530 540 550
ARKDNVIRLW EYLLELLRAR RQRLEMNLGL QKIFQEMLYI MDWMDEMKVL
560 570 580 590 600
VLSQDYGKHL LGVEDLLQKH TLVEADIGIQ AERVRGVNAS AQKFATDGEG
610 620 630 640 650
YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE
660 670 680 690 700
EGWIREKEKI LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE
710 720 730 740 750
GEDMIAEEHF GSEKIRERII YIREQWANLE QLSAIRKKRL EEASLLHQFQ
760 770 780 790 800
ADADDIDAWM LDILKIVSSS DVGHDEYSTQ SLVKKHKDVA EEIANYRPTL
810 820 830 840 850
DTLHEQASAL PQEHAESPDV RGRLSGIEER YKEVAELTRL RKQALQDTLA
860 870 880 890 900
LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN
910 920 930 940 950
QASRVAVVNQ IARQLMHSGH PSEKEIKAQQ DKLNTRWSQF RELVDRKKDA
960 970 980 990 1000
LLSALSIQNY HLECNETKSW IREKTKVIES TQDLGNDLAG VMALQRKLTG
1010 1020 1030 1040 1050
MERDLVAIEA KLSDLQKEAE KLESEHPDQA QAILSRLAEI SDVWEEMKTT
1060 1070 1080 1090 1100
LKNREASLGE ASKLQQFLRD LDDFQSWLSR TQTAIASEDM PNTLTEAEKL
1110 1120 1130 1140 1150
LTQHENIKNE IDNYEEDYQK MRDMGEMVTQ GQTDAQYMFL RQRLQALDTG
1160 1170 1180 1190 1200
WNELHKMWEN RQNLLSQSHA YQQFLRDTKQ AEAFLNNQEY VLAHTEMPTT
1210 1220 1230 1240 1250
LEGAEAAIKK QEDFMTTMDA NEEKINAVVE TGRRLVSDGN INSDRIQEKV
1260 1270 1280 1290 1300
DSIDDRHRKN RETASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD
1310 1320 1330 1340 1350
MSYDEARNLH SKWLKHQAFM AELASNKEWL DKIEKEGMQL ISEKPETEAV
1360 1370 1380 1390 1400
VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN KAELFTQSCA DLDKWLHGLE
1410 1420 1430 1440 1450
SQIQSDDYGK DLTSVNILLK KQQMLENQME VRKKEIEELQ SQAQALSQEG
1460 1470 1480 1490 1500
KSTDEVDSKR LTVQTKFMEL LEPLNERKHN LLASKEIHQF NRDVEDEILW
1510 1520 1530 1540 1550
VGERMPLATS TDHGHNLQTV QLLIKKNQTL QKEIQGHQPR IDDIFERSQN
1560 1570 1580 1590 1600
IVTDSSSLSA EAIRQRLADL KQLWGLLIEE TEKRHRRLEE AHRAQQYYFD
1610 1620 1630 1640 1650
AAEAEAWMSE QELYMMSEEK AKDEQSAVSM LKKHQILEQA VEDYAETVHQ
1660 1670 1680 1690 1700
LSKTSRALVA DSHPESERIS MRQSKVDKLY AGLKDLAEER RGKLDERHRL
1710 1720 1730 1740 1750
FQLNREVDDL EQWIAEREVV AGSHELGQDY EHVTMLQERF REFARDTGNI
1760 1770 1780 1790 1800
GQERVDTVNH LADELINSGH SDAATIAEWK DGLNEAWADL LELIDTRTQI
1810 1820 1830 1840 1850
LAASYELHKF YHDAKEIFGR IQDKHKKLPE ELGRDQNTVE TLQRMHTTFE
1860 1870 1880 1890 1900
HDIQALGTQV RQLQEDAARL QAAYAGDKAD DIQKRENEVL EAWKSLLDAC
1910 1920 1930 1940 1950
ESRRVRLVDT GDKFRFFSMV RDLMLWMEDV IRQIEAQEKP RDVSSVELLM
1960 1970 1980 1990 2000
NNHQGIKAEI DARNDSFTTC IELGKSLLAR KHYASEEIKE KLLQLTEKRK
2010 2020 2030 2040 2050
EMIDKWEDRW EWLRLILEVH QFSRDASVAE AWLLGQEPYL SSREIGQSVD
2060 2070 2080 2090 2100
EVEKLIKRHE AFEKSAATWD ERFSALERLT TLELLEVRRQ QEEEERKRRP
2110 2120 2130 2140 2150
PSPEPSTKVS EEAESQQQWD TSKGEQVSQN GLPAEQGSPR VSYRSQTYQN
2160
YKNFNSRRTA SDQPWSGL
The sequence of this isoform differs from the canonical sequence as follows:
1-49: MTTTVATDYD...FERSRIKALA → MELQRTSSIS...QLEGRFKQLQ
2141-2225: MAETVDTSEM...KASSRSWHNV → VSYRSQTYQNYKNFNSRRTASDQPWSGL
2226-2364: Missing.
10 20 30 40 50
MELQRTSSIS GPLSPAYTGQ VPYNYNQLEG RFKQLQDERE AVQKKTFTKW
60 70 80 90 100
VNSHLARVSC RITDLYTDLR DGRMLIKLLE VLSGERLPKP TKGRMRIHCL
110 120 130 140 150
ENVDKALQFL KEQRVHLENM GSHDIVDGNH RLTLGLIWTI ILRFQIQDIS
160 170 180 190 200
VETEDNKEKK SAKDALLLWC QMKTAGYPNV NIHNFTTSWR DGMAFNALIH
210 220 230 240 250
KHRPDLIDFD KLKKSNAHYN LQNAFNLAEQ HLGLTKLLDP EDISVDHPDE
260 270 280 290 300
KSIITYVVTY YHYFSKMKAL AVEGKRIGKV LDNAIETEKM IEKYESLASD
310 320 330 340 350
LLEWIEQTII ILNNRKFANS LVGVQQQLQA FNTYRTVEKP PKFTEKGNLE
360 370 380 390 400
VLLFTIQSKM RANNQKVYMP REGKLISDIN KAWERLEKAE HERELALRNE
410 420 430 440 450
LIRQEKLEQL ARRFDRKAAM RETWLSENQR LVSQDNFGFD LPAVEAATKK
460 470 480 490 500
HEAIETDIAA YEERVQAVVA VARELEAENY HDIKRITARK DNVIRLWEYL
510 520 530 540 550
LELLRARRQR LEMNLGLQKI FQEMLYIMDW MDEMKVLVLS QDYGKHLLGV
560 570 580 590 600
EDLLQKHTLV EADIGIQAER VRGVNASAQK FATDGEGYKP CDPQVIRDRV
610 620 630 640 650
AHMEFCYQEL CQLAAERRAR LEESRRLWKF FWEMAEEEGW IREKEKILSS
660 670 680 690 700
DDYGKDLTSV MRLLSKHRAF EDEMSGRSGH FEQAIKEGED MIAEEHFGSE
710 720 730 740 750
KIRERIIYIR EQWANLEQLS AIRKKRLEEA SLLHQFQADA DDIDAWMLDI
760 770 780 790 800
LKIVSSSDVG HDEYSTQSLV KKHKDVAEEI ANYRPTLDTL HEQASALPQE
810 820 830 840 850
HAESPDVRGR LSGIEERYKE VAELTRLRKQ ALQDTLALYK MFSEADACEL
860 870 880 890 900
WIDEKEQWLN NMQIPEKLED LEVIQHRFES LEPEMNNQAS RVAVVNQIAR
910 920 930 940 950
QLMHSGHPSE KEIKAQQDKL NTRWSQFREL VDRKKDALLS ALSIQNYHLE
960 970 980 990 1000
CNETKSWIRE KTKVIESTQD LGNDLAGVMA LQRKLTGMER DLVAIEAKLS
1010 1020 1030 1040 1050
DLQKEAEKLE SEHPDQAQAI LSRLAEISDV WEEMKTTLKN REASLGEASK
1060 1070 1080 1090 1100
LQQFLRDLDD FQSWLSRTQT AIASEDMPNT LTEAEKLLTQ HENIKNEIDN
1110 1120 1130 1140 1150
YEEDYQKMRD MGEMVTQGQT DAQYMFLRQR LQALDTGWNE LHKMWENRQN
1160 1170 1180 1190 1200
LLSQSHAYQQ FLRDTKQAEA FLNNQEYVLA HTEMPTTLEG AEAAIKKQED
1210 1220 1230 1240 1250
FMTTMDANEE KINAVVETGR RLVSDGNINS DRIQEKVDSI DDRHRKNRET
1260 1270 1280 1290 1300
ASELLMRLKD NRDLQKFLQD CQELSLWINE KMLTAQDMSY DEARNLHSKW
1310 1320 1330 1340 1350
LKHQAFMAEL ASNKEWLDKI EKEGMQLISE KPETEAVVKE KLTGLHKMWE
1360 1370 1380 1390 1400
VLESTTQTKA QRLFDANKAE LFTQSCADLD KWLHGLESQI QSDDYGKDLT
1410 1420 1430 1440 1450
SVNILLKKQQ MLENQMEVRK KEIEELQSQA QALSQEGKST DEVDSKRLTV
1460 1470 1480 1490 1500
QTKFMELLEP LNERKHNLLA SKEIHQFNRD VEDEILWVGE RMPLATSTDH
1510 1520 1530 1540 1550
GHNLQTVQLL IKKNQTLQKE IQGHQPRIDD IFERSQNIVT DSSSLSAEAI
1560 1570 1580 1590 1600
RQRLADLKQL WGLLIEETEK RHRRLEEAHR AQQYYFDAAE AEAWMSEQEL
1610 1620 1630 1640 1650
YMMSEEKAKD EQSAVSMLKK HQILEQAVED YAETVHQLSK TSRALVADSH
1660 1670 1680 1690 1700
PESERISMRQ SKVDKLYAGL KDLAEERRGK LDERHRLFQL NREVDDLEQW
1710 1720 1730 1740 1750
IAEREVVAGS HELGQDYEHV TMLQERFREF ARDTGNIGQE RVDTVNHLAD
1760 1770 1780 1790 1800
ELINSGHSDA ATIAEWKDGL NEAWADLLEL IDTRTQILAA SYELHKFYHD
1810 1820 1830 1840 1850
AKEIFGRIQD KHKKLPEELG RDQNTVETLQ RMHTTFEHDI QALGTQVRQL
1860 1870 1880 1890 1900
QEDAARLQAA YAGDKADDIQ KRENEVLEAW KSLLDACESR RVRLVDTGDK
1910 1920 1930 1940 1950
FRFFSMVRDL MLWMEDVIRQ IEAQEKPRDV SSVELLMNNH QGIKAEIDAR
1960 1970 1980 1990 2000
NDSFTTCIEL GKSLLARKHY ASEEIKEKLL QLTEKRKEMI DKWEDRWEWL
2010 2020 2030 2040 2050
RLILEVHQFS RDASVAEAWL LGQEPYLSSR EIGQSVDEVE KLIKRHEAFE
2060 2070 2080 2090 2100
KSAATWDERF SALERLTTLE LLEVRRQQEE EERKRRPPSP EPSTKVSEEA
2110 2120 2130 2140 2150
ESQQQWDTSK GEQVSQNGLP AEQGSPRVSY RSQTYQNYKN FNSRRTASDQ
PWSGL
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 583 | R → W in BAD92985 (Ref. 3) 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_032641 | 1411 | D → H2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
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_026054 | 1 – 49 | MTTTV…IKALA → MELQRTSSISGPLSPAYTGQ VPYNYNQLEGRFKQLQ in isoform 2. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 49 | |
| <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_026055 | 2141 – 2225 | MAETV…SWHNV → VSYRSQTYQNYKNFNSRRTA SDQPWSGL in isoform 2. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 85 | |
| <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_000720 | 2141 – 2168 | MAETV…SSPIP → VSYRSQTYQNYKNFNSRRTA SDQPWSGL in isoform Short. 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
| 28 | |
| <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_000721 | 2169 – 2364 | Missing in isoform Short. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 196 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_026056 | 2226 – 2364 | Missing in isoform 2. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 139 |
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 | M96803 mRNA Translation: AAA60580.1 AF327441 mRNA Translation: AAO15362.1 AB209748 mRNA Translation: BAD92985.1 Different initiation. AC093110 Genomic DNA Translation: AAY24229.1 AC092839 Genomic DNA No translation available. CH471053 Genomic DNA Translation: EAX00147.1 BC137282 mRNA Translation: AAI37283.1 BC137283 mRNA Translation: AAI37284.1 S65762 mRNA Translation: AAB28324.1 AJ005694 mRNA Translation: CAA06678.1 AJ238723 Genomic DNA Translation: CAB91088.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS33198.1 [Q01082-1] CCDS33199.1 [Q01082-3] |
Protein sequence database of the Protein Information Resource More...PIRi | A44159 A47213 |
NCBI Reference Sequences More...RefSeqi | NP_003119.2, NM_003128.2 [Q01082-1] NP_842565.2, NM_178313.2 [Q01082-3] XP_005264574.1, XM_005264517.2 [Q01082-1] XP_006712150.1, XM_006712087.2 [Q01082-1] XP_016860268.1, XM_017004779.1 [Q01082-1] XP_016860269.1, XM_017004780.1 [Q01082-1] XP_016860270.1, XM_017004781.1 [Q01082-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.503178 Hs.705692 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000333896; ENSP00000334156; ENSG00000115306 [Q01082-3] ENST00000356805; ENSP00000349259; ENSG00000115306 [Q01082-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 6711 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:6711 |
UCSC genome browser More...UCSCi | uc002rxu.4 human [Q01082-1] |
<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 | |
|---|---|---|---|---|---|
| Q01082 | Spectrin beta chain | 2364 | |||
| Spectrin beta chain | 2364 | ||||
| Spectrin beta chain | 2364 | ||||
| Spectrin beta chain | 2278 | ||||
| Q01082-2 | Beta II spectrin (Fragment) | 82 | |||
| Beta II spectrin-short isoform (Fragment) | 67 | ||||
| Q01082-3 | Spectrin beta chain | 2155 | |||
| Spectrin beta chain | 2155 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q01082 | Spectrin beta chain | 2364 | |||
| Spectrin beta chain | 2364 | ||||
| Spectrin beta chain | 2364 | ||||
| Spectrin beta chain | 2395 | ||||
| Spectrin beta chain | 2380 | ||||
| +306 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q01082 | Spectrin beta chain | 2364 | |||
| Spectrin beta chain | 2364 | ||||
| Spectrin beta chain | 2364 | ||||
| Spectrin beta chain | 2395 | ||||
| Spectrin beta chain | 2380 | ||||
| +1587 | |||||
<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 | M96803 mRNA Translation: AAA60580.1 AF327441 mRNA Translation: AAO15362.1 AB209748 mRNA Translation: BAD92985.1 Different initiation. AC093110 Genomic DNA Translation: AAY24229.1 AC092839 Genomic DNA No translation available. CH471053 Genomic DNA Translation: EAX00147.1 BC137282 mRNA Translation: AAI37283.1 BC137283 mRNA Translation: AAI37284.1 S65762 mRNA Translation: AAB28324.1 AJ005694 mRNA Translation: CAA06678.1 AJ238723 Genomic DNA Translation: CAB91088.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS33198.1 [Q01082-1] CCDS33199.1 [Q01082-3] |
Protein sequence database of the Protein Information Resource More...PIRi | A44159 A47213 |
NCBI Reference Sequences More...RefSeqi | NP_003119.2, NM_003128.2 [Q01082-1] NP_842565.2, NM_178313.2 [Q01082-3] XP_005264574.1, XM_005264517.2 [Q01082-1] XP_006712150.1, XM_006712087.2 [Q01082-1] XP_016860268.1, XM_017004779.1 [Q01082-1] XP_016860269.1, XM_017004780.1 [Q01082-1] XP_016860270.1, XM_017004781.1 [Q01082-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.503178 Hs.705692 |
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 |
| 1AA2 | X-ray | 2.00 | A | 173-280 | [»] | |
| 1BKR | X-ray | 1.10 | A | 172-280 | [»] | |
| 3EDV | X-ray | 1.95 | A/B | 1697-2015 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q01082 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q01082 | |||||
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 | 112589, 143 interactors |
Database of interacting proteins More...DIPi | DIP-33182N |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | Q01082 |
Protein interaction database and analysis system More...IntActi | Q01082, 94 interactors |
Molecular INTeraction database More...MINTi | Q01082 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000349259 |
Chemistry databases
Drug and drug target database More...DrugBanki | DB01373 Calcium |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q01082 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q01082 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q01082 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | SPTBN1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 116242799 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q01082 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q01082 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q01082 |
PeptideAtlas More...PeptideAtlasi | Q01082 |
PRoteomics IDEntifications database More...PRIDEi | Q01082 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 57910 57911 [Q01082-2] 57912 [Q01082-3] |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000333896; ENSP00000334156; ENSG00000115306 [Q01082-3] ENST00000356805; ENSP00000349259; ENSG00000115306 [Q01082-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 6711 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:6711 |
UCSC genome browser More...UCSCi | uc002rxu.4 human [Q01082-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 6711 |
DisGeNET More...DisGeNETi | 6711 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000115306.15 |
GeneCards: human genes, protein and diseases More...GeneCardsi | SPTBN1 |
H-Invitational Database, human transcriptome db More...H-InvDBi | HIX0002055 |
Human Gene Nomenclature Database More...HGNCi | HGNC:11275 SPTBN1 |
Human Protein Atlas More...HPAi | HPA012685 HPA013149 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 182790 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q01082 |
Open Targets More...OpenTargetsi | ENSG00000115306 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA36104 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0035 Eukaryota COG5069 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118813 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG057912 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q01082 |
KEGG Orthology (KO) More...KOi | K06115 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q01082 |
TreeFam database of animal gene trees More...TreeFami | TF313446 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-373753 Nephrin family interactions R-HSA-375165 NCAM signaling for neurite out-growth R-HSA-445095 Interaction between L1 and Ankyrins R-HSA-5673001 RAF/MAP kinase cascade R-HSA-6807878 COPI-mediated anterograde transport |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q01082 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q01082 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | SPTBN1 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q01082 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | SPTBN1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 6711 |
Protein Ontology More...PROi | PR:Q01082 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000115306 |
CleanEx database of gene expression profiles More...CleanExi | HS_SPTBN1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q01082 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q01082 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd00014 CH, 2 hits |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.418.10, 2 hits 2.30.29.30, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001589 Actinin_actin-bd_CS IPR001715 CH-domain IPR036872 CH_dom_sf IPR011993 PH-like_dom_sf IPR001605 PH_dom-spectrin-type IPR001849 PH_domain IPR018159 Spectrin/alpha-actinin IPR016343 Spectrin_bsu IPR002017 Spectrin_repeat |
Pfam protein domain database More...Pfami | View protein in Pfam PF00307 CH, 2 hits PF00435 Spectrin, 17 hits |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF002297 Spectrin_beta_subunit, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00683 SPECTRINPH |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00033 CH, 2 hits SM00233 PH, 1 hit SM00150 SPEC, 17 hits |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF47576 SSF47576, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00019 ACTININ_1, 1 hit PS00020 ACTININ_2, 1 hit PS50021 CH, 2 hits PS50003 PH_DOMAIN, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | SPTB2_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 | Q01082Primary (citable) accession number: Q01082 Secondary accession number(s): B2RP63 , O60837, Q16057, Q53R99, Q59ER3, Q8IX99 | |
| <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: | October 17, 2006 | |
| Last modified: | July 18, 2018 | |
| This is version 196 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 2
Human chromosome 2: 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
