<p>An evidence describes the source of an annotation, e.g. an experiment that has been published in the scientific literature, an orthologous protein, a record from another database, etc.</p>
<p><a href="/manual/evidences">More...</a></p>
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<p>When browsing through different UniProt proteins, you can use the 'basket' to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>
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<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
Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1. May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12 (PubMed:18559503).
Isoform 6 increases water and sodium absorption in the intestine and gall-bladder.
3 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
Cited for: FUNCTION, INTERACTION WITH PTPN12 AND WASF1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEPHOSPHORYLATION BY PTPN12, DOMAIN.
Caution
Was shown to interact with AKT1 and PAK1 (PubMed:15784622). This work has later been retracted due to concerns of image manipulation.1 Publication
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p>
<p><a href="/manual/evidences#ECO:0000305">More...</a></p>
Manual assertion inferred by curator fromi
<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
cytoskeletal anchor activity Source: ProtInc
<p>Traceable Author Statement</p>
<p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p>
Traceable author statementi
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), NUCLEOTIDE SEQUENCE [MRNA] OF 1-1049 (ISOFORM 4), PHOSPHORYLATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH ABL1 AND ABL2, FUNCTION.
identical protein binding Source: IntAct
<p>Inferred from Physical Interaction</p>
<p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p>
Inferred from physical interactioni
Notch signaling pathway Source: GO_Central
<p>Inferred from Biological aspect of Ancestor</p>
<p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p>
Inferred from biological aspect of ancestori
<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%5Fand%5Ftaxonomy%5Fsection">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:
Sorbin and SH3 domain-containing protein 2
Alternative name(s):
Arg-binding protein 2
Short name:
ArgBP2
Arg/Abl-interacting protein 2
Sorbin
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
UP000005640
<p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4
<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
Cited for: FUNCTION, INTERACTION WITH PTPN12 AND WASF1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEPHOSPHORYLATION BY PTPN12, DOMAIN.
Note:Found at the Z-disk sarcomeres, stress fibers, dense bodies and focal adhesion. In pancreatic acinar cells, localized preferentially to the apical membrane. Colocalized with vinculin and filamentous actin at focal adhesions and lamellipodia of pancreatic cells.1 Publication
Z disc Source: UniProtKB
<p>Non-traceable Author Statement</p>
<p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p>
Non-traceable author statementi
<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
<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000344477
Sorbin and SH3 domain-containing protein 2AddBLAST
1100
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
<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
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0007744">More...</a></p>
Manual assertion inferred from combination of experimental and computational evidencei
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-277; SER-301 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-298; SER-299 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 (ISOFORM 11), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORMS 12 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-277; SER-301 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-298; SER-299 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 (ISOFORM 11), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORMS 12 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-298; SER-299 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 (ISOFORM 11), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORMS 12 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-277; SER-301 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-277; SER-301 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-298; SER-299 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 (ISOFORM 11), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORMS 12 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-298; SER-299 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 (ISOFORM 11), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORMS 12 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-298; SER-299 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 (ISOFORM 11), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORMS 12 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-277; SER-301 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-298; SER-299 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 (ISOFORM 11), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORMS 12 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-277; SER-301 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-298; SER-299 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 (ISOFORM 11), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORMS 12 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-298; SER-299 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 (ISOFORM 11), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORMS 12 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-277; SER-301 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-298; SER-299 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 (ISOFORM 11), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORMS 12 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-277; SER-301 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-298; SER-299 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 (ISOFORM 11), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORMS 12 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-277; SER-301 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-298; SER-299 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 (ISOFORM 11), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORMS 12 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-277; SER-301 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-298; SER-299 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 (ISOFORM 11), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORMS 12 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-277; SER-301 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-298; SER-299 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 (ISOFORM 11), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORMS 12 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-277; SER-301 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-298; SER-299 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 (ISOFORM 11), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORMS 12 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-277; SER-301 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-298; SER-299 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 (ISOFORM 11), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORMS 12 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-277; SER-301 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-298; SER-299 AND SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 (ISOFORM 11), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORMS 12 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-157; SER-239; SER-259; SER-287; THR-292; SER-302; SER-304; SER-843 AND SER-1023, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-413; THR-415; SER-439; THR-459 AND SER-474 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-28 (ISOFORM 11), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320; THR-322; SER-346; THR-366 AND SER-381 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-14 (ISOFORMS 12 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-234; THR-236; SER-260 AND SER-295 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-280 (ISOFORMS 3; 4 AND 5), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-282; SER-306; THR-326 AND SER-341 (ISOFORMS 4 AND 5), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311 (ISOFORM 8), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>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
Abundantly expressed in heart. In cardiac muscle cells, located in the Z-disks of sarcomere. Also found, but to a lower extent, in small and large intestine, pancreas, thymus, colon, spleen, prostate, testis, brain, ovary and epithelial cells. In the pancreas, mainly expressed in acinar cells, duct cells and all cell types in islets (at protein level). Tends to be down-regulated in pancreatic adenocarcinomas ans metastases.3 Publications
<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Interacts with ABL, CBL, DNM1, DNM2, FLOT1, AFDN, PTK2B/PYK2, SAPAP, SPTAN1, SYNJ1, SYNJ2, VCL/vinculin and WASF (By similarity).
Interacts with ABL1/c-Abl, ABL2/v-Abl/Arg, ACTN, CBL and PALLD.
Interacts with PTPN12 and WASF1 via its SH3 domains; this interaction may mediate the partial PTPN12 and WASF1 translocation to focal adhesion sites.
Cited for: FUNCTION, INTERACTION WITH PTPN12 AND WASF1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEPHOSPHORYLATION BY PTPN12, DOMAIN.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
<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
Legend: HelixTurnBeta strandPDB Structure known for this area
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> 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
<p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p>
<p><a href="/manual/evidences#ECO:0000213">More...</a></p>
Automatic assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> 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
<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%5Fand%5Fdomains%5Fsection">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
<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
<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
<p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p>
<p><a href="/manual/evidences#ECO:0000256">More...</a></p>
Automatic assertion according to sequence analysisi
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi
<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
The first 2 SH3 domains are required for WASF1-binding. All 3 SH3 domains can bind independently to PTPN12.1 Publication
<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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (12+)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 12
<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 entry has 12 described isoforms and 31 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the
<p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i7E98B196D4DB38E6
The sequence of this isoform differs from the canonical sequence as follows: 1-1: M → MNTGRDSQSPDSAKGFRSVRPNLQDKRSPTQSQITVNGNSGGAVSPM 228-228: P → PTDRINPDDIDLENEPWYKFFSELEFGRPPPKKPLDYVQDHSSGVFNE 308-834: Missing.
The sequence of this isoform differs from the canonical sequence as follows: 228-228: P → PPPLPTTPTPVPREPGRKPLSSSRLGEVTGSPSPPPRSGAPTPSSRAPALSPTRPPKKPLDYVQDHSSGVFNE 308-834: Missing.
The sequence of this isoform differs from the canonical sequence as follows: 1-1: M → MNTGRDSQSPDSAKGFRSVRPNLQDKRSPTQSQITVNGNSGGAVSPM 228-228: P → PPPLPTTPTPVPREPGRKPLSSSRLGEVTGSPSPPPRSGAPTPSSRAPALSPTRPPKKPLDYVQDHSSGVFNE 308-834: Missing.
The sequence of this isoform differs from the canonical sequence as follows: 1-1: M → MNTGRDSQSPDSAKGFRSVRPNLQDKRSPTQSQITVNGNSGGAVSPM 228-228: P → PPPLPTTPTPVPREPGRKPLSSSRLGEVTGSPSPPPRSGAPTPSSRAPALSPTRPPKKPLDYVQDHSSGVFNE 308-834: Missing. 1050-1100: YNYTPRNEDELELRESDVIDVMEKCDDGWFVGTSRRTKFFGTFPGNYVKRL → GYTLT
The sequence of this isoform differs from the canonical sequence as follows: 1-81: Missing. 82-89: GIPTAIRT → MKATTPLQ 229-237: ASLYQSSID → VSKPQAGRR 238-1100: Missing.
The sequence of this isoform differs from the canonical sequence as follows: 1-1: M → MNTGRDSQSPDSAWRSYNDGNQETLNGDATYSSLAAKGFRSVRPNLQDKRSPTQSQITVNGNSGGAVSPM 228-228: P → PPPKKPLDYVQDHSSGVFNE 308-834: Missing.
The sequence of this isoform differs from the canonical sequence as follows: 1-1: M → MYSNEDSRQT...GNSGGAVSPM 228-228: P → PPPLPTTPTPVPREPGRKPLSSSRLGEVTGSPSPPPRSGAPTPSSRAPALSPTRPPKKPLDYVQDHSSGVFNE 308-834: Missing.
The sequence of this isoform differs from the canonical sequence as follows: 1-1: M → MSVTLTSVKR...GNSGGAVSPM 228-228: P → PPPLPTTPTPVPREPGRKPLSSSRLGEVTGSPSPPPRSGAPTPSSRAPALSPTRPPKKPLDYVQDHSSGVFNE 308-834: Missing.
<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi
<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>
<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>
<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>
<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>
<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>
<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>
<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>
<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>
<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>
<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>
<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
The sequence BAA34497 differs from that shown. Reason: Erroneous initiation.Curated
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
<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_045624
<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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_043665
<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
<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
<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
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
<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
SRBS2_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
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi
Integrated into UniProtKB/Swiss-Prot:
July 22, 2008
Last sequence update:
July 22, 2008
Last modified:
February 23, 2022
This is version 184 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi
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
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