UniProt ID | PTBP2_MOUSE | |
---|---|---|
UniProt AC | Q91Z31 | |
Protein Name | Polypyrimidine tract-binding protein 2 | |
Gene Name | Ptbp2 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 531 | |
Subcellular Localization | Nucleus . | |
Protein Description | RNA-binding protein which binds to intronic polypyrimidine tracts and mediates negative regulation of exons splicing. May antagonize in a tissue-specific manner the ability of NOVA1 to activate exon selection. In addition to its function in pre-mRNA splicing, plays also a role in the regulation of translation.. | |
Protein Sequence | MDGIVTEVAVGVKRGSDELLSGSVLSSPNSNMSGMVVTANGNDSKKFKGEDKMDGAPSRVLHIRKLPGEVTETEVIALGLPFGKVTNILMLKGKNQAFLELATEEAAITMVNYYSAVTPHLRNQPIYIQYSNHKELKTDNTLNQRAQVVLQAVTAVQTANTPLSGTTVSESAVTPAQSPVLRIIIDNMYYPVTLDVLHQIFSKFGAVLKIITFTKNNQFQALLQYGDPVNAQQAKLALDGQNIYNACCTLRIDFSKLVNLNVKYNNDKSRDYTRPDLPSGDGQPALDPAIAAAFAKETSLLAVPGALSPLAIPNAAAAAAAAAAGRVGMPGVSAGGNTVLLVSNLNEEMVTPQSLFTLFGVYGDVQRVKILYNKKDSALIQMADGNQSQLAMNHLNGQKMYGKIIRVTLSKHQTVQLPREGLDDQGLTKDFGNSPLHRFKKPGSKNFQNIFPPSATLHLSNIPPSVAEEDLRTLFANTGGTVKAFKFFQDHKMALLQMATVEEAIQALIDLHNYNLGENHHLRVSFSKSTI | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
1 | Acetylation | -------MDGIVTEV -------CCCCEEEE | 10.85 | - | |
16 | Phosphorylation | AVGVKRGSDELLSGS ECEEECCCCCHHCCC | 31.76 | 25293948 | |
21 | Phosphorylation | RGSDELLSGSVLSSP CCCCCHHCCCCCCCC | 41.46 | 25293948 | |
23 | Phosphorylation | SDELLSGSVLSSPNS CCCHHCCCCCCCCCC | 19.26 | 25293948 | |
26 | Phosphorylation | LLSGSVLSSPNSNMS HHCCCCCCCCCCCCC | 41.41 | 27087446 | |
27 | Phosphorylation | LSGSVLSSPNSNMSG HCCCCCCCCCCCCCC | 24.76 | 25521595 | |
30 | Phosphorylation | SVLSSPNSNMSGMVV CCCCCCCCCCCCEEE | 36.98 | 25293948 | |
33 | Phosphorylation | SSPNSNMSGMVVTAN CCCCCCCCCEEEEEC | 28.17 | 25521595 | |
38 | Phosphorylation | NMSGMVVTANGNDSK CCCCEEEEECCCCCC | 11.73 | 25293948 | |
298 | Phosphorylation | AAAFAKETSLLAVPG HHHHHHCCCEEECCC | 24.78 | 23984901 | |
299 | Phosphorylation | AAFAKETSLLAVPGA HHHHHCCCEEECCCC | 23.60 | 23984901 | |
308 | Phosphorylation | LAVPGALSPLAIPNA EECCCCCCCCCCCCH | 19.82 | 26824392 | |
434 | Phosphorylation | LTKDFGNSPLHRFKK CCCCCCCCCCCCCCC | 29.26 | 28066266 | |
444 | Phosphorylation | HRFKKPGSKNFQNIF CCCCCCCCCCCCCCC | 32.71 | 27681418 | |
483 | Ubiquitination | ANTGGTVKAFKFFQD HHCCCCEEEEEHHHH | 48.20 | 22790023 | |
483 (in isoform 2) | Ubiquitination | - | 48.20 | 22790023 | |
527 | Phosphorylation | HHLRVSFSKSTI--- CEEEEEEECCCC--- | 20.42 | 29176673 | |
529 | Phosphorylation | LRVSFSKSTI----- EEEEEECCCC----- | 30.09 | 23684622 | |
530 | Phosphorylation | RVSFSKSTI------ EEEEECCCC------ | 34.15 | 23684622 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of PTBP2_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PTBP2_MOUSE !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of PTBP2_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of PTBP2_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
Phosphorylation | |
Reference | PubMed |
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-308, AND MASSSPECTROMETRY. |