| UniProt ID | 5NTC_MOUSE | |
|---|---|---|
| UniProt AC | Q3V1L4 | |
| Protein Name | Cytosolic purine 5'-nucleotidase | |
| Gene Name | Nt5c2 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 560 | |
| Subcellular Localization | Cytoplasm. | |
| Protein Description | May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other purine nucleotides (By similarity).. | |
| Protein Sequence | MTTSWSDRLQNAADVPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVYKSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLVCAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTSCDTGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMKEVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGTVLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKSKKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQRRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAAHVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLAPQEITHCHDEDDDEEEEEEE | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MTTSWSDRL ------CCCCHHHHH | 29.54 | 26643407 | |
| 3 | Phosphorylation | -----MTTSWSDRLQ -----CCCCHHHHHH | 27.22 | 26643407 | |
| 4 | Phosphorylation | ----MTTSWSDRLQN ----CCCCHHHHHHH | 18.54 | 26643407 | |
| 6 | Phosphorylation | --MTTSWSDRLQNAA --CCCCHHHHHHHHH | 16.78 | 26643407 | |
| 211 | Acetylation | AVDWVHYKGSLKEKT HHHHHHHCCCCCCHH | 27.44 | 22826441 | |
| 254 | Acetylation | LATNSDYKYTDKIMT EECCCCCCCCCCHHH | 46.82 | 23954790 | |
| 292 | Acetylation | LILVDARKPLFFGEG EEEEECCCCCEECCC | 48.03 | 22826441 | |
| 417 | Phosphorylation | SNERPDISSIQRRIK CCCCCCHHHHHHHHH | 28.86 | 28973931 | |
| 418 | Phosphorylation | NERPDISSIQRRIKK CCCCCHHHHHHHHHH | 24.07 | 29514104 | |
| 457 | Phosphorylation | FASQVMRYADLYAAS HHHHHHHHHHHHHHH | 6.08 | 25293948 | |
| 461 | Phosphorylation | VMRYADLYAASFINL HHHHHHHHHHHHHHH | 10.73 | 25293948 | |
| 464 | Phosphorylation | YADLYAASFINLLYY HHHHHHHHHHHHHHH | 20.63 | 25293948 | |
| 470 | Phosphorylation | ASFINLLYYPFSYLF HHHHHHHHHHHHHHH | 16.56 | 25293948 | |
| 471 | Phosphorylation | SFINLLYYPFSYLFR HHHHHHHHHHHHHHH | 9.58 | 25293948 | |
| 474 | Phosphorylation | NLLYYPFSYLFRAAH HHHHHHHHHHHHHHH | 19.20 | 25293948 | |
| 475 | Phosphorylation | LLYYPFSYLFRAAHV HHHHHHHHHHHHHHH | 15.39 | 25293948 | |
| 502 | Phosphorylation | VDINEMESPLATRNR ECHHHCCCCCCCCCC | 24.73 | 26060331 | |
| 510 | Phosphorylation | PLATRNRTSVDFKDT CCCCCCCCCCCCCCC | 36.33 | 26824392 | |
| 511 | Phosphorylation | LATRNRTSVDFKDTD CCCCCCCCCCCCCCH | 19.22 | 26824392 | |
| 527 | Phosphorylation | KRHQLTRSISEIKPP HHHCCHHCHHHCCCC | 25.82 | 26239621 | |
| 529 | Phosphorylation | HQLTRSISEIKPPNL HCCHHCHHHCCCCCC | 34.22 | 21082442 |
| 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 5NTC_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of 5NTC_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 5NTC_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of 5NTC_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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