UniProt ID | TCTP_MOUSE | |
---|---|---|
UniProt AC | P63028 | |
Protein Name | Translationally-controlled tumor protein | |
Gene Name | Tpt1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 172 | |
Subcellular Localization | Cytoplasm. | |
Protein Description | Involved in calcium binding and microtubule stabilization.. | |
Protein Sequence | MIIYRDLISHDELFSDIYKIREIADGLCLEVEGKMVSRTEGAIDDSLIGGNASAEGPEGEGTESTVVTGVDIVMNHHLQETSFTKEAYKKYIKDYMKSLKGKLEEQKPERVKPFMTGAAEQIKHILANFNNYQFFIGENMNPDGMVALLDYREDGVTPFMIFFKDGLEMEKC | |
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 |
---|---|---|---|---|---|
9 | Phosphorylation | IIYRDLISHDELFSD CEEHHCCCCHHHHHH | 31.98 | 26370283 | |
19 | Ubiquitination | ELFSDIYKIREIADG HHHHHHHHHHHHHHC | 35.30 | 22790023 | |
19 | Acetylation | ELFSDIYKIREIADG HHHHHHHHHHHHHHC | 35.30 | 22826441 | |
28 | S-nitrosocysteine | REIADGLCLEVEGKM HHHHHCCEEEEECEE | 3.58 | - | |
28 | S-nitrosylation | REIADGLCLEVEGKM HHHHHCCEEEEECEE | 3.58 | 21278135 | |
28 | Glutathionylation | REIADGLCLEVEGKM HHHHHCCEEEEECEE | 3.58 | 24333276 | |
39 | Phosphorylation | EGKMVSRTEGAIDDS ECEEEECCCCCCCCC | 31.12 | 25619855 | |
46 | Phosphorylation | TEGAIDDSLIGGNAS CCCCCCCCCCCCCCC | 20.38 | 21082442 | |
53 | Phosphorylation | SLIGGNASAEGPEGE CCCCCCCCCCCCCCC | 30.74 | 25619855 | |
62 | Phosphorylation | EGPEGEGTESTVVTG CCCCCCCCCCEEEEE | 23.59 | 25619855 | |
64 | Phosphorylation | PEGEGTESTVVTGVD CCCCCCCCEEEEECC | 26.75 | 25619855 | |
65 | Phosphorylation | EGEGTESTVVTGVDI CCCCCCCEEEEECCE | 16.86 | 25619855 | |
68 | Phosphorylation | GTESTVVTGVDIVMN CCCCEEEEECCEEEC | 27.44 | 25619855 | |
93 | Acetylation | EAYKKYIKDYMKSLK HHHHHHHHHHHHHHC | 39.45 | 23201123 | |
93 | Malonylation | EAYKKYIKDYMKSLK HHHHHHHHHHHHHHC | 39.45 | 26320211 | |
97 | Malonylation | KYIKDYMKSLKGKLE HHHHHHHHHHCCHHH | 46.54 | 26320211 | |
97 | Acetylation | KYIKDYMKSLKGKLE HHHHHHHHHHCCHHH | 46.54 | 22826441 | |
102 | Acetylation | YMKSLKGKLEEQKPE HHHHHCCHHHHCCCH | 51.65 | 22826441 | |
107 | Ubiquitination | KGKLEEQKPERVKPF CCHHHHCCCHHCCCC | 52.72 | - | |
107 | Acetylation | KGKLEEQKPERVKPF CCHHHHCCCHHCCCC | 52.72 | 23806337 | |
112 | Ubiquitination | EQKPERVKPFMTGAA HCCCHHCCCCCCCHH | 38.47 | 27667366 | |
112 | Malonylation | EQKPERVKPFMTGAA HCCCHHCCCCCCCHH | 38.47 | 26320211 | |
112 | Acetylation | EQKPERVKPFMTGAA HCCCHHCCCCCCCHH | 38.47 | 22826441 | |
164 | Ubiquitination | TPFMIFFKDGLEMEK CCEEEEECCCCCEEC | 39.89 | 22790023 | |
172 | S-nitrosocysteine | DGLEMEKC------- CCCCEECC------- | 4.26 | - | |
172 | Glutathionylation | DGLEMEKC------- CCCCEECC------- | 4.26 | 24333276 | |
172 | S-nitrosylation | DGLEMEKC------- CCCCEECC------- | 4.26 | 21278135 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
46 | S | Phosphorylation | Kinase | PLK1 | P53350 | PSP |
46 | S | Phosphorylation | Kinase | PLK1 | Q07832 | PSP |
46 | S | Phosphorylation | Kinase | PLK-FAMILY | - | GPS |
64 | S | Phosphorylation | Kinase | PLK1 | P53350 | PSP |
64 | S | Phosphorylation | Kinase | PLK1 | Q07832 | Uniprot |
64 | S | Phosphorylation | Kinase | PLK-FAMILY | - | GPS |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TCTP_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 TCTP_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
NUCL_MOUSE | Ncl | physical | 21048921 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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