UniProt ID | MARE2_RAT | |
---|---|---|
UniProt AC | Q3B8Q0 | |
Protein Name | Microtubule-associated protein RP/EB family member 2 | |
Gene Name | Mapre2 | |
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 326 | |
Subcellular Localization | Cytoplasm. Cytoplasm, cytoskeleton. Associated with the microtubule network. Accumulates at the plus end of microtubules (By similarity).. | |
Protein Description | May be involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration (By similarity).. | |
Protein Sequence | MPGPTQTLSPNGENNNDIIQDNGTIIPFRKHTVRGERSYSWGMAVNVYSTSITQETMSRHDIIAWVNDIVSLNYTKVEQLCSGAAYCQFMDMLFPGCISLKKVKFQAKLEHEYIHNFKLLQASFKRMNVDKVIPVEKLVKGRFQDNLDFIQWFKKFYDANYDGKEYDPVEARQGQDAIPPPDPGEQIFNLPKKSHHANSPTAGAAKSSPAAKPGSTPSRPSSAKRASSSGSASRSDKDLETQVIQLNEQVHSLKLALEGVEKERDFYFGKLREIELLCQEHGQENDDLVQRLMEVLYASDEQEGQTEEPEVEEQTHDQQPQQQEEY | |
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 |
---|---|---|---|---|---|
5 | Phosphorylation | ---MPGPTQTLSPNG ---CCCCCCCCCCCC | 39.85 | 27097102 | |
7 | Phosphorylation | -MPGPTQTLSPNGEN -CCCCCCCCCCCCCC | 31.51 | 27097102 | |
9 | Phosphorylation | PGPTQTLSPNGENNN CCCCCCCCCCCCCCC | 21.51 | 27097102 | |
104 | Acetylation | CISLKKVKFQAKLEH CEEECEEEEEEECCC | 40.41 | 22902405 | |
108 | Acetylation | KKVKFQAKLEHEYIH CEEEEEEECCCHHHH | 43.56 | 22902405 | |
113 | Phosphorylation | QAKLEHEYIHNFKLL EEECCCHHHHHHHHH | 14.91 | - | |
155 | Ubiquitination | DFIQWFKKFYDANYD HHHHHHHHHHCCCCC | 39.42 | - | |
157 | Phosphorylation | IQWFKKFYDANYDGK HHHHHHHHCCCCCCC | 24.03 | - | |
161 | Phosphorylation | KKFYDANYDGKEYDP HHHHCCCCCCCCCCC | 28.00 | - | |
164 | Ubiquitination | YDANYDGKEYDPVEA HCCCCCCCCCCCCHH | 50.64 | - | |
166 | Phosphorylation | ANYDGKEYDPVEARQ CCCCCCCCCCCHHCC | 29.09 | - | |
194 | Phosphorylation | IFNLPKKSHHANSPT HCCCCCCCCCCCCCC | 26.99 | 22673903 | |
199 | Phosphorylation | KKSHHANSPTAGAAK CCCCCCCCCCCCCCC | 25.14 | 29779826 | |
201 | Phosphorylation | SHHANSPTAGAAKSS CCCCCCCCCCCCCCC | 37.23 | 27097102 | |
208 | Phosphorylation | TAGAAKSSPAAKPGS CCCCCCCCCCCCCCC | 20.18 | 28689409 | |
215 | Phosphorylation | SPAAKPGSTPSRPSS CCCCCCCCCCCCCCC | 45.75 | 28432305 | |
216 | Phosphorylation | PAAKPGSTPSRPSSA CCCCCCCCCCCCCCC | 31.06 | 27097102 | |
218 | Phosphorylation | AKPGSTPSRPSSAKR CCCCCCCCCCCCCCC | 57.84 | 27097102 | |
221 | Phosphorylation | GSTPSRPSSAKRASS CCCCCCCCCCCCCCC | 41.64 | 27097102 | |
222 | Phosphorylation | STPSRPSSAKRASSS CCCCCCCCCCCCCCC | 40.26 | 27097102 | |
227 | Phosphorylation | PSSAKRASSSGSASR CCCCCCCCCCCCCCC | 29.12 | 28551015 | |
228 | Phosphorylation | SSAKRASSSGSASRS CCCCCCCCCCCCCCC | 37.42 | 28551015 | |
229 | Phosphorylation | SAKRASSSGSASRSD CCCCCCCCCCCCCCC | 33.98 | 28551015 | |
231 | Phosphorylation | KRASSSGSASRSDKD CCCCCCCCCCCCCCH | 25.64 | 28551015 | |
237 | Acetylation | GSASRSDKDLETQVI CCCCCCCCHHHHHHH | 66.51 | 22902405 |
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 MARE2_RAT !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MARE2_RAT !! |
* 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 MARE2_RAT !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of MARE2_RAT !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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