UniProt ID | MARE1_HUMAN | |
---|---|---|
UniProt AC | Q15691 | |
Protein Name | Microtubule-associated protein RP/EB family member 1 | |
Gene Name | MAPRE1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 268 | |
Subcellular Localization | Cytoplasm, cytoskeleton . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Golgi apparatus . Associated with the microtubule growing distal tips (PubMed:28814570). Recruitment to the Golgi apparatus requires the presence of PDE4DI | |
Protein Description | Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton. [PubMed: 12388762] | |
Protein Sequence | MAVNVYSTSVTSDNLSRHDMLAWINESLQLNLTKIEQLCSGAAYCQFMDMLFPGSIALKKVKFQAKLEHEYIQNFKILQAGFKRMGVDKIIPVDKLVKGKFQDNFEFVQWFKKFFDANYDGKDYDPVAARQGQETAVAPSLVAPALNKPKKPLTSSSAAPQRPISTQRTAAAPKAGPGVVRKNPGVGNGDDEAAELMQQVNVLKLTVEDLEKERDFYFGKLRNIELICQENEGENDPVLQRIVDILYATDEGFVIPDEGGPQEEQEEY | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MAVNVYSTS ------CCCEEEECC | 11.11 | 22223895 | |
6 | Phosphorylation | --MAVNVYSTSVTSD --CCCEEEECCCCCC | 10.88 | 26552605 | |
7 | Phosphorylation | -MAVNVYSTSVTSDN -CCCEEEECCCCCCC | 15.21 | 26552605 | |
8 | Phosphorylation | MAVNVYSTSVTSDNL CCCEEEECCCCCCCC | 14.99 | 26552605 | |
9 | Phosphorylation | AVNVYSTSVTSDNLS CCEEEECCCCCCCCC | 19.91 | 26552605 | |
11 | Phosphorylation | NVYSTSVTSDNLSRH EEEECCCCCCCCCHH | 30.08 | 27732954 | |
12 | Phosphorylation | VYSTSVTSDNLSRHD EEECCCCCCCCCHHH | 23.50 | 23186163 | |
40 | Phosphorylation | TKIEQLCSGAAYCQF HHHHHHHCHHHHHHH | 39.81 | - | |
60 | Ubiquitination | PGSIALKKVKFQAKL CCCEEEEECCHHHHC | 52.05 | 23000965 | |
60 | Acetylation | PGSIALKKVKFQAKL CCCEEEEECCHHHHC | 52.05 | 129905 | |
62 | Ubiquitination | SIALKKVKFQAKLEH CEEEEECCHHHHCCH | 40.41 | 23000965 | |
66 | Ubiquitination | KKVKFQAKLEHEYIQ EECCHHHHCCHHHHH | 43.56 | 23000965 | |
66 | Malonylation | KKVKFQAKLEHEYIQ EECCHHHHCCHHHHH | 43.56 | 26320211 | |
66 | Acetylation | KKVKFQAKLEHEYIQ EECCHHHHCCHHHHH | 43.56 | 23236377 | |
71 | Phosphorylation | QAKLEHEYIQNFKIL HHHCCHHHHHHHHHH | 15.09 | 28152594 | |
76 | Acetylation | HEYIQNFKILQAGFK HHHHHHHHHHHHHHH | 50.48 | 23954790 | |
76 | Ubiquitination | HEYIQNFKILQAGFK HHHHHHHHHHHHHHH | 50.48 | 23000965 | |
76 | Methylation | HEYIQNFKILQAGFK HHHHHHHHHHHHHHH | 50.48 | - | |
83 | Acetylation | KILQAGFKRMGVDKI HHHHHHHHHCCCCEE | 40.32 | 23749302 | |
83 | Ubiquitination | KILQAGFKRMGVDKI HHHHHHHHHCCCCEE | 40.32 | 23000965 | |
83 | Malonylation | KILQAGFKRMGVDKI HHHHHHHHHCCCCEE | 40.32 | 26320211 | |
89 | Ubiquitination | FKRMGVDKIIPVDKL HHHCCCCEEEEHHHH | 39.88 | 23000965 | |
89 | Acetylation | FKRMGVDKIIPVDKL HHHCCCCEEEEHHHH | 39.88 | 23749302 | |
95 | Ubiquitination | DKIIPVDKLVKGKFQ CEEEEHHHHHCCCCC | 56.25 | 23000965 | |
95 | Acetylation | DKIIPVDKLVKGKFQ CEEEEHHHHHCCCCC | 56.25 | 25953088 | |
98 | Ubiquitination | IPVDKLVKGKFQDNF EEHHHHHCCCCCCCH | 67.81 | 23000965 | |
100 | Ubiquitination | VDKLVKGKFQDNFEF HHHHHCCCCCCCHHH | 33.85 | 23000965 | |
100 | Acetylation | VDKLVKGKFQDNFEF HHHHHCCCCCCCHHH | 33.85 | 25953088 | |
112 | Ubiquitination | FEFVQWFKKFFDANY HHHHHHHHHHHCCCC | 45.79 | 22817900 | |
113 | Acetylation | EFVQWFKKFFDANYD HHHHHHHHHHCCCCC | 41.61 | 25953088 | |
113 | Ubiquitination | EFVQWFKKFFDANYD HHHHHHHHHHCCCCC | 41.61 | 21890473 | |
119 | Phosphorylation | KKFFDANYDGKDYDP HHHHCCCCCCCCCCH | 28.00 | 26552605 | |
122 | Ubiquitination | FDANYDGKDYDPVAA HCCCCCCCCCCHHHH | 50.66 | 32015554 | |
122 | Acetylation | FDANYDGKDYDPVAA HCCCCCCCCCCHHHH | 50.66 | 26051181 | |
124 | Phosphorylation | ANYDGKDYDPVAARQ CCCCCCCCCHHHHHC | 26.15 | 28674151 | |
135 | Phosphorylation | AARQGQETAVAPSLV HHHCCCCCCCCCHHH | 20.67 | 23312004 | |
140 | Phosphorylation | QETAVAPSLVAPALN CCCCCCCHHHHHHHC | 26.24 | 26657352 | |
148 | Acetylation | LVAPALNKPKKPLTS HHHHHHCCCCCCCCC | 60.09 | 23236377 | |
148 | Ubiquitination | LVAPALNKPKKPLTS HHHHHHCCCCCCCCC | 60.09 | 23000965 | |
150 | Ubiquitination | APALNKPKKPLTSSS HHHHCCCCCCCCCCC | 69.50 | 23000965 | |
151 | Ubiquitination | PALNKPKKPLTSSSA HHHCCCCCCCCCCCC | 54.51 | 23000965 | |
151 | Acetylation | PALNKPKKPLTSSSA HHHCCCCCCCCCCCC | 54.51 | 26051181 | |
151 | Methylation | PALNKPKKPLTSSSA HHHCCCCCCCCCCCC | 54.51 | - | |
154 | Phosphorylation | NKPKKPLTSSSAAPQ CCCCCCCCCCCCCCC | 34.78 | 20201521 | |
154 | O-linked_Glycosylation | NKPKKPLTSSSAAPQ CCCCCCCCCCCCCCC | 34.78 | 30059200 | |
155 | Phosphorylation | KPKKPLTSSSAAPQR CCCCCCCCCCCCCCC | 29.94 | 23927012 | |
155 | O-linked_Glycosylation | KPKKPLTSSSAAPQR CCCCCCCCCCCCCCC | 29.94 | 30059200 | |
156 | O-linked_Glycosylation | PKKPLTSSSAAPQRP CCCCCCCCCCCCCCC | 20.82 | 30059200 | |
156 | Phosphorylation | PKKPLTSSSAAPQRP CCCCCCCCCCCCCCC | 20.82 | 23927012 | |
157 | Phosphorylation | KKPLTSSSAAPQRPI CCCCCCCCCCCCCCC | 28.37 | 23927012 | |
157 | O-linked_Glycosylation | KKPLTSSSAAPQRPI CCCCCCCCCCCCCCC | 28.37 | 30059200 | |
165 | Phosphorylation | AAPQRPISTQRTAAA CCCCCCCCCCCCCCC | 22.59 | 12857735 | |
166 | Phosphorylation | APQRPISTQRTAAAP CCCCCCCCCCCCCCC | 23.84 | 23927012 | |
174 | Ubiquitination | QRTAAAPKAGPGVVR CCCCCCCCCCCCCEE | 62.34 | 23000965 | |
182 | Ubiquitination | AGPGVVRKNPGVGNG CCCCCEECCCCCCCC | 56.75 | 29967540 | |
197 | Sulfoxidation | DDEAAELMQQVNVLK CHHHHHHHHHHCCEE | 1.65 | 21406390 | |
204 | Ubiquitination | MQQVNVLKLTVEDLE HHHHCCEEEEHHHHH | 37.52 | 32015554 | |
206 | Phosphorylation | QVNVLKLTVEDLEKE HHCCEEEEHHHHHHH | 21.91 | - | |
212 | Ubiquitination | LTVEDLEKERDFYFG EEHHHHHHHCCEEEE | 66.40 | 21906983 | |
212 | Sumoylation | LTVEDLEKERDFYFG EEHHHHHHHCCEEEE | 66.40 | - | |
212 | Sumoylation | LTVEDLEKERDFYFG EEHHHHHHHCCEEEE | 66.40 | - | |
217 | Phosphorylation | LEKERDFYFGKLRNI HHHHCCEEEEEEECE | 18.73 | - | |
220 | Ubiquitination | ERDFYFGKLRNIELI HCCEEEEEEECEEEE | 34.08 | 22817900 | |
220 | Acetylation | ERDFYFGKLRNIELI HCCEEEEEEECEEEE | 34.08 | 19608861 | |
228 | Glutathionylation | LRNIELICQENEGEN EECEEEEEECCCCCC | 6.93 | 22555962 | |
247 | Phosphorylation | QRIVDILYATDEGFV HHHHHHHHHCCCCCC | 14.06 | 26552605 | |
249 | Phosphorylation | IVDILYATDEGFVIP HHHHHHHCCCCCCCC | 22.49 | 26552605 | |
268 | Phosphorylation | PQEEQEEY------- CHHHHHCC------- | 24.09 | 26552605 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
40 | S | Phosphorylation | Kinase | MAP3K5 | Q99683 | GPS |
154 | T | Phosphorylation | Kinase | MAP3K5 | Q99683 | GPS |
155 | S | Phosphorylation | Kinase | GSK3B | P49841 | PSP |
156 | S | Phosphorylation | Kinase | GSK3B | P49841 | PSP |
206 | T | Phosphorylation | Kinase | MAP3K5 | Q99683 | GPS |
247 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MARE1_HUMAN !! |
* 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 MARE1_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY. | |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND THR-166, ANDMASS SPECTROMETRY. | |
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-124, AND MASSSPECTROMETRY. |