UniProt ID | TIPRL_HUMAN | |
---|---|---|
UniProt AC | O75663 | |
Protein Name | TIP41-like protein | |
Gene Name | TIPRL | |
Organism | Homo sapiens (Human). | |
Sequence Length | 272 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | May be a allosteric regulator of serine/threonine-protein phosphatase 2A (PP2A). Isoform 1 inhibits catalytic activity of the PP2A(D) core complex in vitro. The PP2A(C):TIPRL complex does not show phosphatase activity. Acts as negative regulator of serine/threonine-protein phosphatase 4 probably by inhibiting the formation of the active PPP4C:PPP4R2 complex; the function is proposed to implicate it in DNA damage response by promoting H2AFX phosphorylated on Ser-140 (gamma-H2AFX). May play a role in the regulation of ATM/ATR signaling pathway controlling DNA replication and repair.. | |
Protein Sequence | MMIHGFQSSHRDFCFGPWKLTASKTHIMKSADVEKLADELHMPSLPEMMFGDNVLRIQHGSGFGIEFNATDALRCVNNYQGMLKVACAEEWQESRTEGEHSKEVIKPYDWTYTTDYKGTLLGESLKLKVVPTTDHIDTEKLKAREQIKFFEEVLLFEDELHDHGVSSLSVKIRVMPSSFFLLLRFFLRIDGVLIRMNDTRLYHEADKTYMLREYTSRESKISSLMHVPPSLFTEPNEISQYLPIKEAVCEKLIFPERIDPNPADSQKSTQVE | |
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 |
---|---|---|---|---|---|
8 | Phosphorylation | MMIHGFQSSHRDFCF CCCCCCCCCCCCCCC | 26.33 | 24719451 | |
9 | Phosphorylation | MIHGFQSSHRDFCFG CCCCCCCCCCCCCCC | 16.26 | 26853621 | |
19 | Acetylation | DFCFGPWKLTASKTH CCCCCCCEEEECCCE | 38.81 | 23749302 | |
19 | Ubiquitination | DFCFGPWKLTASKTH CCCCCCCEEEECCCE | 38.81 | - | |
24 | Ubiquitination | PWKLTASKTHIMKSA CCEEEECCCEEHHHC | 41.48 | 29967540 | |
29 | Ubiquitination | ASKTHIMKSADVEKL ECCCEEHHHCCHHHH | 41.72 | 29967540 | |
29 | Acetylation | ASKTHIMKSADVEKL ECCCEEHHHCCHHHH | 41.72 | 25953088 | |
44 | Phosphorylation | ADELHMPSLPEMMFG HHHHCCCCCCHHHHC | 49.32 | 24043423 | |
79 | Phosphorylation | ALRCVNNYQGMLKVA HHHHHHHHCHHHHHH | 10.97 | - | |
84 | Ubiquitination | NNYQGMLKVACAEEW HHHCHHHHHHHHHHH | 20.92 | 32015554 | |
87 | Glutathionylation | QGMLKVACAEEWQES CHHHHHHHHHHHHHH | 5.69 | 22555962 | |
101 | Phosphorylation | SRTEGEHSKEVIKPY HCCCCCCCCCCCCCC | 26.64 | - | |
102 | Ubiquitination | RTEGEHSKEVIKPYD CCCCCCCCCCCCCCC | 58.89 | 23000965 | |
106 (in isoform 2) | Ubiquitination | - | 42.58 | 21890473 | |
106 (in isoform 1) | Ubiquitination | - | 42.58 | 21890473 | |
106 | Ubiquitination | EHSKEVIKPYDWTYT CCCCCCCCCCCCEEE | 42.58 | 23000965 | |
106 | Acetylation | EHSKEVIKPYDWTYT CCCCCCCCCCCCEEE | 42.58 | 19608861 | |
108 | Phosphorylation | SKEVIKPYDWTYTTD CCCCCCCCCCEEECC | 21.07 | 27642862 | |
111 | Phosphorylation | VIKPYDWTYTTDYKG CCCCCCCEEECCCCC | 14.21 | 27642862 | |
112 | Phosphorylation | IKPYDWTYTTDYKGT CCCCCCEEECCCCCE | 11.91 | 27642862 | |
113 | Phosphorylation | KPYDWTYTTDYKGTL CCCCCEEECCCCCEE | 13.05 | 27642862 | |
114 | Phosphorylation | PYDWTYTTDYKGTLL CCCCEEECCCCCEEE | 27.24 | 27642862 | |
117 | Acetylation | WTYTTDYKGTLLGES CEEECCCCCEEECCE | 48.51 | 61253 | |
117 (in isoform 1) | Ubiquitination | - | 48.51 | 21890473 | |
117 | Ubiquitination | WTYTTDYKGTLLGES CEEECCCCCEEECCE | 48.51 | 21963094 | |
117 (in isoform 2) | Ubiquitination | - | 48.51 | 21890473 | |
117 | Sumoylation | WTYTTDYKGTLLGES CEEECCCCCEEECCE | 48.51 | - | |
124 | Phosphorylation | KGTLLGESLKLKVVP CCEEECCEEEEEEEE | 29.07 | 27067055 | |
126 | Ubiquitination | TLLGESLKLKVVPTT EEECCEEEEEEEECC | 56.38 | 21963094 | |
126 | Acetylation | TLLGESLKLKVVPTT EEECCEEEEEEEECC | 56.38 | 25953088 | |
126 (in isoform 2) | Ubiquitination | - | 56.38 | - | |
128 | Ubiquitination | LGESLKLKVVPTTDH ECCEEEEEEEECCCC | 39.33 | 21906983 | |
128 (in isoform 1) | Ubiquitination | - | 39.33 | 21890473 | |
128 (in isoform 2) | Ubiquitination | - | 39.33 | 21890473 | |
132 | Phosphorylation | LKLKVVPTTDHIDTE EEEEEEECCCCCCHH | 32.99 | 29759185 | |
133 | Phosphorylation | KLKVVPTTDHIDTEK EEEEEECCCCCCHHH | 21.36 | 29759185 | |
138 | Phosphorylation | PTTDHIDTEKLKARE ECCCCCCHHHHHHHH | 34.12 | 29759185 | |
140 | Ubiquitination | TDHIDTEKLKAREQI CCCCCHHHHHHHHHH | 58.33 | 33845483 | |
142 | Ubiquitination | HIDTEKLKAREQIKF CCCHHHHHHHHHHHH | 57.37 | - | |
167 | Phosphorylation | LHDHGVSSLSVKIRV HHHCCCCEEEEEEEE | 23.43 | 24719451 | |
202 | Phosphorylation | RMNDTRLYHEADKTY EECCCEEEECCCCCC | 8.36 | 29496907 | |
207 (in isoform 1) | Ubiquitination | - | 48.91 | 21890473 | |
207 | 2-Hydroxyisobutyrylation | RLYHEADKTYMLREY EEEECCCCCCCCHHH | 48.91 | - | |
207 | Acetylation | RLYHEADKTYMLREY EEEECCCCCCCCHHH | 48.91 | 19608861 | |
207 | Ubiquitination | RLYHEADKTYMLREY EEEECCCCCCCCHHH | 48.91 | 22817900 | |
208 | Phosphorylation | LYHEADKTYMLREYT EEECCCCCCCCHHHC | 18.08 | 28064214 | |
209 | Phosphorylation | YHEADKTYMLREYTS EECCCCCCCCHHHCC | 10.41 | 25839225 | |
245 | Ubiquitination | ISQYLPIKEAVCEKL HHHCCCCCHHHHHHH | 37.37 | 29967540 | |
251 | Acetylation | IKEAVCEKLIFPERI CCHHHHHHHCCCCCC | 41.58 | 23749302 | |
251 | Ubiquitination | IKEAVCEKLIFPERI CCHHHHHHHCCCCCC | 41.58 | 29967540 | |
265 | Phosphorylation | IDPNPADSQKSTQVE CCCCCCCCCCCCCCC | 41.43 | 17525332 | |
267 | Ubiquitination | PNPADSQKSTQVE-- CCCCCCCCCCCCC-- | 60.46 | 27667366 | |
267 (in isoform 1) | Ubiquitination | - | 60.46 | 21890473 | |
268 | Phosphorylation | NPADSQKSTQVE--- CCCCCCCCCCCC--- | 19.21 | 22817901 | |
269 | Phosphorylation | PADSQKSTQVE---- CCCCCCCCCCC---- | 43.60 | 23312004 |
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 TIPRL_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TIPRL_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 TIPRL_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
PP2AB_HUMAN | PPP2CB | physical | 16085932 | |
PP4C_HUMAN | PPP4C | physical | 16085932 | |
PPP6_HUMAN | PPP6C | physical | 16085932 | |
A4_HUMAN | APP | physical | 21832049 | |
XPP1_HUMAN | XPNPEP1 | physical | 22939629 | |
VATA_HUMAN | ATP6V1A | physical | 22939629 | |
IGBP1_HUMAN | IGBP1 | physical | 23892082 | |
PP2AA_RAT | Ppp2ca | physical | 23892082 | |
RHG44_HUMAN | ARHGAP44 | physical | 26344197 | |
MCMBP_HUMAN | MCMBP | physical | 26344197 | |
PEPL1_HUMAN | NPEPL1 | physical | 26344197 | |
3BP1_HUMAN | SH3BP1 | physical | 26344197 | |
DYLT1_HUMAN | DYNLT1 | physical | 27173435 | |
TC1D2_HUMAN | TCTEX1D2 | physical | 27173435 |
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 |
"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-106 AND LYS-207, AND MASSSPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, AND MASSSPECTROMETRY. | |
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-209, AND MASSSPECTROMETRY. |