UniProt ID | NCOA5_MOUSE | |
---|---|---|
UniProt AC | Q91W39 | |
Protein Name | Nuclear receptor coactivator 5 | |
Gene Name | Ncoa5 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 579 | |
Subcellular Localization | Nucleus. | |
Protein Description | Nuclear receptor coregulator that can have both coactivator and corepressor functions. Interacts with nuclear receptors for steroids (ESR1 and ESR2) independently of the steroid binding domain (AF-2) of the ESR receptors, and with the orphan nuclear receptor NR1D2. Involved in the coactivation of nuclear steroid receptors (ER) as well as the corepression of MYC in response to 17-beta-estradiol (E2) (By similarity).. | |
Protein Sequence | MNTAPSRPSPTRRDPYSFGDSRDTRRDRSPIRGSPRREPRDGRNGRDARDSRDIRDPRDLRDRRDSRDIRDHRDSRSVREARDLRDFRDFRDLRDSRDFRDHRDPVYDRYRDIRDSRDPLYRREGSYDRYLRVDDYCRRKDDSYFDRYRDSFDGRGPPGPESQSRAKERLKREERRREELYRRYFEEIQRRFDAERPVDCSVIVVNKQTKDYAESVGRKVRDLGMVVDLIFLNTEVSLSQALEDVSRGGSPFAIVITQQHQIHRSCTVNIMFGTPQEHRNMPQADAMVLVARNYERYKNDCREKEREEIARQAAKMANDAILQERDRGGPEEGGRGGHPPAIQSLINLLADNRYLTAEETDKIINYLRERKERLLRSSADSLPGPISRQPLGAASGSSLKSQPSSQPLQSGQVLPSATPTPAAPPTSQQELQAKILSLFNSGAVAANSSSASPSVATGSSQNQNFSTAANSQPQQRPQASGNQPPNIVGQAGSARNMGPRPGAPSQGLFGQPSSRLAPASTMASQRPVSSTGINFDNPSVQKALDTLIQSGPALSHLVSQTAAQVGRPQAPMGSYQRHY | |
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 |
---|---|---|---|---|---|
1 | Acetylation | -------MNTAPSRP -------CCCCCCCC | 10.17 | - | |
3 | Phosphorylation | -----MNTAPSRPSP -----CCCCCCCCCC | 38.35 | 23527152 | |
6 | Phosphorylation | --MNTAPSRPSPTRR --CCCCCCCCCCCCC | 55.12 | 27742792 | |
9 | Phosphorylation | NTAPSRPSPTRRDPY CCCCCCCCCCCCCCC | 37.48 | 23527152 | |
11 | Phosphorylation | APSRPSPTRRDPYSF CCCCCCCCCCCCCCC | 42.55 | 27742792 | |
16 | Phosphorylation | SPTRRDPYSFGDSRD CCCCCCCCCCCCCCC | 22.41 | 21743459 | |
17 | Phosphorylation | PTRRDPYSFGDSRDT CCCCCCCCCCCCCCC | 28.30 | 21743459 | |
21 | Phosphorylation | DPYSFGDSRDTRRDR CCCCCCCCCCCCCCC | 32.22 | 21743459 | |
29 | Phosphorylation | RDTRRDRSPIRGSPR CCCCCCCCCCCCCCC | 29.03 | 25521595 | |
34 | Phosphorylation | DRSPIRGSPRREPRD CCCCCCCCCCCCCCC | 12.84 | 25521595 | |
51 | Phosphorylation | NGRDARDSRDIRDPR CCCCCCCCCCCCCHH | 26.71 | 23684622 | |
66 | Phosphorylation | DLRDRRDSRDIRDHR HHHHCCHHCHHHHHH | 30.00 | 23684622 | |
75 | Phosphorylation | DIRDHRDSRSVREAR HHHHHHHHHHHHHHH | 26.81 | 29899451 | |
88 | Methylation | ARDLRDFRDFRDLRD HHHHHCHHCHHHHHC | 46.58 | 30988625 | |
96 | Phosphorylation | DFRDLRDSRDFRDHR CHHHHHCCCCCHHCC | 27.58 | 25266776 | |
97 | Methylation | FRDLRDSRDFRDHRD HHHHHCCCCCHHCCC | 51.91 | 30988631 | |
107 | Phosphorylation | RDHRDPVYDRYRDIR HHCCCHHHHHHHHHH | 10.49 | 25159016 | |
116 | Phosphorylation | RYRDIRDSRDPLYRR HHHHHHHCCCCCCCC | 28.83 | 25159016 | |
126 | Phosphorylation | PLYRREGSYDRYLRV CCCCCCCCCCCEECH | 21.07 | 23684622 | |
127 | Phosphorylation | LYRREGSYDRYLRVD CCCCCCCCCCEECHH | 18.46 | 22324799 | |
143 | Phosphorylation | YCRRKDDSYFDRYRD HHHCCCCCHHHHCCC | 37.52 | - | |
148 | Phosphorylation | DDSYFDRYRDSFDGR CCCHHHHCCCCCCCC | 22.18 | 28066266 | |
151 | Phosphorylation | YFDRYRDSFDGRGPP HHHHCCCCCCCCCCC | 19.08 | 28066266 | |
162 | Phosphorylation | RGPPGPESQSRAKER CCCCCHHHHHHHHHH | 36.27 | 21659604 | |
164 | Phosphorylation | PPGPESQSRAKERLK CCCHHHHHHHHHHHH | 43.41 | 28285833 | |
215 | Phosphorylation | QTKDYAESVGRKVRD CCHHHHHHHHHHHHH | 23.00 | - | |
274 | Phosphorylation | TVNIMFGTPQEHRNM EEEECCCCHHHHCCC | 15.55 | 25159016 | |
377 | Phosphorylation | RKERLLRSSADSLPG HHHHHHHHCCCCCCC | 29.82 | 27087446 | |
378 | Phosphorylation | KERLLRSSADSLPGP HHHHHHHCCCCCCCC | 29.66 | 27087446 | |
381 | Phosphorylation | LLRSSADSLPGPISR HHHHCCCCCCCCCCC | 35.86 | 25521595 | |
387 | Phosphorylation | DSLPGPISRQPLGAA CCCCCCCCCCCCCCC | 28.17 | 27087446 | |
395 | Phosphorylation | RQPLGAASGSSLKSQ CCCCCCCCCCCCCCC | 38.38 | 29514104 | |
397 | Phosphorylation | PLGAASGSSLKSQPS CCCCCCCCCCCCCCC | 29.96 | 29472430 | |
398 | Phosphorylation | LGAASGSSLKSQPSS CCCCCCCCCCCCCCC | 43.26 | 29472430 | |
401 | Phosphorylation | ASGSSLKSQPSSQPL CCCCCCCCCCCCCCC | 53.25 | 26239621 | |
416 | Phosphorylation | QSGQVLPSATPTPAA CCCCCCCCCCCCCCC | 40.38 | 28285833 | |
426 | Phosphorylation | PTPAAPPTSQQELQA CCCCCCCCCHHHHHH | 37.80 | 26239621 | |
520 | Phosphorylation | SSRLAPASTMASQRP HHHCCCCHHHHCCCC | 20.04 | 27600695 | |
521 | O-linked_Glycosylation | SRLAPASTMASQRPV HHCCCCHHHHCCCCC | 20.89 | 22517741 | |
529 | Phosphorylation | MASQRPVSSTGINFD HHCCCCCCCCCCCCC | 25.51 | 26060331 | |
530 | Phosphorylation | ASQRPVSSTGINFDN HCCCCCCCCCCCCCC | 30.77 | 26060331 | |
531 | Phosphorylation | SQRPVSSTGINFDNP CCCCCCCCCCCCCCH | 34.28 | 26060331 | |
555 | Phosphorylation | IQSGPALSHLVSQTA HHHCHHHHHHHHHHH | 19.51 | 26239621 |
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 NCOA5_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NCOA5_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 NCOA5_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of NCOA5_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-34, AND MASSSPECTROMETRY. | |
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 AND SER-381, ANDMASS SPECTROMETRY. |