NCOA5_MOUSE - dbPTM
NCOA5_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MNTAPSRP
-------CCCCCCCC
10.17-
3Phosphorylation-----MNTAPSRPSP
-----CCCCCCCCCC
38.3523527152
6Phosphorylation--MNTAPSRPSPTRR
--CCCCCCCCCCCCC
55.1227742792
9PhosphorylationNTAPSRPSPTRRDPY
CCCCCCCCCCCCCCC
37.4823527152
11PhosphorylationAPSRPSPTRRDPYSF
CCCCCCCCCCCCCCC
42.5527742792
16PhosphorylationSPTRRDPYSFGDSRD
CCCCCCCCCCCCCCC
22.4121743459
17PhosphorylationPTRRDPYSFGDSRDT
CCCCCCCCCCCCCCC
28.3021743459
21PhosphorylationDPYSFGDSRDTRRDR
CCCCCCCCCCCCCCC
32.2221743459
29PhosphorylationRDTRRDRSPIRGSPR
CCCCCCCCCCCCCCC
29.0325521595
34PhosphorylationDRSPIRGSPRREPRD
CCCCCCCCCCCCCCC
12.8425521595
51PhosphorylationNGRDARDSRDIRDPR
CCCCCCCCCCCCCHH
26.7123684622
66PhosphorylationDLRDRRDSRDIRDHR
HHHHCCHHCHHHHHH
30.0023684622
75PhosphorylationDIRDHRDSRSVREAR
HHHHHHHHHHHHHHH
26.8129899451
88MethylationARDLRDFRDFRDLRD
HHHHHCHHCHHHHHC
46.5830988625
96PhosphorylationDFRDLRDSRDFRDHR
CHHHHHCCCCCHHCC
27.5825266776
97MethylationFRDLRDSRDFRDHRD
HHHHHCCCCCHHCCC
51.9130988631
107PhosphorylationRDHRDPVYDRYRDIR
HHCCCHHHHHHHHHH
10.4925159016
116PhosphorylationRYRDIRDSRDPLYRR
HHHHHHHCCCCCCCC
28.8325159016
126PhosphorylationPLYRREGSYDRYLRV
CCCCCCCCCCCEECH
21.0723684622
127PhosphorylationLYRREGSYDRYLRVD
CCCCCCCCCCEECHH
18.4622324799
143PhosphorylationYCRRKDDSYFDRYRD
HHHCCCCCHHHHCCC
37.52-
148PhosphorylationDDSYFDRYRDSFDGR
CCCHHHHCCCCCCCC
22.1828066266
151PhosphorylationYFDRYRDSFDGRGPP
HHHHCCCCCCCCCCC
19.0828066266
162PhosphorylationRGPPGPESQSRAKER
CCCCCHHHHHHHHHH
36.2721659604
164PhosphorylationPPGPESQSRAKERLK
CCCHHHHHHHHHHHH
43.4128285833
215PhosphorylationQTKDYAESVGRKVRD
CCHHHHHHHHHHHHH
23.00-
274PhosphorylationTVNIMFGTPQEHRNM
EEEECCCCHHHHCCC
15.5525159016
377PhosphorylationRKERLLRSSADSLPG
HHHHHHHHCCCCCCC
29.8227087446
378PhosphorylationKERLLRSSADSLPGP
HHHHHHHCCCCCCCC
29.6627087446
381PhosphorylationLLRSSADSLPGPISR
HHHHCCCCCCCCCCC
35.8625521595
387PhosphorylationDSLPGPISRQPLGAA
CCCCCCCCCCCCCCC
28.1727087446
395PhosphorylationRQPLGAASGSSLKSQ
CCCCCCCCCCCCCCC
38.3829514104
397PhosphorylationPLGAASGSSLKSQPS
CCCCCCCCCCCCCCC
29.9629472430
398PhosphorylationLGAASGSSLKSQPSS
CCCCCCCCCCCCCCC
43.2629472430
401PhosphorylationASGSSLKSQPSSQPL
CCCCCCCCCCCCCCC
53.2526239621
416PhosphorylationQSGQVLPSATPTPAA
CCCCCCCCCCCCCCC
40.3828285833
426PhosphorylationPTPAAPPTSQQELQA
CCCCCCCCCHHHHHH
37.8026239621
520PhosphorylationSSRLAPASTMASQRP
HHHCCCCHHHHCCCC
20.0427600695
521O-linked_GlycosylationSRLAPASTMASQRPV
HHCCCCHHHHCCCCC
20.8922517741
529PhosphorylationMASQRPVSSTGINFD
HHCCCCCCCCCCCCC
25.5126060331
530PhosphorylationASQRPVSSTGINFDN
HCCCCCCCCCCCCCC
30.7726060331
531PhosphorylationSQRPVSSTGINFDNP
CCCCCCCCCCCCCCH
34.2826060331
555PhosphorylationIQSGPALSHLVSQTA
HHHCHHHHHHHHHHH
19.5126239621

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NCOA5_MOUSE !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of NCOA5_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NCOA5_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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