NCOA5_HUMAN - dbPTM
NCOA5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NCOA5_HUMAN
UniProt AC Q9HCD5
Protein Name Nuclear receptor coactivator 5
Gene Name NCOA5
Organism Homo sapiens (Human).
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)..
Protein Sequence MNTAPSRPSPTRRDPYGFGDSRDSRRDRSPIRGSPRREPRDGRNGRDARDSRDIRDPRDLRDHRHSRDLRDHRDSRSVRDVRDVRDLRDFRDLRDSRDFRDQRDPMYDRYRDMRDSRDPMYRREGSYDRYLRMDDYCRRKDDSYFDRYRDSFDGRGPPGPESQSRAKERLKREERRREELYRQYFEEIQRRFDAERPVDCSVIVVNKQTKDYAESVGRKVRDLGMVVDLIFLNTEVSLSQALEDVSRGGSPFAIVITQQHQIHRSCTVNIMFGTPQEHRNMPQADAMVLVARNYERYKNECREKEREEIARQAAKMADEAILQERERGGPEEGVRGGHPPAIQSLINLLADNRYLTAEETDKIINYLRERKERLMRSSTDSLPGPISRQPLGATSGASLKTQPSSQPLQSGQVLPSATPTPSAPPTSQQELQAKILSLFNSGTVTANSSSASPSVAAGNTPNQNFSTAANSQPQQRSQASGNQPPSILGQGGSAQNMGPRPGAPSQGLFGQPSSRLAPASNMTSQRPVSSTGINFDNPSVQKALDTLIQSGPALSHLVSQTTAQMGQPQAPMGSYQRHY
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		10.1721406692
3Phosphorylation-----MNTAPSRPSP
-----CCCCCCCCCC		38.3529255136
6Phosphorylation--MNTAPSRPSPTRR
--CCCCCCCCCCCCC		55.1223401153
9PhosphorylationNTAPSRPSPTRRDPY
CCCCCCCCCCCCCCC		37.4829255136
11PhosphorylationAPSRPSPTRRDPYGF
CCCCCCCCCCCCCCC		42.5523401153
13MethylationSRPSPTRRDPYGFGD
CCCCCCCCCCCCCCC		52.30115388787
16PhosphorylationSPTRRDPYGFGDSRD
CCCCCCCCCCCCCCC		29.4028152594
21PhosphorylationDPYGFGDSRDSRRDR
CCCCCCCCCCCCCCC		38.0621130716
24PhosphorylationGFGDSRDSRRDRSPI
CCCCCCCCCCCCCCC		28.2723663014
29PhosphorylationRDSRRDRSPIRGSPR
CCCCCCCCCCCCCCC		29.0329255136
34PhosphorylationDRSPIRGSPRREPRD
CCCCCCCCCCCCCCC		12.8429255136
51PhosphorylationNGRDARDSRDIRDPR
CCCCCCCCCCCCCHH		26.7130108239
66PhosphorylationDLRDHRHSRDLRDHR
HHHCCCHHHHHHHHC		27.7024719451
75PhosphorylationDLRDHRDSRSVRDVR
HHHHHCCCCCCCCCC		26.8127251275
77PhosphorylationRDHRDSRSVRDVRDV
HHHCCCCCCCCCCCH		26.0024719451
96PhosphorylationDFRDLRDSRDFRDQR
HHHHHHHCCCHHHHC		27.5823401153
107PhosphorylationRDQRDPMYDRYRDMR
HHHCCHHHHHHHHHH		11.58-
110PhosphorylationRDPMYDRYRDMRDSR
CCHHHHHHHHHHHCC		14.2026074081
116PhosphorylationRYRDMRDSRDPMYRR
HHHHHHHCCCCCCCC		28.3723401153
121PhosphorylationRDSRDPMYRREGSYD
HHCCCCCCCCCCCHH		16.3526074081
126PhosphorylationPMYRREGSYDRYLRM
CCCCCCCCHHHHCCH		21.0723401153
127PhosphorylationMYRREGSYDRYLRMD
CCCCCCCHHHHCCHH		18.4626329039
130PhosphorylationREGSYDRYLRMDDYC
CCCCHHHHCCHHHHH		8.8623403867
136PhosphorylationRYLRMDDYCRRKDDS
HHCCHHHHHHCCCCC		5.42-
143PhosphorylationYCRRKDDSYFDRYRD
HHHCCCCCHHHHCCC		37.5221815630
144PhosphorylationCRRKDDSYFDRYRDS
HHCCCCCHHHHCCCC		19.2523186163
148PhosphorylationDDSYFDRYRDSFDGR
CCCHHHHCCCCCCCC		22.1823927012
151PhosphorylationYFDRYRDSFDGRGPP
HHHHCCCCCCCCCCC		19.0823401153
162PhosphorylationRGPPGPESQSRAKER
CCCCCHHHHHHHHHH		36.2721815630
164PhosphorylationPPGPESQSRAKERLK
CCCHHHHHHHHHHHH		43.4125850435
184PhosphorylationREELYRQYFEEIQRR
HHHHHHHHHHHHHHH		12.17-
207AcetylationCSVIVVNKQTKDYAE
CEEEEEECCCHHHHH		47.9725953088
215PhosphorylationQTKDYAESVGRKVRD
CCHHHHHHHHHHHHH		23.0025159151
265PhosphorylationQQHQIHRSCTVNIMF
CCCCCCCCCEEEECC		10.4423403867
267PhosphorylationHQIHRSCTVNIMFGT
CCCCCCCEEEECCCC		20.1723403867
274PhosphorylationTVNIMFGTPQEHRNM
EEEECCCCHHHHCCC		15.5523401153
298AcetylationARNYERYKNECREKE
HHHHHHHHHHHHHHH		53.1126051181
316SulfoxidationIARQAAKMADEAILQ
HHHHHHHHHHHHHHH		4.9521406390
362UbiquitinationLTAEETDKIINYLRE
CCHHHHHHHHHHHHH		53.5629967540
362AcetylationLTAEETDKIINYLRE
CCHHHHHHHHHHHHH		53.5625953088
377PhosphorylationRKERLMRSSTDSLPG
HHHHHHHHCCCCCCC		24.5125159151
378PhosphorylationKERLMRSSTDSLPGP
HHHHHHHCCCCCCCC		26.3525159151
379PhosphorylationERLMRSSTDSLPGPI
HHHHHHCCCCCCCCC		30.7423927012
381PhosphorylationLMRSSTDSLPGPISR
HHHHCCCCCCCCCCC		36.2323927012
387PhosphorylationDSLPGPISRQPLGAT
CCCCCCCCCCCCCCC		28.1723927012
394PhosphorylationSRQPLGATSGASLKT
CCCCCCCCCCCCCCC		26.3721406692
395PhosphorylationRQPLGATSGASLKTQ
CCCCCCCCCCCCCCC		31.6521406692
395O-linked_GlycosylationRQPLGATSGASLKTQ
CCCCCCCCCCCCCCC		31.6530059200
398PhosphorylationLGATSGASLKTQPSS
CCCCCCCCCCCCCCC		33.6427050516
401PhosphorylationTSGASLKTQPSSQPL
CCCCCCCCCCCCCCC		51.5126074081
401O-linked_GlycosylationTSGASLKTQPSSQPL
CCCCCCCCCCCCCCC		51.5130059200
404PhosphorylationASLKTQPSSQPLQSG
CCCCCCCCCCCCCCC		31.6116094384
405PhosphorylationSLKTQPSSQPLQSGQ
CCCCCCCCCCCCCCC		42.3626074081
410PhosphorylationPSSQPLQSGQVLPSA
CCCCCCCCCCCCCCC		38.5926074081
416PhosphorylationQSGQVLPSATPTPSA
CCCCCCCCCCCCCCC		40.3825159151
416O-linked_GlycosylationQSGQVLPSATPTPSA
CCCCCCCCCCCCCCC		40.3830059200
418PhosphorylationGQVLPSATPTPSAPP
CCCCCCCCCCCCCCC		31.8425159151
418O-linked_GlycosylationGQVLPSATPTPSAPP
CCCCCCCCCCCCCCC		31.8430059200
420PhosphorylationVLPSATPTPSAPPTS
CCCCCCCCCCCCCCC		26.0616094384
420O-linked_GlycosylationVLPSATPTPSAPPTS
CCCCCCCCCCCCCCC		26.0630059200
422O-linked_GlycosylationPSATPTPSAPPTSQQ
CCCCCCCCCCCCCHH		56.7530059200
422PhosphorylationPSATPTPSAPPTSQQ
CCCCCCCCCCCCCHH		56.7526074081
426PhosphorylationPTPSAPPTSQQELQA
CCCCCCCCCHHHHHH		37.8026074081
426O-linked_GlycosylationPTPSAPPTSQQELQA
CCCCCCCCCHHHHHH		37.8030059200
427O-linked_GlycosylationTPSAPPTSQQELQAK
CCCCCCCCHHHHHHH		35.3230059200
427PhosphorylationTPSAPPTSQQELQAK
CCCCCCCCHHHHHHH		35.3226074081
437O-linked_GlycosylationELQAKILSLFNSGTV
HHHHHHHHHHHCCEE		34.0930059200
449O-linked_GlycosylationGTVTANSSSASPSVA
CEEEECCCCCCCCCC		29.7230059200
449PhosphorylationGTVTANSSSASPSVA
CEEEECCCCCCCCCC		29.7228348404
450PhosphorylationTVTANSSSASPSVAA
EEEECCCCCCCCCCC		32.3628348404
450O-linked_GlycosylationTVTANSSSASPSVAA
EEEECCCCCCCCCCC		32.3630059200
452PhosphorylationTANSSSASPSVAAGN
EECCCCCCCCCCCCC		21.4728348404
454O-linked_GlycosylationNSSSASPSVAAGNTP
CCCCCCCCCCCCCCC		23.1530059200
454PhosphorylationNSSSASPSVAAGNTP
CCCCCCCCCCCCCCC		23.1528348404
460PhosphorylationPSVAAGNTPNQNFST
CCCCCCCCCCCCCCC		23.7729802988
460O-linked_GlycosylationPSVAAGNTPNQNFST
CCCCCCCCCCCCCCC		23.7730059200
471O-linked_GlycosylationNFSTAANSQPQQRSQ
CCCCCCCCCHHHHHH		38.2130059200
477PhosphorylationNSQPQQRSQASGNQP
CCCHHHHHHHCCCCC		26.26-
500MethylationSAQNMGPRPGAPSQG
CCCCCCCCCCCCCCC		36.23115484617
505PhosphorylationGPRPGAPSQGLFGQP
CCCCCCCCCCCCCCC		36.02-
515MethylationLFGQPSSRLAPASNM
CCCCCHHHCCCCCCC		38.93115484625
520PhosphorylationSSRLAPASNMTSQRP
HHHCCCCCCCCCCCC		26.5229978859
523PhosphorylationLAPASNMTSQRPVSS
CCCCCCCCCCCCCCC		26.4229978859
524PhosphorylationAPASNMTSQRPVSST
CCCCCCCCCCCCCCC		17.2729978859
529PhosphorylationMTSQRPVSSTGINFD
CCCCCCCCCCCCCCC		25.5129978859
530PhosphorylationTSQRPVSSTGINFDN
CCCCCCCCCCCCCCC		30.7724719451
530O-linked_GlycosylationTSQRPVSSTGINFDN
CCCCCCCCCCCCCCC		30.7730059200
531PhosphorylationSQRPVSSTGINFDNP
CCCCCCCCCCCCCCH		34.2829978859
539PhosphorylationGINFDNPSVQKALDT
CCCCCCHHHHHHHHH		43.3529978859
546PhosphorylationSVQKALDTLIQSGPA
HHHHHHHHHHHHCHH		26.9820068231
550PhosphorylationALDTLIQSGPALSHL
HHHHHHHHCHHHHHH		39.4922210691
555PhosphorylationIQSGPALSHLVSQTT
HHHCHHHHHHHHHHH		19.5120068231
559PhosphorylationPALSHLVSQTTAQMG
HHHHHHHHHHHHHCC		28.3320068231
561PhosphorylationLSHLVSQTTAQMGQP
HHHHHHHHHHHCCCC		19.3220068231
562PhosphorylationSHLVSQTTAQMGQPQ
HHHHHHHHHHCCCCC		13.7820068231
574PhosphorylationQPQAPMGSYQRHY--
CCCCCCCCCCCCC--		16.3120068231
575PhosphorylationPQAPMGSYQRHY---
CCCCCCCCCCCC---		12.1120068231
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NCOA5_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NCOA5_HUMANNCOA5physical
20211142
NCOA5_HUMANNCOA5physical
25416956
SYT16_HUMANSYT16physical
25416956
KHDR2_HUMANKHDRBS2physical
25416956
AMZ2_HUMANAMZ2physical
26186194
GALC_HUMANGALCphysical
26186194
NCOA5_HUMANNCOA5physical
21516116
GALC_HUMANGALCphysical
28514442
Drug and Disease Associations
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.
Regulatory Network of NCOA5_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-3; SER-9; THR-379 AND SER-381, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378; THR-379 ANDSER-381, AND MASS SPECTROMETRY.
"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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-3; SER-9; THR-379 AND SER-381, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378 AND SER-381, ANDMASS SPECTROMETRY.
"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-377 AND SER-387, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-127 AND SER-151, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404 AND THR-420, ANDMASS SPECTROMETRY.

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