NUCKS_HUMAN - dbPTM
NUCKS_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NUCKS_HUMAN
UniProt AC Q9H1E3
Protein Name Nuclear ubiquitous casein and cyclin-dependent kinase substrate 1
Gene Name NUCKS1
Organism Homo sapiens (Human).
Sequence Length 243
Subcellular Localization Nucleus.
Protein Description
Protein Sequence MSRPVRNRKVVDYSQFQESDDADEDYGRDSGPPTKKIRSSPREAKNKRRSGKNSQEDSEDSEDKDVKTKKDDSHSAEDSEDEKEDHKNVRQQRQAASKAASKQREMLMEDVGSEEEQEEEDEAPFQEKDSGSDEDFLMEDDDDSDYGSSKKKNKKMVKKSKPERKEKKMPKPRLKATVTPSPVKGKGKVGRPTASKASKEKTPSPKEEDEEPESPPEKKTSTSPPPEKSGDEGSEDEAPSGED
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
2Phosphorylation------MSRPVRNRK
------CCCCCCCCC		45.3426074081
2Acetylation------MSRPVRNRK
------CCCCCCCCC		45.3418491381
9MethylationSRPVRNRKVVDYSQF
CCCCCCCCCCCHHHH		50.5918491381
9AcetylationSRPVRNRKVVDYSQF
CCCCCCCCCCCHHHH		50.5923236377
9UbiquitinationSRPVRNRKVVDYSQF
CCCCCCCCCCCHHHH		50.5929967540
13PhosphorylationRNRKVVDYSQFQESD
CCCCCCCHHHHCCCC		7.8623927012
14PhosphorylationNRKVVDYSQFQESDD
CCCCCCHHHHCCCCC		21.7623927012
19PhosphorylationDYSQFQESDDADEDY
CHHHHCCCCCCCCCC		29.9719664994
26PhosphorylationSDDADEDYGRDSGPP
CCCCCCCCCCCCCCC		16.4123927012
28MethylationDADEDYGRDSGPPTK
CCCCCCCCCCCCCCH		28.79115485713
30PhosphorylationDEDYGRDSGPPTKKI
CCCCCCCCCCCCHHH		52.4123927012
34PhosphorylationGRDSGPPTKKIRSSP
CCCCCCCCHHHCCCH		48.3723927012
35AcetylationRDSGPPTKKIRSSPR
CCCCCCCHHHCCCHH		52.5623954790
35MethylationRDSGPPTKKIRSSPR
CCCCCCCHHHCCCHH		52.56133359
35UbiquitinationRDSGPPTKKIRSSPR
CCCCCCCHHHCCCHH		52.5633845483
36UbiquitinationDSGPPTKKIRSSPRE
CCCCCCHHHCCCHHH		45.9224816145
36AcetylationDSGPPTKKIRSSPRE
CCCCCCHHHCCCHHH		45.927708539
39PhosphorylationPPTKKIRSSPREAKN
CCCHHHCCCHHHHHH		48.4425159151
40PhosphorylationPTKKIRSSPREAKNK
CCHHHCCCHHHHHHH		20.3725159151
50PhosphorylationEAKNKRRSGKNSQED
HHHHHHHCCCCCCCC		59.1423927012
52AcetylationKNKRRSGKNSQEDSE
HHHHHCCCCCCCCCC		55.4618491381
54PhosphorylationKRRSGKNSQEDSEDS
HHHCCCCCCCCCCCC		38.1329255136
58PhosphorylationGKNSQEDSEDSEDKD
CCCCCCCCCCCCCCC		42.4229255136
61PhosphorylationSQEDSEDSEDKDVKT
CCCCCCCCCCCCCCC		43.5829255136
64MethylationDSEDSEDKDVKTKKD
CCCCCCCCCCCCCCC		61.4418491381
68PhosphorylationSEDKDVKTKKDDSHS
CCCCCCCCCCCCCCC		43.0830576142
73PhosphorylationVKTKKDDSHSAEDSE
CCCCCCCCCCCCCCH		29.4929255136
75PhosphorylationTKKDDSHSAEDSEDE
CCCCCCCCCCCCHHH		36.9929255136
79PhosphorylationDSHSAEDSEDEKEDH
CCCCCCCCHHHHHHH		38.1529255136
97PhosphorylationRQQRQAASKAASKQR
HHHHHHHHHHHHHHH		26.3317924679
98MethylationQQRQAASKAASKQRE
HHHHHHHHHHHHHHH		43.1512435625
98AcetylationQQRQAASKAASKQRE
HHHHHHHHHHHHHHH		43.1525953088
101PhosphorylationQAASKAASKQREMLM
HHHHHHHHHHHHHHH		33.8917924679
102UbiquitinationAASKAASKQREMLME
HHHHHHHHHHHHHHH		48.9624816145
102AcetylationAASKAASKQREMLME
HHHHHHHHHHHHHHH		48.9625953088
113PhosphorylationMLMEDVGSEEEQEEE
HHHHHHCCHHHHHHH		41.5019664994
130PhosphorylationAPFQEKDSGSDEDFL
CCCCCCCCCCCCCCC		51.7920201521
132PhosphorylationFQEKDSGSDEDFLME
CCCCCCCCCCCCCCC		41.6020201521
144PhosphorylationLMEDDDDSDYGSSKK
CCCCCCCCCCCCCHH		39.4620201521
146PhosphorylationEDDDDSDYGSSKKKN
CCCCCCCCCCCHHHC		23.9020201521
148PhosphorylationDDDSDYGSSKKKNKK
CCCCCCCCCHHHCHH		32.5223927012
149PhosphorylationDDSDYGSSKKKNKKM
CCCCCCCCHHHCHHH		44.1023927012
160PhosphorylationNKKMVKKSKPERKEK
CHHHHHCCCHHHHHC		47.9626074081
166UbiquitinationKSKPERKEKKMPKPR
CCCHHHHHCCCCCCC		65.2224816145
167UbiquitinationSKPERKEKKMPKPRL
CCHHHHHCCCCCCCC		58.3624816145
168AcetylationKPERKEKKMPKPRLK
CHHHHHCCCCCCCCC		62.6218585999
171AcetylationRKEKKMPKPRLKATV
HHHCCCCCCCCCCEE		38.9918586009
174UbiquitinationKKMPKPRLKATVTPS
CCCCCCCCCCEECCC		6.3327667366
175MalonylationKMPKPRLKATVTPSP
CCCCCCCCCEECCCC		43.2026320211
175MethylationKMPKPRLKATVTPSP
CCCCCCCCCEECCCC		43.2018491381
175UbiquitinationKMPKPRLKATVTPSP
CCCCCCCCCEECCCC		43.2027667366
175AcetylationKMPKPRLKATVTPSP
CCCCCCCCCEECCCC		43.2018491381
177PhosphorylationPKPRLKATVTPSPVK
CCCCCCCEECCCCCC		24.2722167270
179PhosphorylationPRLKATVTPSPVKGK
CCCCCEECCCCCCCC		17.4429255136
181PhosphorylationLKATVTPSPVKGKGK
CCCEECCCCCCCCCC		32.7219664994
183UbiquitinationATVTPSPVKGKGKVG
CEECCCCCCCCCCCC		17.5024816145
184MethylationTVTPSPVKGKGKVGR
EECCCCCCCCCCCCC		59.285182599
184UbiquitinationTVTPSPVKGKGKVGR
EECCCCCCCCCCCCC		59.2827667366
184AcetylationTVTPSPVKGKGKVGR
EECCCCCCCCCCCCC		59.2825953088
186MethylationTPSPVKGKGKVGRPT
CCCCCCCCCCCCCCC		50.25115974279
187UbiquitinationPSPVKGKGKVGRPTA
CCCCCCCCCCCCCCC		38.2527667366
188UbiquitinationSPVKGKGKVGRPTAS
CCCCCCCCCCCCCCC		45.0318491381
188AcetylationSPVKGKGKVGRPTAS
CCCCCCCCCCCCCCC		45.0323749302
193PhosphorylationKGKVGRPTASKASKE
CCCCCCCCCCHHHCC		42.0523403867
195PhosphorylationKVGRPTASKASKEKT
CCCCCCCCHHHCCCC		31.0923403867
196UbiquitinationVGRPTASKASKEKTP
CCCCCCCHHHCCCCC		54.9718491381
196AcetylationVGRPTASKASKEKTP
CCCCCCCHHHCCCCC		54.9725953088
198PhosphorylationRPTASKASKEKTPSP
CCCCCHHHCCCCCCC		45.1228258704
201AcetylationASKASKEKTPSPKEE
CCHHHCCCCCCCCCC		70.2726051181
202PhosphorylationSKASKEKTPSPKEED
CHHHCCCCCCCCCCC		30.0429255136
204PhosphorylationASKEKTPSPKEEDEE
HHCCCCCCCCCCCCC		54.5629255136
214PhosphorylationEEDEEPESPPEKKTS
CCCCCCCCCCCCCCC		57.3729255136
218AcetylationEPESPPEKKTSTSPP
CCCCCCCCCCCCCCC		68.1026051181
218MethylationEPESPPEKKTSTSPP
CCCCCCCCCCCCCCC		68.1018491381
220PhosphorylationESPPEKKTSTSPPPE
CCCCCCCCCCCCCCC		48.5930266825
221PhosphorylationSPPEKKTSTSPPPEK
CCCCCCCCCCCCCCC		35.4523927012
222PhosphorylationPPEKKTSTSPPPEKS
CCCCCCCCCCCCCCC		50.9525159151
223PhosphorylationPEKKTSTSPPPEKSG
CCCCCCCCCCCCCCC		34.8729255136
228PhosphoglycerylationSTSPPPEKSGDEGSE
CCCCCCCCCCCCCCC		66.56-
229PhosphorylationTSPPPEKSGDEGSED
CCCCCCCCCCCCCCC		50.2225159151
234PhosphorylationEKSGDEGSEDEAPSG
CCCCCCCCCCCCCCC		39.5725159151
240PhosphorylationGSEDEAPSGED----
CCCCCCCCCCC----		62.9625159151
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
181SPhosphorylationKinaseCDK1P06493
PSP
181SPhosphorylationKinaseCDK2P24941
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NUCKS_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 NUCKS_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KAD5_HUMANAK5physical
16169070
ORC2_HUMANORC2physical
22939629
RBM42_HUMANRBM42physical
22939629
CSN2_HUMANCOPS2physical
26344197
HEXI1_HUMANHEXIM1physical
26344197
HUWE1_HUMANHUWE1physical
26344197
PHAX_HUMANPHAXphysical
26344197
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 NUCKS_HUMAN

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Related Literatures of Post-Translational Modification
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-19; SER-58; SER-61;SER-113; THR-179 AND SER-181, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-113; THR-177;THR-179; SER-181; SER-214; SER-234 AND SER-240, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-54; SER-58;SER-61; SER-73; SER-75; SER-79; SER-130; SER-132; SER-144; SER-214;SER-229; SER-234 AND SER-240, AND MASS SPECTROMETRY.
"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-19; TYR-26; SER-73;SER-75; SER-79; SER-113; SER-130; SER-132; SER-144; SER-149; THR-179;SER-181; THR-202; SER-204; SER-214; SER-229; SER-234 AND SER-240, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-179 AND SER-181, ANDMASS SPECTROMETRY.
"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-14 AND SER-19, AND MASSSPECTROMETRY.
"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-214, AND MASSSPECTROMETRY.
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-101; THR-179 ANDSER-181, AND MASS SPECTROMETRY.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-179; SER-181; THR-202;SER-204 AND SER-214, AND MASS 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 SER-19; SER-58; SER-61;SER-73; SER-75; SER-79; SER-113; SER-130; SER-132; SER-144; THR-179;SER-181; THR-202; SER-204; SER-214; SER-229; SER-234 AND SER-240, ANDMASS SPECTROMETRY.
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC.";
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.;
Proteomics 5:3589-3599(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASSSPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-58 AND SER-61,AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-58; SER-61;SER-144; THR-179; SER-181; SER-204; SER-214; SER-223 AND SER-229, ANDMASS SPECTROMETRY.

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