NUCL_MOUSE - dbPTM
NUCL_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NUCL_MOUSE
UniProt AC P09405
Protein Name Nucleolin
Gene Name Ncl
Organism Mus musculus (Mouse).
Sequence Length 707
Subcellular Localization Nucleus, nucleolus. Cytoplasm. Localized in cytoplasmic mRNP granules containing untranslated mRNAs..
Protein Description Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats (By similarity)..
Protein Sequence MVKLAKAGKTHGEAKKMAPPPKEVEEDSEDEEMSEDEDDSSGEEEVVIPQKKGKKATTTPAKKVVVSQTKKAAVPTPAKKAAVTPGKKAVATPAKKNITPAKVIPTPGKKGAAQAKALVPTPGKKGAATPAKGAKNGKNAKKEDSDEDEDEEDEDDSDEDEDDEEEDEFEPPIVKGVKPAKAAPAAPASEDEEDDEDEDDEEDDDEEEEDDSEEEVMEITTAKGKKTPAKVVPMKAKSVAEEEDDEEEDEDDEDEDDEEEDDEDDDEEEEEEEPVKAAPGKRKKEMTKQKEAPEAKKQKVEGSEPTTPFNLFIGNLNPNKSVNELKFAISELFAKNDLAVVDVRTGTNRKFGYVDFESAEDLEKALELTGLKVFGNEIKLEKPKGRDSKKVRAARTLLAKNLSFNITEDELKEVFEDAMEIRLVSQDGKSKGIAYIEFKSEADAEKNLEEKQGAEIDGRSVSLYYTGEKGQRQERTGKTSTWSGESKTLVLSNLSYSATKETLEEVFEKATFIKVPQNPHGKPKGYAFIEFASFEDAKEALNSCNKMEIEGRTIRLELQGSNSRSQPSKTLFVKGLSEDTTEETLKESFEGSVRARIVTDRETGSSKGFGFVDFNSEEDAKAAKEAMEDGEIDGNKVTLDWAKPKGEGGFGGRGGGRGGFGGRGGGRGGRGGFGGRGRGGFGGRGGFRGGRGGGGDFKPQGKKTKFE
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
9AcetylationVKLAKAGKTHGEAKK
CCCCCCCCCCCCHHH
42.0623806337
15AcetylationGKTHGEAKKMAPPPK
CCCCCCHHHCCCCCC
38.4923806337
16AcetylationKTHGEAKKMAPPPKE
CCCCCHHHCCCCCCC
47.5523806337
28PhosphorylationPKEVEEDSEDEEMSE
CCCCCCCCCCHHHCC
50.6724925903
33OxidationEDSEDEEMSEDEDDS
CCCCCHHHCCCCCCC
5.1017242355
34PhosphorylationDSEDEEMSEDEDDSS
CCCCHHHCCCCCCCC
45.2124925903
40PhosphorylationMSEDEDDSSGEEEVV
HCCCCCCCCCCEEEE
53.1924925903
41PhosphorylationSEDEDDSSGEEEVVI
CCCCCCCCCCEEEEC
58.1624925903
57PhosphorylationQKKGKKATTTPAKKV
CCCCCCCCCCCCCEE
39.8324453211
58PhosphorylationKKGKKATTTPAKKVV
CCCCCCCCCCCCEEE
35.3226745281
59PhosphorylationKGKKATTTPAKKVVV
CCCCCCCCCCCEEEE
19.5218779572
63AcetylationATTTPAKKVVVSQTK
CCCCCCCEEEECCCC
42.2223806337
63MalonylationATTTPAKKVVVSQTK
CCCCCCCEEEECCCC
42.2226320211
63UbiquitinationATTTPAKKVVVSQTK
CCCCCCCEEEECCCC
42.2227667366
67PhosphorylationPAKKVVVSQTKKAAV
CCCEEEECCCCCCCC
22.1128066266
69PhosphorylationKKVVVSQTKKAAVPT
CEEEECCCCCCCCCC
27.3228066266
70AcetylationKVVVSQTKKAAVPTP
EEEECCCCCCCCCCC
32.55129269
71AcetylationVVVSQTKKAAVPTPA
EEECCCCCCCCCCCC
44.9923806337
71MalonylationVVVSQTKKAAVPTPA
EEECCCCCCCCCCCC
44.9926320211
71SuccinylationVVVSQTKKAAVPTPA
EEECCCCCCCCCCCC
44.9923806337
76PhosphorylationTKKAAVPTPAKKAAV
CCCCCCCCCCHHCCC
29.3126824392
79AcetylationAAVPTPAKKAAVTPG
CCCCCCCHHCCCCCC
44.12133265
79MalonylationAAVPTPAKKAAVTPG
CCCCCCCHHCCCCCC
44.1226320211
79UbiquitinationAAVPTPAKKAAVTPG
CCCCCCCHHCCCCCC
44.1227667366
84PhosphorylationPAKKAAVTPGKKAVA
CCHHCCCCCCCCCCC
22.9224453211
86UbiquitinationKKAAVTPGKKAVATP
HHCCCCCCCCCCCCC
34.4327667366
87AcetylationKAAVTPGKKAVATPA
HCCCCCCCCCCCCCC
38.4723201123
92PhosphorylationPGKKAVATPAKKNIT
CCCCCCCCCCCCCCC
19.7226824392
95AcetylationKAVATPAKKNITPAK
CCCCCCCCCCCCCCE
47.7823201123
96AcetylationAVATPAKKNITPAKV
CCCCCCCCCCCCCEE
56.5423806337
96MalonylationAVATPAKKNITPAKV
CCCCCCCCCCCCCEE
56.5426320211
99PhosphorylationTPAKKNITPAKVIPT
CCCCCCCCCCEECCC
26.9624453211
102AcetylationKKNITPAKVIPTPGK
CCCCCCCEECCCCCC
41.7323806337
102UbiquitinationKKNITPAKVIPTPGK
CCCCCCCEECCCCCC
41.7327667366
106PhosphorylationTPAKVIPTPGKKGAA
CCCEECCCCCCCCHH
33.2826824392
108UbiquitinationAKVIPTPGKKGAAQA
CEECCCCCCCCHHHH
46.9527667366
109AcetylationKVIPTPGKKGAAQAK
EECCCCCCCCHHHHE
49.6023806337
109MalonylationKVIPTPGKKGAAQAK
EECCCCCCCCHHHHE
49.6026320211
116AcetylationKKGAAQAKALVPTPG
CCCHHHHEEECCCCC
30.1223806337
116MalonylationKKGAAQAKALVPTPG
CCCHHHHEEECCCCC
30.1226320211
116SuccinylationKKGAAQAKALVPTPG
CCCHHHHEEECCCCC
30.1223806337
121PhosphorylationQAKALVPTPGKKGAA
HHEEECCCCCCCCCC
36.8726824392
124AcetylationALVPTPGKKGAATPA
EECCCCCCCCCCCCC
49.6069993
124MalonylationALVPTPGKKGAATPA
EECCCCCCCCCCCCC
49.6026320211
124UbiquitinationALVPTPGKKGAATPA
EECCCCCCCCCCCCC
49.6027667366
125AcetylationLVPTPGKKGAATPAK
ECCCCCCCCCCCCCC
60.7523806337
129PhosphorylationPGKKGAATPAKGAKN
CCCCCCCCCCCCCCC
24.2024453211
132AcetylationKGAATPAKGAKNGKN
CCCCCCCCCCCCCCC
61.6823806337
145PhosphorylationKNAKKEDSDEDEDEE
CCCCCCCCCCCCCCC
43.9524925903
157PhosphorylationDEEDEDDSDEDEDDE
CCCCCCCCCCCCCCC
56.0425521595
189PhosphorylationAAPAAPASEDEEDDE
CCCCCCCCCCCCCCC
44.5123684622
212PhosphorylationDEEEEDDSEEEVMEI
CCCCCCCCHHHHHHH
60.2623684622
220PhosphorylationEEEVMEITTAKGKKT
HHHHHHHHHCCCCCC
13.8521149613
221PhosphorylationEEVMEITTAKGKKTP
HHHHHHHHCCCCCCC
31.8421149613
230AcetylationKGKKTPAKVVPMKAK
CCCCCCCEEEECCCC
44.9923806337
230MalonylationKGKKTPAKVVPMKAK
CCCCCCCEEEECCCC
44.9926320211
238PhosphorylationVVPMKAKSVAEEEDD
EEECCCCCCCCCCCC
31.2726239621
303PhosphorylationKKQKVEGSEPTTPFN
HHHHCCCCCCCCCCE
27.2227087446
306PhosphorylationKVEGSEPTTPFNLFI
HCCCCCCCCCCEEEE
42.9520469934
307PhosphorylationVEGSEPTTPFNLFIG
CCCCCCCCCCEEEEE
36.2822942356
320AcetylationIGNLNPNKSVNELKF
EECCCCCCCHHHHHH
57.9722826441
320UbiquitinationIGNLNPNKSVNELKF
EECCCCCCCHHHHHH
57.9722790023
321PhosphorylationGNLNPNKSVNELKFA
ECCCCCCCHHHHHHH
36.4929514104
326AcetylationNKSVNELKFAISELF
CCCHHHHHHHHHHHH
26.9422826441
326UbiquitinationNKSVNELKFAISELF
CCCHHHHHHHHHHHH
26.9422790023
330PhosphorylationNELKFAISELFAKND
HHHHHHHHHHHHCCC
25.4722006019
335UbiquitinationAISELFAKNDLAVVD
HHHHHHHCCCEEEEE
43.5922790023
345PhosphorylationLAVVDVRTGTNRKFG
EEEEECCCCCCCEEE
48.4818779572
347PhosphorylationVVDVRTGTNRKFGYV
EEECCCCCCCEEEEC
31.1018779572
350AcetylationVRTGTNRKFGYVDFE
CCCCCCCEEEECCCC
45.2523806337
350MalonylationVRTGTNRKFGYVDFE
CCCCCCCEEEECCCC
45.2526320211
358PhosphorylationFGYVDFESAEDLEKA
EEECCCCCHHHHHHH
36.6326745281
369PhosphorylationLEKALELTGLKVFGN
HHHHHHHHCCEEECC
30.9727600695
372AcetylationALELTGLKVFGNEIK
HHHHHCCEEECCEEE
36.5423806337
372SuccinylationALELTGLKVFGNEIK
HHHHHCCEEECCEEE
36.5423806337
372UbiquitinationALELTGLKVFGNEIK
HHHHHCCEEECCEEE
36.54-
379AcetylationKVFGNEIKLEKPKGR
EEECCEEEECCCCCC
44.4023806337
389AcetylationKPKGRDSKKVRAART
CCCCCCHHHHHHHHH
60.627720353
396PhosphorylationKKVRAARTLLAKNLS
HHHHHHHHHHHHHCC
22.7726239621
400AcetylationAARTLLAKNLSFNIT
HHHHHHHHHCCCCCC
59.3923236377
400UbiquitinationAARTLLAKNLSFNIT
HHHHHHHHHCCCCCC
59.3922790023
403PhosphorylationTLLAKNLSFNITEDE
HHHHHHCCCCCCHHH
26.1624925903
407PhosphorylationKNLSFNITEDELKEV
HHCCCCCCHHHHHHH
38.1926239621
425PhosphorylationAMEIRLVSQDGKSKG
HHHEEEECCCCCCCC
27.4427149854
429AcetylationRLVSQDGKSKGIAYI
EEECCCCCCCCEEEE
58.2323806337
431AcetylationVSQDGKSKGIAYIEF
ECCCCCCCCEEEEEE
58.8023806337
431MalonylationVSQDGKSKGIAYIEF
ECCCCCCCCEEEEEE
58.8026320211
431SuccinylationVSQDGKSKGIAYIEF
ECCCCCCCCEEEEEE
58.8023806337
435UbiquitinationGKSKGIAYIEFKSEA
CCCCCEEEEEECCHH
10.0827667366
440PhosphorylationIAYIEFKSEADAEKN
EEEEEECCHHHHHHC
43.2529514104
446AcetylationKSEADAEKNLEEKQG
CCHHHHHHCHHHHCC
69.4323806337
451UbiquitinationAEKNLEEKQGAEIDG
HHHCHHHHCCCCCCC
44.6622790023
453UbiquitinationKNLEEKQGAEIDGRS
HCHHHHCCCCCCCEE
35.9227667366
460PhosphorylationGAEIDGRSVSLYYTG
CCCCCCEEEEEEEEC
22.9122942356
462PhosphorylationEIDGRSVSLYYTGEK
CCCCEEEEEEEECCC
16.3528833060
462UbiquitinationEIDGRSVSLYYTGEK
CCCCEEEEEEEECCC
16.3527667366
464PhosphorylationDGRSVSLYYTGEKGQ
CCEEEEEEEECCCCC
7.4728833060
465PhosphorylationGRSVSLYYTGEKGQR
CEEEEEEEECCCCCE
17.3528833060
466PhosphorylationRSVSLYYTGEKGQRQ
EEEEEEEECCCCCEE
25.8828833060
469AcetylationSLYYTGEKGQRQERT
EEEEECCCCCEEEEC
62.7823806337
469UbiquitinationSLYYTGEKGQRQERT
EEEEECCCCCEEEEC
62.7822790023
478AcetylationQRQERTGKTSTWSGE
CEEEECCCCCCCCCC
38.3923806337
478MalonylationQRQERTGKTSTWSGE
CEEEECCCCCCCCCC
38.3926320211
478UbiquitinationQRQERTGKTSTWSGE
CEEEECCCCCCCCCC
38.3927667366
479PhosphorylationRQERTGKTSTWSGES
EEEECCCCCCCCCCC
32.5027600695
480PhosphorylationQERTGKTSTWSGESK
EEECCCCCCCCCCCC
31.2228285833
492PhosphorylationESKTLVLSNLSYSAT
CCCEEEEECCCCCCC
28.3926745281
495PhosphorylationTLVLSNLSYSATKET
EEEEECCCCCCCHHH
22.6925266776
496PhosphorylationLVLSNLSYSATKETL
EEEECCCCCCCHHHH
12.9023984901
497PhosphorylationVLSNLSYSATKETLE
EEECCCCCCCHHHHH
26.5326745281
499PhosphorylationSNLSYSATKETLEEV
ECCCCCCCHHHHHHH
24.3926745281
500UbiquitinationNLSYSATKETLEEVF
CCCCCCCHHHHHHHH
48.71-
506UbiquitinationTKETLEEVFEKATFI
CHHHHHHHHHHCCEE
5.6927667366
509AcetylationTLEEVFEKATFIKVP
HHHHHHHHCCEEECC
41.0622826441
509UbiquitinationTLEEVFEKATFIKVP
HHHHHHHHCCEEECC
41.0622790023
514AcetylationFEKATFIKVPQNPHG
HHHCCEEECCCCCCC
43.61-
514MalonylationFEKATFIKVPQNPHG
HHHCCEEECCCCCCC
43.6126320211
522AcetylationVPQNPHGKPKGYAFI
CCCCCCCCCCCEEEE
40.2923806337
522UbiquitinationVPQNPHGKPKGYAFI
CCCCCCCCCCCEEEE
40.2927667366
533PhosphorylationYAFIEFASFEDAKEA
EEEEEECCHHHHHHH
34.1926745281
544S-nitrosocysteineAKEALNSCNKMEIEG
HHHHHHHCCCEEECC
5.73-
544GlutathionylationAKEALNSCNKMEIEG
HHHHHHHCCCEEECC
5.7324333276
544S-nitrosylationAKEALNSCNKMEIEG
HHHHHHHCCCEEECC
5.7320925432
546AcetylationEALNSCNKMEIEGRT
HHHHHCCCEEECCEE
42.0923806337
546MalonylationEALNSCNKMEIEGRT
HHHHHCCCEEECCEE
42.0926320211
546UbiquitinationEALNSCNKMEIEGRT
HHHHHCCCEEECCEE
42.09-
553UbiquitinationKMEIEGRTIRLELQG
CEEECCEEEEEEEEC
22.7027667366
561PhosphorylationIRLELQGSNSRSQPS
EEEEEECCCCCCCCC
20.7628066266
563PhosphorylationLELQGSNSRSQPSKT
EEEECCCCCCCCCEE
34.7028066266
569AcetylationNSRSQPSKTLFVKGL
CCCCCCCEEEEEECC
56.8023806337
569UbiquitinationNSRSQPSKTLFVKGL
CCCCCCCEEEEEECC
56.8027667366
574AcetylationPSKTLFVKGLSEDTT
CCEEEEEECCCCCCC
46.9623806337
574MalonylationPSKTLFVKGLSEDTT
CCEEEEEECCCCCCC
46.9626320211
574UbiquitinationPSKTLFVKGLSEDTT
CCEEEEEECCCCCCC
46.96-
577PhosphorylationTLFVKGLSEDTTEET
EEEEECCCCCCCHHH
41.9425521595
580PhosphorylationVKGLSEDTTEETLKE
EECCCCCCCHHHHHH
31.8628833060
581PhosphorylationKGLSEDTTEETLKES
ECCCCCCCHHHHHHH
44.1128833060
584PhosphorylationSEDTTEETLKESFEG
CCCCCHHHHHHHHCC
36.5823984901
586UbiquitinationDTTEETLKESFEGSV
CCCHHHHHHHHCCCE
59.7522790023
588PhosphorylationTEETLKESFEGSVRA
CHHHHHHHHCCCEEE
27.3230635358
592PhosphorylationLKESFEGSVRARIVT
HHHHHCCCEEEEEEE
10.9627841257
599PhosphorylationSVRARIVTDRETGSS
CEEEEEEECCCCCCC
27.2829472430
603PhosphorylationRIVTDRETGSSKGFG
EEEECCCCCCCCCCC
43.1729472430
605PhosphorylationVTDRETGSSKGFGFV
EECCCCCCCCCCCCC
35.9730352176
606PhosphorylationTDRETGSSKGFGFVD
ECCCCCCCCCCCCCC
37.8429514104
607AcetylationDRETGSSKGFGFVDF
CCCCCCCCCCCCCCC
61.0123236377
607UbiquitinationDRETGSSKGFGFVDF
CCCCCCCCCCCCCCC
61.0122790023
616PhosphorylationFGFVDFNSEEDAKAA
CCCCCCCCHHHHHHH
42.2127087446
621AcetylationFNSEEDAKAAKEAME
CCCHHHHHHHHHHHH
62.2923806337
624UbiquitinationEEDAKAAKEAMEDGE
HHHHHHHHHHHHHCC
51.3622790023
643AcetylationKVTLDWAKPKGEGGF
EEEEEECCCCCCCCC
42.9023806337
643MalonylationKVTLDWAKPKGEGGF
EEEEEECCCCCCCCC
42.9026320211
643SuccinylationKVTLDWAKPKGEGGF
EEEEEECCCCCCCCC
42.9023806337
653Asymmetric dimethylarginineGEGGFGGRGGGRGGF
CCCCCCCCCCCCCCC
40.75-
653MethylationGEGGFGGRGGGRGGF
CCCCCCCCCCCCCCC
40.7518958051
657Asymmetric dimethylarginineFGGRGGGRGGFGGRG
CCCCCCCCCCCCCCC
45.39-
657MethylationFGGRGGGRGGFGGRG
CCCCCCCCCCCCCCC
45.3918967237
663Asymmetric dimethylarginineGRGGFGGRGGGRGGR
CCCCCCCCCCCCCCC
40.75-
663MethylationGRGGFGGRGGGRGGR
CCCCCCCCCCCCCCC
40.75-
667Asymmetric dimethylarginineFGGRGGGRGGRGGFG
CCCCCCCCCCCCCCC
47.90-
667MethylationFGGRGGGRGGRGGFG
CCCCCCCCCCCCCCC
47.90-
670Asymmetric dimethylarginineRGGGRGGRGGFGGRG
CCCCCCCCCCCCCCC
44.90-
670MethylationRGGGRGGRGGFGGRG
CCCCCCCCCCCCCCC
44.90-
676MethylationGRGGFGGRGRGGFGG
CCCCCCCCCCCCCCC
31.82-
678MethylationGGFGGRGRGGFGGRG
CCCCCCCCCCCCCCC
40.47-
684MethylationGRGGFGGRGGFRGGR
CCCCCCCCCCCCCCC
42.3025056301
688MethylationFGGRGGFRGGRGGGG
CCCCCCCCCCCCCCC
50.3516288839
691MethylationRGGFRGGRGGGGDFK
CCCCCCCCCCCCCCC
43.3324129315
702AcetylationGDFKPQGKKTKFE--
CCCCCCCCCCCCC--
52.617616583

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 NUCL_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NUCL_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 NUCL_MOUSE !!

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

Oops, there are no PPI records of NUCL_MOUSE !!

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

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-34; SER-40 ANDSER-41, AND MASS SPECTROMETRY.
"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-28; SER-34; SER-40 ANDSER-41, AND MASS SPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND SER-157, ANDMASS SPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND SER-157, ANDMASS SPECTROMETRY.

TOP