NOLC1_HUMAN - dbPTM
NOLC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NOLC1_HUMAN
UniProt AC Q14978
Protein Name Nucleolar and coiled-body phosphoprotein 1 {ECO:0000305}
Gene Name NOLC1 {ECO:0000312|HGNC:HGNC:15608}
Organism Homo sapiens (Human).
Sequence Length 699
Subcellular Localization Nucleus, nucleolus . Cytoplasm . Shuttles between the nucleolus and the cytoplasm. At telophase it begins to assemble into granular-like pre-nucleolar bodies which are subsequently relocated to nucleoli at the early G1-phase.
Protein Description Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification. [PubMed: 10567578]
Protein Sequence MADAGIRRVVPSDLYPLVLGFLRDNQLSEVANKFAKATGATQQDANASSLLDIYSFWLKSAKVPERKLQANGPVAKKAKKKASSSDSEDSSEEEEEVQGPPAKKAAVPAKRVGLPPGKAAAKASESSSSEESSDDDDEEDQKKQPVQKGVKPQAKAAKAPPKKAKSSDSDSDSSSEDEPPKNQKPKITPVTVKAQTKAPPKPARAAPKIANGKAASSSSSSSSSSSSDDSEEEKAAATPKKTVPKKQVVAKAPVKAATTPTRKSSSSEDSSSDEEEEQKKPMKNKPGPYSSVPPPSAPPPKKSLGTQPPKKAVEKQQPVESSEDSSDESDSSSEEEKKPPTKAVVSKATTKPPPAKKAAESSSDSSDSDSSEDDEAPSKPAGTTKNSSNKPAVTTKSPAVKPAAAPKQPVGGGQKLLTRKADSSSSEEESSSSEEEKTKKMVATTKPKATAKAALSLPAKQAPQGSRDSSSDSDSSSSEEEEEKTSKSAVKKKPQKVAGGAAPSKPASAKKGKAESSNSSSSDDSSEEEEEKLKGKGSPRPQAPKANGTSALTAQNGKAAKNSEEEEEEKKKAAVVVSKSGSLKKRKQNEAAKEAETPQAKKIKLQTPNTFPKRKKGEKRASSPFRRVREEEIEVDSRVADNSFDAKRGAAGDWGERANQVLKFTKGKSFRHEKTKKKRGSYRGGSISVQVNSIKFDSE
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
7Methylation-MADAGIRRVVPSDL
-CCCCCCCCCCCHHH
25.15115485301
28PhosphorylationFLRDNQLSEVANKFA
HHCCCHHHHHHHHHH
21.9121815630
33AcetylationQLSEVANKFAKATGA
HHHHHHHHHHHHHCC
36.6419608861
33UbiquitinationQLSEVANKFAKATGA
HHHHHHHHHHHHHCC
36.6421890473
33 (in isoform 1)Ubiquitination-36.6421890473
33 (in isoform 2)Malonylation-36.6426320211
33 (in isoform 2)Ubiquitination-36.6421890473
33 (in isoform 3)Ubiquitination-36.6421890473
36AcetylationEVANKFAKATGATQQ
HHHHHHHHHHCCCHH
50.0021466224
36UbiquitinationEVANKFAKATGATQQ
HHHHHHHHHHCCCHH
50.00-
38PhosphorylationANKFAKATGATQQDA
HHHHHHHHCCCHHCC
27.0024043423
41PhosphorylationFAKATGATQQDANAS
HHHHHCCCHHCCCHH
28.2724043423
48PhosphorylationTQQDANASSLLDIYS
CHHCCCHHHHHHHHH
22.7124043423
49PhosphorylationQQDANASSLLDIYSF
HHCCCHHHHHHHHHH
30.4624043423
54PhosphorylationASSLLDIYSFWLKSA
HHHHHHHHHHHHHHC
9.4724043423
55PhosphorylationSSLLDIYSFWLKSAK
HHHHHHHHHHHHHCC
15.4124043423
59UbiquitinationDIYSFWLKSAKVPER
HHHHHHHHHCCCCHH
38.68-
60 (in isoform 3)Methylation-31.02-
67SumoylationSAKVPERKLQANGPV
HCCCCHHHHHHCCHH
43.20-
67SumoylationSAKVPERKLQANGPV
HCCCCHHHHHHCCHH
43.2028112733
76AcetylationQANGPVAKKAKKKAS
HHCCHHHHHHHHHHC
54.2023749302
76SumoylationQANGPVAKKAKKKAS
HHCCHHHHHHHHHHC
54.2028112733
80MethylationPVAKKAKKKASSSDS
HHHHHHHHHHCCCCC
59.4323748837
83PhosphorylationKKAKKKASSSDSEDS
HHHHHHHCCCCCCCC
38.9725159151
84PhosphorylationKAKKKASSSDSEDSS
HHHHHHCCCCCCCCH
42.9223927012
85PhosphorylationAKKKASSSDSEDSSE
HHHHHCCCCCCCCHH
42.5323927012
85 (in isoform 2)Phosphorylation-42.5321406692
87PhosphorylationKKASSSDSEDSSEEE
HHHCCCCCCCCHHHH
45.3023927012
87 (in isoform 2)Phosphorylation-45.3021406692
90PhosphorylationSSSDSEDSSEEEEEV
CCCCCCCCHHHHHHH
35.2825159151
90 (in isoform 2)Phosphorylation-35.2821406692
91PhosphorylationSSDSEDSSEEEEEVQ
CCCCCCCHHHHHHHC
62.4425159151
110AcetylationKKAAVPAKRVGLPPG
HHCCCCHHHHCCCCC
41.3625953088
118AcetylationRVGLPPGKAAAKASE
HHCCCCCHHHHHHCC
40.4025953088
124PhosphorylationGKAAAKASESSSSEE
CHHHHHHCCCCCCCC
36.9920873877
126PhosphorylationAAAKASESSSSEESS
HHHHHCCCCCCCCCC
32.7820873877
127PhosphorylationAAKASESSSSEESSD
HHHHCCCCCCCCCCC
33.5620873877
128PhosphorylationAKASESSSSEESSDD
HHHCCCCCCCCCCCC
51.5620873877
129PhosphorylationKASESSSSEESSDDD
HHCCCCCCCCCCCCC
47.5320873877
132PhosphorylationESSSSEESSDDDDEE
CCCCCCCCCCCCCHH
34.7120873877
133PhosphorylationSSSSEESSDDDDEED
CCCCCCCCCCCCHHH
48.6221815630
166PhosphorylationAPPKKAKSSDSDSDS
CCCCCCCCCCCCCCC
44.2130177828
167PhosphorylationPPKKAKSSDSDSDSS
CCCCCCCCCCCCCCC
40.1930576142
169PhosphorylationKKAKSSDSDSDSSSE
CCCCCCCCCCCCCCC
40.7530576142
171PhosphorylationAKSSDSDSDSSSEDE
CCCCCCCCCCCCCCC
43.2621815630
173PhosphorylationSSDSDSDSSSEDEPP
CCCCCCCCCCCCCCC
39.4530576142
174PhosphorylationSDSDSDSSSEDEPPK
CCCCCCCCCCCCCCC
42.6130576142
175PhosphorylationDSDSDSSSEDEPPKN
CCCCCCCCCCCCCCC
53.6829888752
186SumoylationPPKNQKPKITPVTVK
CCCCCCCCCCCEEEC
67.2728112733
188PhosphorylationKNQKPKITPVTVKAQ
CCCCCCCCCEEECEE
20.1730266825
188 (in isoform 2)Phosphorylation-20.1721406692
191PhosphorylationKPKITPVTVKAQTKA
CCCCCCEEECEECCC
19.9330266825
193SumoylationKITPVTVKAQTKAPP
CCCCEEECEECCCCC
25.97-
193AcetylationKITPVTVKAQTKAPP
CCCCEEECEECCCCC
25.9725953088
193SumoylationKITPVTVKAQTKAPP
CCCCEEECEECCCCC
25.9728112733
193UbiquitinationKITPVTVKAQTKAPP
CCCCEEECEECCCCC
25.97-
197AcetylationVTVKAQTKAPPKPAR
EEECEECCCCCCCCC
46.9825953088
197UbiquitinationVTVKAQTKAPPKPAR
EEECEECCCCCCCCC
46.98-
216PhosphorylationIANGKAASSSSSSSS
CCCCCCCCCCCCCCC
35.3023312004
217PhosphorylationANGKAASSSSSSSSS
CCCCCCCCCCCCCCC
29.5223312004
218PhosphorylationNGKAASSSSSSSSSS
CCCCCCCCCCCCCCC
31.5723312004
219PhosphorylationGKAASSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8721712546
220PhosphorylationKAASSSSSSSSSSSS
CCCCCCCCCCCCCCC
35.8723312004
221PhosphorylationAASSSSSSSSSSSSD
CCCCCCCCCCCCCCC
35.8721712546
222PhosphorylationASSSSSSSSSSSSDD
CCCCCCCCCCCCCCC
35.8729888752
223PhosphorylationSSSSSSSSSSSSDDS
CCCCCCCCCCCCCCH
35.8729888752
224PhosphorylationSSSSSSSSSSSDDSE
CCCCCCCCCCCCCHH
35.8729888752
225PhosphorylationSSSSSSSSSSDDSEE
CCCCCCCCCCCCHHH
35.4929888752
226PhosphorylationSSSSSSSSSDDSEEE
CCCCCCCCCCCHHHH
39.4729888752
227PhosphorylationSSSSSSSSDDSEEEK
CCCCCCCCCCHHHHH
47.5926657352
230PhosphorylationSSSSSDDSEEEKAAA
CCCCCCCHHHHHHHC
52.4726657352
238PhosphorylationEEEKAAATPKKTVPK
HHHHHHCCCCCCCCH
30.8030576142
238 (in isoform 2)Phosphorylation-30.8028985074
242PhosphorylationAAATPKKTVPKKQVV
HHCCCCCCCCHHHEE
48.4420068231
244 (in isoform 2)Phosphorylation-43.2720068231
246 (in isoform 2)Phosphorylation-42.1026434776
247 (in isoform 2)Phosphorylation-40.8326434776
251AcetylationPKKQVVAKAPVKAAT
CHHHEEECCCCCCCC
41.4326822725
251UbiquitinationPKKQVVAKAPVKAAT
CHHHEEECCCCCCCC
41.43-
255AcetylationVVAKAPVKAATTPTR
EEECCCCCCCCCCCC
31.1125953088
258PhosphorylationKAPVKAATTPTRKSS
CCCCCCCCCCCCCCC
37.8625072903
259PhosphorylationAPVKAATTPTRKSSS
CCCCCCCCCCCCCCC
20.2425072903
261PhosphorylationVKAATTPTRKSSSSE
CCCCCCCCCCCCCCC
48.9520068231
264PhosphorylationATTPTRKSSSSEDSS
CCCCCCCCCCCCCCC
31.9621955146
265PhosphorylationTTPTRKSSSSEDSSS
CCCCCCCCCCCCCCC
40.7030108239
266PhosphorylationTPTRKSSSSEDSSSD
CCCCCCCCCCCCCCH
44.8530108239
267PhosphorylationPTRKSSSSEDSSSDE
CCCCCCCCCCCCCHH
47.5830108239
270PhosphorylationKSSSSEDSSSDEEEE
CCCCCCCCCCHHHHH
27.9120068231
271PhosphorylationSSSSEDSSSDEEEEQ
CCCCCCCCCHHHHHH
54.8820068231
272PhosphorylationSSSEDSSSDEEEEQK
CCCCCCCCHHHHHHH
53.6621955146
285AcetylationQKKPMKNKPGPYSSV
HHCCCCCCCCCCCCC
45.9226051181
285UbiquitinationQKKPMKNKPGPYSSV
HHCCCCCCCCCCCCC
45.92-
289PhosphorylationMKNKPGPYSSVPPPS
CCCCCCCCCCCCCCC
21.3516997485
290PhosphorylationKNKPGPYSSVPPPSA
CCCCCCCCCCCCCCC
28.1716997485
291PhosphorylationNKPGPYSSVPPPSAP
CCCCCCCCCCCCCCC
32.5728796482
296PhosphorylationYSSVPPPSAPPPKKS
CCCCCCCCCCCCCCC
60.2128555341
299 (in isoform 2)Phosphorylation-53.7327642862
301AcetylationPPSAPPPKKSLGTQP
CCCCCCCCCCCCCCC
61.8526051181
303PhosphorylationSAPPPKKSLGTQPPK
CCCCCCCCCCCCCCH
37.8525159151
306PhosphorylationPPKKSLGTQPPKKAV
CCCCCCCCCCCHHHH
43.1029396449
306 (in isoform 2)Phosphorylation-43.1027642862
321PhosphorylationEKQQPVESSEDSSDE
HCCCCCCCCCCCCCC
38.9829888752
322PhosphorylationKQQPVESSEDSSDES
CCCCCCCCCCCCCCC
31.7324505115
325PhosphorylationPVESSEDSSDESDSS
CCCCCCCCCCCCCCC
35.3229888752
326PhosphorylationVESSEDSSDESDSSS
CCCCCCCCCCCCCCC
58.6929888752
329PhosphorylationSEDSSDESDSSSEEE
CCCCCCCCCCCCHHH
48.0227174698
331PhosphorylationDSSDESDSSSEEEKK
CCCCCCCCCCHHHHC
45.0724505115
332PhosphorylationSSDESDSSSEEEKKP
CCCCCCCCCHHHHCC
46.9221712546
333PhosphorylationSDESDSSSEEEKKPP
CCCCCCCCHHHHCCC
53.6426657352
341PhosphorylationEEEKKPPTKAVVSKA
HHHHCCCCCHHHCCC
39.9127174698
342SumoylationEEKKPPTKAVVSKAT
HHHCCCCCHHHCCCC
44.9828112733
347AcetylationPTKAVVSKATTKPPP
CCCHHHCCCCCCCCC
37.8425953088
347SumoylationPTKAVVSKATTKPPP
CCCHHHCCCCCCCCC
37.8428112733
349PhosphorylationKAVVSKATTKPPPAK
CHHHCCCCCCCCCCH
38.8028348404
351AcetylationVVSKATTKPPPAKKA
HHCCCCCCCCCCHHH
51.6925953088
356AcetylationTTKPPPAKKAAESSS
CCCCCCCHHHHHCCC
49.0330584347
361PhosphorylationPAKKAAESSSDSSDS
CCHHHHHCCCCCCCC
30.3423663014
362PhosphorylationAKKAAESSSDSSDSD
CHHHHHCCCCCCCCC
29.6628355574
363PhosphorylationKKAAESSSDSSDSDS
HHHHHCCCCCCCCCC
51.2823927012
365PhosphorylationAAESSSDSSDSDSSE
HHHCCCCCCCCCCCC
37.6823927012
366PhosphorylationAESSSDSSDSDSSED
HHCCCCCCCCCCCCC
46.2323927012
368PhosphorylationSSSDSSDSDSSEDDE
CCCCCCCCCCCCCCC
41.1423663014
370PhosphorylationSDSSDSDSSEDDEAP
CCCCCCCCCCCCCCC
39.3123663014
371PhosphorylationDSSDSDSSEDDEAPS
CCCCCCCCCCCCCCC
50.4626657352
378PhosphorylationSEDDEAPSKPAGTTK
CCCCCCCCCCCCCCC
59.3223663014
383PhosphorylationAPSKPAGTTKNSSNK
CCCCCCCCCCCCCCC
36.3823663014
384PhosphorylationPSKPAGTTKNSSNKP
CCCCCCCCCCCCCCC
27.5823663014
387PhosphorylationPAGTTKNSSNKPAVT
CCCCCCCCCCCCCEE
36.5224732914
388PhosphorylationAGTTKNSSNKPAVTT
CCCCCCCCCCCCEEC
59.2624732914
390AcetylationTTKNSSNKPAVTTKS
CCCCCCCCCCEECCC
35.9823749302
390SumoylationTTKNSSNKPAVTTKS
CCCCCCCCCCEECCC
35.9828112733
394PhosphorylationSSNKPAVTTKSPAVK
CCCCCCEECCCCCCC
30.5224732914
395PhosphorylationSNKPAVTTKSPAVKP
CCCCCEECCCCCCCC
23.9520201521
396AcetylationNKPAVTTKSPAVKPA
CCCCEECCCCCCCCC
45.1125953088
396SumoylationNKPAVTTKSPAVKPA
CCCCEECCCCCCCCC
45.1128112733
397PhosphorylationKPAVTTKSPAVKPAA
CCCEECCCCCCCCCC
18.9229255136
397 (in isoform 2)Phosphorylation-18.9221406692
401AcetylationTTKSPAVKPAAAPKQ
ECCCCCCCCCCCCCC
30.9223749302
401SumoylationTTKSPAVKPAAAPKQ
ECCCCCCCCCCCCCC
30.9228112733
407AcetylationVKPAAAPKQPVGGGQ
CCCCCCCCCCCCCCC
63.6126051181
407SumoylationVKPAAAPKQPVGGGQ
CCCCCCCCCCCCCCC
63.6128112733
407 (in isoform 2)Phosphorylation-63.6121406692
415AcetylationQPVGGGQKLLTRKAD
CCCCCCCEEEEEECC
49.0619608861
415SumoylationQPVGGGQKLLTRKAD
CCCCCCCEEEEEECC
49.0625114211
416AcetylationPVGGGQKLLTRKADS
CCCCCCEEEEEECCC
4.5419608861
423PhosphorylationLLTRKADSSSSEEES
EEEEECCCCCCCCCC
36.6623401153
424PhosphorylationLTRKADSSSSEEESS
EEEECCCCCCCCCCC
38.1323401153
425PhosphorylationTRKADSSSSEEESSS
EEECCCCCCCCCCCC
45.8023401153
426PhosphorylationRKADSSSSEEESSSS
EECCCCCCCCCCCCC
51.4823401153
430PhosphorylationSSSSEEESSSSEEEK
CCCCCCCCCCCHHHH
38.5123401153
431PhosphorylationSSSEEESSSSEEEKT
CCCCCCCCCCHHHHH
40.9623401153
432PhosphorylationSSEEESSSSEEEKTK
CCCCCCCCCHHHHHH
51.5620873877
433PhosphorylationSEEESSSSEEEKTKK
CCCCCCCCHHHHHHH
51.4821815630
438PhosphorylationSSSEEEKTKKMVATT
CCCHHHHHHHHHHCC
38.8929888752
440SumoylationSEEEKTKKMVATTKP
CHHHHHHHHHHCCCC
43.7828112733
446AcetylationKKMVATTKPKATAKA
HHHHHCCCCHHHHHH
39.9223749302
452AcetylationTKPKATAKAALSLPA
CCCHHHHHHHHCCCH
29.8225953088
452SumoylationTKPKATAKAALSLPA
CCCHHHHHHHHCCCH
29.8228112733
456PhosphorylationATAKAALSLPAKQAP
HHHHHHHCCCHHHCC
27.8125159151
466PhosphorylationAKQAPQGSRDSSSDS
HHHCCCCCCCCCCCC
27.8928192239
469PhosphorylationAPQGSRDSSSDSDSS
CCCCCCCCCCCCCCC
30.5420873877
470PhosphorylationPQGSRDSSSDSDSSS
CCCCCCCCCCCCCCC
42.3120873877
471PhosphorylationQGSRDSSSDSDSSSS
CCCCCCCCCCCCCCC
45.1223312004
473PhosphorylationSRDSSSDSDSSSSEE
CCCCCCCCCCCCCHH
41.1420873877
475PhosphorylationDSSSDSDSSSSEEEE
CCCCCCCCCCCHHHH
35.7520873877
476PhosphorylationSSSDSDSSSSEEEEE
CCCCCCCCCCHHHHH
42.7620873877
477PhosphorylationSSDSDSSSSEEEEEK
CCCCCCCCCHHHHHH
45.8020873877
478PhosphorylationSDSDSSSSEEEEEKT
CCCCCCCCHHHHHHH
51.4824275569
485PhosphorylationSEEEEEKTSKSAVKK
CHHHHHHHCHHHHHH
44.6723312004
486PhosphorylationEEEEEKTSKSAVKKK
HHHHHHHCHHHHHHC
35.3623312004
504PhosphorylationVAGGAAPSKPASAKK
CCCCCCCCCCCCCCC
46.6930266825
505AcetylationAGGAAPSKPASAKKG
CCCCCCCCCCCCCCC
43.4723749302
505SumoylationAGGAAPSKPASAKKG
CCCCCCCCCCCCCCC
43.4728112733
508PhosphorylationAAPSKPASAKKGKAE
CCCCCCCCCCCCCCC
49.5029255136
510AcetylationPSKPASAKKGKAESS
CCCCCCCCCCCCCCC
60.6123749302
511AcetylationSKPASAKKGKAESSN
CCCCCCCCCCCCCCC
66.427338259
514 (in isoform 2)Phosphorylation-30.4921406692
516PhosphorylationAKKGKAESSNSSSSD
CCCCCCCCCCCCCCC
39.4128192239
517PhosphorylationKKGKAESSNSSSSDD
CCCCCCCCCCCCCCC
32.0330108239
518 (in isoform 2)Phosphorylation-56.0121406692
519PhosphorylationGKAESSNSSSSDDSS
CCCCCCCCCCCCCCC
33.2830108239
520PhosphorylationKAESSNSSSSDDSSE
CCCCCCCCCCCCCCH
37.8030108239
521PhosphorylationAESSNSSSSDDSSEE
CCCCCCCCCCCCCHH
37.2930108239
522PhosphorylationESSNSSSSDDSSEEE
CCCCCCCCCCCCHHH
47.5930108239
525PhosphorylationNSSSSDDSSEEEEEK
CCCCCCCCCHHHHHH
44.6430108239
526PhosphorylationSSSSDDSSEEEEEKL
CCCCCCCCHHHHHHH
56.9026657352
538PhosphorylationEKLKGKGSPRPQAPK
HHHCCCCCCCCCCCC
22.6320201521
548 (in isoform 2)Phosphorylation-26.3821406692
549PhosphorylationQAPKANGTSALTAQN
CCCCCCCCCCCHHCC
15.6126074081
550PhosphorylationAPKANGTSALTAQNG
CCCCCCCCCCHHCCC
23.7626074081
553PhosphorylationANGTSALTAQNGKAA
CCCCCCCHHCCCCCC
26.3926074081
558AcetylationALTAQNGKAAKNSEE
CCHHCCCCCCCCCHH
53.3625953088
563PhosphorylationNGKAAKNSEEEEEEK
CCCCCCCCHHHHHHH
45.7529255136
572SumoylationEEEEEKKKAAVVVSK
HHHHHHHHHEEEECC
53.2825114211
573 (in isoform 2)Phosphorylation-17.8621406692
578PhosphorylationKKAAVVVSKSGSLKK
HHHEEEECCCCHHHH
14.9721712546
579AcetylationKAAVVVSKSGSLKKR
HHEEEECCCCHHHHH
47.4225953088
579SumoylationKAAVVVSKSGSLKKR
HHEEEECCCCHHHHH
47.4228112733
580PhosphorylationAAVVVSKSGSLKKRK
HEEEECCCCHHHHHH
26.5526055452
582PhosphorylationVVVSKSGSLKKRKQN
EEECCCCHHHHHHHH
44.0726055452
593AcetylationRKQNEAAKEAETPQA
HHHHHHHHHCCCHHH
65.5926051181
597PhosphorylationEAAKEAETPQAKKIK
HHHHHCCCHHHHHCC
27.9628176443
601AcetylationEAETPQAKKIKLQTP
HCCCHHHHHCCCCCC
50.1923749302
602AcetylationAETPQAKKIKLQTPN
CCCHHHHHCCCCCCC
48.3525953088
604SumoylationTPQAKKIKLQTPNTF
CHHHHHCCCCCCCCC
43.34-
604AcetylationTPQAKKIKLQTPNTF
CHHHHHCCCCCCCCC
43.3425953088
604SumoylationTPQAKKIKLQTPNTF
CHHHHHCCCCCCCCC
43.3428112733
607PhosphorylationAKKIKLQTPNTFPKR
HHHCCCCCCCCCCCC
29.0122167270
610PhosphorylationIKLQTPNTFPKRKKG
CCCCCCCCCCCCCCC
42.3819664994
613SumoylationQTPNTFPKRKKGEKR
CCCCCCCCCCCCCCC
73.0628112733
617 (in isoform 2)Phosphorylation-49.0121406692
620 (in isoform 2)Phosphorylation-35.0921406692
622PhosphorylationKKGEKRASSPFRRVR
CCCCCCCCCCCCHHH
42.4422167270
623PhosphorylationKGEKRASSPFRRVRE
CCCCCCCCCCCHHHH
27.3712167624
632 (in isoform 2)Phosphorylation-39.4321406692
633 (in isoform 2)Phosphorylation-7.6621406692
637PhosphorylationEEEIEVDSRVADNSF
HHHCEECCHHHCCCC
33.5525159151
638MethylationEEIEVDSRVADNSFD
HHCEECCHHHCCCCC
24.15115485317
643PhosphorylationDSRVADNSFDAKRGA
CCHHHCCCCCHHCCC
25.6729255136
647AcetylationADNSFDAKRGAAGDW
HCCCCCHHCCCCCCH
53.8923749302
647SumoylationADNSFDAKRGAAGDW
HCCCCCHHCCCCCCH
53.8928112733
647UbiquitinationADNSFDAKRGAAGDW
HCCCCCHHCCCCCCH
53.892190698
647 (in isoform 1)Ubiquitination-53.8921890473
648MethylationDNSFDAKRGAAGDWG
CCCCCHHCCCCCCHH
41.52115485309
648 (in isoform 3)Ubiquitination-41.5221890473
653 (in isoform 2)Phosphorylation-45.5421406692
657 (in isoform 2)Ubiquitination-34.5921890473
663SumoylationERANQVLKFTKGKSF
HHHHHHHHHHCCCCC
52.73-
663AcetylationERANQVLKFTKGKSF
HHHHHHHHHHCCCCC
52.7319608861
663MethylationERANQVLKFTKGKSF
HHHHHHHHHHCCCCC
52.7322638443
663SumoylationERANQVLKFTKGKSF
HHHHHHHHHHCCCCC
52.7328112733
663UbiquitinationERANQVLKFTKGKSF
HHHHHHHHHHCCCCC
52.73-
664AcetylationRANQVLKFTKGKSFR
HHHHHHHHHCCCCCC
8.1519608861
665PhosphorylationANQVLKFTKGKSFRH
HHHHHHHHCCCCCCC
36.9830576142
669PhosphorylationLKFTKGKSFRHEKTK
HHHHCCCCCCCCCCC
35.8626074081
675PhosphorylationKSFRHEKTKKKRGSY
CCCCCCCCCCCCCCC
45.15-
681PhosphorylationKTKKKRGSYRGGSIS
CCCCCCCCCCCCCEE
18.7125159151
682PhosphorylationTKKKRGSYRGGSISV
CCCCCCCCCCCCEEE
18.9921712546
683MethylationKKKRGSYRGGSISVQ
CCCCCCCCCCCEEEE
44.7024129315
686PhosphorylationRGSYRGGSISVQVNS
CCCCCCCCEEEEEEE
17.9523401153
688PhosphorylationSYRGGSISVQVNSIK
CCCCCCEEEEEEEEE
14.2723927012
693PhosphorylationSISVQVNSIKFDSE-
CEEEEEEEEEECCC-
28.4422167270
695SumoylationSVQVNSIKFDSE---
EEEEEEEEECCC---
42.8328112733
696 (in isoform 2)Phosphorylation-13.7321406692
698PhosphorylationVNSIKFDSE------
EEEEEECCC------
48.6222167270
698 (in isoform 2)Phosphorylation-48.6221406692
708 (in isoform 2)Phosphorylation-21406692

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
607TPhosphorylationKinaseCDK1P06493
PSP
610TPhosphorylationKinaseCDK1P06493
PSP
623SPhosphorylationKinasePKA-FAMILY-GPS
623SPhosphorylationKinasePKA_GROUP-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NOLC1_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 NOLC1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COIL_HUMANCOILphysical
9679133
RPA1_HUMANPOLR1Aphysical
10567578
CEBPB_HUMANCEBPBphysical
9553145
A4_HUMANAPPphysical
21832049
RS14_HUMANRPS14physical
22939629
NOP56_HUMANNOP56physical
22939629
RL1D1_HUMANRSL1D1physical
22939629
RL15_HUMANRPL15physical
22939629
RL23A_HUMANRPL23Aphysical
22939629
RL18A_HUMANRPL18Aphysical
22939629
RL19_HUMANRPL19physical
22939629
RL6_HUMANRPL6physical
22939629
RL11_HUMANRPL11physical
22939629
NOP58_HUMANNOP58physical
22939629
RS6_HUMANRPS6physical
22939629
RS23_HUMANRPS23physical
22939629
RL5_HUMANRPL5physical
22939629
RL4_HUMANRPL4physical
22939629
RS4X_HUMANRPS4Xphysical
22939629
RRP7A_HUMANRRP7Aphysical
22939629
UT14A_HUMANUTP14Aphysical
22939629
CAVN1_HUMANPTRFphysical
22939629
RED_HUMANIKphysical
22939629
NOP16_HUMANNOP16physical
22939629
RAI3_HUMANGPRC5Aphysical
22939629
RRS1_HUMANRRS1physical
22939629
SAP18_HUMANSAP18physical
22939629
TF3C1_HUMANGTF3C1physical
22939629
BRX1_HUMANBRIX1physical
26344197
SSRP1_HUMANSSRP1physical
26344197
WDR36_HUMANWDR36physical
26344197
TCOF_HUMANTCOF1physical
26399832
KBTB8_HUMANKBTBD8physical
26399832
ARRB1_HUMANARRB1physical
26399832
ARRB2_HUMANARRB2physical
26399832
RPA1_HUMANPOLR1Aphysical
26399832
RPA2_HUMANPOLR1Bphysical
26399832
DKC1_HUMANDKC1physical
26399832
NHP2_HUMANNHP2physical
26399832
NOP58_HUMANNOP58physical
26399832
NOP56_HUMANNOP56physical
26399832
CSK21_HUMANCSNK2A1physical
26399832
GT2D1_HUMANGTF2IRD1physical
28514442
RPA43_HUMANTWISTNBphysical
28514442
HXB9_HUMANHOXB9physical
28514442
AP3B1_HUMANAP3B1physical
27173435
EAF1_HUMANEAF1physical
27173435
DPOD1_HUMANPOLD1physical
27173435
CC154_HUMANCCDC154physical
27173435
MFAP1_HUMANMFAP1physical
27173435

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 NOLC1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33; LYS-415 AND LYS-663, ANDMASS SPECTROMETRY.
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 THR-607; THR-610; SER-643AND SER-698, 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 THR-188; THR-607; THR-610;SER-623 AND SER-698, 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-563, 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-83; SER-85; SER-87;SER-90; SER-91; SER-366; SER-397; SER-508; SER-580; SER-582; THR-607;THR-610; SER-622; SER-623; SER-643; SER-686 AND SER-698, 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 SER-698, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397; SER-508; SER-538AND SER-643, AND MASS 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-538, 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-698, 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-397; SER-508; SER-538;THR-607; THR-610 AND SER-643, AND MASS SPECTROMETRY.
"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-607; THR-610; SER-643AND SER-698, 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-83; SER-84; SER-85;SER-87; SER-90; SER-91; SER-538; SER-563; THR-607; THR-610 ANDSER-698, 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-698, AND MASSSPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-607 AND THR-610, ANDMASS SPECTROMETRY.

TOP