NVL_HUMAN - dbPTM
NVL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NVL_HUMAN
UniProt AC O15381
Protein Name Nuclear valosin-containing protein-like
Gene Name NVL
Organism Homo sapiens (Human).
Sequence Length 856
Subcellular Localization Isoform 2: Nucleus, nucleoplasm .
Isoform 1: Nucleus, nucleolus . Nucleus, nucleoplasm . Expressed predominantly in the nucleolus. Associates with pre-ribosomal particles in the nucleus.
Protein Description Participates in the assembly of the telomerase holoenzyme and effecting of telomerase activity via its interaction with TERT. [PubMed: 22226966 May play a role in 60S ribosomal subunit biogenesis]
Protein Sequence MKPRPAGFVDNKLKQRVIQYLTSNKCGKYVDIGVLASDLQRVYSIDYGRRKRNAFRIQVEKVFSIISSEKELKNLTELEDEHLAKRARQGEEDNEYTESYSDDDSSMEDYPDPQSANHMNSSLLSLYRKGNPDSVSNTPEMEQRETTSSTPRISSKTGSIPLKTPAKDSEGGWFIDKTPSVKKDSFFLDLSCEKSNPKKPITEIQDSKDSSLLESDMKRKGKLKNKGSKRKKEDLQEVDGEIEAVLQKKAKARGLEFQISNVKFEDVGGNDMTLKEVCKMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMCAVNRVLMKLQEQQKKNPEMEDLPSKGVQEERLGTEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALSSVQPSAKREGFVTVPNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRLAILKTITKNGTKPPLDADVNLEAIAGDLRCDCYTGADLSALVREASICALRQEMARQKSGNEKGELKVSHKHFEEAFKKVRSSISKKDQIMYERLQESLSR
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
1Sulfoxidation-------MKPRPAGF
-------CCCCCCCC		14.0531801345
12UbiquitinationPAGFVDNKLKQRVIQ
CCCCCCHHHHHHHHH		53.23-
15 (in isoform 2)Phosphorylation-56.14-
20PhosphorylationLKQRVIQYLTSNKCG
HHHHHHHHHHCCCCC		10.7920068231
22PhosphorylationQRVIQYLTSNKCGKY
HHHHHHHHCCCCCCE		25.8920068231
23PhosphorylationRVIQYLTSNKCGKYV
HHHHHHHCCCCCCEE		31.5320068231
25UbiquitinationIQYLTSNKCGKYVDI
HHHHHCCCCCCEEEE		44.10-
28AcetylationLTSNKCGKYVDIGVL
HHCCCCCCEEEEEEH		52.1226051181
28 (in isoform 2)Phosphorylation-52.12-
29PhosphorylationTSNKCGKYVDIGVLA
HCCCCCCEEEEEEHH		6.6622817900
32 (in isoform 2)Phosphorylation-2.68-
37PhosphorylationVDIGVLASDLQRVYS
EEEEEHHHHHHHHHH		34.3924719451
43PhosphorylationASDLQRVYSIDYGRR
HHHHHHHHHCCCCCC		11.3322817900
44PhosphorylationSDLQRVYSIDYGRRK
HHHHHHHHCCCCCCC		13.2121815630
47PhosphorylationQRVYSIDYGRRKRNA
HHHHHCCCCCCCCCE		15.7422817900
53 (in isoform 2)Phosphorylation-46.60-
64PhosphorylationIQVEKVFSIISSEKE
HHHHHHHHHHCCHHH		23.2329523821
67PhosphorylationEKVFSIISSEKELKN
HHHHHHHCCHHHHCC		30.6724505115
68PhosphorylationKVFSIISSEKELKNL
HHHHHHCCHHHHCCC		42.1329523821
70AcetylationFSIISSEKELKNLTE
HHHHCCHHHHCCCHH		71.0023749302
70UbiquitinationFSIISSEKELKNLTE
HHHHCCHHHHCCCHH		71.00-
73UbiquitinationISSEKELKNLTELED
HCCHHHHCCCHHHCH		51.51-
76PhosphorylationEKELKNLTELEDEHL
HHHHCCCHHHCHHHH		48.1728555341
79 (in isoform 2)Phosphorylation-55.94-
85AcetylationLEDEHLAKRARQGEE
HCHHHHHHHHHCCCC		53.6125953088
85UbiquitinationLEDEHLAKRARQGEE
HCHHHHHHHHHCCCC		53.61-
85 (in isoform 2)Phosphorylation-53.61-
89 (in isoform 2)Phosphorylation-63.77-
101PhosphorylationNEYTESYSDDDSSME
CCCCCCCCCCCCCCC		43.7919691289
101 (in isoform 2)Phosphorylation-43.79-
104 (in isoform 2)Phosphorylation-47.83-
105PhosphorylationESYSDDDSSMEDYPD
CCCCCCCCCCCCCCC		38.2819691289
105 (in isoform 2)Phosphorylation-38.28-
109 (in isoform 2)Phosphorylation-52.18-
110PhosphorylationDDSSMEDYPDPQSAN
CCCCCCCCCCHHHHC		9.0226307563
115PhosphorylationEDYPDPQSANHMNSS
CCCCCHHHHCCCCHH		36.1026307563
121PhosphorylationQSANHMNSSLLSLYR
HHHCCCCHHHHHHHH		18.1320068231
122PhosphorylationSANHMNSSLLSLYRK
HHCCCCHHHHHHHHH		28.4626307563
125PhosphorylationHMNSSLLSLYRKGNP
CCCHHHHHHHHHCCC		28.7526307563
127PhosphorylationNSSLLSLYRKGNPDS
CHHHHHHHHHCCCCC		13.6026307563
129AcetylationSLLSLYRKGNPDSVS
HHHHHHHHCCCCCCC		49.8619815419
129UbiquitinationSLLSLYRKGNPDSVS
HHHHHHHHCCCCCCC		49.86-
134PhosphorylationYRKGNPDSVSNTPEM
HHHCCCCCCCCCCHH		28.8025159151
136PhosphorylationKGNPDSVSNTPEMEQ
HCCCCCCCCCCHHHH		38.6521712546
138PhosphorylationNPDSVSNTPEMEQRE
CCCCCCCCCHHHHHH		17.0825159151
141SulfoxidationSVSNTPEMEQRETTS
CCCCCCHHHHHHCCC		5.8321406390
147PhosphorylationEMEQRETTSSTPRIS
HHHHHHCCCCCCCCC		18.87-
149PhosphorylationEQRETTSSTPRISSK
HHHHCCCCCCCCCCC		40.1025159151
150PhosphorylationQRETTSSTPRISSKT
HHHCCCCCCCCCCCC		19.1625159151
156AcetylationSTPRISSKTGSIPLK
CCCCCCCCCCCCCCC		50.5525953088
156UbiquitinationSTPRISSKTGSIPLK
CCCCCCCCCCCCCCC		50.55-
157PhosphorylationTPRISSKTGSIPLKT
CCCCCCCCCCCCCCC		37.8029396449
159PhosphorylationRISSKTGSIPLKTPA
CCCCCCCCCCCCCCC		26.6821815630
163UbiquitinationKTGSIPLKTPAKDSE
CCCCCCCCCCCCCCC		47.29-
164PhosphorylationTGSIPLKTPAKDSEG
CCCCCCCCCCCCCCC		35.8425159151
167AcetylationIPLKTPAKDSEGGWF
CCCCCCCCCCCCCEE		64.0926051181
167UbiquitinationIPLKTPAKDSEGGWF
CCCCCCCCCCCCCEE		64.09-
177AcetylationEGGWFIDKTPSVKKD
CCCEEECCCCCCCCC		58.4826051181
177UbiquitinationEGGWFIDKTPSVKKD
CCCEEECCCCCCCCC		58.48-
178PhosphorylationGGWFIDKTPSVKKDS
CCEEECCCCCCCCCC		19.6325159151
180PhosphorylationWFIDKTPSVKKDSFF
EEECCCCCCCCCCEE		52.3725159151
185PhosphorylationTPSVKKDSFFLDLSC
CCCCCCCCEEEEEEC		27.1225159151
191PhosphorylationDSFFLDLSCEKSNPK
CCEEEEEECCCCCCC		21.6425159151
192GlutathionylationSFFLDLSCEKSNPKK
CEEEEEECCCCCCCC		11.2522555962
194UbiquitinationFLDLSCEKSNPKKPI
EEEEECCCCCCCCCC		60.92-
195PhosphorylationLDLSCEKSNPKKPIT
EEEECCCCCCCCCCC		35.7520068231
199UbiquitinationCEKSNPKKPITEIQD
CCCCCCCCCCCCCCC		42.80-
202PhosphorylationSNPKKPITEIQDSKD
CCCCCCCCCCCCCCC		35.2530108239
207PhosphorylationPITEIQDSKDSSLLE
CCCCCCCCCCCCHHH		23.2225159151
208SumoylationITEIQDSKDSSLLES
CCCCCCCCCCCHHHH		70.67-
208SumoylationITEIQDSKDSSLLES
CCCCCCCCCCCHHHH		70.6728112733
210PhosphorylationEIQDSKDSSLLESDM
CCCCCCCCCHHHHHH		26.9925159151
211PhosphorylationIQDSKDSSLLESDMK
CCCCCCCCHHHHHHH		47.2925159151
215PhosphorylationKDSSLLESDMKRKGK
CCCCHHHHHHHHHCC		42.8726166824
249 (in isoform 2)Phosphorylation-42.00-
275AcetylationGGNDMTLKEVCKMLI
CCCCCCHHHHHHHHH		38.6526051181
290PhosphorylationHMRHPEVYHHLGVVP
HHCCHHHHHCCCCCC		5.05-
336PhosphorylationVAAPEIVSGVSGESE
HCCCHHHHCCCCCCH		38.8620860994
345UbiquitinationVSGESEQKLRELFEQ
CCCCCHHHHHHHHHH		45.52-
355PhosphorylationELFEQAVSNAPCIIF
HHHHHHHHCCCEEEE		30.2320058876
370PhosphorylationIDEIDAITPKREVAS
EEECCCCCCCHHHCC		25.2024719451
410PhosphorylationRVLVIGATNRPDSLD
EEEEEECCCCCCCCC		26.9220068231
492UbiquitinationAVNRVLMKLQEQQKK
HHHHHHHHHHHHHHH		42.74-
498AcetylationMKLQEQQKKNPEMED
HHHHHHHHHCCCHHH		54.9622361351
499UbiquitinationKLQEQQKKNPEMEDL
HHHHHHHHCCCHHHC		73.69-
508PhosphorylationPEMEDLPSKGVQEER
CCHHHCCCCCCCHHH		49.7124719451
509AcetylationEMEDLPSKGVQEERL
CHHHCCCCCCCHHHH		62.2526051181
509UbiquitinationEMEDLPSKGVQEERL
CHHHCCCCCCCHHHH		62.25-
562 (in isoform 3)Ubiquitination-26.1421890473
570UbiquitinationVQPSAKREGFVTVPN
CCCCCCCCCCEECCC		57.1721890473
626GlutathionylationLLAGPPGCGKTLLAK
EEECCCCCCHHHHHH		6.6122555962
628AcetylationAGPPGCGKTLLAKAV
ECCCCCCHHHHHHHH		39.8226051181
629PhosphorylationGPPGCGKTLLAKAVA
CCCCCCHHHHHHHHH		16.5822817900
633UbiquitinationCGKTLLAKAVANESG
CCHHHHHHHHHCCCC		43.28-
653 (in isoform 2)Ubiquitination-32.1521890473
655PhosphorylationGPELLNMYVGESERA
CHHHHHHHHCCHHHH		12.2920068231
668UbiquitinationRAVRQVFQRAKNSAP
HHHHHHHHHHHHCCC		45.6321890473
671UbiquitinationRQVFQRAKNSAPCVI
HHHHHHHHHCCCEEE		54.33-
695 (in isoform 2)Phosphorylation-38.65-
759UbiquitinationADRLAILKTITKNGT
HHHHHHHHHHHCCCC		31.5921890473
759 (in isoform 1)Ubiquitination-31.5921890473
794PhosphorylationCYTGADLSALVREAS
CCCCCCHHHHHHHHH		21.8020068231
801PhosphorylationSALVREASICALRQE
HHHHHHHHHHHHHHH		17.2820068231
814PhosphorylationQEMARQKSGNEKGEL
HHHHHHHCCCCCCCC		38.2121406692
826UbiquitinationGELKVSHKHFEEAFK
CCCCCCHHHHHHHHH		42.35-
833AcetylationKHFEEAFKKVRSSIS
HHHHHHHHHHHHHCC		58.3626051181
837PhosphorylationEAFKKVRSSISKKDQ
HHHHHHHHHCCHHHH		34.7026699800
838PhosphorylationAFKKVRSSISKKDQI
HHHHHHHHCCHHHHH		21.9526699800
840PhosphorylationKKVRSSISKKDQIMY
HHHHHHCCHHHHHHH		35.2821406692
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 NVL_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NVL_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 NVL_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DPYL1_HUMANCRMP1physical
16169070
UBC9_HUMANUBE2Iphysical
21516116
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 NVL_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-134; THR-138; SER-185AND SER-191, AND MASS SPECTROMETRY.
"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-134; THR-138; SER-159;SER-207 AND SER-211, AND MASS SPECTROMETRY.

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