NOP14_HUMAN - dbPTM
NOP14_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NOP14_HUMAN
UniProt AC P78316
Protein Name Nucleolar protein 14
Gene Name NOP14
Organism Homo sapiens (Human).
Sequence Length 857
Subcellular Localization Nucleus, nucleolus.
Protein Description Involved in nucleolar processing of pre-18S ribosomal RNA. Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm (By similarity)..
Protein Sequence MAKAKKVGARRKASGAPAGARGGPAKANSNPFEVKVNRQKFQILGRKTRHDVGLPGVSRARALRKRTQTLLKEYKERDKSNVFRDKRFGEYNSNMSPEEKMMKRFALEQQRHHEKKSIYNLNEDEELTHYGQSLADIEKHNDIVDSDSDAEDRGTLSAELTAAHFGGGGGLLHKKTQQEGEEREKPKSRKELIEELIAKSKQEKRERQAQREDALELTEKLDQDWKEIQTLLSHKTPKSENRDKKEKPKPDAYDMMVRELGFEMKAQPSNRMKTEAELAKEEQEHLRKLEAERLRRMLGKDEDENVKKPKHMSADDLNDGFVLDKDDRRLLSYKDGKMNVEEDVQEEQSKEASDPESNEEEGDSSGGEDTEESDSPDSHLDLESNVESEEENEKPAKEQRQTPGKGLISGKERAGKATRDELPYTFAAPESYEELRSLLLGRSMEEQLLVVERIQKCNHPSLAEGNKAKLEKLFGFLLEYVGDLATDDPPDLTVIDKLVVHLYHLCQMFPESASDAIKFVLRDAMHEMEEMIETKGRAALPGLDVLIYLKITGLLFPTSDFWHPVVTPALVCLSQLLTKCPILSLQDVVKGLFVCCLFLEYVALSQRFIPELINFLLGILYIATPNKASQGSTLVHPFRALGKNSELLVVSAREDVATWQQSSLSLRWASRLRAPTSTEANHIRLSCLAVGLALLKRCVLMYGSLPSFHAIMGPLQALLTDHLADCSHPQELQELCQSTLTEMESQKQLCRPLTCEKSKPVPLKLFTPRLVKVLEFGRKQGSSKEEQERKRLIHKHKREFKGAVREIRKDNQFLARMQLSEIMERDAERKRKVKQLFNSLATQEGEWKALKRKKFKK
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
6Methylation--MAKAKKVGARRKA
--CCCCCCCCCCHHC		51.24116252527
12MethylationKKVGARRKASGAPAG
CCCCCCHHCCCCCCC		41.157395423
12AcetylationKKVGARRKASGAPAG
CCCCCCHHCCCCCCC		41.157395423
14PhosphorylationVGARRKASGAPAGAR
CCCCHHCCCCCCCCC		38.22-
21MethylationSGAPAGARGGPAKAN
CCCCCCCCCCCCCCC		50.08115386023
26UbiquitinationGARGGPAKANSNPFE
CCCCCCCCCCCCCCE		51.7621906983
26 (in isoform 1)Ubiquitination-51.7621890473
26 (in isoform 2)Ubiquitination-51.7621906983
26AcetylationGARGGPAKANSNPFE
CCCCCCCCCCCCCCE		51.7625953088
29PhosphorylationGGPAKANSNPFEVKV
CCCCCCCCCCCEEEE		51.22-
35 (in isoform 1)Ubiquitination-26.9621890473
35 (in isoform 2)Ubiquitination-26.9621906983
35UbiquitinationNSNPFEVKVNRQKFQ
CCCCCEEEECHHHEE		26.9621906983
40AcetylationEVKVNRQKFQILGRK
EEEECHHHEEECCCC		35.6825953088
59MethylationVGLPGVSRARALRKR
CCCCCHHHHHHHHHH		26.20115485401
67PhosphorylationARALRKRTQTLLKEY
HHHHHHHHHHHHHHH		29.0126074081
69PhosphorylationALRKRTQTLLKEYKE
HHHHHHHHHHHHHHH		33.1826074081
74PhosphorylationTQTLLKEYKERDKSN
HHHHHHHHHHHHCCC		19.30-
91PhosphorylationRDKRFGEYNSNMSPE
CCCCHHCCCCCCCHH		25.0324732914
93PhosphorylationKRFGEYNSNMSPEEK
CCHHCCCCCCCHHHH		32.7622167270
96PhosphorylationGEYNSNMSPEEKMMK
HCCCCCCCHHHHHHH		33.1522167270
116UbiquitinationQQRHHEKKSIYNLNE
HHHHHCCCCCCCCCC		38.82-
117PhosphorylationQRHHEKKSIYNLNED
HHHHCCCCCCCCCCC		41.1829978859
119PhosphorylationHHEKKSIYNLNEDEE
HHCCCCCCCCCCCHH		22.2327642862
128PhosphorylationLNEDEELTHYGQSLA
CCCCHHHHHHHHHHH		19.1424144214
130PhosphorylationEDEELTHYGQSLADI
CCHHHHHHHHHHHHH		16.1827642862
133PhosphorylationELTHYGQSLADIEKH
HHHHHHHHHHHHHHH		22.5924144214
146PhosphorylationKHNDIVDSDSDAEDR
HHCCCCCCCCCHHHH		28.2829255136
148PhosphorylationNDIVDSDSDAEDRGT
CCCCCCCCCHHHHCC		42.5529255136
155PhosphorylationSDAEDRGTLSAELTA
CCHHHHCCCEEEEHH		20.5929255136
157PhosphorylationAEDRGTLSAELTAAH
HHHHCCCEEEEHHHH		21.3829255136
161PhosphorylationGTLSAELTAAHFGGG
CCCEEEEHHHHHCCC		17.1922115753
226 (in isoform 2)Ubiquitination-53.9121906983
226 (in isoform 1)Ubiquitination-53.9121890473
226UbiquitinationEKLDQDWKEIQTLLS
HHHHHHHHHHHHHHH		53.9121906983
230PhosphorylationQDWKEIQTLLSHKTP
HHHHHHHHHHHCCCC		35.0129978859
233PhosphorylationKEIQTLLSHKTPKSE
HHHHHHHHCCCCCCC		26.5020873877
235AcetylationIQTLLSHKTPKSENR
HHHHHHCCCCCCCCC		64.2525953088
236PhosphorylationQTLLSHKTPKSENRD
HHHHHCCCCCCCCCC		30.4426055452
239PhosphorylationLSHKTPKSENRDKKE
HHCCCCCCCCCCCCC		41.1120873877
245UbiquitinationKSENRDKKEKPKPDA
CCCCCCCCCCCCCCH		75.2221906983
247AcetylationENRDKKEKPKPDAYD
CCCCCCCCCCCCHHH		68.1925953088
249UbiquitinationRDKKEKPKPDAYDMM
CCCCCCCCCCHHHHH		67.6021906983
253PhosphorylationEKPKPDAYDMMVREL
CCCCCCHHHHHHHHH		16.26-
265SumoylationRELGFEMKAQPSNRM
HHHCCCCCCCCCCHH		36.35-
265UbiquitinationRELGFEMKAQPSNRM
HHHCCCCCCCCCCHH		36.35-
265SumoylationRELGFEMKAQPSNRM
HHHCCCCCCCCCCHH		36.35-
269O-linked_GlycosylationFEMKAQPSNRMKTEA
CCCCCCCCCHHHHHH		25.6130379171
273SumoylationAQPSNRMKTEAELAK
CCCCCHHHHHHHHHH		39.72-
273SumoylationAQPSNRMKTEAELAK
CCCCCHHHHHHHHHH		39.72-
280AcetylationKTEAELAKEEQEHLR
HHHHHHHHHHHHHHH		74.5326051181
308 (in isoform 2)Ubiquitination-55.82-
310 (in isoform 2)Ubiquitination-61.90-
313PhosphorylationVKKPKHMSADDLNDG
CCCCCCCCHHHCCCC		28.4120873877
325AcetylationNDGFVLDKDDRRLLS
CCCEEECCCCCEEEH		58.3226051181
332PhosphorylationKDDRRLLSYKDGKMN
CCCCEEEHHHCCCCC		34.4322210691
333PhosphorylationDDRRLLSYKDGKMNV
CCCEEEHHHCCCCCH		17.05-
334AcetylationDRRLLSYKDGKMNVE
CCEEEHHHCCCCCHH		57.5425953088
349PhosphorylationEDVQEEQSKEASDPE
HHHHHHHHHHHCCCC		35.4228355574
388PhosphorylationDLESNVESEEENEKP
CHHHCCCCHHHHCCC		46.1319007248
402PhosphorylationPAKEQRQTPGKGLIS
CHHHHHCCCCCCCCC		35.88-
411AcetylationGKGLISGKERAGKAT
CCCCCCCCHHCCCCC		36.9223749302
424PhosphorylationATRDELPYTFAAPES
CCCCCCCCCCCCCCC		27.4127642862
444SulfoxidationSLLLGRSMEEQLLVV
HHHCCCCHHHHHHHH		6.7321406390
456UbiquitinationLVVERIQKCNHPSLA
HHHHHHHHCCCHHHH		34.33-
456AcetylationLVVERIQKCNHPSLA
HHHHHHHHCCCHHHH		34.3325953088
503PhosphorylationDKLVVHLYHLCQMFP
HHHHHHHHHHHHHCC		4.2920068231
512PhosphorylationLCQMFPESASDAIKF
HHHHCCCCHHHHHHH		33.0520068231
514PhosphorylationQMFPESASDAIKFVL
HHCCCCHHHHHHHHH		36.5320068231
535 (in isoform 2)Ubiquitination-33.3421906983
5352-HydroxyisobutyrylationMEEMIETKGRAALPG
HHHHHHHHCCCCCCC		33.34-
535 (in isoform 1)Ubiquitination-33.3421890473
535UbiquitinationMEEMIETKGRAALPG
HHHHHHHHCCCCCCC		33.3421906983
643UbiquitinationHPFRALGKNSELLVV
CCCHHCCCCCEEEEE		59.14-
643AcetylationHPFRALGKNSELLVV
CCCHHCCCCCEEEEE		59.1423749302
663PhosphorylationVATWQQSSLSLRWAS
HHHHHHHHHHHHHHH		20.0317081983
665PhosphorylationTWQQSSLSLRWASRL
HHHHHHHHHHHHHHC		20.1717081983
670PhosphorylationSLSLRWASRLRAPTS
HHHHHHHHHCCCCCC		25.5326074081
676PhosphorylationASRLRAPTSTEANHI
HHHCCCCCCCCCCHH		47.5026074081
677PhosphorylationSRLRAPTSTEANHIR
HHCCCCCCCCCCHHH		24.1626074081
678PhosphorylationRLRAPTSTEANHIRL
HCCCCCCCCCCHHHH		41.4126074081
767PhosphorylationPVPLKLFTPRLVKVL
CCCHHHCCHHHHHHH		20.2427174698
772UbiquitinationLFTPRLVKVLEFGRK
HCCHHHHHHHHHHHH		45.7719608861
772AcetylationLFTPRLVKVLEFGRK
HCCHHHHHHHHHHHH		45.7719608861
783PhosphorylationFGRKQGSSKEEQERK
HHHHCCCCHHHHHHH		51.4128674151
809UbiquitinationGAVREIRKDNQFLAR
HHHHHHHHCCHHHHH		67.69-
820PhosphorylationFLARMQLSEIMERDA
HHHHHHHHHHHHHHH		14.2626074081
834UbiquitinationAERKRKVKQLFNSLA
HHHHHHHHHHHHHHH		44.3021890473
834 (in isoform 1)Ubiquitination-44.3021890473
848UbiquitinationATQEGEWKALKRKKF
HCCCCHHHHHHHHHC		39.27-
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 NOP14_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NOP14_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 NOP14_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAXI1_HUMANPAXIP1physical
22939629
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 NOP14_HUMAN

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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-772, AND MASS 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 SER-96; SER-146 AND SER-148,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-96, AND MASSSPECTROMETRY.
"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-146 AND SER-148, ANDMASS 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-96; SER-146 AND SER-148,AND MASS 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-96, 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-96; SER-146; SER-148 ANDSER-388, AND MASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND MASSSPECTROMETRY.
"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-96; SER-146 AND SER-148,AND MASS SPECTROMETRY.

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