NOG1_HUMAN - dbPTM
NOG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NOG1_HUMAN
UniProt AC Q9BZE4
Protein Name Nucleolar GTP-binding protein 1
Gene Name GTPBP4
Organism Homo sapiens (Human).
Sequence Length 634
Subcellular Localization Nucleus, nucleolus .
Protein Description Involved in the biogenesis of the 60S ribosomal subunit..
Protein Sequence MAHYNFKKITVVPSAKDFIDLTLSKTQRKTPTVIHKHYQIHRIRHFYMRKVKFTQQNYHDRLSQILTDFPKLDDIHPFYADLMNILYDKDHYKLALGQINIAKNLVDNVAKDYVRLMKYGDSLYRCKQLKRAALGRMCTVIKRQKQSLEYLEQVRQHLSRLPTIDPNTRTLLLCGYPNVGKSSFINKVTRADVDVQPYAFTTKSLFVGHMDYKYLRWQVVDTPGILDHPLEDRNTIEMQAITALAHLRAAVLYVMDLSEQCGHGLREQLELFQNIRPLFINKPLIVVANKCDVKRIAELSEDDQKIFTDLQSEGFPVIETSTLTEEGVIKVKTEACDRLLAHRVETKMKGNKVNEVLNRLHLAIPTRRDDKERPPFIPEGVVARRKRMETEESRKKRERDLELEMGDDYILDLQKYWDLMNLSEKHDKIPEIWEGHNIADYIDPAIMKKLEELEKEEELRTAAGEYDSVSESEDEEMLEIRQLAKQIREKKKLKILESKEKNTQGPRMPRTAKKVQRTVLEKEMRSLGVDMDDKDDAHYAVQARRSRSITRKRKREDSAPPSSVARSGSCSRTPRDVSGLRDVKMVKKAKTMMKNAQKKMNRLGKKGEADRHVFDMKPKHLLSGKRKAGKKDRR
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
2Acetylation------MAHYNFKKI
------CCCCCCCEE		17.55-
7Acetylation-MAHYNFKKITVVPS
-CCCCCCCEEEECCC		39.3625825284
7Ubiquitination-MAHYNFKKITVVPS
-CCCCCCCEEEECCC		39.36-
8SumoylationMAHYNFKKITVVPSA
CCCCCCCEEEECCCH		39.20-
8SumoylationMAHYNFKKITVVPSA
CCCCCCCEEEECCCH		39.20-
8UbiquitinationMAHYNFKKITVVPSA
CCCCCCCEEEECCCH		39.20-
10PhosphorylationHYNFKKITVVPSAKD
CCCCCEEEECCCHHH		25.0821406692
14PhosphorylationKKITVVPSAKDFIDL
CEEEECCCHHHHHHH		36.0221406692
16SumoylationITVVPSAKDFIDLTL
EEECCCHHHHHHHCC		58.47-
16UbiquitinationITVVPSAKDFIDLTL
EEECCCHHHHHHHCC		58.47-
24PhosphorylationDFIDLTLSKTQRKTP
HHHHHCCCCCCCCCC		28.5521712546
25AcetylationFIDLTLSKTQRKTPT
HHHHCCCCCCCCCCC		52.3626051181
25SumoylationFIDLTLSKTQRKTPT
HHHHCCCCCCCCCCC		52.36-
25UbiquitinationFIDLTLSKTQRKTPT
HHHHCCCCCCCCCCC		52.3621890473
26UbiquitinationIDLTLSKTQRKTPTV
HHHCCCCCCCCCCCE		30.17-
29UbiquitinationTLSKTQRKTPTVIHK
CCCCCCCCCCCEEHH		49.38-
29UbiquitinationTLSKTQRKTPTVIHK
CCCCCCCCCCCEEHH		49.38-
30PhosphorylationLSKTQRKTPTVIHKH
CCCCCCCCCCEEHHH		26.7820860994
36AcetylationKTPTVIHKHYQIHRI
CCCCEEHHHHHHHHH		32.6525825284
38PhosphorylationPTVIHKHYQIHRIRH
CCEEHHHHHHHHHHH		17.6118083107
52AcetylationHFYMRKVKFTQQNYH
HHHHCCCCCCCCCHH		45.8126051181
56UbiquitinationRKVKFTQQNYHDRLS
CCCCCCCCCHHHHHH		49.76-
61MethylationTQQNYHDRLSQILTD
CCCCHHHHHHHHHHC		23.95-
63PhosphorylationQNYHDRLSQILTDFP
CCHHHHHHHHHHCCC		18.9725159151
64UbiquitinationNYHDRLSQILTDFPK
CHHHHHHHHHHCCCC		39.02-
65UbiquitinationYHDRLSQILTDFPKL
HHHHHHHHHHCCCCC		3.93-
71UbiquitinationQILTDFPKLDDIHPF
HHHHCCCCCCCCCHH		65.62-
71UbiquitinationQILTDFPKLDDIHPF
HHHHCCCCCCCCCHH		65.62-
87UbiquitinationADLMNILYDKDHYKL
HHHHHHHCCCCCHHH		19.70-
89AcetylationLMNILYDKDHYKLAL
HHHHHCCCCCHHHHH		32.6126051181
93UbiquitinationLYDKDHYKLALGQIN
HCCCCCHHHHHHHHH		24.70-
97UbiquitinationDHYKLALGQINIAKN
CCHHHHHHHHHHHHH		22.25-
103UbiquitinationLGQINIAKNLVDNVA
HHHHHHHHHHHHHHH		47.2021890473
103UbiquitinationLGQINIAKNLVDNVA
HHHHHHHHHHHHHHH		47.2021890473
103UbiquitinationLGQINIAKNLVDNVA
HHHHHHHHHHHHHHH		47.2021890473
103AcetylationLGQINIAKNLVDNVA
HHHHHHHHHHHHHHH		47.2019608861
103SumoylationLGQINIAKNLVDNVA
HHHHHHHHHHHHHHH		47.2028112733
103UbiquitinationLGQINIAKNLVDNVA
HHHHHHHHHHHHHHH		47.2021906983
111UbiquitinationNLVDNVAKDYVRLMK
HHHHHHHHHHHHHHH		45.3621890473
118UbiquitinationKDYVRLMKYGDSLYR
HHHHHHHHHCCHHHH		51.1521890473
118UbiquitinationKDYVRLMKYGDSLYR
HHHHHHHHHCCHHHH		51.1521890473
118UbiquitinationKDYVRLMKYGDSLYR
HHHHHHHHHCCHHHH		51.1521890473
118AcetylationKDYVRLMKYGDSLYR
HHHHHHHHHCCHHHH		51.1525825284
118UbiquitinationKDYVRLMKYGDSLYR
HHHHHHHHHCCHHHH		51.1521890473
119PhosphorylationDYVRLMKYGDSLYRC
HHHHHHHHCCHHHHH		16.5223186163
122PhosphorylationRLMKYGDSLYRCKQL
HHHHHCCHHHHHHHH		23.9628152594
127UbiquitinationGDSLYRCKQLKRAAL
CCHHHHHHHHHHHHH		50.06-
142AcetylationGRMCTVIKRQKQSLE
HHHHHHHHHHHHHHH		44.4326051181
142UbiquitinationGRMCTVIKRQKQSLE
HHHHHHHHHHHHHHH		44.43-
145UbiquitinationCTVIKRQKQSLEYLE
HHHHHHHHHHHHHHH		45.9821890473
145UbiquitinationCTVIKRQKQSLEYLE
HHHHHHHHHHHHHHH		45.9821890473
145UbiquitinationCTVIKRQKQSLEYLE
HHHHHHHHHHHHHHH		45.9821890473
145UbiquitinationCTVIKRQKQSLEYLE
HHHHHHHHHHHHHHH		45.9821890473
150PhosphorylationRQKQSLEYLEQVRQH
HHHHHHHHHHHHHHH		22.34-
159PhosphorylationEQVRQHLSRLPTIDP
HHHHHHHHCCCCCCC		29.6421406692
163PhosphorylationQHLSRLPTIDPNTRT
HHHHCCCCCCCCCCE		42.4720860994
166UbiquitinationSRLPTIDPNTRTLLL
HCCCCCCCCCCEEEE		40.00-
168PhosphorylationLPTIDPNTRTLLLCG
CCCCCCCCCEEEEEC		30.3420860994
170PhosphorylationTIDPNTRTLLLCGYP
CCCCCCCEEEEECCC		21.5125137130
176PhosphorylationRTLLLCGYPNVGKSS
CEEEEECCCCCCCHH		7.2228152594
181SumoylationCGYPNVGKSSFINKV
ECCCCCCCHHHHCCC		38.35-
181AcetylationCGYPNVGKSSFINKV
ECCCCCCCHHHHCCC		38.3526051181
181SumoylationCGYPNVGKSSFINKV
ECCCCCCCHHHHCCC		38.35-
181UbiquitinationCGYPNVGKSSFINKV
ECCCCCCCHHHHCCC		38.3521890473
187UbiquitinationGKSSFINKVTRADVD
CCHHHHCCCCCCCCC		39.92-
203UbiquitinationQPYAFTTKSLFVGHM
CCCCEECCEEEEEEC		41.9521890473
203UbiquitinationQPYAFTTKSLFVGHM
CCCCEECCEEEEEEC		41.9521890473
203UbiquitinationQPYAFTTKSLFVGHM
CCCCEECCEEEEEEC		41.9521890473
203AcetylationQPYAFTTKSLFVGHM
CCCCEECCEEEEEEC		41.9526051181
203UbiquitinationQPYAFTTKSLFVGHM
CCCCEECCEEEEEEC		41.9521890473
213AcetylationFVGHMDYKYLRWQVV
EEEECCHHHEEEEEE		33.2825825284
213UbiquitinationFVGHMDYKYLRWQVV
EEEECCHHHEEEEEE		33.28-
214PhosphorylationVGHMDYKYLRWQVVD
EEECCHHHEEEEEEC		8.6820860994
233MethylationLDHPLEDRNTIEMQA
CCCCCCCCCHHHHHH		32.58-
255UbiquitinationRAAVLYVMDLSEQCG
HHHHHHHHHHHHHCC		2.44-
282UbiquitinationIRPLFINKPLIVVAN
CHHHCCCCCEEEEEC		36.06-
300PhosphorylationVKRIAELSEDDQKIF
HHHHHHCCHHHHHHH		30.4121815630
305SumoylationELSEDDQKIFTDLQS
HCCHHHHHHHHHHHH		46.94-
305UbiquitinationELSEDDQKIFTDLQS
HCCHHHHHHHHHHHH		46.94-
332SumoylationEEGVIKVKTEACDRL
CCCEEEEHHHHHHHH		35.33-
332AcetylationEEGVIKVKTEACDRL
CCCEEEEHHHHHHHH		35.3326051181
332SumoylationEEGVIKVKTEACDRL
CCCEEEEHHHHHHHH		35.3328112733
333UbiquitinationEGVIKVKTEACDRLL
CCEEEEHHHHHHHHH		31.63-
338MethylationVKTEACDRLLAHRVE
EHHHHHHHHHHHHHH		31.33-
346PhosphorylationLLAHRVETKMKGNKV
HHHHHHHHHCCCCHH		33.3129449344
347UbiquitinationLAHRVETKMKGNKVN
HHHHHHHHCCCCHHH		25.71-
352SumoylationETKMKGNKVNEVLNR
HHHCCCCHHHHHHHH		55.92-
352SumoylationETKMKGNKVNEVLNR
HHHCCCCHHHHHHHH		55.92-
352UbiquitinationETKMKGNKVNEVLNR
HHHCCCCHHHHHHHH		55.92-
371UbiquitinationIPTRRDDKERPPFIP
CCCCCCCCCCCCCCC		60.97-
378UbiquitinationKERPPFIPEGVVARR
CCCCCCCCHHHHHHH		32.44-
390PhosphorylationARRKRMETEESRKKR
HHHHHHCCHHHHHHH		35.3926074081
393PhosphorylationKRMETEESRKKRERD
HHHCCHHHHHHHHHH		43.0726074081
406AcetylationRDLELEMGDDYILDL
HHHHHHCCCCEEHHH		18.43-
406UbiquitinationRDLELEMGDDYILDL
HHHHHHCCCCEEHHH		18.43-
409PhosphorylationELEMGDDYILDLQKY
HHHCCCCEEHHHHHH		14.2327642862
416PhosphorylationYILDLQKYWDLMNLS
EEHHHHHHHHHHCHH		7.3828509920
423PhosphorylationYWDLMNLSEKHDKIP
HHHHHCHHHHHCCCC		39.3321815630
425UbiquitinationDLMNLSEKHDKIPEI
HHHCHHHHHCCCCHH		54.44-
428UbiquitinationNLSEKHDKIPEIWEG
CHHHHHCCCCHHHCC		60.94-
441PhosphorylationEGHNIADYIDPAIMK
CCCCHHHHCCHHHHH		9.7528796482
448UbiquitinationYIDPAIMKKLEELEK
HCCHHHHHHHHHHHH		48.36-
449SumoylationIDPAIMKKLEELEKE
CCHHHHHHHHHHHHH		43.69-
449AcetylationIDPAIMKKLEELEKE
CCHHHHHHHHHHHHH		43.6926051181
449SumoylationIDPAIMKKLEELEKE
CCHHHHHHHHHHHHH		43.69-
449UbiquitinationIDPAIMKKLEELEKE
CCHHHHHHHHHHHHH		43.69-
455AcetylationKKLEELEKEEELRTA
HHHHHHHHHHHHHHH		80.9726051181
461PhosphorylationEKEEELRTAAGEYDS
HHHHHHHHHCCCCCC		33.2221712546
466PhosphorylationLRTAAGEYDSVSESE
HHHHCCCCCCCCCCC		16.7621712546
468PhosphorylationTAAGEYDSVSESEDE
HHCCCCCCCCCCCCH		27.0025159151
470PhosphorylationAGEYDSVSESEDEEM
CCCCCCCCCCCCHHH		39.0825159151
472PhosphorylationEYDSVSESEDEEMLE
CCCCCCCCCCHHHHH		42.7325159151
494SumoylationIREKKKLKILESKEK
HHHHHHHHHHHCHHH		54.87-
494SumoylationIREKKKLKILESKEK
HHHHHHHHHHHCHHH		54.87-
494UbiquitinationIREKKKLKILESKEK
HHHHHHHHHHHCHHH		54.87-
513MethylationPRMPRTAKKVQRTVL
CCCCHHHHHHHHHHH		53.52-
522AcetylationVQRTVLEKEMRSLGV
HHHHHHHHHHHHCCC		53.2819608861
522UbiquitinationVQRTVLEKEMRSLGV
HHHHHHHHHHHHCCC		53.2819608861
526PhosphorylationVLEKEMRSLGVDMDD
HHHHHHHHCCCCCCC		28.3229214152
534SumoylationLGVDMDDKDDAHYAV
CCCCCCCCCHHHHHH		53.92-
534AcetylationLGVDMDDKDDAHYAV
CCCCCCCCCHHHHHH		53.9226051181
534SumoylationLGVDMDDKDDAHYAV
CCCCCCCCCHHHHHH		53.9228112733
539PhosphorylationDDKDDAHYAVQARRS
CCCCHHHHHHHHHHH		15.3628796482
558PhosphorylationRKRKREDSAPPSSVA
CHHHCCCCCCCCHHH		37.6129255136
562PhosphorylationREDSAPPSSVARSGS
CCCCCCCCHHHCCCC		36.0629255136
563PhosphorylationEDSAPPSSVARSGSC
CCCCCCCHHHCCCCC		26.1029255136
567PhosphorylationPPSSVARSGSCSRTP
CCCHHHCCCCCCCCC		25.8926074081
569PhosphorylationSSVARSGSCSRTPRD
CHHHCCCCCCCCCCC		15.3426074081
571PhosphorylationVARSGSCSRTPRDVS
HHCCCCCCCCCCCCC		40.6726074081
573PhosphorylationRSGSCSRTPRDVSGL
CCCCCCCCCCCCCCC		13.3328102081
578PhosphorylationSRTPRDVSGLRDVKM
CCCCCCCCCCCHHHH		36.0823401153
581MethylationPRDVSGLRDVKMVKK
CCCCCCCCHHHHHHH		50.64-
584SumoylationVSGLRDVKMVKKAKT
CCCCCHHHHHHHHHH		42.12-
584SumoylationVSGLRDVKMVKKAKT
CCCCCHHHHHHHHHH		42.12-
591O-linked_GlycosylationKMVKKAKTMMKNAQK
HHHHHHHHHHHHHHH		27.6231492838
617AcetylationDRHVFDMKPKHLLSG
HHHCCCCCHHHHHCC		53.4025953088
619UbiquitinationHVFDMKPKHLLSGKR
HCCCCCHHHHHCCCC		41.17-
623PhosphorylationMKPKHLLSGKRKAGK
CCHHHHHCCCCCCCC		48.9424719451
625AcetylationPKHLLSGKRKAGKKD
HHHHHCCCCCCCCCC		47.5525953088
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 NOG1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NOG1_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 NOG1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZA2G_HUMANAZGP1physical
24778252
DICER_HUMANDICER1physical
24778252
IF6_HUMANEIF6physical
24778252
IFRD1_HUMANIFRD1physical
24778252
KCTD2_HUMANKCTD2physical
24778252
MRT4_HUMANMRTO4physical
24778252
PNMA2_HUMANPNMA2physical
24778252
POP1_HUMANPOP1physical
24778252
PRKRA_HUMANPRKRAphysical
24778252
PSME3_HUMANPSME3physical
24778252
STAU1_HUMANSTAU1physical
24778252
BRX1_HUMANBRIX1physical
26344197
CEBPZ_HUMANCEBPZphysical
26344197
DDX47_HUMANDDX47physical
26344197
DDX5_HUMANDDX5physical
26344197
DDX55_HUMANDDX55physical
26344197
DDX56_HUMANDDX56physical
26344197
EBP2_HUMANEBNA1BP2physical
26344197
NOP53_HUMANGLTSCR2physical
26344197
NOG2_HUMANGNL2physical
26344197
GNL3L_HUMANGNL3Lphysical
26344197
GRWD1_HUMANGRWD1physical
26344197
IMP3_HUMANIMP3physical
26344197
MPP10_HUMANMPHOSPH10physical
26344197
NMD3_HUMANNMD3physical
26344197
NOC2L_HUMANNOC2Lphysical
26344197
NOP2_HUMANNOP2physical
26344197
NSA2_HUMANNSA2physical
26344197
RPF2_HUMANRPF2physical
26344197
RL27_HUMANRPL27physical
26344197
RL36_HUMANRPL36physical
26344197
RRS1_HUMANRRS1physical
26344197
SDA1_HUMANSDAD1physical
26344197
TBL3_HUMANTBL3physical
26344197
UT14A_HUMANUTP14Aphysical
26344197
SAS10_HUMANUTP3physical
26344197
WDR36_HUMANWDR36physical
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 NOG1_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-103 AND LYS-522, AND MASSSPECTROMETRY.
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-468; SER-470 ANDSER-472, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578, 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-468; SER-470; SER-472;SER-558 AND SER-578, 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-468; SER-470 ANDSER-472, 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-563 AND SER-578, ANDMASS 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-468; SER-470 ANDSER-472, AND MASS SPECTROMETRY.

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