NOG2_HUMAN - dbPTM
NOG2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NOG2_HUMAN
UniProt AC Q13823
Protein Name Nucleolar GTP-binding protein 2
Gene Name GNL2
Organism Homo sapiens (Human).
Sequence Length 731
Subcellular Localization Nucleus, nucleolus .
Protein Description GTPase that associates with pre-60S ribosomal subunits in the nucleolus and is required for their nuclear export and maturation (By similarity). May promote cell proliferation possibly by increasing p53/TP53 protein levels, and consequently those of its downstream product CDKN1A/p21, and decreasing RPL23A protein levels. [PubMed: 26203195]
Protein Sequence MVKPKYKGRSTINPSKASTNPDRVQGAGGQNMRDRATIRRLNMYRQKERRNSRGKIIKPLQYQSTVASGTVARVEPNIKWFGNTRVIKQSSLQKFQEEMDTVMKDPYKVVMKQSKLPMSLLHDRIRPHNLKVHILDTESFETTFGPKSQRKRPNLFASDMQSLIENAEMSTESYDQGKDRDLVTEDTGVRNEAQEEIYKKGQSKRIWGELYKVIDSSDVVVQVLDARDPMGTRSPHIETYLKKEKPWKHLIFVLNKCDLVPTWATKRWVAVLSQDYPTLAFHASLTNPFGKGAFIQLLRQFGKLHTDKKQISVGFIGYPNVGKSSVINTLRSKKVCNVAPIAGETKVWQYITLMRRIFLIDCPGVVYPSEDSETDIVLKGVVQVEKIKSPEDHIGAVLERAKPEYISKTYKIDSWENAEDFLEKLAFRTGKLLKGGEPDLQTVGKMVLNDWQRGRIPFFVKPPNAEPLVAPQLLPSSSLEVVPEAAQNNPGEEVTETAGEGSESIIKEETEENSHCDANTEMQQILTRVRQNFGKINVVPQFSGDDLVPVEVSDLEEELESFSDEEEEEQEQQRDDAEESSSEPEEENVGNDTKAVIKALDEKIAKYQKFLDKAKAKKFSAVRISKGLSEKIFAKPEEQRKTLEEDVDDRAPSKKGKKRKAQREEEQEHSNKAPRALTSKERRRAVRQQRPKKVGVRYYETHNVKNRNRNKKKTNDSEGQKHKRKKFRQKQ
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
1Acetylation-------MVKPKYKG
-------CCCCCCCC		8.6822814378
16MethylationRSTINPSKASTNPDR
CCCCCCCCCCCCCHH		47.84-
23MethylationKASTNPDRVQGAGGQ
CCCCCCHHCCCCCCC		24.74-
32SulfoxidationQGAGGQNMRDRATIR
CCCCCCCHHHHHHHH		3.4721406390
55AcetylationERRNSRGKIIKPLQY
HHHCCCCCCCCCCCC		39.9026051181
58UbiquitinationNSRGKIIKPLQYQST
CCCCCCCCCCCCCCC		43.05-
58AcetylationNSRGKIIKPLQYQST
CCCCCCCCCCCCCCC		43.0526051181
68PhosphorylationQYQSTVASGTVARVE
CCCCCCCCCCEEEEC		30.5725627689
70PhosphorylationQSTVASGTVARVEPN
CCCCCCCCEEEECCC		14.4324260401
79UbiquitinationARVEPNIKWFGNTRV
EEECCCCCCCCCCEE		43.01-
88UbiquitinationFGNTRVIKQSSLQKF
CCCCEEECHHHHHHH		41.07-
101PhosphorylationKFQEEMDTVMKDPYK
HHHHHHHHHHCCHHH		22.6120860994
119PhosphorylationKQSKLPMSLLHDRIR
CCCCCCHHHHCCCCC		26.3228555341
137PhosphorylationLKVHILDTESFETTF
CEEEEECCCCCCCCC		30.0430624053
139PhosphorylationVHILDTESFETTFGP
EEEECCCCCCCCCCC		30.4030624053
158PhosphorylationKRPNLFASDMQSLIE
CCCCCCHHHHHHHHH		26.70-
162PhosphorylationLFASDMQSLIENAEM
CCHHHHHHHHHHHCC		25.36-
198PhosphorylationNEAQEEIYKKGQSKR
HHHHHHHHHHCCHHH		15.21-
199UbiquitinationEAQEEIYKKGQSKRI
HHHHHHHHHCCHHHH		56.972190698
234PhosphorylationRDPMGTRSPHIETYL
CCCCCCCCCCHHHHH		22.2220873877
242UbiquitinationPHIETYLKKEKPWKH
CCHHHHHHCCCCCHH		48.77-
242SumoylationPHIETYLKKEKPWKH
CCHHHHHHCCCCCHH		48.77-
242AcetylationPHIETYLKKEKPWKH
CCHHHHHHCCCCCHH		48.7726051181
242SumoylationPHIETYLKKEKPWKH
CCHHHHHHCCCCCHH		48.77-
266AcetylationLVPTWATKRWVAVLS
CCCHHHCHHHHHHHC		36.1926051181
312PhosphorylationHTDKKQISVGFIGYP
CCCCCCEEEEEECCC		17.44-
318PhosphorylationISVGFIGYPNVGKSS
EEEEEECCCCCCCHH		6.19-
323UbiquitinationIGYPNVGKSSVINTL
ECCCCCCCHHHHHHH		34.96-
325PhosphorylationYPNVGKSSVINTLRS
CCCCCCHHHHHHHCC		30.4220860994
329PhosphorylationGKSSVINTLRSKKVC
CCHHHHHHHCCCCCC		16.66-
388UbiquitinationVVQVEKIKSPEDHIG
EEEEEECCCHHHHHH		71.65-
389PhosphorylationVQVEKIKSPEDHIGA
EEEEECCCHHHHHHH		36.6720873877
402AcetylationGAVLERAKPEYISKT
HHHHHHCCHHHHCCE		44.6026051181
407PhosphorylationRAKPEYISKTYKIDS
HCCHHHHCCEEECCC		20.31-
408UbiquitinationAKPEYISKTYKIDSW
CCHHHHCCEEECCCC		46.44-
411UbiquitinationEYISKTYKIDSWENA
HHHCCEEECCCCCCH		45.31-
424UbiquitinationNAEDFLEKLAFRTGK
CHHHHHHHHHHHHCC		47.46-
434UbiquitinationFRTGKLLKGGEPDLQ
HHHCCCCCCCCCCHH		75.26-
442PhosphorylationGGEPDLQTVGKMVLN
CCCCCHHHHHHHHHC		38.2225278378
504PhosphorylationTAGEGSESIIKEETE
CCCCCCCHHCCHHHC		31.1724719451
507SumoylationEGSESIIKEETEENS
CCCCHHCCHHHCCCC		48.07-
510PhosphorylationESIIKEETEENSHCD
CHHCCHHHCCCCCCC		50.0929449344
514PhosphorylationKEETEENSHCDANTE
CHHHCCCCCCCCCHH		28.8625159151
520PhosphorylationNSHCDANTEMQQILT
CCCCCCCHHHHHHHH		34.2623898821
543PhosphorylationINVVPQFSGDDLVPV
CCEECCCCCCCCEEE		35.7421406692
553PhosphorylationDLVPVEVSDLEEELE
CCEEEEHHHHHHHHH		23.9920873877
561PhosphorylationDLEEELESFSDEEEE
HHHHHHHCCCHHHHH		42.5520873877
563PhosphorylationEEELESFSDEEEEEQ
HHHHHCCCHHHHHHH		54.0820873877
580PhosphorylationQRDDAEESSSEPEEE
HHHHHHHCCCCCCHH		30.5722167270
581PhosphorylationRDDAEESSSEPEEEN
HHHHHHCCCCCCHHC		41.8422167270
582PhosphorylationDDAEESSSEPEEENV
HHHHHCCCCCCHHCC		67.4622167270
603UbiquitinationVIKALDEKIAKYQKF
HHHHHHHHHHHHHHH		47.86-
603AcetylationVIKALDEKIAKYQKF
HHHHHHHHHHHHHHH		47.8623749302
625PhosphorylationKFSAVRISKGLSEKI
CCCEEEECCCHHHHH		15.3125159151
635AcetylationLSEKIFAKPEEQRKT
HHHHHCCCHHHHHHC		42.0626051181
654AcetylationVDDRAPSKKGKKRKA
CCCCCCCHHHHHHHH		65.5725953088
698PhosphorylationPKKVGVRYYETHNVK
CCCCCCCHHHHCCCC		11.84-
699PhosphorylationKKVGVRYYETHNVKN
CCCCCCHHHHCCCCC		12.0927642862
705UbiquitinationYYETHNVKNRNRNKK
HHHHCCCCCCCCCCC		56.35-
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 NOG2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NOG2_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 NOG2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
RL23A_HUMANRPL23Aphysical
26203195
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 NOG2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-553; SER-561 ANDSER-563, AND MASS SPECTROMETRY.

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