NOL9_HUMAN - dbPTM
NOL9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NOL9_HUMAN
UniProt AC Q5SY16
Protein Name Polynucleotide 5'-hydroxyl-kinase NOL9
Gene Name NOL9
Organism Homo sapiens (Human).
Sequence Length 702
Subcellular Localization Nucleus. Nucleus, nucleolus . Colocalizes with pre-60S rRNP particles.
Protein Description Polynucleotide 5'-kinase involved in rRNA processing. The kinase activity is required for the processing of the 32S precursor into 5.8S and 28S rRNAs, more specifically for the generation of the major 5.8S(S) form. In vitro, has both DNA and RNA 5'-kinase activities. Probably binds RNA..
Protein Sequence MADSGLLLKRGSCRSTWLRVRKARPQLILSRRPRRRLGSLRWCGRRRLRWRLLQAQASGVDWREGARQVSRAAAARRPNTATPSPIPSPTPASEPESEPELESASSCHRPLLIPPVRPVGPGRALLLLPVEQGFTFSGICRVTCLYGQVQVFGFTISQGQPAQDIFSVYTHSCLSIHALHYSQPEKSKKELKREARNLLKSHLNLDDRRWSMQNFSPQCSIVLLEHLKTATVNFITSYPGSSYIFVQESPTPQIKPEYLALRSVGIRREKKRKGLQLTESTLSALEELVNVSCEEVDGCPVILVCGSQDVGKSTFNRYLINHLLNSLPCVDYLECDLGQTEFTPPGCISLLNITEPVLGPPFTHLRTPQKMVYYGKPSCKNNYENYIDIVKYVFSAYKRESPLIVNTMGWVSDQGLLLLIDLIRLLSPSHVVQFRSDHSKYMPDLTPQYVDDMDGLYTKSKTKMRNRRFRLAAFADALEFADEEKESPVEFTGHKLIGVYTDFAFRITPRNRESHNKILRDLSILSYLSQLQPPMPKPLSPLHSLTPYQVPFNAVALRITHSDVAPTHILYAVNASWVGLCKIQDDVRGYTNGPILLAQTPICDCLGFGICRGIDMEKRLYHILTPVPPEELRTVNCLLVGAIAIPHCVLKCQRGIEGTVPYVTTDYNFKLPGASEKIGAREPEEAHKEKPYRRPKFCRKMK
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------MADSGLLLK
------CCCCCCEEC		21.4822223895
4Phosphorylation----MADSGLLLKRG
----CCCCCCEECCC		23.0822199227
9UbiquitinationADSGLLLKRGSCRST
CCCCCEECCCCCHHH		55.47-
9MethylationADSGLLLKRGSCRST
CCCCCEECCCCCHHH		55.47115974137
22UbiquitinationSTWLRVRKARPQLIL
HHHHHHHHHCCCEEC		45.98-
30PhosphorylationARPQLILSRRPRRRL
HCCCEECCCCCCCHH		21.1728555341
39PhosphorylationRPRRRLGSLRWCGRR
CCCCHHCCCCCCCHH		21.2524719451
70UbiquitinationREGARQVSRAAAARR
HHHHHHHHHHHHHCC		14.0922817900
80PhosphorylationAAARRPNTATPSPIP
HHHCCCCCCCCCCCC		34.2925850435
82PhosphorylationARRPNTATPSPIPSP
HCCCCCCCCCCCCCC		23.4325850435
84PhosphorylationRPNTATPSPIPSPTP
CCCCCCCCCCCCCCC		30.9826657352
88PhosphorylationATPSPIPSPTPASEP
CCCCCCCCCCCCCCC		41.9726657352
89UbiquitinationTPSPIPSPTPASEPE
CCCCCCCCCCCCCCC		36.7322817900
90PhosphorylationPSPIPSPTPASEPES
CCCCCCCCCCCCCCC		35.5130576142
91UbiquitinationSPIPSPTPASEPESE
CCCCCCCCCCCCCCC		36.8522817900
93UbiquitinationIPSPTPASEPESEPE
CCCCCCCCCCCCCCC		55.6922817900
93PhosphorylationIPSPTPASEPESEPE
CCCCCCCCCCCCCCC		55.6930576142
97PhosphorylationTPASEPESEPELESA
CCCCCCCCCCCCCCC		69.9926657352
103PhosphorylationESEPELESASSCHRP
CCCCCCCCCCCCCCC		46.1830576142
105PhosphorylationEPELESASSCHRPLL
CCCCCCCCCCCCCEE		42.6630576142
106PhosphorylationPELESASSCHRPLLI
CCCCCCCCCCCCEEC		17.4130576142
135PhosphorylationLPVEQGFTFSGICRV
EEECCCCCEEHHHHH		24.5830576742
137PhosphorylationVEQGFTFSGICRVTC
ECCCCCEEHHHHHEE		24.9630576742
147UbiquitinationCRVTCLYGQVQVFGF
HHHEEEECCEEEEEE		14.2924816145
153UbiquitinationYGQVQVFGFTISQGQ
ECCEEEEEEEECCCC		21.6722817900
172UbiquitinationIFSVYTHSCLSIHAL
HHHHHHHHHHHHHHH		14.6722817900
174UbiquitinationSVYTHSCLSIHALHY
HHHHHHHHHHHHHHC		6.3722817900
176UbiquitinationYTHSCLSIHALHYSQ
HHHHHHHHHHHHCCC		1.1022817900
189AcetylationSQPEKSKKELKREAR
CCCCHHHHHHHHHHH		75.3126051181
200MethylationREARNLLKSHLNLDD
HHHHHHHHHHCCCCC		38.71115974129
200UbiquitinationREARNLLKSHLNLDD
HHHHHHHHHHCCCCC		38.71-
230UbiquitinationLLEHLKTATVNFITS
HHHHHHHEEEEEEEC		14.1524816145
237PhosphorylationATVNFITSYPGSSYI
EEEEEEECCCCCCEE		25.2328348404
238PhosphorylationTVNFITSYPGSSYIF
EEEEEECCCCCCEEE		11.7228348404
241PhosphorylationFITSYPGSSYIFVQE
EEECCCCCCEEEEEE		18.5725627689
242PhosphorylationITSYPGSSYIFVQES
EECCCCCCEEEEEEC		28.3225627689
249PhosphorylationSYIFVQESPTPQIKP
CEEEEEECCCCCCCH		19.5825159151
251PhosphorylationIFVQESPTPQIKPEY
EEEEECCCCCCCHHH		36.7825627689
300UbiquitinationCEEVDGCPVILVCGS
CHHCCCCCEEEEECC		23.0121890473
307UbiquitinationPVILVCGSQDVGKST
CEEEEECCCCCCHHH		20.3422817900
370AcetylationTHLRTPQKMVYYGKP
CCCCCCCEEEECCCC		31.3826051181
376MalonylationQKMVYYGKPSCKNNY
CEEEECCCCCCCCCH		20.0332601280
376UbiquitinationQKMVYYGKPSCKNNY
CEEEECCCCCCCCCH		20.0329967540
378PhosphorylationMVYYGKPSCKNNYEN
EEECCCCCCCCCHHH		41.0120068231
380UbiquitinationYYGKPSCKNNYENYI
ECCCCCCCCCHHHHH		53.1929967540
383UbiquitinationKPSCKNNYENYIDIV
CCCCCCCHHHHHHHH		18.2321890473
383PhosphorylationKPSCKNNYENYIDIV
CCCCCCCHHHHHHHH		18.2320068231
386PhosphorylationCKNNYENYIDIVKYV
CCCCHHHHHHHHHHH		6.5020068231
390UbiquitinationYENYIDIVKYVFSAY
HHHHHHHHHHHHHHH		3.0422817900
392PhosphorylationNYIDIVKYVFSAYKR
HHHHHHHHHHHHHCC		8.8820068231
395PhosphorylationDIVKYVFSAYKRESP
HHHHHHHHHHCCCCC		22.2020068231
397PhosphorylationVKYVFSAYKRESPLI
HHHHHHHHCCCCCEE		14.9120068231
427PhosphorylationIDLIRLLSPSHVVQF
HHHHHHHCHHHEEEE		29.02-
436PhosphorylationSHVVQFRSDHSKYMP
HHEEEECCCCHHHCC		40.7523322592
439PhosphorylationVQFRSDHSKYMPDLT
EEECCCCHHHCCCCC		30.3923322592
440UbiquitinationQFRSDHSKYMPDLTP
EECCCCHHHCCCCCH		41.9921906983
441PhosphorylationFRSDHSKYMPDLTPQ
ECCCCHHHCCCCCHH		19.5223322592
446PhosphorylationSKYMPDLTPQYVDDM
HHHCCCCCHHHHHCC		18.7423322592
458PhosphorylationDDMDGLYTKSKTKMR
HCCCCCCCCCHHHHH		33.6123322592
459UbiquitinationDMDGLYTKSKTKMRN
CCCCCCCCCHHHHHC		36.0822817900
460PhosphorylationMDGLYTKSKTKMRNR
CCCCCCCCHHHHHCH		37.4423322592
461UbiquitinationDGLYTKSKTKMRNRR
CCCCCCCHHHHHCHH		54.4422817900
463UbiquitinationLYTKSKTKMRNRRFR
CCCCCHHHHHCHHHH		39.3322817900
485AcetylationLEFADEEKESPVEFT
HHHCCCCCCCCCEEC		62.5426051181
485SumoylationLEFADEEKESPVEFT
HHHCCCCCCCCCEEC		62.5428112733
485UbiquitinationLEFADEEKESPVEFT
HHHCCCCCCCCCEEC		62.5429967540
487PhosphorylationFADEEKESPVEFTGH
HCCCCCCCCCEECCC		45.3625159151
492PhosphorylationKESPVEFTGHKLIGV
CCCCCEECCCEEEEE		25.5230266825
517UbiquitinationRNRESHNKILRDLSI
CCHHHHHHHHHHHHH		37.3824816145
571PhosphorylationVAPTHILYAVNASWV
CCCHHEEEEEECCEE		14.11-
618UbiquitinationCRGIDMEKRLYHILT
ECCCCHHHHHHHHHC		40.85-
651UbiquitinationAIPHCVLKCQRGIEG
HHHHHHHHCCCCCCC		14.13-
651AcetylationAIPHCVLKCQRGIEG
HHHHHHHHCCCCCCC		14.1325953088
670UbiquitinationVTTDYNFKLPGASEK
EEECCCCCCCCHHHC		50.5722817900
677UbiquitinationKLPGASEKIGAREPE
CCCCHHHCCCCCCHH		43.9027667366
677AcetylationKLPGASEKIGAREPE
CCCCHHHCCCCCCHH		43.9025953088
6772-HydroxyisobutyrylationKLPGASEKIGAREPE
CCCCHHHCCCCCCHH		43.90-
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 NOL9_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NOL9_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 NOL9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KCTD9_HUMANKCTD9physical
28514442
TEX10_HUMANTEX10physical
28514442
SENP3_HUMANSENP3physical
28514442
PELP1_HUMANPELP1physical
28514442
MRS2_HUMANMRS2physical
28514442
SHCBP_HUMANSHCBP1physical
28514442
ZN638_HUMANZNF638physical
28514442
IPO5_HUMANIPO5physical
28514442
RNBP6_HUMANRANBP6physical
28514442
DCAF1_HUMANVPRBPphysical
28514442
C1QBP_HUMANC1QBPphysical
28514442
PHF10_HUMANPHF10physical
28514442
K0232_HUMANKIAA0232physical
28514442
LTV1_HUMANLTV1physical
28514442
JPH1_HUMANJPH1physical
28514442
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 NOL9_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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