NSUN5_HUMAN - dbPTM
NSUN5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NSUN5_HUMAN
UniProt AC Q96P11
Protein Name Probable 28S rRNA (cytosine-C(5))-methyltransferase
Gene Name NSUN5
Organism Homo sapiens (Human).
Sequence Length 429
Subcellular Localization
Protein Description S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 3782 in 28S rRNA..
Protein Sequence MGLYAAAAGVLAGVESRQGSIKGLVYSSNFQNVKQLYALVCETQRYSAVLDAVIASAGLLRAEKKLRPHLAKVLVYELLLGKGFRGGGGRWKALLGRHQARLKAELARLKVHRGVSRNEDLLEVGSRPGPASQLPRFVRVNTLKTCSDDVVDYFKRQGFSYQGRASSLDDLRALKGKHFLLDPLMPELLVFPAQTDLHEHPLYRAGHLILQDRASCLPAMLLDPPPGSHVIDACAAPGNKTSHLAALLKNQGKIFAFDLDAKRLASMATLLARAGVSCCELAEEDFLAVSPSDPRYHEVHYILLDPSCSGSGMPSRQLEEPGAGTPSPVRLHALAGFQQRALCHALTFPSLQRLVYSTCSLCQEENEDVVRDALQQNPGAFRLAPALPAWPHRGLSTFPGAEHCLRASPETTLSSGFFVAVIERVEVPR
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------MGLYAAAAG
------CCHHHHHHH		27.65-
4Phosphorylation----MGLYAAAAGVL
----CCHHHHHHHHH		6.6120068231
22UbiquitinationESRQGSIKGLVYSSN
HHCCCCEEEEEECCC		48.1421890473
22 (in isoform 2)Ubiquitination-48.1421890473
22 (in isoform 4)Ubiquitination-48.14-
22UbiquitinationESRQGSIKGLVYSSN
HHCCCCEEEEEECCC		48.1421890473
22UbiquitinationESRQGSIKGLVYSSN
HHCCCCEEEEEECCC		48.1421890473
22 (in isoform 1)Ubiquitination-48.1421890473
26PhosphorylationGSIKGLVYSSNFQNV
CCEEEEEECCCCCCH		16.0728152594
27PhosphorylationSIKGLVYSSNFQNVK
CEEEEEECCCCCCHH		16.0128152594
28PhosphorylationIKGLVYSSNFQNVKQ
EEEEEECCCCCCHHH		24.7928152594
34UbiquitinationSSNFQNVKQLYALVC
CCCCCCHHHHHHHHH		41.9821963094
37PhosphorylationFQNVKQLYALVCETQ
CCCHHHHHHHHHHHH		8.73-
46PhosphorylationLVCETQRYSAVLDAV
HHHHHHHHHHHHHHH		7.3729496907
76PhosphorylationHLAKVLVYELLLGKG
HHHHHHHHHHHHCCC		9.1929496907
82 (in isoform 1)Ubiquitination-55.6421890473
82UbiquitinationVYELLLGKGFRGGGG
HHHHHHCCCCCCCCH		55.6421890473
82UbiquitinationVYELLLGKGFRGGGG
HHHHHHCCCCCCCCH		55.6421963094
82 (in isoform 4)Ubiquitination-55.64-
82 (in isoform 2)Ubiquitination-55.6421890473
85MethylationLLLGKGFRGGGGRWK
HHHCCCCCCCCHHHH		52.06115485669
92 (in isoform 2)Ubiquitination-28.00-
92UbiquitinationRGGGGRWKALLGRHQ
CCCCHHHHHHHHHHH		28.00-
103SumoylationGRHQARLKAELARLK
HHHHHHHHHHHHHHH		33.97-
103SumoylationGRHQARLKAELARLK
HHHHHHHHHHHHHHH		33.97-
103UbiquitinationGRHQARLKAELARLK
HHHHHHHHHHHHHHH		33.97-
103 (in isoform 2)Ubiquitination-33.97-
106UbiquitinationQARLKAELARLKVHR
HHHHHHHHHHHHHHC		3.9221963094
116PhosphorylationLKVHRGVSRNEDLLE
HHHHCCCCCCCCHHH		32.0128555341
117UbiquitinationKVHRGVSRNEDLLEV
HHHCCCCCCCCHHHC		48.4227667366
137UbiquitinationPASQLPRFVRVNTLK
CHHHCCCEEECCCCC		3.7722817900
139UbiquitinationSQLPRFVRVNTLKTC
HHCCCEEECCCCCCC		17.1621963094
142PhosphorylationPRFVRVNTLKTCSDD
CCEEECCCCCCCCHH		27.1230301811
144SumoylationFVRVNTLKTCSDDVV
EEECCCCCCCCHHHH		45.51-
144MethylationFVRVNTLKTCSDDVV
EEECCCCCCCCHHHH		45.5182983213
144UbiquitinationFVRVNTLKTCSDDVV
EEECCCCCCCCHHHH		45.5121963094
144SumoylationFVRVNTLKTCSDDVV
EEECCCCCCCCHHHH		45.51-
144 (in isoform 2)Ubiquitination-45.51-
145PhosphorylationVRVNTLKTCSDDVVD
EECCCCCCCCHHHHH		21.9830301811
147PhosphorylationVNTLKTCSDDVVDYF
CCCCCCCCHHHHHHH		41.9230301811
155 (in isoform 2)Ubiquitination-37.27-
155AcetylationDDVVDYFKRQGFSYQ
HHHHHHHHHCCCCCC		37.2726051181
155UbiquitinationDDVVDYFKRQGFSYQ
HHHHHHHHHCCCCCC		37.2727667366
155MethylationDDVVDYFKRQGFSYQ
HHHHHHHHHCCCCCC		37.2782983219
166PhosphorylationFSYQGRASSLDDLRA
CCCCCCCCCHHHHHH		30.0330266825
167PhosphorylationSYQGRASSLDDLRAL
CCCCCCCCHHHHHHH		34.5330266825
175UbiquitinationLDDLRALKGKHFLLD
HHHHHHHCCCCCCCC		66.0022817900
177UbiquitinationDLRALKGKHFLLDPL
HHHHHCCCCCCCCCC		29.6021963094
177 (in isoform 2)Ubiquitination-29.60-
195PhosphorylationLLVFPAQTDLHEHPL
HEEEECCCCCCCCCH		42.5120068231
203PhosphorylationDLHEHPLYRAGHLIL
CCCCCCHHHCCCHHH		11.6724043423
211UbiquitinationRAGHLILQDRASCLP
HCCCHHHCCHHHCCC		31.0221963094
215UbiquitinationLILQDRASCLPAMLL
HHHCCHHHCCCHHHC		19.6521963094
224UbiquitinationLPAMLLDPPPGSHVI
CCHHHCCCCCCCCHH		36.6321963094
249UbiquitinationSHLAALLKNQGKIFA
HHHHHHHHHCCCEEE		48.3421963094
249 (in isoform 2)Ubiquitination-48.3421890473
249 (in isoform 1)Ubiquitination-48.3421890473
253UbiquitinationALLKNQGKIFAFDLD
HHHHHCCCEEEEECC		25.5321963094
253 (in isoform 2)Ubiquitination-25.5321890473
253 (in isoform 1)Ubiquitination-25.5321890473
262AcetylationFAFDLDAKRLASMAT
EEEECCHHHHHHHHH		47.8425953088
262UbiquitinationFAFDLDAKRLASMAT
EEEECCHHHHHHHHH		47.8421963094
262 (in isoform 2)Ubiquitination-47.8421890473
262 (in isoform 1)Ubiquitination-47.8421890473
296PhosphorylationVSPSDPRYHEVHYIL
CCCCCCCCEEEEEEE		14.0229496907
301PhosphorylationPRYHEVHYILLDPSC
CCCEEEEEEEECCCC		9.8429496907
307PhosphorylationHYILLDPSCSGSGMP
EEEEECCCCCCCCCC		22.1526074081
309PhosphorylationILLDPSCSGSGMPSR
EEECCCCCCCCCCCC		40.0926074081
311PhosphorylationLDPSCSGSGMPSRQL
ECCCCCCCCCCCCCC		18.6726074081
315PhosphorylationCSGSGMPSRQLEEPG
CCCCCCCCCCCCCCC		24.6226074081
325PhosphorylationLEEPGAGTPSPVRLH
CCCCCCCCCCCHHHH		21.7629255136
327PhosphorylationEPGAGTPSPVRLHAL
CCCCCCCCCHHHHHH		35.5519664994
340MethylationALAGFQQRALCHALT
HHCHHHHHHHHHHHH		20.8124411403
350PhosphorylationCHALTFPSLQRLVYS
HHHHHCHHHHHHHHH		32.7026091039
408PhosphorylationAEHCLRASPETTLSS
CHHHHHCCCCCCCCC		19.4827251275
432 (in isoform 2)Phosphorylation-17525332
435UbiquitinationPR-------------
CC-------------		27667366
435 (in isoform 2)Ubiquitination-21890473
442 (in isoform 2)Phosphorylation-25849741
444 (in isoform 2)Phosphorylation-25849741
444 (in isoform 4)Phosphorylation-24719451
462 (in isoform 2)Phosphorylation-25159151
466 (in isoform 2)Phosphorylation-20068231
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 NSUN5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NSUN5_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 NSUN5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPAC1_HUMANPOLR1Cphysical
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 NSUN5_HUMAN

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Related Literatures of Post-Translational Modification
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-167, 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 THR-325 AND SER-327, ANDMASS SPECTROMETRY.

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