RT29_HUMAN - dbPTM
RT29_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RT29_HUMAN
UniProt AC P51398
Protein Name 28S ribosomal protein S29, mitochondrial
Gene Name DAP3
Organism Homo sapiens (Human).
Sequence Length 398
Subcellular Localization Mitochondrion .
Protein Description Involved in mediating interferon-gamma-induced cell death..
Protein Sequence MMLKGITRLISRIHKLDPGRFLHMGTQARQSIAAHLDNQVPVESPRAISRTNENDPAKHGDQHEGQHYNISPQDLETVFPHGLPPRFVMQVKTFSEACLMVRKPALELLHYLKNTSFAYPAIRYLLYGEKGTGKTLSLCHVIHFCAKQDWLILHIPDAHLWVKNCRDLLQSSYNKQRFDQPLEASTWLKNFKTTNERFLNQIKVQEKYVWNKRESTEKGSPLGEVVEQGITRVRNATDAVGIVLKELKRQSSLGMFHLLVAVDGINALWGRTTLKREDKSPIAPEELALVHNLRKMMKNDWHGGAIVSALSQTGSLFKPRKAYLPQELLGKEGFDALDPFIPILVSNYNPKEFESCIQYYLENNWLQHEKAPTEEGKKELLFLSNANPSLLERHCAYL
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
31PhosphorylationMGTQARQSIAAHLDN
CCHHHHHHHHHHCCC		14.5118227431
44PhosphorylationDNQVPVESPRAISRT
CCCCCCCCCCCCCCC		21.6625159151
89UbiquitinationGLPPRFVMQVKTFSE
CCCCCCEEEEEEHHH		3.3129967540
93PhosphorylationRFVMQVKTFSEACLM
CCEEEEEEHHHHHHH		33.2717924679
96UbiquitinationMQVKTFSEACLMVRK
EEEEEHHHHHHHHHH		38.9329967540
100UbiquitinationTFSEACLMVRKPALE
EHHHHHHHHHHHHHH		2.4924816145
103UbiquitinationEACLMVRKPALELLH
HHHHHHHHHHHHHHH		24.19-
103AcetylationEACLMVRKPALELLH
HHHHHHHHHHHHHHH		24.1926051181
111PhosphorylationPALELLHYLKNTSFA
HHHHHHHHHHCCCCH		21.2428152594
114UbiquitinationELLHYLKNTSFAYPA
HHHHHHHCCCCHHHH		38.0621963094
117UbiquitinationHYLKNTSFAYPAIRY
HHHHCCCCHHHHHHH		7.7022817900
124PhosphorylationFAYPAIRYLLYGEKG
CHHHHHHHHHHCCCC		8.5719835603
130UbiquitinationRYLLYGEKGTGKTLS
HHHHHCCCCCCHHHH		58.3629967540
1302-HydroxyisobutyrylationRYLLYGEKGTGKTLS
HHHHHCCCCCCHHHH		58.36-
130SuccinylationRYLLYGEKGTGKTLS
HHHHHCCCCCCHHHH		58.3623954790
134UbiquitinationYGEKGTGKTLSLCHV
HCCCCCCHHHHHHHH		46.2424816145
134AcetylationYGEKGTGKTLSLCHV
HCCCCCCHHHHHHHH		46.2419608861
137UbiquitinationKGTGKTLSLCHVIHF
CCCCHHHHHHHHHHH		33.8923503661
141UbiquitinationKTLSLCHVIHFCAKQ
HHHHHHHHHHHHHCC		3.3824816145
141AcetylationKTLSLCHVIHFCAKQ
HHHHHHHHHHHHHCC		3.3819608861
143UbiquitinationLSLCHVIHFCAKQDW
HHHHHHHHHHHCCCE		15.6222817900
148UbiquitinationVIHFCAKQDWLILHI
HHHHHHCCCEEEEEC		28.6921963094
151UbiquitinationFCAKQDWLILHIPDA
HHHCCCEEEEECCCH		3.9322817900
155UbiquitinationQDWLILHIPDAHLWV
CCEEEEECCCHHHHH		2.7121963094
158UbiquitinationLILHIPDAHLWVKNC
EEEECCCHHHHHHHH		8.3622817900
162UbiquitinationIPDAHLWVKNCRDLL
CCCHHHHHHHHHHHH		3.9329967540
166UbiquitinationHLWVKNCRDLLQSSY
HHHHHHHHHHHHHHH		47.1829967540
166AcetylationHLWVKNCRDLLQSSY
HHHHHHHHHHHHHHH		47.1819608861
169UbiquitinationVKNCRDLLQSSYNKQ
HHHHHHHHHHHHHHH		5.6329967540
171UbiquitinationNCRDLLQSSYNKQRF
HHHHHHHHHHHHHCC		34.4623503661
173UbiquitinationRDLLQSSYNKQRFDQ
HHHHHHHHHHHCCCC		31.4629967540
173AcetylationRDLLQSSYNKQRFDQ
HHHHHHHHHHHCCCC		31.4619608861
175AcetylationLLQSSYNKQRFDQPL
HHHHHHHHHCCCCCC		34.3219608861
175UbiquitinationLLQSSYNKQRFDQPL
HHHHHHHHHCCCCCC		34.3224816145
175MalonylationLLQSSYNKQRFDQPL
HHHHHHHHHCCCCCC		34.3226320211
175SuccinylationLLQSSYNKQRFDQPL
HHHHHHHHHCCCCCC		34.3227452117
177UbiquitinationQSSYNKQRFDQPLEA
HHHHHHHCCCCCCHH		38.4229967540
178UbiquitinationSSYNKQRFDQPLEAS
HHHHHHCCCCCCHHH		10.6923503661
184UbiquitinationRFDQPLEASTWLKNF
CCCCCCHHHHHHHHC		21.6829967540
185PhosphorylationFDQPLEASTWLKNFK
CCCCCHHHHHHHHCC		15.6718227431
186PhosphorylationDQPLEASTWLKNFKT
CCCCHHHHHHHHCCC		41.6918227431
189UbiquitinationLEASTWLKNFKTTNE
CHHHHHHHHCCCCCH		52.4821963094
192UbiquitinationSTWLKNFKTTNERFL
HHHHHHCCCCCHHHH		64.9322817900
192AcetylationSTWLKNFKTTNERFL
HHHHHHCCCCCHHHH		64.9325953088
193PhosphorylationTWLKNFKTTNERFLN
HHHHHCCCCCHHHHH		30.6222210691
203UbiquitinationERFLNQIKVQEKYVW
HHHHHHHHHHEECCC		28.2729967540
203MalonylationERFLNQIKVQEKYVW
HHHHHHHHHHEECCC		28.2726320211
203SuccinylationERFLNQIKVQEKYVW
HHHHHHHHHHEECCC		28.2723954790
204UbiquitinationRFLNQIKVQEKYVWN
HHHHHHHHHEECCCC		10.7024816145
207AcetylationNQIKVQEKYVWNKRE
HHHHHHEECCCCCCC		28.1919608861
207UbiquitinationNQIKVQEKYVWNKRE
HHHHHHEECCCCCCC		28.1919608861
2072-HydroxyisobutyrylationNQIKVQEKYVWNKRE
HHHHHHEECCCCCCC		28.19-
207MalonylationNQIKVQEKYVWNKRE
HHHHHHEECCCCCCC		28.1926320211
207SuccinylationNQIKVQEKYVWNKRE
HHHHHHEECCCCCCC		28.1927452117
211UbiquitinationVQEKYVWNKRESTEK
HHEECCCCCCCCCCC		24.3824816145
212UbiquitinationQEKYVWNKRESTEKG
HEECCCCCCCCCCCC		41.6623503661
212AcetylationQEKYVWNKRESTEKG
HEECCCCCCCCCCCC		41.6626051181
215PhosphorylationYVWNKRESTEKGSPL
CCCCCCCCCCCCCCH		45.9918227431
216PhosphorylationVWNKRESTEKGSPLG
CCCCCCCCCCCCCHH		36.6418227431
218UbiquitinationNKRESTEKGSPLGEV
CCCCCCCCCCCHHHH		65.8522817900
218MalonylationNKRESTEKGSPLGEV
CCCCCCCCCCCHHHH		65.8526320211
218AcetylationNKRESTEKGSPLGEV
CCCCCCCCCCCHHHH		65.8525953088
220PhosphorylationRESTEKGSPLGEVVE
CCCCCCCCCHHHHHH		28.1921815630
231PhosphorylationEVVEQGITRVRNATD
HHHHHHHHHHHCHHH		29.9021406692
237PhosphorylationITRVRNATDAVGIVL
HHHHHCHHHHHHHHH		28.2118227431
238UbiquitinationTRVRNATDAVGIVLK
HHHHCHHHHHHHHHH		36.5224816145
243UbiquitinationATDAVGIVLKELKRQ
HHHHHHHHHHHHHHH		5.2723503661
245UbiquitinationDAVGIVLKELKRQSS
HHHHHHHHHHHHHCC		50.5424816145
246UbiquitinationAVGIVLKELKRQSSL
HHHHHHHHHHHHCCC		56.1923503661
250UbiquitinationVLKELKRQSSLGMFH
HHHHHHHHCCCCHHH		35.4723503661
251PhosphorylationLKELKRQSSLGMFHL
HHHHHHHCCCCHHHH		31.4018227431
252PhosphorylationKELKRQSSLGMFHLL
HHHHHHCCCCHHHHH		22.1718227431
252UbiquitinationKELKRQSSLGMFHLL
HHHHHHCCCCHHHHH		22.1724816145
253UbiquitinationELKRQSSLGMFHLLV
HHHHHCCCCHHHHHH		7.5423503661
257UbiquitinationQSSLGMFHLLVAVDG
HCCCCHHHHHHHHHH		14.9023503661
260UbiquitinationLGMFHLLVAVDGINA
CCHHHHHHHHHHHHH		6.5023503661
272PhosphorylationINALWGRTTLKREDK
HHHHCCCCCCCCCCC		32.3222817900
273PhosphorylationNALWGRTTLKREDKS
HHHCCCCCCCCCCCC		28.99-
277UbiquitinationGRTTLKREDKSPIAP
CCCCCCCCCCCCCCH		69.1023503661
279UbiquitinationTTLKREDKSPIAPEE
CCCCCCCCCCCCHHH		54.0724816145
280PhosphorylationTLKREDKSPIAPEEL
CCCCCCCCCCCHHHH		33.5825849741
280UbiquitinationTLKREDKSPIAPEEL
CCCCCCCCCCCHHHH		33.5823503661
284UbiquitinationEDKSPIAPEELALVH
CCCCCCCHHHHHHHH		35.9923503661
287UbiquitinationSPIAPEELALVHNLR
CCCCHHHHHHHHHHH		4.2123503661
291UbiquitinationPEELALVHNLRKMMK
HHHHHHHHHHHHHHH		28.5823503661
294UbiquitinationLALVHNLRKMMKNDW
HHHHHHHHHHHHCCC		30.0923503661
308PhosphorylationWHGGAIVSALSQTGS
CCHHHHHHHHHCCCC		19.8520873877
311PhosphorylationGAIVSALSQTGSLFK
HHHHHHHHCCCCCCC		25.9720873877
313PhosphorylationIVSALSQTGSLFKPR
HHHHHHCCCCCCCCC		25.9227251275
315PhosphorylationSALSQTGSLFKPRKA
HHHHCCCCCCCCCCC		33.7420873877
318UbiquitinationSQTGSLFKPRKAYLP
HCCCCCCCCCCCCCC		49.5623503661
318AcetylationSQTGSLFKPRKAYLP
HCCCCCCCCCCCCCC		49.5626051181
321UbiquitinationGSLFKPRKAYLPQEL
CCCCCCCCCCCCHHH		50.3223503661
329UbiquitinationAYLPQELLGKEGFDA
CCCCHHHHCCCCCCC		10.1629967540
336UbiquitinationLGKEGFDALDPFIPI
HCCCCCCCCCCCHHE		16.1729967540
337UbiquitinationGKEGFDALDPFIPIL
CCCCCCCCCCCHHEE		10.4029967540
343UbiquitinationALDPFIPILVSNYNP
CCCCCHHEEECCCCH		5.1929967540
344UbiquitinationLDPFIPILVSNYNPK
CCCCHHEEECCCCHH		2.6529967540
370UbiquitinationNNWLQHEKAPTEEGK
CCCCCCCCCCCHHHH		58.5029967540
377UbiquitinationKAPTEEGKKELLFLS
CCCCHHHHHHHEHHC		46.4829967540
378UbiquitinationAPTEEGKKELLFLSN
CCCHHHHHHHEHHCC		65.5329967540
389PhosphorylationFLSNANPSLLERHCA
HHCCCCHHHHHHHHH		45.45-
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
31SPhosphorylationKinasePRKACAP17612
GPS
31SPhosphorylationKinasePRKCDQ05655
GPS
185SPhosphorylationKinasePRKACAP17612
GPS
185SPhosphorylationKinasePRKCDQ05655
GPS
186TPhosphorylationKinasePRKACAP17612
GPS
186TPhosphorylationKinasePRKCDQ05655
GPS
220SPhosphorylationKinasePRKACAP17612
GPS
237TPhosphorylationKinasePRKCDQ05655
GPS
280SPhosphorylationKinasePRKCDQ05655
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RT29_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 RT29_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GCR_HUMANNR3C1physical
10903152
PPARA_HUMANPPARAphysical
10903152
HS90A_HUMANHSP90AA1physical
10903152
HIF1A_HUMANHIF1Aphysical
10903152
AHR_HUMANAHRphysical
10903152
ESR1_HUMANESR1physical
10903152
ESR2_HUMANESR2physical
10903152
PRGR_HUMANPGRphysical
10903152
THA_HUMANTHRAphysical
10903152
ANDR_HUMANARphysical
10903152
RT29_HUMANDAP3physical
10903152
FADD_HUMANFADDphysical
11376335
STML2_HUMANSTOML2physical
22939629
YMEL1_HUMANYME1L1physical
22939629
RT35_HUMANMRPS35physical
26186194
RT10_HUMANMRPS10physical
26186194
WDFY2_HUMANWDFY2physical
26186194
IF2M_HUMANMTIF2physical
26186194
PNM6A_HUMANPNMA6Aphysical
26186194
RT18B_HUMANMRPS18Bphysical
26344197
RT02_HUMANMRPS2physical
26344197
RT22_HUMANMRPS22physical
26344197
RT23_HUMANMRPS23physical
26344197
RT28_HUMANMRPS28physical
26344197
RT05_HUMANMRPS5physical
26344197
RT09_HUMANMRPS9physical
26344197
LYST_HUMANLYSTphysical
26496610
CO4A5_HUMANCOL4A5physical
26496610
KC1D_HUMANCSNK1Dphysical
26496610
MBNL1_HUMANMBNL1physical
26496610
P5CR1_HUMANPYCR1physical
26496610
AP3D1_HUMANAP3D1physical
26496610
POC1A_HUMANPOC1Aphysical
26496610
RT11_HUMANMRPS11physical
26496610
WDFY2_HUMANWDFY2physical
28514442
PNM6A_HUMANPNMA6Aphysical
28514442
RT27_HUMANMRPS27physical
28514442
RT35_HUMANMRPS35physical
28514442
RT10_HUMANMRPS10physical
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 RT29_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-175 AND LYS-207, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-272, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93, AND MASSSPECTROMETRY.

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