RTCB_HUMAN - dbPTM
RTCB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RTCB_HUMAN
UniProt AC Q9Y3I0
Protein Name tRNA-splicing ligase RtcB homolog {ECO:0000255|HAMAP-Rule:MF_03144}
Gene Name RTCB {ECO:0000255|HAMAP-Rule:MF_03144}
Organism Homo sapiens (Human).
Sequence Length 505
Subcellular Localization Nucleus . Cytoplasm . Enters into the nucleus in case of active transcription while it accumulates in cytosol when transcription level is low.
Protein Description Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'-phosphodiester. May act as an RNA ligase with broad substrate specificity, and may function toward other RNAs..
Protein Sequence MSRSYNDELQFLEKINKNCWRIKKGFVPNMQVEGVFYVNDALEKLMFEELRNACRGGGVGGFLPAMKQIGNVAALPGIVHRSIGLPDVHSGYGFAIGNMAAFDMNDPEAVVSPGGVGFDINCGVRLLRTNLDESDVQPVKEQLAQAMFDHIPVGVGSKGVIPMNAKDLEEALEMGVDWSLREGYAWAEDKEHCEEYGRMLQADPNKVSARAKKRGLPQLGTLGAGNHYAEIQVVDEIFNEYAAKKMGIDHKGQVCVMIHSGSRGLGHQVATDALVAMEKAMKRDKIIVNDRQLACARIASPEGQDYLKGMAAAGNYAWVNRSSMTFLTRQAFAKVFNTTPDDLDLHVIYDVSHNIAKVEQHVVDGKERTLLVHRKGSTRAFPPHHPLIAVDYQLTGQPVLIGGTMGTCSYVLTGTEQGMTETFGTTCHGAGRALSRAKSRRNLDFQDVLDKLADMGIAIRVASPKLVMEEAPESYKNVTDVVNTCHDAGISKKAIKLRPIAVIKG
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------MSRSYNDEL
------CCCCHHHHH		29.9019413330
2Phosphorylation------MSRSYNDEL
------CCCCHHHHH		29.9025627689
4Phosphorylation----MSRSYNDELQF
----CCCCHHHHHHH		22.4528152594
5Phosphorylation---MSRSYNDELQFL
---CCCCHHHHHHHH		26.0628152594
14AcetylationDELQFLEKINKNCWR
HHHHHHHHHHHHCCH		54.4425953088
14UbiquitinationDELQFLEKINKNCWR
HHHHHHHHHHHHCCH		54.4423000965
17AcetylationQFLEKINKNCWRIKK
HHHHHHHHHCCHHCC		57.8826051181
17UbiquitinationQFLEKINKNCWRIKK
HHHHHHHHHCCHHCC		57.8823000965
23UbiquitinationNKNCWRIKKGFVPNM
HHHCCHHCCCCCCCC		37.9723000965
44UbiquitinationYVNDALEKLMFEELR
ECHHHHHHHHHHHHH		46.2117623298
46SulfoxidationNDALEKLMFEELRNA
HHHHHHHHHHHHHHH		6.1821406390
51MethylationKLMFEELRNACRGGG
HHHHHHHHHHHCCCC		31.79115492975
66SulfoxidationVGGFLPAMKQIGNVA
CCCHHHHHHHHCCCC		2.8721406390
67AcetylationGGFLPAMKQIGNVAA
CCHHHHHHHHCCCCC		40.6525953088
67UbiquitinationGGFLPAMKQIGNVAA
CCHHHHHHHHCCCCC		40.6523000965
81DimethylationALPGIVHRSIGLPDV
CCCCCHHHHCCCCCC		21.05-
81MethylationALPGIVHRSIGLPDV
CCCCCHHHHCCCCCC		21.0530761963
134PhosphorylationLRTNLDESDVQPVKE
EECCCCHHHCHHHHH		42.6321815630
140UbiquitinationESDVQPVKEQLAQAM
HHHCHHHHHHHHHHH		46.5621906983
140AcetylationESDVQPVKEQLAQAM
HHHCHHHHHHHHHHH		46.5626051181
158UbiquitinationIPVGVGSKGVIPMNA
CCCCCCCCCCCCCCH		51.7921906983
158AcetylationIPVGVGSKGVIPMNA
CCCCCCCCCCCCCCH		51.7926051181
174SulfoxidationDLEEALEMGVDWSLR
HHHHHHHHCCCHHHH		7.0630846556
179PhosphorylationLEMGVDWSLREGYAW
HHHCCCHHHHCCCCC		17.0624719451
184PhosphorylationDWSLREGYAWAEDKE
CHHHHCCCCCCCCHH		8.3329496907
190AcetylationGYAWAEDKEHCEEYG
CCCCCCCHHHHHHHH		40.6426822725
190UbiquitinationGYAWAEDKEHCEEYG
CCCCCCCHHHHHHHH		40.6421963094
196PhosphorylationDKEHCEEYGRMLQAD
CHHHHHHHHHHHHCC		6.4229496907
199SulfoxidationHCEEYGRMLQADPNK
HHHHHHHHHHCCCCH		2.5621406390
2062-HydroxyisobutyrylationMLQADPNKVSARAKK
HHHCCCCHHHHHHHH		42.85-
206AcetylationMLQADPNKVSARAKK
HHHCCCCHHHHHHHH		42.8526051181
206UbiquitinationMLQADPNKVSARAKK
HHHCCCCHHHHHHHH		42.8521906983
228PhosphorylationTLGAGNHYAEIQVVD
CCCCCCCCEEEEEHH		15.2127642862
241PhosphorylationVDEIFNEYAAKKMGI
HHHHHHHHHHHHCCC		16.9827642862
244UbiquitinationIFNEYAAKKMGIDHK
HHHHHHHHHCCCCCC		34.8132015554
245UbiquitinationFNEYAAKKMGIDHKG
HHHHHHHHCCCCCCC		37.3229967540
255GlutathionylationIDHKGQVCVMIHSGS
CCCCCCEEEEEECCC		1.0122555962
279UbiquitinationDALVAMEKAMKRDKI
HHHHHHHHHHHCCCE		40.4732015554
279AcetylationDALVAMEKAMKRDKI
HHHHHHHHHHHCCCE		40.4725953088
2852-HydroxyisobutyrylationEKAMKRDKIIVNDRQ
HHHHHCCCEEECCHH		38.06-
285MalonylationEKAMKRDKIIVNDRQ
HHHHHCCCEEECCHH		38.0626320211
285AcetylationEKAMKRDKIIVNDRQ
HHHHHCCCEEECCHH		38.0623749302
285UbiquitinationEKAMKRDKIIVNDRQ
HHHHHCCCEEECCHH		38.0629967540
291MethylationDKIIVNDRQLACARI
CCEEECCHHHHHHHH		28.36115492967
300PhosphorylationLACARIASPEGQDYL
HHHHHHCCCCCHHHH		22.5525159151
306PhosphorylationASPEGQDYLKGMAAA
CCCCCHHHHHHHHHC		11.48-
308AcetylationPEGQDYLKGMAAAGN
CCCHHHHHHHHHCCC		40.1726051181
308UbiquitinationPEGQDYLKGMAAAGN
CCCHHHHHHHHHCCC		40.1721906983
310SulfoxidationGQDYLKGMAAAGNYA
CHHHHHHHHHCCCEE		1.8830846556
316PhosphorylationGMAAAGNYAWVNRSS
HHHHCCCEEEECCHH		10.8326074081
322PhosphorylationNYAWVNRSSMTFLTR
CEEEECCHHCHHHHH		21.1826074081
323PhosphorylationYAWVNRSSMTFLTRQ
EEEECCHHCHHHHHH		20.7126074081
325PhosphorylationWVNRSSMTFLTRQAF
EECCHHCHHHHHHHH		19.9026074081
328PhosphorylationRSSMTFLTRQAFAKV
CHHCHHHHHHHHHHH		19.2826074081
334UbiquitinationLTRQAFAKVFNTTPD
HHHHHHHHHHCCCCC		40.69-
349PhosphorylationDLDLHVIYDVSHNIA
CCCEEEEEECCCCEE		14.8128796482
352PhosphorylationLHVIYDVSHNIAKVE
EEEEEECCCCEEEEE		14.1228796482
357UbiquitinationDVSHNIAKVEQHVVD
ECCCCEEEEEEEEEC		42.3729967540
366AcetylationEQHVVDGKERTLLVH
EEEEECCCEEEEEEE		39.2926051181
3662-HydroxyisobutyrylationEQHVVDGKERTLLVH
EEEEECCCEEEEEEE		39.29-
366UbiquitinationEQHVVDGKERTLLVH
EEEEECCCEEEEEEE		39.2921906983
369PhosphorylationVVDGKERTLLVHRKG
EECCCEEEEEEECCC		26.0723312004
439PhosphorylationRALSRAKSRRNLDFQ
HHHHHHHHHCCCCHH		35.1729514088
455SulfoxidationVLDKLADMGIAIRVA
HHHHHHHCCEEEEEC		3.3021406390
465AcetylationAIRVASPKLVMEEAP
EEEECCCHHHHCCCC		51.7426051181
465UbiquitinationAIRVASPKLVMEEAP
EEEECCCHHHHCCCC		51.7423000965
468SulfoxidationVASPKLVMEEAPESY
ECCCHHHHCCCCHHH		5.8130846556
474PhosphorylationVMEEAPESYKNVTDV
HHCCCCHHHCCHHHH		40.1123401153
475PhosphorylationMEEAPESYKNVTDVV
HCCCCHHHCCHHHHH		12.6221406692
476UbiquitinationEEAPESYKNVTDVVN
CCCCHHHCCHHHHHH		54.9722505724
476AcetylationEEAPESYKNVTDVVN
CCCCHHHCCHHHHHH		54.9726051181
485GlutathionylationVTDVVNTCHDAGISK
HHHHHHHHHHCCCCH		2.0022555962
492AcetylationCHDAGISKKAIKLRP
HHHCCCCHHHEECEE		44.2825953088
492UbiquitinationCHDAGISKKAIKLRP
HHHCCCCHHHEECEE		44.2823000965
4922-HydroxyisobutyrylationCHDAGISKKAIKLRP
HHHCCCCHHHEECEE		44.28-
493UbiquitinationHDAGISKKAIKLRPI
HHCCCCHHHEECEEE		48.8623000965
496SumoylationGISKKAIKLRPIAVI
CCCHHHEECEEEEEE		43.2228112733
496UbiquitinationGISKKAIKLRPIAVI
CCCHHHEECEEEEEE		43.2223000965
496AcetylationGISKKAIKLRPIAVI
CCCHHHEECEEEEEE		43.2223954790
496MalonylationGISKKAIKLRPIAVI
CCCHHHEECEEEEEE		43.2226320211
504UbiquitinationLRPIAVIKG------
CEEEEEECC------		52.5527667366
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 RTCB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RTCB_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 RTCB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDX1_HUMANDDX1physical
22939629
FA98B_HUMANFAM98Bphysical
22939629
ABCF1_HUMANABCF1physical
22863883
CN166_HUMANC14orf166physical
22863883
HNRPM_HUMANHNRNPMphysical
22863883
IF2B3_HUMANIGF2BP3physical
22863883
ILF2_HUMANILF2physical
22863883
MRE11_HUMANMRE11Aphysical
22863883
NMT1_HUMANNMT1physical
22863883
RPAC1_HUMANPOLR1Cphysical
22863883
PRKDC_HUMANPRKDCphysical
22863883
SYQ_HUMANQARSphysical
22863883
RFC2_HUMANRFC2physical
22863883
RFC4_HUMANRFC4physical
22863883
RL26L_HUMANRPL26L1physical
22863883
RL27_HUMANRPL27physical
22863883
CN166_HUMANC14orf166physical
26344197
CCD22_HUMANCCDC22physical
26344197
DPH2_HUMANDPH2physical
26344197
FA98B_HUMANFAM98Bphysical
26344197
HNRH1_HUMANHNRNPH1physical
26344197
HNRPM_HUMANHNRNPMphysical
26344197
ECM29_HUMANKIAA0368physical
26344197
MTMRC_HUMANMTMR12physical
26344197
NDRG1_HUMANNDRG1physical
26344197
PP1R8_HUMANPPP1R8physical
26344197
RAVR1_HUMANRAVER1physical
26344197
WDR12_HUMANWDR12physical
26344197
DP13A_HUMANAPPL1physical
25814554
HDAC1_HUMANHDAC1physical
27173435
XYLT2_HUMANXYLT2physical
27173435
MTA2_HUMANMTA2physical
27173435
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 RTCB_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-496, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND MASSSPECTROMETRY.

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