RTCA_HUMAN - dbPTM
RTCA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RTCA_HUMAN
UniProt AC O00442
Protein Name RNA 3'-terminal phosphate cyclase
Gene Name RTCA
Organism Homo sapiens (Human).
Sequence Length 366
Subcellular Localization Nucleus, nucleoplasm.
Protein Description Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing..
Protein Sequence MAGPRVEVDGSIMEGGGQILRVSTALSCLLGLPLRVQKIRAGRSTPGLRPQHLSGLEMIRDLCDGQLEGAEIGSTEITFTPEKIKGGIHTADTKTAGSVCLLMQVSMPCVLFAASPSELHLKGGTNAEMAPQIDYTVMVFKPIVEKFGFIFNCDIKTRGYYPKGGGEVIVRMSPVKQLNPINLTERGCVTKIYGRAFVAGVLPFKVAKDMAAAAVRCIRKEIRDLYVNIQPVQEPKDQAFGNGNGIIIIAETSTGCLFAGSSLGKRGVNADKVGIEAAEMLLANLRHGGTVDEYLQDQLIVFMALANGVSRIKTGPVTLHTQTAIHFAEQIAKAKFIVKKSEDEEDAAKDTYIIECQGIGMTNPNL
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
27PhosphorylationLRVSTALSCLLGLPL
EEHHHHHHHHHCCCC		10.56-
28UbiquitinationRVSTALSCLLGLPLR
EHHHHHHHHHCCCCE		3.6527667366
44PhosphorylationQKIRAGRSTPGLRPQ
EEHHCCCCCCCCCHH		37.7328857561
45PhosphorylationKIRAGRSTPGLRPQH
EHHCCCCCCCCCHHH		21.7328857561
49 (in isoform 2)Phosphorylation-34.45-
50 (in isoform 2)Phosphorylation-30.87-
85UbiquitinationTFTPEKIKGGIHTAD
EECHHHCCCCCCCCC		63.2527667366
98UbiquitinationADTKTAGSVCLLMQV
CCCCCCHHHHHHEEE		13.7527667366
99UbiquitinationDTKTAGSVCLLMQVS
CCCCCHHHHHHEEEC		2.3321963094
106UbiquitinationVCLLMQVSMPCVLFA
HHHHEEECCCEEEEE		10.5021890473
141UbiquitinationDYTVMVFKPIVEKFG
CEEEEEEHHHHHHHC		23.56-
154 (in isoform 2)Ubiquitination-46.66-
156AcetylationFIFNCDIKTRGYYPK
EEEECEECCCCCCCC		20.9326051181
156UbiquitinationFIFNCDIKTRGYYPK
EEEECEECCCCCCCC		20.9321963094
160PhosphorylationCDIKTRGYYPKGGGE
CEECCCCCCCCCCCE		17.1928102081
161PhosphorylationDIKTRGYYPKGGGEV
EECCCCCCCCCCCEE		10.9928102081
163 (in isoform 1)Ubiquitination-54.8121890473
163AcetylationKTRGYYPKGGGEVIV
CCCCCCCCCCCEEEE		54.8123954790
163UbiquitinationKTRGYYPKGGGEVIV
CCCCCCCCCCCEEEE		54.8121890473
163UbiquitinationKTRGYYPKGGGEVIV
CCCCCCCCCCCEEEE		54.8127667366
163MalonylationKTRGYYPKGGGEVIV
CCCCCCCCCCCEEEE		54.8126320211
169 (in isoform 2)Ubiquitination-1.10-
169UbiquitinationPKGGGEVIVRMSPVK
CCCCCEEEEECCCCC		1.1021963094
173PhosphorylationGEVIVRMSPVKQLNP
CEEEEECCCCCCCCC		18.9025159151
176UbiquitinationIVRMSPVKQLNPINL
EEECCCCCCCCCCCC		53.0727667366
176UbiquitinationIVRMSPVKQLNPINL
EEECCCCCCCCCCCC		53.0721890473
176 (in isoform 2)Ubiquitination-53.0721890473
184PhosphorylationQLNPINLTERGCVTK
CCCCCCCCCCCCEEE		21.1020068231
189UbiquitinationNLTERGCVTKIYGRA
CCCCCCCEEEEECCH		7.3229967540
189 (in isoform 2)Ubiquitination-7.32-
191AcetylationTERGCVTKIYGRAFV
CCCCCEEEEECCHHH		17.3425953088
191UbiquitinationTERGCVTKIYGRAFV
CCCCCEEEEECCHHH		17.34-
204 (in isoform 2)Ubiquitination-9.69-
205MethylationVAGVLPFKVAKDMAA
HEECCCHHHHHHHHH		39.07115977427
205AcetylationVAGVLPFKVAKDMAA
HEECCCHHHHHHHHH		39.0725953088
208MalonylationVLPFKVAKDMAAAAV
CCCHHHHHHHHHHHH		51.5326320211
208UbiquitinationVLPFKVAKDMAAAAV
CCCHHHHHHHHHHHH		51.5329967540
210SulfoxidationPFKVAKDMAAAAVRC
CHHHHHHHHHHHHHH		2.4230846556
221 (in isoform 2)Ubiquitination-33.15-
221UbiquitinationAVRCIRKEIRDLYVN
HHHHHHHHHHHHCCC		33.1529967540
272UbiquitinationKRGVNADKVGIEAAE
HCCCCHHHHHHHHHH		39.69-
285 (in isoform 2)Ubiquitination-3.39-
314PhosphorylationNGVSRIKTGPVTLHT
CCCCEEECCCEEEEH		44.3329255136
318PhosphorylationRIKTGPVTLHTQTAI
EEECCCEEEEHHHHH		18.8929255136
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 RTCA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RTCA_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 RTCA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL21_HUMANRPL21physical
17353931
FBRL_HUMANFBLphysical
17353931
RL23A_HUMANRPL23Aphysical
17353931
RL18A_HUMANRPL18Aphysical
17353931
DDX21_HUMANDDX21physical
17353931
ZCCHV_HUMANZC3HAV1physical
22939629
HNRH1_HUMANHNRNPH1physical
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 RTCA_HUMAN

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Related Literatures of Post-Translational Modification

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