QTRT2_HUMAN - dbPTM
QTRT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID QTRT2_HUMAN
UniProt AC Q9H974
Protein Name Queuine tRNA-ribosyltransferase accessory subunit 2 {ECO:0000255|HAMAP-Rule:MF_03043}
Gene Name QTRT2 {ECO:0000255|HAMAP-Rule:MF_03043}
Organism Homo sapiens (Human).
Sequence Length 415
Subcellular Localization Cytoplasm . Mitochondrion outer membrane
Peripheral membrane protein
Cytoplasmic side . May associate with the mitochondrion outer membrane.
Protein Description Non-catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine)..
Protein Sequence MKLSLTKVVNGCRLGKIKNLGKTGDHTMDIPGCLLYTKTGSAPHLTHHTLHNIHGVPAMAQLTLSSLAEHHEVLTEYKEGVGKFIGMPESLLYCSLHDPVSPCPAGYVTNKSVSVWSVAGRVEMTVSKFMAIQKALQPDWFQCLSDGEVSCKEATSIKRVRKSVDRSLLFLDNCLRLQEESEVLQKSVIIGVIEGGDVMEERLRSARETAKRPVGGFLLDGFQGNPTTLEARLRLLSSVTAELPEDKPRLISGVSRPDEVLECIERGVDLFESFFPYQVTERGCALTFSFDYQPNPEETLLQQNGTQEEIKCMDQIKKIETTGCNQEITSFEINLKEKKYQEDFNPLVRGCSCYCCKNHTRAYIHHLLVTNELLAGVLLMMHNFEHYFGFFHYIREALKSDKLAQLKELIHRQAS
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
2Methylation------MKLSLTKVV
------CCCCCCEEE
115976007
4Phosphorylation----MKLSLTKVVNG
----CCCCCCEEECC
24719451
7Ubiquitination-MKLSLTKVVNGCRL
-CCCCCCEEECCEEE
27667366
19UbiquitinationCRLGKIKNLGKTGDH
EEECCCCCCCCCCCC
27667366
29UbiquitinationKTGDHTMDIPGCLLY
CCCCCCCCCCCEEEE
29967540
35UbiquitinationMDIPGCLLYTKTGSA
CCCCCEEEEECCCCC
27667366
46UbiquitinationTGSAPHLTHHTLHNI
CCCCCCCCHHHHCCC
29967540
52UbiquitinationLTHHTLHNIHGVPAM
CCHHHHCCCCCCCHH
27667366
63UbiquitinationVPAMAQLTLSSLAEH
CCHHHHCHHHHHHHH
21963094
72UbiquitinationSSLAEHHEVLTEYKE
HHHHHHHHHHHHHHH
27667366
80UbiquitinationVLTEYKEGVGKFIGM
HHHHHHHCCHHHCCC
21963094
83UbiquitinationEYKEGVGKFIGMPES
HHHHCCHHHCCCCHH
21906983
88UbiquitinationVGKFIGMPESLLYCS
CHHHCCCCHHHEEEC
21890473
88UbiquitinationVGKFIGMPESLLYCS
CHHHCCCCHHHEEEC
21890473
95UbiquitinationPESLLYCSLHDPVSP
CHHHEEECCCCCCCC
29967540
100UbiquitinationYCSLHDPVSPCPAGY
EECCCCCCCCCCCCE
21963094
105UbiquitinationDPVSPCPAGYVTNKS
CCCCCCCCCEECCCC
21890473
105UbiquitinationDPVSPCPAGYVTNKS
CCCCCCCCCEECCCC
21890473
124UbiquitinationSVAGRVEMTVSKFMA
EECEEEEEEHHHHHH
24816145
125UbiquitinationVAGRVEMTVSKFMAI
ECEEEEEEHHHHHHH
21890473
128UbiquitinationRVEMTVSKFMAIQKA
EEEEEHHHHHHHHHH
-
134UbiquitinationSKFMAIQKALQPDWF
HHHHHHHHHHCCCHH
-
141UbiquitinationKALQPDWFQCLSDGE
HHHCCCHHHHCCCCC
24816145
152UbiquitinationSDGEVSCKEATSIKR
CCCCEECCCCCCHHH
29967540
158UbiquitinationCKEATSIKRVRKSVD
CCCCCCHHHHHHHHH
27667366
161UbiquitinationATSIKRVRKSVDRSL
CCCHHHHHHHHHHHH
24816145
164UbiquitinationIKRVRKSVDRSLLFL
HHHHHHHHHHHHHHH
29967540
170UbiquitinationSVDRSLLFLDNCLRL
HHHHHHHHHHHHHHH
27667366
186UbiquitinationEESEVLQKSVIIGVI
HHHHHHHHHHEEEEE
21963094
195UbiquitinationVIIGVIEGGDVMEER
HEEEEEECCHHHHHH
29967540
198UbiquitinationGVIEGGDVMEERLRS
EEEECCHHHHHHHHH
21963094
211UbiquitinationRSARETAKRPVGGFL
HHHHHHHCCCCCEEE
21906983
212UbiquitinationSARETAKRPVGGFLL
HHHHHHCCCCCEEEC
29967540
213UbiquitinationARETAKRPVGGFLLD
HHHHHCCCCCEEECC
29967540
216UbiquitinationTAKRPVGGFLLDGFQ
HHCCCCCEEECCCCC
27667366
223UbiquitinationGFLLDGFQGNPTTLE
EEECCCCCCCCCCHH
21890473
230UbiquitinationQGNPTTLEARLRLLS
CCCCCCHHHHHHHHH
29967540
233UbiquitinationPTTLEARLRLLSSVT
CCCHHHHHHHHHHHC
27667366
237PhosphorylationEARLRLLSSVTAELP
HHHHHHHHHHCCCCC
29255136
238PhosphorylationARLRLLSSVTAELPE
HHHHHHHHHCCCCCC
29255136
240PhosphorylationLRLLSSVTAELPEDK
HHHHHHHCCCCCCCC
29255136
247UbiquitinationTAELPEDKPRLISGV
CCCCCCCCCCEECCC
21906983
253UbiquitinationDKPRLISGVSRPDEV
CCCCEECCCCCHHHH
27667366
259UbiquitinationSGVSRPDEVLECIER
CCCCCHHHHHHHHHH
24816145
279UbiquitinationESFFPYQVTERGCAL
HHHCCEEECCCCEEE
29967540
296UbiquitinationSFDYQPNPEETLLQQ
EECCCCCHHHHHHHC
29967540
318UbiquitinationKCMDQIKKIETTGCN
HHHHHHEEEEECCCC
29967540
330UbiquitinationGCNQEITSFEINLKE
CCCCEEEEEEEECCC
29967540
336UbiquitinationTSFEINLKEKKYQED
EEEEEECCCCHHHHC
29967540
339UbiquitinationEINLKEKKYQEDFNP
EEECCCCHHHHCCCH
21906983
348UbiquitinationQEDFNPLVRGCSCYC
HHCCCHHHCCCEEEE
29967540
351UbiquitinationFNPLVRGCSCYCCKN
CCHHHCCCEEEECCC
27667366
400PhosphorylationYIREALKSDKLAQLK
HHHHHHHHCHHHHHH
20068231
402UbiquitinationREALKSDKLAQLKEL
HHHHHHCHHHHHHHH
21906983
407UbiquitinationSDKLAQLKELIHRQA
HCHHHHHHHHHHHHC
21906983
414UbiquitinationKELIHRQAS------
HHHHHHHCC------
29967540

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 QTRT2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of QTRT2_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 QTRT2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WAC_HUMANWACphysical
22939629
TGT_HUMANQTRT1physical
26344197
MARC1_HUMANMARC1physical
27173435
AGM1_HUMANPGM3physical
27173435
BDH_HUMANBDH1physical
27173435

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of QTRT2_HUMAN

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Related Literatures of Post-Translational Modification

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