PUS7_HUMAN - dbPTM
PUS7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PUS7_HUMAN
UniProt AC Q96PZ0
Protein Name Pseudouridylate synthase 7 homolog {ECO:0000305}
Gene Name PUS7 {ECO:0000312|HGNC:HGNC:26033}
Organism Homo sapiens (Human).
Sequence Length 661
Subcellular Localization Nucleus .
Protein Description Pseudouridylate synthase that catalyzes pseudouridylation of RNAs. [PubMed: 28073919]
Protein Sequence MEMTEMTGVSLKRGALVVEDNDSGVPVEETKKQKLSECSLTKGQDGLQNDFLSISEDVPRPPDTVSTGKGGKNSEAQLEDEEEEEEDGLSEECEEEESESFADMMKHGLTEADVGITKFVSSHQGFSGILKERYSDFVVHEIGKDGRISHLNDLSIPVDEEDPSEDIFTVLTAEEKQRLEELQLFKNKETSVAIEVIEDTKEKRTIIHQAIKSLFPGLETKTEDREGKKYIVAYHAAGKKALANPRKHSWPKSRGSYCHFVLYKENKDTMDAINVLSKYLRVKPNIFSYMGTKDKRAITVQEIAVLKITAQRLAHLNKCLMNFKLGNFSYQKNPLKLGELQGNHFTVVLRNITGTDDQVQQAMNSLKEIGFINYYGMQRFGTTAVPTYQVGRAILQNSWTEVMDLILKPRSGAEKGYLVKCREEWAKTKDPTAALRKLPVKRCVEGQLLRGLSKYGMKNIVSAFGIIPRNNRLMYIHSYQSYVWNNMVSKRIEDYGLKPVPGDLVLKGATATYIEEDDVNNYSIHDVVMPLPGFDVIYPKHKIQEAYREMLTADNLDIDNMRHKIRDYSLSGAYRKIIIRPQNVSWEVVAYDDPKIPLFNTDVDNLEGKTPPVFASEGKYRALKMDFSLPPSTYATMAIREVLKMDTSIKNQTQLNTTWLR
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
1Acetylation-------MEMTEMTG
-------CCCCCCCC
7.7822814378
4O-linked_Glycosylation----MEMTEMTGVSL
----CCCCCCCCEEE
14.8630379171
10PhosphorylationMTEMTGVSLKRGALV
CCCCCCEEEECCEEE
29.5324114839
13MethylationMTGVSLKRGALVVED
CCCEEEECCEEEEEE
40.69115489675
23PhosphorylationLVVEDNDSGVPVEET
EEEEECCCCCCCHHH
48.2025159151
31AcetylationGVPVEETKKQKLSEC
CCCCHHHHHCCHHHC
57.3926051181
36PhosphorylationETKKQKLSECSLTKG
HHHHCCHHHCCCCCC
43.5220873877
39PhosphorylationKQKLSECSLTKGQDG
HCCHHHCCCCCCCCC
34.7121815630
41PhosphorylationKLSECSLTKGQDGLQ
CHHHCCCCCCCCCCC
19.4825850435
53PhosphorylationGLQNDFLSISEDVPR
CCCCCCCCCCCCCCC
24.8627251275
55PhosphorylationQNDFLSISEDVPRPP
CCCCCCCCCCCCCCC
25.1128348404
64PhosphorylationDVPRPPDTVSTGKGG
CCCCCCCCCCCCCCC
23.3325159151
66PhosphorylationPRPPDTVSTGKGGKN
CCCCCCCCCCCCCCC
33.2730576142
67PhosphorylationRPPDTVSTGKGGKNS
CCCCCCCCCCCCCCC
38.2827732954
69AcetylationPDTVSTGKGGKNSEA
CCCCCCCCCCCCCCC
65.6625953088
74PhosphorylationTGKGGKNSEAQLEDE
CCCCCCCCCCCCCCH
37.4830576142
90PhosphorylationEEEEDGLSEECEEEE
HHHHCCCCHHHHHHH
36.5627422710
98PhosphorylationEECEEEESESFADMM
HHHHHHHHHHHHHHH
41.6522210691
100PhosphorylationCEEEESESFADMMKH
HHHHHHHHHHHHHHC
34.7122210691
118AcetylationEADVGITKFVSSHQG
HHHHCHHHHHHCCCC
41.6826051181
121PhosphorylationVGITKFVSSHQGFSG
HCHHHHHHCCCCCCH
25.8225159151
122PhosphorylationGITKFVSSHQGFSGI
CHHHHHHCCCCCCHH
17.9625627689
127PhosphorylationVSSHQGFSGILKERY
HHCCCCCCHHHHHHH
31.5825159151
131AcetylationQGFSGILKERYSDFV
CCCCHHHHHHHCCEE
37.9219608861
134PhosphorylationSGILKERYSDFVVHE
CHHHHHHHCCEEEEE
17.4329214152
135PhosphorylationGILKERYSDFVVHEI
HHHHHHHCCEEEEEC
30.6928555341
144UbiquitinationFVVHEIGKDGRISHL
EEEEECCCCCCCEEC
63.77-
144AcetylationFVVHEIGKDGRISHL
EEEEECCCCCCCEEC
63.7725953088
155PhosphorylationISHLNDLSIPVDEED
CEECCCCCCCCCCCC
27.9225159151
176UbiquitinationTVLTAEEKQRLEELQ
EEEEHHHHHHHHHHH
32.0221890473
190PhosphorylationQLFKNKETSVAIEVI
HHHCCCCCCEEEEEE
30.0626074081
191PhosphorylationLFKNKETSVAIEVIE
HHCCCCCCEEEEEEC
15.6126074081
200PhosphorylationAIEVIEDTKEKRTII
EEEEECCCCHHHHHH
28.4526074081
213PhosphorylationIIHQAIKSLFPGLET
HHHHHHHHHCCCCCC
29.1821406692
220PhosphorylationSLFPGLETKTEDREG
HHCCCCCCCCCCCCC
48.5921406692
221UbiquitinationLFPGLETKTEDREGK
HCCCCCCCCCCCCCC
40.31-
230PhosphorylationEDREGKKYIVAYHAA
CCCCCCEEEEEEECC
12.2420068231
234PhosphorylationGKKYIVAYHAAGKKA
CCEEEEEEECCCHHH
4.9020068231
239AcetylationVAYHAAGKKALANPR
EEEECCCHHHHCCCC
30.1026051181
249PhosphorylationLANPRKHSWPKSRGS
HCCCCCCCCCCCCCC
48.3826091039
254MethylationKHSWPKSRGSYCHFV
CCCCCCCCCCEEEEE
44.17115489683
263PhosphorylationSYCHFVLYKENKDTM
CEEEEEEEECCCCHH
15.7922817900
269PhosphorylationLYKENKDTMDAINVL
EEECCCCHHHHHHHH
20.6829116813
270SulfoxidationYKENKDTMDAINVLS
EECCCCHHHHHHHHH
4.7421406390
277PhosphorylationMDAINVLSKYLRVKP
HHHHHHHHHHHCCCC
18.2529116813
278UbiquitinationDAINVLSKYLRVKPN
HHHHHHHHHHCCCCC
44.1121906983
279PhosphorylationAINVLSKYLRVKPNI
HHHHHHHHHCCCCCC
9.0729116813
292PhosphorylationNIFSYMGTKDKRAIT
CCHHHCCCCCCCCEE
21.3829116813
318AcetylationQRLAHLNKCLMNFKL
HHHHHHHHHHHHCCC
34.8025953088
318UbiquitinationQRLAHLNKCLMNFKL
HHHHHHHHHHHHCCC
34.8021906983
324UbiquitinationNKCLMNFKLGNFSYQ
HHHHHHCCCCCCCCC
50.9421906983
332UbiquitinationLGNFSYQKNPLKLGE
CCCCCCCCCCCCCCC
52.91-
353PhosphorylationTVVLRNITGTDDQVQ
EEEEEECCCCHHHHH
37.2621406692
355PhosphorylationVLRNITGTDDQVQQA
EEEECCCCHHHHHHH
27.9621406692
365PhosphorylationQVQQAMNSLKEIGFI
HHHHHHHHHHHHCCE
27.9421406692
403SulfoxidationQNSWTEVMDLILKPR
HCCHHHHHHHHHCCC
2.5628183972
411PhosphorylationDLILKPRSGAEKGYL
HHHHCCCCCCCCCEE
51.3822210691
415UbiquitinationKPRSGAEKGYLVKCR
CCCCCCCCCEEEEEH
52.93-
420UbiquitinationAEKGYLVKCREEWAK
CCCCEEEEEHHHHHH
25.61-
450MethylationCVEGQLLRGLSKYGM
HHHHHHHHHHHHHCC
53.2330988967
455PhosphorylationLLRGLSKYGMKNIVS
HHHHHHHHCCCHHHH
21.0523532336
462PhosphorylationYGMKNIVSAFGIIPR
HCCCHHHHHHCEECC
17.6822199227
475PhosphorylationPRNNRLMYIHSYQSY
CCCCEEEEEEEEHHH
10.48-
479PhosphorylationRLMYIHSYQSYVWNN
EEEEEEEEHHHHHHH
6.31-
482PhosphorylationYIHSYQSYVWNNMVS
EEEEEHHHHHHHHHC
8.24-
495PhosphorylationVSKRIEDYGLKPVPG
HCHHHHHCCCCCCCC
16.15-
542UbiquitinationDVIYPKHKIQEAYRE
CEEECHHHHHHHHHH
52.81-
550SulfoxidationIQEAYREMLTADNLD
HHHHHHHHHHCCCCC
2.7421406390
568PhosphorylationMRHKIRDYSLSGAYR
HHHHHHHCCCCCCEE
11.1520068231
569PhosphorylationRHKIRDYSLSGAYRK
HHHHHHCCCCCCEEE
21.9820068231
571PhosphorylationKIRDYSLSGAYRKII
HHHHCCCCCCEEEEE
18.5520068231
574PhosphorylationDYSLSGAYRKIIIRP
HCCCCCCEEEEEECC
18.9020068231
585PhosphorylationIIRPQNVSWEVVAYD
EECCCCEEEEEEEEC
25.6822210691
601PhosphorylationPKIPLFNTDVDNLEG
CCCCCCCCCCHHCCC
30.0228176443
609SumoylationDVDNLEGKTPPVFAS
CCHHCCCCCCCCCCC
48.78-
609UbiquitinationDVDNLEGKTPPVFAS
CCHHCCCCCCCCCCC
48.78-
610PhosphorylationVDNLEGKTPPVFASE
CHHCCCCCCCCCCCC
43.6229255136
616PhosphorylationKTPPVFASEGKYRAL
CCCCCCCCCCCEEEE
35.1028176443
619SumoylationPVFASEGKYRALKMD
CCCCCCCCEEEEECC
27.75-
619SumoylationPVFASEGKYRALKMD
CCCCCCCCEEEEECC
27.75-
619UbiquitinationPVFASEGKYRALKMD
CCCCCCCCEEEEECC
27.75-
619AcetylationPVFASEGKYRALKMD
CCCCCCCCEEEEECC
27.7523954790
628PhosphorylationRALKMDFSLPPSTYA
EEEECCCCCCHHHHH
35.38-
648PhosphorylationEVLKMDTSIKNQTQL
HHHCCCCCCCCCCCC
27.5725003641
657PhosphorylationKNQTQLNTTWLR---
CCCCCCCCCCCC---
28.1323186163
658PhosphorylationNQTQLNTTWLR----
CCCCCCCCCCC----
22.7925159151
661MethylationQLNTTWLR-------
CCCCCCCC-------
35.73115489667

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 PUS7_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PUS7_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 PUS7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WDR74_HUMANWDR74physical
22939629
HS105_HUMANHSPH1physical
22863883
STAT3_HUMANSTAT3physical
22863883
ACO13_HUMANACOT13physical
26344197
ACTN4_HUMANACTN4physical
26344197
BYST_HUMANBYSLphysical
26344197
DDX3X_HUMANDDX3Xphysical
26344197
DHX15_HUMANDHX15physical
26344197
DHX16_HUMANDHX16physical
26344197
DOHH_HUMANDOHHphysical
26344197
IF4G1_HUMANEIF4G1physical
26344197
IF4G3_HUMANEIF4G3physical
26344197
ENOPH_HUMANENOPH1physical
26344197
MCM3_HUMANMCM3physical
26344197
MCM5_HUMANMCM5physical
26344197
NH2L1_HUMANNHP2L1physical
26344197
NOC3L_HUMANNOC3Lphysical
26344197
NSUN2_HUMANNSUN2physical
26344197
RPB4_HUMANPOLR2Dphysical
26344197
RPB7_HUMANPOLR2Gphysical
26344197
RBM8A_HUMANRBM8Aphysical
26344197
LA_HUMANSSBphysical
26344197
ZO2_HUMANTJP2physical
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 PUS7_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
"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-131, AND MASS SPECTROMETRY.
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 THR-610, AND MASSSPECTROMETRY.

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