PUS7L_HUMAN - dbPTM
PUS7L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PUS7L_HUMAN
UniProt AC Q9H0K6
Protein Name Pseudouridylate synthase 7 homolog-like protein
Gene Name PUS7L {ECO:0000312|HGNC:HGNC:25276}
Organism Homo sapiens (Human).
Sequence Length 701
Subcellular Localization
Protein Description Pseudouridylate synthase that catalyzes pseudouridylation of RNAs..
Protein Sequence MEEDTDYRIRFSSLCFFNDHVGFHGTIKSSPSDFIVIEIDEQGQLVNKTIDEPIFKISEIQLEPNNFPKKPKLDLQNLSLEDGRNQEVHTLIKYTDGDQNHQSGSEKEDTIVDGTSKCEEKADVLSSFLDEKTHELLNNFACDVREKWLSKTELIGLPPEFSIGRILDKNQRASLHSAIRQKFPFLVTVGKNSEIVVKPNLEYKELCHLVSEEEAFDFFKYLDAKKENSKFTFKPDTNKDHRKAVHHFVNKKFGNLVETKSFSKMNCSAGNPNVVVTVRFREKAHKRGKRPLSECQEGKVIYTAFTLRKENLEMFEAIGFLAIKLGVIPSDFSYAGLKDKKAITYQAMVVRKVTPERLKNIEKEIEKKRMNVFNIRSVDDSLRLGQLKGNHFDIVIRNLKKQINDSANLRERIMEAIENVKKKGFVNYYGPQRFGKGRKVHTDQIGLALLKNEMMKAIKLFLTPEDLDDPVNRAKKYFLQTEDAKGTLSLMPEFKVRERALLEALHRFGMTEEGCIQAWFSLPHSMRIFYVHAYTSKIWNEAVSYRLETYGARVVQGDLVCLDEDIDDENFPNSKIHLVTEEEGSANMYAIHQVVLPVLGYNIQYPKNKVGQWYHDILSRDGLQTCRFKVPTLKLNIPGCYRQILKHPCNLSYQLMEDHDIDVKTKGSHIDETALSLLISFDLDASCYATVCLKEIMKHDV
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
5Phosphorylation---MEEDTDYRIRFS
---CCCCCCCEEEEE
37.90-
25UbiquitinationNDHVGFHGTIKSSPS
CCCCEECCEECCCCC
27.2029967540
28UbiquitinationVGFHGTIKSSPSDFI
CEECCEECCCCCCEE
44.72-
49PhosphorylationQGQLVNKTIDEPIFK
CCCEECCCCCCCCEE
28.58-
54UbiquitinationNKTIDEPIFKISEIQ
CCCCCCCCEEEEEEE
5.3024816145
56UbiquitinationTIDEPIFKISEIQLE
CCCCCCEEEEEEECC
46.1529967540
75UbiquitinationPKKPKLDLQNLSLED
CCCCCCCCCCCCCCC
5.43-
79PhosphorylationKLDLQNLSLEDGRNQ
CCCCCCCCCCCCCCC
36.9425159151
88UbiquitinationEDGRNQEVHTLIKYT
CCCCCCEEEEEEEEC
2.77-
88UbiquitinationEDGRNQEVHTLIKYT
CCCCCCEEEEEEEEC
2.7729967540
94PhosphorylationEVHTLIKYTDGDQNH
EEEEEEEECCCCCCC
11.7628450419
95PhosphorylationVHTLIKYTDGDQNHQ
EEEEEEECCCCCCCC
28.6228450419
103PhosphorylationDGDQNHQSGSEKEDT
CCCCCCCCCCCCCCE
36.4128450419
105PhosphorylationDQNHQSGSEKEDTIV
CCCCCCCCCCCCEEC
51.2228450419
108UbiquitinationHQSGSEKEDTIVDGT
CCCCCCCCCEECCCC
57.23-
110PhosphorylationSGSEKEDTIVDGTSK
CCCCCCCEECCCCCH
24.8023186163
110UbiquitinationSGSEKEDTIVDGTSK
CCCCCCCEECCCCCH
24.80-
121UbiquitinationGTSKCEEKADVLSSF
CCCHHHHHHHHHHHH
27.8229967540
127PhosphorylationEKADVLSSFLDEKTH
HHHHHHHHHHCHHHH
26.1821082442
146UbiquitinationNFACDVREKWLSKTE
HHCCHHHHHHHHHCH
48.7229967540
163UbiquitinationGLPPEFSIGRILDKN
CCCCCCCHHHHCCCC
5.3729967540
172UbiquitinationRILDKNQRASLHSAI
HHCCCCHHHHHHHHH
35.22-
261PhosphorylationGNLVETKSFSKMNCS
CCEEECCCCCCCCCC
42.0224719451
264MethylationVETKSFSKMNCSAGN
EECCCCCCCCCCCCC
31.93115975943
293PhosphorylationKRGKRPLSECQEGKV
HCCCCCHHHHHCCCC
38.7225159151
306PhosphorylationKVIYTAFTLRKENLE
CCEEEEEEECHHHHH
24.1624719451
321UbiquitinationMFEAIGFLAIKLGVI
HHHHHHHHHHHHCCC
3.98-
338UbiquitinationDFSYAGLKDKKAITY
CCCCCCCCCCCCEEE
67.5929967540
341UbiquitinationYAGLKDKKAITYQAM
CCCCCCCCCEEEEEE
55.97-
341AcetylationYAGLKDKKAITYQAM
CCCCCCCCCEEEEEE
55.9724888479
344PhosphorylationLKDKKAITYQAMVVR
CCCCCCEEEEEEEEE
17.9122210691
345PhosphorylationKDKKAITYQAMVVRK
CCCCCEEEEEEEEEC
6.5322210691
352AcetylationYQAMVVRKVTPERLK
EEEEEEECCCHHHHH
38.5624888487
367UbiquitinationNIEKEIEKKRMNVFN
HHHHHHHHHCCCCCC
51.8724816145
376UbiquitinationRMNVFNIRSVDDSLR
CCCCCCCCCCCCCCC
31.5624816145
377PhosphorylationMNVFNIRSVDDSLRL
CCCCCCCCCCCCCCH
26.5429396449
379UbiquitinationVFNIRSVDDSLRLGQ
CCCCCCCCCCCCHHC
40.8224816145
381PhosphorylationNIRSVDDSLRLGQLK
CCCCCCCCCCHHCCC
15.7829396449
388UbiquitinationSLRLGQLKGNHFDIV
CCCHHCCCCCHHHHH
50.18-
388MethylationSLRLGQLKGNHFDIV
CCCHHCCCCCHHHHH
50.18115975949
401UbiquitinationIVIRNLKKQINDSAN
HHHHHHHHHCCCCHH
60.6229967540
421UbiquitinationMEAIENVKKKGFVNY
HHHHHHHHHCCCCCC
61.42-
422UbiquitinationEAIENVKKKGFVNYY
HHHHHHHHCCCCCCC
54.57-
423UbiquitinationAIENVKKKGFVNYYG
HHHHHHHCCCCCCCC
52.44-
428PhosphorylationKKKGFVNYYGPQRFG
HHCCCCCCCCCCCCC
12.42-
429PhosphorylationKKGFVNYYGPQRFGK
HCCCCCCCCCCCCCC
19.6829496907
459UbiquitinationNEMMKAIKLFLTPED
HHHHHHHHHHCCHHH
37.7429967540
476UbiquitinationDPVNRAKKYFLQTED
CHHHHHHHHHCCCCC
40.0029967540
485UbiquitinationFLQTEDAKGTLSLMP
HCCCCCCCCCCCCCC
65.82-
489PhosphorylationEDAKGTLSLMPEFKV
CCCCCCCCCCCCHHH
23.59-
614PhosphorylationKNKVGQWYHDILSRD
CCCCCHHHHHHHCCC
5.0330206219
619PhosphorylationQWYHDILSRDGLQTC
HHHHHHHCCCCCCCC
28.7630206219
625PhosphorylationLSRDGLQTCRFKVPT
HCCCCCCCCEEECCC
15.6430206219
634UbiquitinationRFKVPTLKLNIPGCY
EEECCCEECCCCCHH
41.80-

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 PUS7L_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PUS7L_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 PUS7L_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
TRI41_HUMANTRIM41physical
25416956

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PUS7L_HUMAN

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Related Literatures of Post-Translational Modification

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