ZN552_HUMAN - dbPTM
ZN552_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN552_HUMAN
UniProt AC Q9H707
Protein Name Zinc finger protein 552
Gene Name ZNF552
Organism Homo sapiens (Human).
Sequence Length 407
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MAAAALRFPVQGTVTFEDVAVKFTQEEWNLLSEAQRCLYRDVTLENLALMSSLGCWCGVEDEAAPSKQSIYIQRETQVRTPMAGVSPKKAHPCEMCGPILGDILHVADHQGTHHKQKLHRCEAWGNKLYDSGNFHQHQNEHIGEKPYRGSVEEALFAKRCKLHVSGESSVFSESGKDFLLRSGLLQQEATHTGKSNSKTECVSLFHGGKSHYSCGGCMKHFSTKDILSQHERLLPTEEPSVWCECGKSSSKYDSFSNHQGVHTREKPYTCGICGKLFNSKSHLLVHQRIHTGEKPYECEVCQKFFRHKYHLIAHQRVHTGERPYECSDCGKSFTHSSTFRVHKRVHTGQKPYECSECGKSFAESSSLTKHRRVHTGEKPYGCSECEKKFRQISSLRHHQRVHKRKGL
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
39PhosphorylationSEAQRCLYRDVTLEN
HHHHHHHHCCCCHHH
14.3722210691
43PhosphorylationRCLYRDVTLENLALM
HHHHCCCCHHHHHHH
32.4222210691
51PhosphorylationLENLALMSSLGCWCG
HHHHHHHHHCCCCCC
24.2222210691
80PhosphorylationQRETQVRTPMAGVSP
EEECCCCCCCCCCCC
20.6826853621
86O-linked_GlycosylationRTPMAGVSPKKAHPC
CCCCCCCCCCCCCCC
30.0430379171
86PhosphorylationRTPMAGVSPKKAHPC
CCCCCCCCCCCCCCC
30.0425159151
88SumoylationPMAGVSPKKAHPCEM
CCCCCCCCCCCCCCC
55.90-
88SumoylationPMAGVSPKKAHPCEM
CCCCCCCCCCCCCCC
55.90-
127SumoylationRCEAWGNKLYDSGNF
HHHHHHCCEECCCCC
44.48-
127SumoylationRCEAWGNKLYDSGNF
HHHHHHCCEECCCCC
44.48-
145UbiquitinationQNEHIGEKPYRGSVE
CCCCCCCCCCCCCHH
41.98-
150PhosphorylationGEKPYRGSVEEALFA
CCCCCCCCHHHHHHH
19.8422985185
158UbiquitinationVEEALFAKRCKLHVS
HHHHHHHHHCEEEEC
51.50-
161SumoylationALFAKRCKLHVSGES
HHHHHHCEEEECCCC
45.73-
161SumoylationALFAKRCKLHVSGES
HHHHHHCEEEECCCC
45.73-
165PhosphorylationKRCKLHVSGESSVFS
HHCEEEECCCCHHCC
26.5428555341
168PhosphorylationKLHVSGESSVFSESG
EEEECCCCHHCCCCC
35.0119053533
172PhosphorylationSGESSVFSESGKDFL
CCCCHHCCCCCCHHH
28.7919053533
176SumoylationSVFSESGKDFLLRSG
HHCCCCCCHHHHHCC
55.3728112733
176AcetylationSVFSESGKDFLLRSG
HHCCCCCCHHHHHCC
55.3726051181
176SumoylationSVFSESGKDFLLRSG
HHCCCCCCHHHHHCC
55.37-
194UbiquitinationQEATHTGKSNSKTEC
EECCCCCCCCCCCEE
47.85-
198SumoylationHTGKSNSKTECVSLF
CCCCCCCCCEEEEEE
53.22-
198UbiquitinationHTGKSNSKTECVSLF
CCCCCCCCCEEEEEE
53.22-
198SumoylationHTGKSNSKTECVSLF
CCCCCCCCCEEEEEE
53.2228112733
222PhosphorylationGGCMKHFSTKDILSQ
CCHHHCCCHHHHHHH
33.9822817900
223PhosphorylationGCMKHFSTKDILSQH
CHHHCCCHHHHHHHH
31.6222817900
224UbiquitinationCMKHFSTKDILSQHE
HHHCCCHHHHHHHHH
41.39-
228PhosphorylationFSTKDILSQHERLLP
CCHHHHHHHHHHHCC
29.8022817900
251SumoylationECGKSSSKYDSFSNH
ECCCCCCCCCCCCCC
55.8325218447
251UbiquitinationECGKSSSKYDSFSNH
ECCCCCCCCCCCCCC
55.83-
251SumoylationECGKSSSKYDSFSNH
ECCCCCCCCCCCCCC
55.83-
254PhosphorylationKSSSKYDSFSNHQGV
CCCCCCCCCCCCCCC
27.7328555341
266SumoylationQGVHTREKPYTCGIC
CCCCCCCCCEECCCC
39.78-
266SumoylationQGVHTREKPYTCGIC
CCCCCCCCCEECCCC
39.7825218447
280SumoylationCGKLFNSKSHLLVHQ
CCCCCCCCCCEEEEE
42.89-
280SumoylationCGKLFNSKSHLLVHQ
CCCCCCCCCCEEEEE
42.89-
291PhosphorylationLVHQRIHTGEKPYEC
EEEEEECCCCCCCCC
44.6721712546
308SumoylationCQKFFRHKYHLIAHQ
HHHHHHHCCEEEEEC
30.06-
308SumoylationCQKFFRHKYHLIAHQ
HHHHHHHCCEEEEEC
30.0628112733
309PhosphorylationQKFFRHKYHLIAHQR
HHHHHHCCEEEEECC
8.85-
319PhosphorylationIAHQRVHTGERPYEC
EEECCCCCCCCCEEC
37.5728348404
327PhosphorylationGERPYECSDCGKSFT
CCCCEECCCCCCCEE
24.8128348404
347PhosphorylationRVHKRVHTGQKPYEC
EEECEEECCCCCEEC
38.1528674419
350SumoylationKRVHTGQKPYECSEC
CEEECCCCCEECCCC
51.41-
350SumoylationKRVHTGQKPYECSEC
CEEECCCCCEECCCC
51.41-
369UbiquitinationAESSSLTKHRRVHTG
HHCCCCCCCCCCCCC
40.17-
369SumoylationAESSSLTKHRRVHTG
HHCCCCCCCCCCCCC
40.17-
369SumoylationAESSSLTKHRRVHTG
HHCCCCCCCCCCCCC
40.17-
375PhosphorylationTKHRRVHTGEKPYGC
CCCCCCCCCCCCCCC
44.1528674419
393PhosphorylationEKKFRQISSLRHHQR
HHHHHHHHHHHHHHH
18.2524719451
394PhosphorylationKKFRQISSLRHHQRV
HHHHHHHHHHHHHHH
30.9325954137

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 ZN552_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN552_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 ZN552_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN552_HUMAN !!

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 ZN552_HUMAN

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Related Literatures of Post-Translational Modification

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