ZN417_HUMAN - dbPTM
ZN417_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN417_HUMAN
UniProt AC Q8TAU3
Protein Name Zinc finger protein 417
Gene Name ZNF417
Organism Homo sapiens (Human).
Sequence Length 575
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MAAAAPRRPTQQGTVTFEDVAVNFSQEEWCLLSEAQRCLYRDVMLENLALISSLGCWCGSKDEEAPCKQRISVQRESQSRTPRAGVSPKKAHPCEMCGLILEDVFHFADHQETHHKQKLNRSGACGKNLDDTAYLHQHQKQHIGEKFYRKSVREASFVKKRKLRVSQEPFVFREFGKDVLPSSGLCQEAAAVEKTDSETMHGPPFQEGKTNYSCGKRTKAFSTKHSVIPHQKLFTRDGCYVCSDCGKSFSRYVSFSNHQRDHTAKGPYDCGECGKSYSRKSSLIQHQRVHTGKTAYPCEECGKSFSQKGSLISHQRVHTGERPYECREYGKSFGQKGNLIQHQQGHTGERAYHCGECGKSFRQKFCFINHQRVHTGERPYKCGECGKSFGQKGNLVQHQRGHTGERPYECKECGKSFRYRSHLTEHQRLHTGERPYNCRECGKLFNRKYHLLVHERVHTGERPYACEVCGKLFGNKNCVTIHQRIHTGERPYECNECGKSFLSSSALHVHKRVHSGQKPYKCSECGKSFAECSSLIKHRRIHTGERPYECTKCGKTFQRSSTLLHHQSSHRRKAL
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
77PhosphorylationRISVQRESQSRTPRA
CEEEHHHHHCCCCCC
35.3328555341
81PhosphorylationQRESQSRTPRAGVSP
HHHHHCCCCCCCCCC
23.5228555341
127UbiquitinationNRSGACGKNLDDTAY
CCCCCCCCCCCCHHH
54.97-
132PhosphorylationCGKNLDDTAYLHQHQ
CCCCCCCHHHHHHHH
19.5028555341
140UbiquitinationAYLHQHQKQHIGEKF
HHHHHHHHHHHHHHH
41.54-
159AcetylationVREASFVKKRKLRVS
HHHHHHEECCCCCCC
44.8730593733
160AcetylationREASFVKKRKLRVSQ
HHHHHEECCCCCCCC
49.847366067
166PhosphorylationKKRKLRVSQEPFVFR
ECCCCCCCCCCCHHH
23.5328555341
224UbiquitinationRTKAFSTKHSVIPHQ
CCCCCCCCCCCCCCC
32.46-
232SumoylationHSVIPHQKLFTRDGC
CCCCCCCCCCCCCCE
42.40-
232UbiquitinationHSVIPHQKLFTRDGC
CCCCCCCCCCCCCCE
42.40-
232SumoylationHSVIPHQKLFTRDGC
CCCCCCCCCCCCCCE
42.40-
250PhosphorylationSDCGKSFSRYVSFSN
CCCCCCHHHEEECCC
29.7717081983
254PhosphorylationKSFSRYVSFSNHQRD
CCHHHEEECCCCCCC
17.6427251275
280SumoylationCGKSYSRKSSLIQHQ
CCCCCCCCCCCCCCC
38.16-
280UbiquitinationCGKSYSRKSSLIQHQ
CCCCCCCCCCCCCCC
38.16-
280SumoylationCGKSYSRKSSLIQHQ
CCCCCCCCCCCCCCC
38.16-
281PhosphorylationGKSYSRKSSLIQHQR
CCCCCCCCCCCCCCC
29.3028555341
308UbiquitinationCGKSFSQKGSLISHQ
HCCCHHCCCCCEECC
49.63-
319PhosphorylationISHQRVHTGERPYEC
EECCEECCCCCCCHH
37.5729214152
336SumoylationYGKSFGQKGNLIQHQ
HHHHHCCCCCCCCCC
50.58-
336UbiquitinationYGKSFGQKGNLIQHQ
HHHHHCCCCCCCCCC
50.58-
336SumoylationYGKSFGQKGNLIQHQ
HHHHHCCCCCCCCCC
50.58-
347PhosphorylationIQHQQGHTGERAYHC
CCCCCCCCCCCCEEC
47.7825159151
354S-palmitoylationTGERAYHCGECGKSF
CCCCCEECCCCCHHH
2.9829575903
364SumoylationCGKSFRQKFCFINHQ
CCHHHHHEEEEEECC
39.58-
364SumoylationCGKSFRQKFCFINHQ
CCHHHHHEEEEEECC
39.58-
375PhosphorylationINHQRVHTGERPYKC
EECCCCCCCCCCEEC
37.5727251275
381SumoylationHTGERPYKCGECGKS
CCCCCCEECCCCCCC
38.15-
381SumoylationHTGERPYKCGECGKS
CCCCCCEECCCCCCC
38.15-
403PhosphorylationVQHQRGHTGERPYEC
EECCCCCCCCCCCCC
43.4928674419
411SumoylationGERPYECKECGKSFR
CCCCCCCCCCCCCEE
44.06-
411SumoylationGERPYECKECGKSFR
CCCCCCCCCCCCCEE
44.06-
419PhosphorylationECGKSFRYRSHLTEH
CCCCCEECCCCCCCC
17.9223532336
421PhosphorylationGKSFRYRSHLTEHQR
CCCEECCCCCCCCCC
17.5723532336
431PhosphorylationTEHQRLHTGERPYNC
CCCCCCCCCCCCCCH
45.3829759185
436PhosphorylationLHTGERPYNCRECGK
CCCCCCCCCHHHHHH
32.8729759185
459PhosphorylationLVHERVHTGERPYAC
EEEECCCCCCCCCHH
37.5721712546
480PhosphorylationFGNKNCVTIHQRIHT
HCCCCCEEEEEEEEC
18.23-
487PhosphorylationTIHQRIHTGERPYEC
EEEEEEECCCCCCCC
38.0628348404
504PhosphorylationCGKSFLSSSALHVHK
CCCCHHCCCCEEHHH
23.0628555341
505PhosphorylationGKSFLSSSALHVHKR
CCCHHCCCCEEHHHH
31.3228555341
511SumoylationSSALHVHKRVHSGQK
CCCEEHHHHHHCCCC
55.84-
511SumoylationSSALHVHKRVHSGQK
CCCEEHHHHHHCCCC
55.84-
532S-palmitoylationCGKSFAECSSLIKHR
CCCCHHHHHHHHHHC
2.7629575903
534PhosphorylationKSFAECSSLIKHRRI
CCHHHHHHHHHHCCC
45.8624719451
543PhosphorylationIKHRRIHTGERPYEC
HHHCCCCCCCCCEEC
38.0629214152
550S-palmitoylationTGERPYECTKCGKTF
CCCCCEECCCCCCEE
3.4829575903
553S-palmitoylationRPYECTKCGKTFQRS
CCEECCCCCCEEEHH
3.4929575903
561PhosphorylationGKTFQRSSTLLHHQS
CCEEEHHHHHHHHCH
25.8428555341

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 ZN417_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN417_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 ZN417_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KLC3_HUMANKLC3physical
25416956
CCD57_HUMANCCDC57physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR101_HUMANKRTAP10-1physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
LURA1_HUMANLURAP1physical
25416956
ZBT8A_HUMANZBTB8Aphysical
25416956
NINL_HUMANNINLphysical
21516116
CCDB1_HUMANCCNDBP1physical
21516116
TFP11_HUMANTFIP11physical
21516116
TRI27_HUMANTRIM27physical
21516116
CEP44_HUMANCEP44physical
21516116

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN417_HUMAN

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Related Literatures of Post-Translational Modification

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