ZN234_HUMAN - dbPTM
ZN234_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN234_HUMAN
UniProt AC Q14588
Protein Name Zinc finger protein 234
Gene Name ZNF234
Organism Homo sapiens (Human).
Sequence Length 700
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MTTFKEGLTFKDVAVVFTEEELGLLDPVQRNLYQDVMLENFRNLLSVGHHPFKHDVFLLEKEKKLDIMKTATQRKGKSADKIQSEVETVPEAGRHEELYWGQIWKQIASDLIKYEDSMISISRFPRQGDLSCQVRAGLYTTHTGQKFYQCDEYKKSFTDVFNFDLHQQLHSGEKSHTCDECGKSFCYISALHIHQRVHMGEKCYKCDVCGKEFSQSSHLQTHQRVHTVEKPFKCVECGKGFSRRSTLTVHCKLHSGEKPYNCEECGRAFIHASHLQEHQRIHTGEKPFKCDTCGKNFRRRSALNNHCMVHTGEKPYKCEDCGKCFTCSSNLRIHQRVHTGEKPYKCEECGKCFIQPSQFQAHRRIHTGEKPYVCKVCGKGFIYSSSFQAHQGVHTGEKPYKCNECGKSFRMKIHYQVHLVVHTGEKPYKCEVCGKAFRQSSYLKIHLKAHSVQKPFKCEECGQGFNQSSRLQIHQLIHTGEKPYKCEECGKGFSRRADLKIHCRIHTGEKPYNCEECGKVFSQASHLLTHQRVHSGEKPFKCEECGKSFSRSAHLQAHQKVHTGEKPYKCGECGKGFKWSLNLDMHQRVHTGEKPYTCGECGKHFSQASSLQLHQSVHTGEKPYKCDVCGKVFSRSSQLQYHRRVHTGEKPYKCEICGKRFSWRSNLVSHHKIHAAGTFYENDENSKNIRELSEGGSSTR
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
5Acetylation---MTTFKEGLTFKD
---CCCCCCCCCCCC
49.1023236377
18PhosphorylationKDVAVVFTEEELGLL
CCEEEEEEHHHHCCC
30.77-
33PhosphorylationDPVQRNLYQDVMLEN
CHHHHHHHHHHHHHH
13.2520860994
64SumoylationFLLEKEKKLDIMKTA
EEEEHHHHHHHHHHH
53.11-
64SumoylationFLLEKEKKLDIMKTA
EEEEHHHHHHHHHHH
53.11-
70PhosphorylationKKLDIMKTATQRKGK
HHHHHHHHHHHHCCC
19.9829759185
72PhosphorylationLDIMKTATQRKGKSA
HHHHHHHHHHCCCCH
33.8529759185
77UbiquitinationTATQRKGKSADKIQS
HHHHHCCCCHHHHHH
45.57-
78PhosphorylationATQRKGKSADKIQSE
HHHHCCCCHHHHHHH
50.82-
81UbiquitinationRKGKSADKIQSEVET
HCCCCHHHHHHHEEE
42.22-
84PhosphorylationKSADKIQSEVETVPE
CCHHHHHHHEEECCC
47.27-
88PhosphorylationKIQSEVETVPEAGRH
HHHHHEEECCCCCCC
46.68-
114PhosphorylationIASDLIKYEDSMISI
HHHHHHHHHHCEEEE
20.27-
117PhosphorylationDLIKYEDSMISISRF
HHHHHHHCEEEEECC
13.18-
140PhosphorylationQVRAGLYTTHTGQKF
EEECEEEECCCCCEE
19.6923532336
141PhosphorylationVRAGLYTTHTGQKFY
EECEEEECCCCCEEE
12.1323532336
204PhosphorylationVHMGEKCYKCDVCGK
HHCCCCEEECCCCCC
26.2222817900
233SumoylationHTVEKPFKCVECGKG
ECCCCCEEEEECCCC
45.99-
233SumoylationHTVEKPFKCVECGKG
ECCCCCEEEEECCCC
45.99-
245PhosphorylationGKGFSRRSTLTVHCK
CCCCCCCCEEEEEEE
27.02-
246PhosphorylationKGFSRRSTLTVHCKL
CCCCCCCEEEEEEEE
25.33-
255PhosphorylationTVHCKLHSGEKPYNC
EEEEEECCCCCCCCH
60.1126074081
258AcetylationCKLHSGEKPYNCEEC
EEECCCCCCCCHHHH
57.2225953088
260PhosphorylationLHSGEKPYNCEECGR
ECCCCCCCCHHHHHH
43.4426074081
273PhosphorylationGRAFIHASHLQEHQR
HHEEEEHHHHHHHCC
15.5726074081
283PhosphorylationQEHQRIHTGEKPFKC
HHHCCCCCCCCCCCC
44.6718669648
311PhosphorylationNNHCMVHTGEKPYKC
HCCCEEECCCCCEEC
35.3129496963
314SumoylationCMVHTGEKPYKCEDC
CEEECCCCCEECCCC
55.80-
314SumoylationCMVHTGEKPYKCEDC
CEEECCCCCEECCCC
55.80-
314UbiquitinationCMVHTGEKPYKCEDC
CEEECCCCCEECCCC
55.80-
317SumoylationHTGEKPYKCEDCGKC
ECCCCCEECCCCCCE
39.41-
317SumoylationHTGEKPYKCEDCGKC
ECCCCCEECCCCCCE
39.41-
339PhosphorylationRIHQRVHTGEKPYKC
EEECEEECCCCCEEC
44.1529496963
342SumoylationQRVHTGEKPYKCEEC
CEEECCCCCEECCCC
55.80-
342SumoylationQRVHTGEKPYKCEEC
CEEECCCCCEECCCC
55.80-
342UbiquitinationQRVHTGEKPYKCEEC
CEEECCCCCEECCCC
55.80-
344PhosphorylationVHTGEKPYKCEECGK
EECCCCCEECCCCCC
39.06-
345SumoylationHTGEKPYKCEECGKC
ECCCCCEECCCCCCE
43.63-
345SumoylationHTGEKPYKCEECGKC
ECCCCCEECCCCCCE
43.63-
345UbiquitinationHTGEKPYKCEECGKC
ECCCCCEECCCCCCE
43.63-
367PhosphorylationQAHRRIHTGEKPYVC
CCCCCCCCCCCCEEE
44.6727732954
395PhosphorylationQAHQGVHTGEKPYKC
ECCCCCCCCCCCEEE
44.6329496963
398SumoylationQGVHTGEKPYKCNEC
CCCCCCCCCEEECCC
55.80-
398UbiquitinationQGVHTGEKPYKCNEC
CCCCCCCCCEEECCC
55.80-
398SumoylationQGVHTGEKPYKCNEC
CCCCCCCCCEEECCC
55.80-
401SumoylationHTGEKPYKCNECGKS
CCCCCCEEECCCCCE
38.83-
401SumoylationHTGEKPYKCNECGKS
CCCCCCEEECCCCCE
38.83-
423PhosphorylationQVHLVVHTGEKPYKC
EEEEEEECCCCCEEE
35.1129496963
426SumoylationLVVHTGEKPYKCEVC
EEEECCCCCEEEEEC
55.80-
426SumoylationLVVHTGEKPYKCEVC
EEEECCCCCEEEEEC
55.80-
426UbiquitinationLVVHTGEKPYKCEVC
EEEECCCCCEEEEEC
55.80-
428PhosphorylationVHTGEKPYKCEVCGK
EECCCCCEEEEECCH
39.06-
429SumoylationHTGEKPYKCEVCGKA
ECCCCCEEEEECCHH
32.23-
429SumoylationHTGEKPYKCEVCGKA
ECCCCCEEEEECCHH
32.23-
440PhosphorylationCGKAFRQSSYLKIHL
CCHHHHHCCEEEEEE
19.3928348404
441PhosphorylationGKAFRQSSYLKIHLK
CHHHHHCCEEEEEEE
26.5828348404
442PhosphorylationKAFRQSSYLKIHLKA
HHHHHCCEEEEEEEE
19.7728348404
457SumoylationHSVQKPFKCEECGQG
ECCCCCEECCCCCCC
49.62-
457SumoylationHSVQKPFKCEECGQG
ECCCCCEECCCCCCC
49.62-
479PhosphorylationQIHQLIHTGEKPYKC
EEEEHHHCCCCCEEC
39.7929496963
482UbiquitinationQLIHTGEKPYKCEEC
EHHHCCCCCEECCCC
55.80-
484PhosphorylationIHTGEKPYKCEECGK
HHCCCCCEECCCCCC
39.06-
485SumoylationHTGEKPYKCEECGKG
HCCCCCEECCCCCCC
43.63-
485SumoylationHTGEKPYKCEECGKG
HCCCCCEECCCCCCC
43.63-
485UbiquitinationHTGEKPYKCEECGKG
HCCCCCEECCCCCCC
43.63-
507PhosphorylationKIHCRIHTGEKPYNC
EEEEEEECCCCCCCH
44.6727282143
535PhosphorylationLTHQRVHSGEKPFKC
HHCCCCCCCCCCEEC
45.8720068231
538UbiquitinationQRVHSGEKPFKCEEC
CCCCCCCCCEECHHH
60.32-
541SumoylationHSGEKPFKCEECGKS
CCCCCCEECHHHCCC
49.62-
541SumoylationHSGEKPFKCEECGKS
CCCCCCEECHHHCCC
49.62-
550PhosphorylationEECGKSFSRSAHLQA
HHHCCCCCHHHHHHH
32.2017081983
563PhosphorylationQAHQKVHTGEKPYKC
HHHCCCCCCCCCEEC
50.4529496963
566SumoylationQKVHTGEKPYKCGEC
CCCCCCCCCEECCCC
55.80-
566SumoylationQKVHTGEKPYKCGEC
CCCCCCCCCEECCCC
55.80-
566UbiquitinationQKVHTGEKPYKCGEC
CCCCCCCCCEECCCC
55.80-
569SumoylationHTGEKPYKCGECGKG
CCCCCCEECCCCCCC
44.27-
569SumoylationHTGEKPYKCGECGKG
CCCCCCEECCCCCCC
44.27-
591PhosphorylationDMHQRVHTGEKPYTC
CCCCCCCCCCCCCCC
44.15-
619PhosphorylationQLHQSVHTGEKPYKC
EEHHCHHCCCCCEEC
44.9029496963
622SumoylationQSVHTGEKPYKCDVC
HCHHCCCCCEECCCC
55.80-
622UbiquitinationQSVHTGEKPYKCDVC
HCHHCCCCCEECCCC
55.80-
622SumoylationQSVHTGEKPYKCDVC
HCHHCCCCCEECCCC
55.80-
647PhosphorylationQYHRRVHTGEKPYKC
CCCCCCCCCCCCEEC
44.1529496963
650SumoylationRRVHTGEKPYKCEIC
CCCCCCCCCEECEEC
55.80-
650UbiquitinationRRVHTGEKPYKCEIC
CCCCCCCCCEECEEC
55.80-
650SumoylationRRVHTGEKPYKCEIC
CCCCCCCCCEECEEC
55.80-
678PhosphorylationHKIHAAGTFYENDEN
CEEEECCCCCCCCCC
20.5128060719
680PhosphorylationIHAAGTFYENDENSK
EEECCCCCCCCCCCC
17.4128060719

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 ZN234_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN234_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 ZN234_HUMAN !!

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

Oops, there are no PPI records of ZN234_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN234_HUMAN

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Related Literatures of Post-Translational Modification

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