ZN304_HUMAN - dbPTM
ZN304_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN304_HUMAN
UniProt AC Q9HCX3
Protein Name Zinc finger protein 304 {ECO:0000312|HGNC:HGNC:13505}
Gene Name ZNF304 {ECO:0000312|HGNC:HGNC:13505}
Organism Homo sapiens (Human).
Sequence Length 659
Subcellular Localization Nucleus . Associates with chromatin (PubMed:24623306).
Protein Description Acts as transcriptional regulator and plays a role in gene silencing. [PubMed: 24623306]
Protein Sequence MAAAVLMDRVQSCVTFEDVFVYFSREEWELLEEAQRFLYRDVMLENFALVATLGFWCEAEHEAPSEQSVSVEGVSQVRTAESGLFQKAHPCEMCDPLLKDILHLAEHQGSHLTQKLCTRGLCRRRFSFSANFYQHQKQHNGENCFRGDDGGASFVKSCTVHMLGRSFTCREEGMDLPDSSGLFQHQTTYNRVSPCRRTECMESFPHSSSLRQHQGDYDGQMLFSCGDEGKAFLDTFTLLDSQMTHAEVRPFRCLPCGNVFKEKSALINHRKIHSGEISHVCKECGKAFIHLHHLKMHQKFHTGKRHYTCSECGKAFSRKDTLVQHQRVHTGERSYDCSECGKAYSRSSHLVQHQRIHTGERPYKCNKCGKAFSRKDTLVQHQRFHTGERPYECSECGKFFSQSSHLIEHWRIHTGARPYECIECGKFFSHNSSLIKHRRVHTGARSYVCSKCGKAFGCKDTLVQHQIIHTGARPYECSECGKAFSRKDTLVQHQKIHTGERPYECGECGKFFSHSSNLIVHQRIHTGAKPYECNECGKCFSHNSSLILHQRVHTGARPYVCSECGKAYISSSHLVQHKKVHTGARPYECSECGKFFSRNSGLILHQRVHTGEKPYVCSECGKAYSRSSHLVRHQKAHTGERAHECNSFGGPLAASLKLV
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
99UbiquitinationEMCDPLLKDILHLAE
CCCHHHHHHHHHHHH
50.86-
127PhosphorylationGLCRRRFSFSANFYQ
HCCHHHCCCCCCCHH
19.2423898821
129PhosphorylationCRRRFSFSANFYQHQ
CHHHCCCCCCCHHHH
22.5428348404
209PhosphorylationESFPHSSSLRQHQGD
HHCCCCHHHHHCCCC
30.5025690035
263UbiquitinationCGNVFKEKSALINHR
CCCCCCCCCCEEECC
41.44-
271SumoylationSALINHRKIHSGEIS
CCEEECCCCCCCHHH
36.90-
271UbiquitinationSALINHRKIHSGEIS
CCEEECCCCCCCHHH
36.90-
271SumoylationSALINHRKIHSGEIS
CCEEECCCCCCCHHH
36.90-
274PhosphorylationINHRKIHSGEISHVC
EECCCCCCCHHHHHH
41.4125159151
308PhosphorylationHTGKRHYTCSECGKA
CCCCCEEEHHHHCCC
11.93-
314UbiquitinationYTCSECGKAFSRKDT
EEHHHHCCCCCCCCC
58.90-
317PhosphorylationSECGKAFSRKDTLVQ
HHHCCCCCCCCCEEE
43.19-
319SumoylationCGKAFSRKDTLVQHQ
HCCCCCCCCCEEEEC
54.59-
319UbiquitinationCGKAFSRKDTLVQHQ
HCCCCCCCCCEEEEC
54.59-
319SumoylationCGKAFSRKDTLVQHQ
HCCCCCCCCCEEEEC
54.59-
330PhosphorylationVQHQRVHTGERSYDC
EEECEECCCCCCEEH
37.57-
334PhosphorylationRVHTGERSYDCSECG
EECCCCCCEEHHHHH
22.48-
338PhosphorylationGERSYDCSECGKAYS
CCCCEEHHHHHCEEC
32.78-
358PhosphorylationVQHQRIHTGERPYKC
HCCCCCCCCCCCCCC
38.0624719451
375UbiquitinationCGKAFSRKDTLVQHQ
CCCCCCCCCCCEECC
54.59-
375SumoylationCGKAFSRKDTLVQHQ
CCCCCCCCCCCEECC
54.59-
375SumoylationCGKAFSRKDTLVQHQ
CCCCCCCCCCCEECC
54.59-
386PhosphorylationVQHQRFHTGERPYEC
EECCCCCCCCCCEEC
37.7228555341
414PhosphorylationIEHWRIHTGARPYEC
HHHEEECCCCCCEEE
30.1128555341
432PhosphorylationGKFFSHNSSLIKHRR
CCCCCCCCCHHCCCC
22.5425627689
433PhosphorylationKFFSHNSSLIKHRRV
CCCCCCCCHHCCCCC
39.1625159151
442PhosphorylationIKHRRVHTGARSYVC
HCCCCCCCCCHHEEE
29.67-
470PhosphorylationVQHQIIHTGARPYEC
EECEEEECCCCCEEC
23.3328555341
482UbiquitinationYECSECGKAFSRKDT
EECCCCCCCCCCCCC
58.90-
485PhosphorylationSECGKAFSRKDTLVQ
CCCCCCCCCCCCCEE
43.19-
487SumoylationCGKAFSRKDTLVQHQ
CCCCCCCCCCCEECC
54.59-
487UbiquitinationCGKAFSRKDTLVQHQ
CCCCCCCCCCCEECC
54.59-
498PhosphorylationVQHQKIHTGERPYEC
EECCEECCCCCCEEC
44.1828555341
526PhosphorylationIVHQRIHTGAKPYEC
EEEEEECCCCCCEEC
36.1421712546
545PhosphorylationKCFSHNSSLILHQRV
CCCCCCCCEEEEECC
25.4223186163
554PhosphorylationILHQRVHTGARPYVC
EEEECCCCCCCCEEE
29.6728555341
597PhosphorylationSECGKFFSRNSGLIL
CCCCCCCCCCCCEEE
33.4125394399
600PhosphorylationGKFFSRNSGLILHQR
CCCCCCCCCEEEEEE
33.5928555341
610PhosphorylationILHQRVHTGEKPYVC
EEEEEEECCCCCEEE
44.1521712546
647PhosphorylationERAHECNSFGGPLAA
CCHHHCCCCCCCCHH
36.6124719451

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 ZN304_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN304_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 ZN304_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBP28_HUMANUSP28physical
24623306

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN304_HUMAN

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Related Literatures of Post-Translational Modification

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