FIZ1_HUMAN - dbPTM
FIZ1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FIZ1_HUMAN
UniProt AC Q96SL8
Protein Name Flt3-interacting zinc finger protein 1
Gene Name FIZ1
Organism Homo sapiens (Human).
Sequence Length 496
Subcellular Localization Cytoplasm. Nucleus.
Protein Description May be a transcriptional repressor of NRL function in photoreceptors. Does not repress CRX-mediated transactivation (By similarity)..
Protein Sequence MDDVPAPTPAPAPPAAAAPRVPFHCSECGKSFRYRSDLRRHFARHTALKPHACPRCGKGFKHSFNLANHLRSHTGERPYRCSACPKGFRDSTGLLHHQVVHTGEKPYCCLVCELRFSSRSSLGRHLKRQHRGVLPSPLQPGPGLPALSAPCSVCCNVGPCSVCGGSGAGGGEGPEGAGAGLGSWGLAEAAAAAAASLPPFACGACARRFDHGRELAAHWAAHTDVKPFKCPRCERDFNAPALLERHKLTHDLQGPGAPPAQAWAAGPGAGPETAGEGTAAEAGDAPLASDRRLLLGPAGGGVPKLGGLLPEGGGEAPAPAAAAEPSEDTLYQCDCGTFFASAAALASHLEAHSGPATYGCGHCGALYAALAALEEHRRVSHGEGGGEEAATAAREREPASGEPPSGSGRGKKIFGCSECEKLFRSPRDLERHVLVHTGEKPFPCLECGKFFRHECYLKRHRLLHGTERPFPCHICGKGFITLSNLSRHLKLHRGMD
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
1Acetylation-------MDDVPAPT
-------CCCCCCCC
10.0322814378
46PhosphorylationRRHFARHTALKPHAC
HHHHHHHHHCCCCCC
28.2928555341
63PhosphorylationCGKGFKHSFNLANHL
CCCCCHHCHHHHHHH
19.2028555341
74PhosphorylationANHLRSHTGERPYRC
HHHHHHCCCCCCCCC
41.8229496963
102PhosphorylationLHHQVVHTGEKPYCC
CCEEEEECCCCCEEE
35.1125159151
107PhosphorylationVHTGEKPYCCLVCEL
EECCCCCEEEEEEEE
13.58-
329PhosphorylationAAEPSEDTLYQCDCG
CCCCCCCCCEECCHH
24.26-
400PhosphorylationAREREPASGEPPSGS
HHHCCCCCCCCCCCC
55.1728122231
405PhosphorylationPASGEPPSGSGRGKK
CCCCCCCCCCCCCCE
57.2028122231
409MethylationEPPSGSGRGKKIFGC
CCCCCCCCCCEEECC
56.29-
437PhosphorylationERHVLVHTGEKPFPC
HCCEEEECCCCCCCE
39.2925159151
449UbiquitinationFPCLECGKFFRHECY
CCEEHHCCEECCHHH
53.65-
481PhosphorylationICGKGFITLSNLSRH
CCCCCEEEHHHHHHH
23.13-
483PhosphorylationGKGFITLSNLSRHLK
CCCEEEHHHHHHHHH
27.37-
486PhosphorylationFITLSNLSRHLKLHR
EEEHHHHHHHHHHHC
23.16-

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 FIZ1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FIZ1_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 FIZ1_HUMAN !!

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

Oops, there are no PPI records of FIZ1_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 FIZ1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74, AND MASSSPECTROMETRY.

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